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Conserved domains on  [gi|24585132|ref|NP_724161|]
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Lim3, isoform B [Drosophila melanogaster]

Protein Classification

homeobox domain-containing protein( domain architecture ID 10873403)

homeobox domain-containing protein similar to double homeobox protein that may act as a transcription factor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LIM2_Lhx3_Lhx4 cd09376
The second LIM domain of Lhx3-Lhx4 family; The second LIM domain of Lhx3-Lhx4 family: Lhx3 and ...
181-236 3.42e-35

The second LIM domain of Lhx3-Lhx4 family; The second LIM domain of Lhx3-Lhx4 family: Lhx3 and Lhx4 belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. The LHX3 and LHX4 LIM-homeodomain transcription factors play essential roles in pituitary gland and nervous system development. Although LHX3 and LHX4 share marked sequence homology, the genes have different expression patterns. They play overlapping, but distinct functions during the establishment of the specialized cells of the mammalian pituitary gland and the nervous system. Lhx3 proteins have been demonstrated the ability to directly bind to the promoters/enhancers of several pituitary hormone gene promoters to cause increased transcription.Lhx3a and Lhx3b, whose mRNAs have distinct temporal expression profiles during development, are two isoforms of Lhx3. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


:

Pssm-ID: 188762  Cd Length: 56  Bit Score: 125.54  E-value: 3.42e-35
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDRKLICKRDY 236
Cdd:cd09376   1 CAGCDEGIPPTQVVRRAQDNVYHLECFACFMCKRQLETGDEFYLMEDDRLVCKKDY 56
LIM1_Lhx3_Lhx4 cd09368
The first LIM domain of Lhx3 and Lhx4 family; The first LIM domain of Lhx3-Lhx4 family: Lhx3 ...
122-173 6.93e-29

The first LIM domain of Lhx3 and Lhx4 family; The first LIM domain of Lhx3-Lhx4 family: Lhx3 and Lhx4 belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. The LHX3 and LHX4 LIM-homeodomain transcription factors play essential roles in pituitary gland and nervous system development. Although LHX3 and LHX4 share marked sequence homology, the genes have different expression patterns. They play overlapping, but distinct functions during the establishment of the specialized cells of the mammalian pituitary gland and the nervous system. Lhx3 proteins have been demonstrated the ability to directly bind to the promoters/enhancers of several pituitary hormone gene promoters to cause increased transcription. Lhx3a and Lhx3b, whose mRNAs have distinct temporal expression profiles during development, are two isoforms of Lhx3. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


:

Pssm-ID: 188754  Cd Length: 52  Bit Score: 108.28  E-value: 6.93e-29
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFARNGQLFCKEDF 173
Cdd:cd09368   1 CGGCQEHILDRFILKVLDRTWHAKCLKCNDCGAQLTDKCFARNGHVYCKDDF 52
Homeodomain pfam00046
Homeodomain;
257-313 2.36e-24

Homeodomain;


:

Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 95.64  E-value: 2.36e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24585132   257 KRPRTTITAKQLETLKTAYNNSPKPARHVREQLSQDTGLDMRVVQVWFQNRRAKEKR 313
Cdd:pfam00046   1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
 
Name Accession Description Interval E-value
LIM2_Lhx3_Lhx4 cd09376
The second LIM domain of Lhx3-Lhx4 family; The second LIM domain of Lhx3-Lhx4 family: Lhx3 and ...
181-236 3.42e-35

The second LIM domain of Lhx3-Lhx4 family; The second LIM domain of Lhx3-Lhx4 family: Lhx3 and Lhx4 belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. The LHX3 and LHX4 LIM-homeodomain transcription factors play essential roles in pituitary gland and nervous system development. Although LHX3 and LHX4 share marked sequence homology, the genes have different expression patterns. They play overlapping, but distinct functions during the establishment of the specialized cells of the mammalian pituitary gland and the nervous system. Lhx3 proteins have been demonstrated the ability to directly bind to the promoters/enhancers of several pituitary hormone gene promoters to cause increased transcription.Lhx3a and Lhx3b, whose mRNAs have distinct temporal expression profiles during development, are two isoforms of Lhx3. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188762  Cd Length: 56  Bit Score: 125.54  E-value: 3.42e-35
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDRKLICKRDY 236
Cdd:cd09376   1 CAGCDEGIPPTQVVRRAQDNVYHLECFACFMCKRQLETGDEFYLMEDDRLVCKKDY 56
LIM1_Lhx3_Lhx4 cd09368
The first LIM domain of Lhx3 and Lhx4 family; The first LIM domain of Lhx3-Lhx4 family: Lhx3 ...
122-173 6.93e-29

The first LIM domain of Lhx3 and Lhx4 family; The first LIM domain of Lhx3-Lhx4 family: Lhx3 and Lhx4 belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. The LHX3 and LHX4 LIM-homeodomain transcription factors play essential roles in pituitary gland and nervous system development. Although LHX3 and LHX4 share marked sequence homology, the genes have different expression patterns. They play overlapping, but distinct functions during the establishment of the specialized cells of the mammalian pituitary gland and the nervous system. Lhx3 proteins have been demonstrated the ability to directly bind to the promoters/enhancers of several pituitary hormone gene promoters to cause increased transcription. Lhx3a and Lhx3b, whose mRNAs have distinct temporal expression profiles during development, are two isoforms of Lhx3. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188754  Cd Length: 52  Bit Score: 108.28  E-value: 6.93e-29
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFARNGQLFCKEDF 173
Cdd:cd09368   1 CGGCQEHILDRFILKVLDRTWHAKCLKCNDCGAQLTDKCFARNGHVYCKDDF 52
Homeodomain pfam00046
Homeodomain;
257-313 2.36e-24

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 95.64  E-value: 2.36e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24585132   257 KRPRTTITAKQLETLKTAYNNSPKPARHVREQLSQDTGLDMRVVQVWFQNRRAKEKR 313
Cdd:pfam00046   1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
257-315 1.30e-19

Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.


Pssm-ID: 238039 [Multi-domain]  Cd Length: 59  Bit Score: 82.29  E-value: 1.30e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24585132 257 KRPRTTITAKQLETLKTAYNNSPKPARHVREQLSQDTGLDMRVVQVWFQNRRAKEKRLK 315
Cdd:cd00086   1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
256-312 1.38e-19

Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes


Pssm-ID: 197696 [Multi-domain]  Cd Length: 57  Bit Score: 82.30  E-value: 1.38e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24585132    256 NKRPRTTITAKQLETLKTAYNNSPKPARHVREQLSQDTGLDMRVVQVWFQNRRAKEK 312
Cdd:smart00389   1 KRRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
122-177 7.56e-17

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 74.68  E-value: 7.56e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24585132   122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFA-RNGQLFCKEDFFKRY 177
Cdd:pfam00412   1 CAGCNRPIYDRELVRALGKVWHPECFRCAVCGKPLTTGDFYeKDGKLYCKHDYYKLF 57
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
181-240 1.92e-13

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 64.66  E-value: 1.92e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585132   181 CSACDMGIPPTQVVRrAQDNVYHLQCFLCAMCSRTLNTGDEFYLmeDRKLICKRDYEEAK 240
Cdd:pfam00412   1 CAGCNRPIYDRELVR-ALGKVWHPECFRCAVCGKPLTTGDFYEK--DGKLYCKHDYYKLF 57
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
233-324 1.22e-12

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 65.54  E-value: 1.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585132 233 KRDYEEAkAKGLYLDGSLDGDQPNKRPRTTITAKQLETLKTAYNNSPKPARHVREQLSQDTGLDMRVVQVWFQNRRAKEK 312
Cdd:COG5576  29 KREVEAA-DSEMKLERKQDGSSPPKSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEK 107
                        90
                ....*....|..
gi 24585132 313 RLKKDAGRTRWS 324
Cdd:COG5576 108 KKRSGKVEQRPG 119
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
180-235 1.10e-11

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 59.70  E-value: 1.10e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132    180 KCSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNtgDEFYLMEDRKLICKRD 235
Cdd:smart00132   1 KCAGCGKPIYGTERVLRALGKVWHPECFKCATCGKPLS--GDTFFEKDGKLYCKDC 54
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
121-172 2.87e-11

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 58.55  E-value: 2.87e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24585132    121 KCGGCHELILDR-FILKVLERTWHAKCLQCSECHGQL-NDKCFARNGQLFCKED 172
Cdd:smart00132   1 KCAGCGKPIYGTeRVLRALGKVWHPECFKCATCGKPLsGDTFFEKDGKLYCKDC 54
 
Name Accession Description Interval E-value
LIM2_Lhx3_Lhx4 cd09376
The second LIM domain of Lhx3-Lhx4 family; The second LIM domain of Lhx3-Lhx4 family: Lhx3 and ...
181-236 3.42e-35

The second LIM domain of Lhx3-Lhx4 family; The second LIM domain of Lhx3-Lhx4 family: Lhx3 and Lhx4 belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. The LHX3 and LHX4 LIM-homeodomain transcription factors play essential roles in pituitary gland and nervous system development. Although LHX3 and LHX4 share marked sequence homology, the genes have different expression patterns. They play overlapping, but distinct functions during the establishment of the specialized cells of the mammalian pituitary gland and the nervous system. Lhx3 proteins have been demonstrated the ability to directly bind to the promoters/enhancers of several pituitary hormone gene promoters to cause increased transcription.Lhx3a and Lhx3b, whose mRNAs have distinct temporal expression profiles during development, are two isoforms of Lhx3. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188762  Cd Length: 56  Bit Score: 125.54  E-value: 3.42e-35
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDRKLICKRDY 236
Cdd:cd09376   1 CAGCDEGIPPTQVVRRAQDNVYHLECFACFMCKRQLETGDEFYLMEDDRLVCKKDY 56
LIM1_Lhx3_Lhx4 cd09368
The first LIM domain of Lhx3 and Lhx4 family; The first LIM domain of Lhx3-Lhx4 family: Lhx3 ...
122-173 6.93e-29

The first LIM domain of Lhx3 and Lhx4 family; The first LIM domain of Lhx3-Lhx4 family: Lhx3 and Lhx4 belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. The LHX3 and LHX4 LIM-homeodomain transcription factors play essential roles in pituitary gland and nervous system development. Although LHX3 and LHX4 share marked sequence homology, the genes have different expression patterns. They play overlapping, but distinct functions during the establishment of the specialized cells of the mammalian pituitary gland and the nervous system. Lhx3 proteins have been demonstrated the ability to directly bind to the promoters/enhancers of several pituitary hormone gene promoters to cause increased transcription. Lhx3a and Lhx3b, whose mRNAs have distinct temporal expression profiles during development, are two isoforms of Lhx3. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188754  Cd Length: 52  Bit Score: 108.28  E-value: 6.93e-29
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFARNGQLFCKEDF 173
Cdd:cd09368   1 CGGCQEHILDRFILKVLDRTWHAKCLKCNDCGAQLTDKCFARNGHVYCKDDF 52
LIM1_Lhx3a cd09466
The first LIM domain of Lhx3a; The first LIM domain of Lhx3a: Lhx3a is a member of LHX protein ...
119-174 3.42e-25

The first LIM domain of Lhx3a; The first LIM domain of Lhx3a: Lhx3a is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx3a is one of the two isoforms of Lhx3. The Lhx3 gene is expressed in the ventral spinal cord, the pons, the medulla oblongata, and the pineal gland of the developing nervous system during mouse embryogenesis, and transcripts are found in the emergent pituitary gland. Lhx3 functions in concert with other transcription factors to specify interneuron and motor neuron fates during development. Lhx3 proteins have been demonstrated to directly bind to the promoters of several pituitary hormone gene promoters. The Lhx3 gene encodes two isoforms, LHX3a and LHX3b that differ in their amino-terminal sequences, where Lhx3a has longer N-terminal. They show differential activation of pituitary hormone genes and distinct DNA binding properties. In human, Lhx3a trans-activated the alpha-glycoprotein subunit promoter and genes containing a high-affinity Lhx3 binding site more effectively than the hLhx3b isoform. In addition, hLhx3a induce transcription of the TSHbeta-subunit gene by acting on pituitary POU domain factor, Pit-1, while hLhx3b does not. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188850 [Multi-domain]  Cd Length: 56  Bit Score: 97.93  E-value: 3.42e-25
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 119 IPKCGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFARNGQLFCKEDFF 174
Cdd:cd09466   1 IPKCAGCDHPIFDRFILKVQDKPWHSKCLKCVDCQAQLTDKCFSRGGQVYCKEDFF 56
Homeodomain pfam00046
Homeodomain;
257-313 2.36e-24

Homeodomain;


Pssm-ID: 459649 [Multi-domain]  Cd Length: 57  Bit Score: 95.64  E-value: 2.36e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24585132   257 KRPRTTITAKQLETLKTAYNNSPKPARHVREQLSQDTGLDMRVVQVWFQNRRAKEKR 313
Cdd:pfam00046   1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
LIM2_Lhx3b cd09472
The second LIM domain of Lhx3b; The second LIM domain of Lhx3b. Lhx3b is a member of LHX ...
180-236 5.28e-24

The second LIM domain of Lhx3b; The second LIM domain of Lhx3b. Lhx3b is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx3b is one of the two isoforms of Lhx3. The Lhx3 gene is expressed in the ventral spinal cord, the pons, the medulla oblongata, and the pineal gland of the developing nervous system during mouse embryogenesis, and transcripts are found in the emergent pituitary gland. Lhx3 functions in concert with other transcription factors to specify interneuron and motor neuron fates during development. Lhx3 proteins have been demonstrated to directly bind to the promoters of several pituitary hormone gene promoters. The Lhx3 gene encodes two isoforms, LHX3a and LHX3b that differ in their amino-terminal sequences, where Lhx3a has longer N-terminal. They show differential activation of pituitary hormone genes and distinct DNA binding properties. In human, Lhx3a trans-activated the alpha-glycoprotein subunit promoter and genes containing a high-affinity Lhx3 binding site more effectively than the hLhx3b isoform. In addition, hLhx3a induce transcription of the TSHbeta-subunit gene by acting on pituitary POU domain factor, Pit-1, while hLhx3b does not. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein


Pssm-ID: 188856  Cd Length: 57  Bit Score: 94.76  E-value: 5.28e-24
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24585132 180 KCSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDRKLICKRDY 236
Cdd:cd09472   1 KCAACQQGIPPTQVVRRAQDFVYHLHCFACIVCKRQLATGDEFYLMEDSRLVCKADY 57
LIM2_Lhx4 cd09473
The second LIM domain of Lhx4; The second LIM domain of Lhx4. Lhx4 belongs to the LHX protein ...
181-236 3.65e-23

The second LIM domain of Lhx4; The second LIM domain of Lhx4. Lhx4 belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188857  Cd Length: 56  Bit Score: 92.39  E-value: 3.65e-23
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDRKLICKRDY 236
Cdd:cd09473   1 CTACQQGIPPTQVVRKAQDFVYHLHCFACIICSRQLATGDEFYLMEDGRLVCKEDY 56
LIM2_Lhx1_Lhx5 cd09375
The second LIM domain of Lhx1 (also known as Lim1) and Lhx5; The second LIM domain of Lhx1 ...
181-236 2.77e-22

The second LIM domain of Lhx1 (also known as Lim1) and Lhx5; The second LIM domain of Lhx1 (also known as Lim1) and Lhx5. Lhx1 and Lhx5 are closely related members of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx1 is required for regulating the vertebrate head organizer, the nervous system, and female reproductive tract development. During embryogenesis in the mouse, Lhx1 is expressed early in mesodermal tissue, then later during urogenital, kidney, liver, and nervous system development. In the adult, expression is restricted to the kidney and brain. A mouse embryos with Lhx1 gene knockout cannot grow normal anterior head structures, kidneys, and gonads, but with normally developed trunk and tail morphology. In the developing nervous system, Lhx1 is required to direct the trajectories of motor axons in the limb. Lhx1 null female mice lack the oviducts and uterus. Lhx5 protein may play complementary or overlapping roles with Lhx1. The expression of Lhx5 in the anterior portion of the mouse neural tube suggests a role in patterning of the forebrain. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188761  Cd Length: 56  Bit Score: 89.73  E-value: 2.77e-22
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDRKLICKRDY 236
Cdd:cd09375   1 CAGCDQGISPNDLVRRARDKVFHLNCFTCMVCRKQLSTGEELYILDENKFICKEDY 56
LIM1_Lhx1_Lhx5 cd09367
The first LIM domain of Lhx1 (also known as Lim1) and Lhx5; The first LIM domain of Lhx1 (also ...
122-173 2.53e-21

The first LIM domain of Lhx1 (also known as Lim1) and Lhx5; The first LIM domain of Lhx1 (also known as Lim1) and Lhx5. Lhx1 and Lhx5 are closely related members of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx1 is required for regulating the vertebrate head organizer, the nervous system, and female reproductive tract development. During embryogenesis in the mouse, Lhx1 is expressed early in mesodermal tissue, then later during urogenital, kidney, liver, and nervous system development. In the adult, expression is restricted to the kidney and brain. A mouse embryos with Lhx1 gene knockout cannot grow normal anterior head structures, kidneys, and gonads, but with normally developed trunk and tail morphology. In the developing nervous system, Lhx1 is required to direct the trajectories of motor axons in the limb. Lhx1 null female mice lack the oviducts and uterus. Lhx5 protein may play complementary or overlapping roles with Lhx1. The expression of Lhx5 in the anterior portion of the mouse neural tube suggests a role in patterning of the forebrain. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188753 [Multi-domain]  Cd Length: 52  Bit Score: 87.10  E-value: 2.53e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFARNGQLFCKEDF 173
Cdd:cd09367   1 CAGCDRPILDKFLLNVLDRAWHAKCVQCCDCKCPLTEKCFSREGKLYCRNDF 52
LIM1_Lhx3b cd09467
The first LIM domain of Lhx3b; The first LIM domain of Lhx3b. Lhx3b is a member of LHX protein ...
119-173 3.44e-21

The first LIM domain of Lhx3b; The first LIM domain of Lhx3b. Lhx3b is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx3b is one of the two isoforms of Lhx3. The Lhx3 gene is expressed in the ventral spinal cord, the pons, the medulla oblongata, and the pineal gland of the developing nervous system during mouse embryogenesis, and transcripts are found in the emergent pituitary gland. Lhx3 functions in concert with other transcription factors to specify interneuron and motor neuron fates during development. Lhx3 proteins have been demonstrated to directly bind to the promoters of several pituitary hormone gene promoters. The Lhx3 gene encodes two isoforms, LHX3a and LHX3b that differ in their amino-terminal sequences, where Lhx3a has longer N-terminal. They show differential activation of pituitary hormone genes and distinct DNA binding properties. In human, Lhx3a trans-activated the alpha-glycoprotein subunit promoter and genes containing a high-affinity Lhx3 binding site more effectively than the hLhx3b isoform. In addition, hLhx3a induce transcription of the TSHbeta-subunit gene by acting on pituitary POU domain factor, Pit-1, while hLhx3b does not. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188851 [Multi-domain]  Cd Length: 55  Bit Score: 86.91  E-value: 3.44e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24585132 119 IPKCGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFARNGQLFCKEDF 173
Cdd:cd09467   1 IPLCAGCNQHIVDRFILKVLDRHWHSKCLKCSDCQTQLAEKCFSRGDSVYCKDDF 55
LIM1_Lhx4 cd09468
The first LIM domain of Lhx4; The first LIM domain of Lhx4. Lhx4 belongs to the LHX protein ...
122-173 9.37e-21

The first LIM domain of Lhx4; The first LIM domain of Lhx4. Lhx4 belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. LHX4 plays essential roles in pituitary gland and nervous system development. In mice, the lhx4 gene is expressed in the developing hindbrain, cerebral cortex, pituitary gland, and spinal cord. LHX4 shows significant sequence similarity to LHX3, particularly to isoforms Lhx3a. In gene regulation experiments, the LHX4 protein exhibits regulation roles towards pituitary genes, acting on their promoters/enhancers. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188852  Cd Length: 52  Bit Score: 85.41  E-value: 9.37e-21
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFARNGQLFCKEDF 173
Cdd:cd09468   1 CAGCNQHILDKFILKVLDRHWHSSCLKCADCQMQLAERCFSRAGNVYCKEDF 52
homeodomain cd00086
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ...
257-315 1.30e-19

Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.


Pssm-ID: 238039 [Multi-domain]  Cd Length: 59  Bit Score: 82.29  E-value: 1.30e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24585132 257 KRPRTTITAKQLETLKTAYNNSPKPARHVREQLSQDTGLDMRVVQVWFQNRRAKEKRLK 315
Cdd:cd00086   1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE 59
HOX smart00389
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ...
256-312 1.38e-19

Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes


Pssm-ID: 197696 [Multi-domain]  Cd Length: 57  Bit Score: 82.30  E-value: 1.38e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 24585132    256 NKRPRTTITAKQLETLKTAYNNSPKPARHVREQLSQDTGLDMRVVQVWFQNRRAKEK 312
Cdd:smart00389   1 KRRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
LIM1_Lmx1b cd09371
The first LIM domain of Lmx1b; The first LIM domain of Lmx1b: Lmx1b belongs to the LHX protein ...
122-173 1.39e-18

The first LIM domain of Lmx1b; The first LIM domain of Lmx1b: Lmx1b belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. In mouse, Lmx1b functions in the developing limbs and eyes, the kidneys, the brain, and in cranial mesenchyme. The disruption of Lmx1b gene results kidney and limb defects. In the brain, Lmx1b is important for generation of mesencephalic dopamine neurons and the differentiation of serotonergic neurons. In the mouse eye, Lmx1b regulates anterior segment (cornea, iris, ciliary body, trabecular meshwork, and lens) development. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188757 [Multi-domain]  Cd Length: 53  Bit Score: 79.34  E-value: 1.39e-18
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFARNGQLFCKEDF 173
Cdd:cd09371   1 CAGCQRPISDRYLLRVNERSWHEECLQCSVCQQPLTTSCYFRDRKLYCKQDY 52
LIM1_Lhx2_Lhx9 cd09369
The first LIM domain of Lhx2 and Lhx9 family; The first LIM domain of Lhx2 and Lhx9 family: ...
122-173 8.90e-18

The first LIM domain of Lhx2 and Lhx9 family; The first LIM domain of Lhx2 and Lhx9 family: Lhx2 and Lhx9 are highly homologous LHX regulatory proteins. They belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Although Lhx2 and Lhx9 are highly homologous, they seems to play regulatory roles in different organs. In animals, Lhx2 plays important roles in eye, cerebral cortex, limb, the olfactory organs, and erythrocyte development. Lhx2 gene knockout mice exhibit impaired patterning of the cortical hem and the telencephalon of the developing brain, and a lack of development in olfactory structures. Lhx9 is expressed in several regions of the developing mouse brain , the spinal cord, the pancreas, in limb mesenchyme, and in the urogenital region. Lhx9 plays critical roles in gonad development. Homozygous mice lacking functional Lhx9 alleles exhibit numerous urogenital defects, such as gonadal agenesis, infertility, and undetectable levels of testosterone and estradiol coupled with high FSH levels. Lhx9 null mice are phenotypically female, even those that are genotypically male. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188755 [Multi-domain]  Cd Length: 54  Bit Score: 76.99  E-value: 8.90e-18
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLND--KCFARNGQLFCKEDF 173
Cdd:cd09369   1 CAGCGEKIQDRFYLLAVDRQWHASCLKCCECRLPLDSelSCFSRDGNIYCKEDY 54
LIM2_AWH cd09379
The second LIM domain of Arrowhead (AWH); The second LIM domain of Arrowhead (AWH): Arrowhead ...
181-236 2.42e-17

The second LIM domain of Arrowhead (AWH); The second LIM domain of Arrowhead (AWH): Arrowhead belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs such as the pituitary gland and the pancreas. During embryogenesis of Drosophila, Arrowhead is expressed in each abdominal segment and in the labial segment. Late in embryonic development, expression of arrowhead is refined to the abdominal histoblasts and salivary gland imaginal ring cells themselves. The Arrowhead gene required for establishment of a subset of imaginal tissues: the abdominal histoblasts and the salivary gland imaginal rings. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188765  Cd Length: 55  Bit Score: 75.92  E-value: 2.42e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDRkLICKRDY 236
Cdd:cd09379   1 CAKCSRNISASDWVRRARDHVYHLACFACDACKRQLSTGEEFALIEDR-VLCKAHY 55
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
122-177 7.56e-17

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 74.68  E-value: 7.56e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24585132   122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFA-RNGQLFCKEDFFKRY 177
Cdd:pfam00412   1 CAGCNRPIYDRELVRALGKVWHPECFRCAVCGKPLTTGDFYeKDGKLYCKHDYYKLF 57
LIM1_AWH cd09373
The first LIM domain of Arrowhead (AWH); The first LIM domain of Arrowhead (AWH): Arrowhead ...
122-173 1.42e-16

The first LIM domain of Arrowhead (AWH); The first LIM domain of Arrowhead (AWH): Arrowhead belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. During embryogenesis of Drosophila, Arrowhead is expressed in each abdominal segment and in the labial segment. Late in embryonic development, expression of arrowhead is refined to the abdominal histoblasts and salivary gland imaginal ring cells themselves. The Arrowhead gene required for establishment of a subset of imaginal tissues: the abdominal histoblasts and the salivary gland imaginal rings. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188759 [Multi-domain]  Cd Length: 54  Bit Score: 73.56  E-value: 1.42e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDK--CFARNGQLFCKEDF 173
Cdd:cd09373   1 CTGCGEPITDRFLLKVSGRSWHVSCLRCCVCQTPLERQpsCFTRDRQIYCKADY 54
LIM2_Lmx1a_Lmx1b cd09378
The second LIM domain of Lmx1a and Lmx1b; The second LIM domain of Lmx1a and Lmx1b: Lmx1a and ...
181-236 7.78e-15

The second LIM domain of Lmx1a and Lmx1b; The second LIM domain of Lmx1a and Lmx1b: Lmx1a and Lmx1b belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs such as the pituitary gland and the pancreas. Mouse Lmx1a is expressed in multiple tissues, including the roof plate of the neural tube, the developing brain, the otic vesicles, the notochord, and the pancreas. In mouse, mutations in Lmx1a result in failure of the roof plate to develop. Lmx1a may act upstream of other roof plate markers such as MafB, Gdf7, Bmp6, and Bmp7. Further characterization of these mice reveals numerous defects including disorganized cerebellum, hippocampus, and cortex; altered pigmentation; female sterility, skeletal defects, and behavioral abnormalities. In the mouse, Lmx1b functions in the developing limbs and eyes, the kidneys, the brain, and in cranial mesenchyme. The disruption of Lmx1b gene results kidney and limb defects. In the brain, Lmx1b is important for generation of mesencephalic dopamine neurons and the differentiation of serotonergic neurons. In the mouse eye, Lmx1b regulates anterior segment (cornea, iris, ciliary body, trabecular meshwork, and lens) development. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188764  Cd Length: 55  Bit Score: 68.63  E-value: 7.78e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDRkLICKRDY 236
Cdd:cd09378   1 CSGCLEKIAPSELVMRALENVYHLRCFCCCVCERQLQKGDEFVLKEGQ-LLCKSDY 55
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
122-173 8.03e-15

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 68.50  E-value: 8.03e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQL-NDKCFARNGQLFCKEDF 173
Cdd:cd08368   1 CAGCGKPIEGRELLRALGKKWHPECFKCAECGKPLgGDSFYEKDGKPYCEKCY 53
LIM1_LIMK cd09364
The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain ...
122-174 1.41e-13

The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain Kinase ): LIMK protein family is comprised of two members LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerisation. LIMKs can function in both cytoplasm and nucleus and are expressed in all tissues. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. However, LIMK1 and LIMk2 have different cellular locations. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The LIM domains of LIMK have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188750 [Multi-domain]  Cd Length: 53  Bit Score: 65.20  E-value: 1.41e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFARNGQLFCKEDFF 174
Cdd:cd09364   1 CAGCRGKILDSQYVQALNQDWHCDCFRCSVCSDSLSNWYFEKDGKLYCRKDYW 53
LIM1_Lmx1a cd09370
The first LIM domain of Lmx1a; The first LIM domain of Lmx1a: Lmx1a belongs to the LHX protein ...
122-173 1.88e-13

The first LIM domain of Lmx1a; The first LIM domain of Lmx1a: Lmx1a belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Mouse Lmx1a is expressed in multiple tissues, including the roof plate of the neural tube, the developing brain, the otic vesicles, the notochord, and the pancreas. Human Lmx1a can be found in pancreas, skeletal muscle, adipose tissue, developing brain, mammary glands, and pituitary. The functions of Lmx1a in the developing nervous system were revealed by studies of mutant mouse. In mouse, mutations in Lmx1a result in failure of the roof plate to develop. Lmx1a may act upstream of other roof plate markers such as MafB, Gdf7, Bmp 6, and Bmp7. Further characterization of these mice reveals numerous defects including disorganized cerebellum, hippocampus, and cortex; altered pigmentation; female sterility; skeletal defects; and behavioral abnormalities. Within pancreatic cells, the Lmx1a protein interacts synergistically with the bHLH transcription factor E47 to activate the insulin gene enhancer/promoter. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188756 [Multi-domain]  Cd Length: 52  Bit Score: 64.79  E-value: 1.88e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFARNGQLFCKEDF 173
Cdd:cd09370   1 CEGCNRVIQDRFLLRVNDSLWHERCLQCASCKEPLETTCFYRDKKLYCKEDY 52
LIM pfam00412
LIM domain; This family represents two copies of the LIM structural domain.
181-240 1.92e-13

LIM domain; This family represents two copies of the LIM structural domain.


Pssm-ID: 395333 [Multi-domain]  Cd Length: 57  Bit Score: 64.66  E-value: 1.92e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585132   181 CSACDMGIPPTQVVRrAQDNVYHLQCFLCAMCSRTLNTGDEFYLmeDRKLICKRDYEEAK 240
Cdd:pfam00412   1 CAGCNRPIYDRELVR-ALGKVWHPECFRCAVCGKPLTTGDFYEK--DGKLYCKHDYYKLF 57
LIM1_Isl cd09366
The first LIM domain of Isl, a member of LHX protein family; The first LIM domain of Isl: Isl ...
122-173 9.80e-13

The first LIM domain of Isl, a member of LHX protein family; The first LIM domain of Isl: Isl is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Isl1 and Isl2 are the two conserved members of this family. Proteins in this group are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Isl-1 is one of the LHX proteins isolated originally by virtue of its ability to bind DNA sequences from the 5'-flanking region of the rat insulin gene in pancreatic insulin-producing cells. Mice deficient in Isl-1 fail to form the dorsal exocrine pancreas and islet cells fail to differentiate. On the other hand, Isl-1 takes part in the pituitary development by activating the gonadotropin-releasing hormone receptor gene together with LHX3 and steroidogenic factor 1. Mouse Is l2 is expressed in the retinal ganglion cells and the developing spinal cord where it plays a role in motor neuron development. Same as Isl1, Isl2 may also be able to bind to the insulin gene enhancer to promote gene activation. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188752 [Multi-domain]  Cd Length: 55  Bit Score: 62.75  E-value: 9.80e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24585132 122 CGGCHELILDRFILKV---LErtWHAKCLQCSECHGQLNDK--CFARNGQLFCKEDF 173
Cdd:cd09366   1 CVGCGGKIHDQYILRVapdLE--WHAACLKCAECGQYLDETctCFVRDGKTYCKRDY 55
LIM2_Lhx2_Lhx9 cd09377
The second LIM domain of Lhx2 and Lhx9 family; The second LIM domain of Lhx2 and Lhx9 family: ...
180-236 1.16e-12

The second LIM domain of Lhx2 and Lhx9 family; The second LIM domain of Lhx2 and Lhx9 family: Lhx2 and Lhx9 are highly homologous LHX regulatory proteins. They belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Although Lhx2 and Lhx9 are highly homologous, they seems to play regulatory roles in different organs. In animals, Lhx2 plays important roles in eye, cerebral cortex, limb, the olfactory organs, and erythrocyte development. Lhx2 gene knockout mice exhibit impaired patterning of the cortical hem and the telencephalon of the developing brain, and a lack of development in olfactory structures. Lhx9 is expressed in several regions of the developing mouse brain, the spinal cord, the pancreas, in limb mesenchyme, and in the urogenital region. Lhx9 plays critical roles in gonad development. Homozygous mice lacking functional Lhx9 alleles exhibit numerous urogenital defects, such as gonadal agenesis, infertility, and undetectable levels of testosterone and estradiol coupled with high FSH levels. Lhx9 null mice are phenotypically female, even those that are genotypically male. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188763  Cd Length: 59  Bit Score: 62.68  E-value: 1.16e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24585132 180 KCSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYlMEDRKLICKRDY 236
Cdd:cd09377   4 RCARCHLGISASELVMRARDLVFHLNCFTCATCNKPLTKGDHFG-MRDGLVYCRLHY 59
COG5576 COG5576
Homeodomain-containing transcription factor [Transcription];
233-324 1.22e-12

Homeodomain-containing transcription factor [Transcription];


Pssm-ID: 227863 [Multi-domain]  Cd Length: 156  Bit Score: 65.54  E-value: 1.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24585132 233 KRDYEEAkAKGLYLDGSLDGDQPNKRPRTTITAKQLETLKTAYNNSPKPARHVREQLSQDTGLDMRVVQVWFQNRRAKEK 312
Cdd:COG5576  29 KREVEAA-DSEMKLERKQDGSSPPKSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEK 107
                        90
                ....*....|..
gi 24585132 313 RLKKDAGRTRWS 324
Cdd:COG5576 108 KKRSGKVEQRPG 119
LIM2_dLMO cd09390
The second LIM domain of dLMO (Beaderx); The second LIM domain of dLMO (Beaderx): dLMO is a ...
181-236 2.59e-12

The second LIM domain of dLMO (Beaderx); The second LIM domain of dLMO (Beaderx): dLMO is a nuclear protein that plays important roles in transcriptional regulation and development. In Drosophila dLMO modulates the activity of LIM-homeodomain protein Apterous (Ap), which regulates the formation of the dorsal-ventral axis of the Drosophila wing. Biochemical analysis shows that dLMO protein influences the activity of Apterous by binding of its cofactor Chip. Further studies shown that dLMO proteins might function in an evolutionarily conserved mechanism involved in patterning the appendages. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188776  Cd Length: 55  Bit Score: 61.80  E-value: 2.59e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDrKLICKRDY 236
Cdd:cd09390   1 CAACSKTIPAFEMVMRARTNVYHLECFACQRCNHRFCVGDRFYLCEN-KILCEYDY 55
LIM2_LMO4 cd09387
The second LIM domain of LMO4 (LIM domain only protein 4); The second LIM domain of LMO4 (LIM ...
181-235 3.74e-12

The second LIM domain of LMO4 (LIM domain only protein 4); The second LIM domain of LMO4 (LIM domain only protein 4): LMO4 is a nuclear protein that plays important roles in transcriptional regulation and development. LMO4 is involved in various functions in tumorigenesis and cellular differentiation. LMO4 proteins regulate gene expression by interacting with a wide variety of transcription factors and cofactors to form large transcription complexes. It can interact with Smad proteins, and associate with the promoter of the PAI-1 (plasminogen activator inhibitor-1) gene in a TGFbeta (transforming growth factor beta)-dependent manner. LMO4 can also form a complex with transcription regulator CREB (cAMP response element-binding protein) and interact with CLIM1 and CLIM2. In breast tissue, LMO4 interacts with multiple proteins, including the cofactor CtIP [CtBP (C-terminal binding protein)-interacting protein], the breast and ovarian tumor suppressor BRCA1 (breast-cancer susceptibility gene 1) and the LIM-domain-binding protein LDB1. Functionally, LMO4 is shown to repress BRCA1-mediated transcription activation, thus invoking a potential role for LMO4 as a negative regulator of BRCA1 in sporadic breast cancer. LMO4 also forms complex to both ERa (oestrogen receptor alpha), MTA1 (metastasis tumor antigen 1), and HDACs (histone deacetylases), implying that LMO4 is also a component of the MTA1 corepressor complex. Over-expressed LMO4 represses ERa transactivation functions in an HDAC-dependent manner, and contributes to the process of breast cancer progression by allowing the development of Era-negative phenotypes. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188773  Cd Length: 55  Bit Score: 60.96  E-value: 3.74e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDRkLICKRD 235
Cdd:cd09387   1 CSACGQSIPASELVMRAQGNVYHLKCFTCSTCHNQLVPGDRFHYVNGS-LFCEHD 54
LIM1_LMO4 cd09386
The first LIM domain of LMO4 (LIM domain only protein 4); The first LIM domain of LMO4 (LIM ...
122-173 5.55e-12

The first LIM domain of LMO4 (LIM domain only protein 4); The first LIM domain of LMO4 (LIM domain only protein 4): LMO4 is a nuclear protein that plays important roles in transcriptional regulation and development. LMO4 is involved in various functions in tumorigenesis and cellular differentiation. LMO4 proteins regulate gene expression by interacting with a wide variety of transcription factors and cofactors to form large transcription complexes. It can interact with Smad proteins, and associate with the promoter of the PAI-1 (plasminogen activator inhibitor-1) gene in a TGFbeta (transforming growth factor beta)-dependent manner. LMO4 can also form a complex with transcription regulator CREB (cAMP response element-binding protein) and interact with CLIM1 and CLIM2. In breast tissue, LMO4 interacts with multiple proteins, including the cofactor CtIP [CtBP (C-terminal binding protein)-interacting protein], the breast and ovarian tumor suppressor BRCA1 (breast-cancer susceptibility gene 1) and the LIM-domain-binding protein LDB1. Functionally, LMO4 is shown to repress BRCA1-mediated transcription activation, thus invoking a potential role for LMO4 as a negative regulator of BRCA1 in sporadic breast cancer. LMO4 also forms complex to both ERa (oestrogen receptor alpha), MTA1 (metastasis tumor antigen 1), and HDACs (histone deacetylases), implying that LMO4 is also a component of the MTA1 corepressor complex. Over-expressed LMO4 represses ERa transactivation functions in an HDAC-dependent manner, and contributes to the process of breast cancer progression by allowing the development of Era-negative phenotypes. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188772 [Multi-domain]  Cd Length: 55  Bit Score: 60.52  E-value: 5.55e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLND---KCFARNGQLFCKEDF 173
Cdd:cd09386   1 CAGCGGKIVDRFLLHALDRYWHNGCLKCSCCQAQLGEigsSCYTKGGMILCKNDY 55
LIM2_Isl cd09374
The second LIM domain of Isl, a member of LHX protein family; The second LIM domain of Isl: ...
181-236 6.89e-12

The second LIM domain of Isl, a member of LHX protein family; The second LIM domain of Isl: Isl is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Isl1 and Isl2 are the two conserved members of this family. Proteins in this group are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Isl-1 is one of the LHX proteins isolated originally by virtue of its ability to bind DNA sequences from the 5'-flanking region of the rat insulin gene in pancreatic insulin-producing cells. Mice deficient in Isl-1 fail to form the dorsal exocrine pancreas and islet cells fail to differentiate. On the other hand, Isl-1 takes part in the pituitary development by activating the gonadotropin-releasing hormone receptor gene together with LHX3 and steroidogenic factor 1. Mouse Isl2 is expressed in the retinal ganglion cells and the developing spinal cord where it plays a role in motor neuron development. Same as Isl1, Isl2 may also be able to bind to the insulin gene enhancer to promote gene activation. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188760  Cd Length: 55  Bit Score: 60.53  E-value: 6.89e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDrKLICKRDY 236
Cdd:cd09374   1 CAKCQQSFSKNDFVMRARTKIYHIECFRCSACSRQLIPGDEFALRDD-GLFCKADH 55
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
180-235 1.10e-11

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 59.70  E-value: 1.10e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132    180 KCSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNtgDEFYLMEDRKLICKRD 235
Cdd:smart00132   1 KCAGCGKPIYGTERVLRALGKVWHPECFKCATCGKPLS--GDTFFEKDGKLYCKDC 54
LIM2_Isl2 cd09471
The second LIM domain of Isl2; The second LIM domain of Isl2: Isl is a member of LHX protein ...
181-236 1.69e-11

The second LIM domain of Isl2; The second LIM domain of Isl2: Isl is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Isl proteins are found in the nucleus and act as transcription factors or cofactors. Isl1 and Isl2 are the two conserved members of this family. Mouse Isl2 is expressed in the retinal ganglion cells and the developing spinal cord where it plays a role in motor neuron development. Isl2 may be able to bind to the insulin gene enhancer to promote gene activation. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188855  Cd Length: 55  Bit Score: 59.17  E-value: 1.69e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEdRKLICKRDY 236
Cdd:cd09471   1 CAQCRLGFSSSDLVMRARDSVYHIECFRCSVCSRQLLPGDEFCLRE-HELLCRADH 55
LIM smart00132
Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ...
121-172 2.87e-11

Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM domains bind protein partners via tyrosine-containing motifs. LIM domains are found in many key regulators of developmental pathways.


Pssm-ID: 214528 [Multi-domain]  Cd Length: 54  Bit Score: 58.55  E-value: 2.87e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24585132    121 KCGGCHELILDR-FILKVLERTWHAKCLQCSECHGQL-NDKCFARNGQLFCKED 172
Cdd:smart00132   1 KCAGCGKPIYGTeRVLRALGKVWHPECFKCATCGKPLsGDTFFEKDGKLYCKDC 54
LIM1_Lhx7_Lhx8 cd09381
The first LIM domain of Lhx7 and Lhx8; The first LIM domain of Lhx7 and Lhx8: Lhx7 and Lhx8 ...
122-174 2.44e-10

The first LIM domain of Lhx7 and Lhx8; The first LIM domain of Lhx7 and Lhx8: Lhx7 and Lhx8 belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs such as the pituitary gland and the pancreas. Studies using mutant mice have revealed roles for Lhx7 and Lhx8 in the development of cholinergic neurons in the telencephalon and in basal forebrain development. Mice lacking alleles of the LIM-homeobox gene Lhx7 or Lhx8 display dramatically reduced number of forebrain cholinergic neurons. In addition, Lhx7 mutation affects male and female mice differently, with females appearing more affected than males. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188767 [Multi-domain]  Cd Length: 56  Bit Score: 56.14  E-value: 2.44e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQL--NDKCFARNGQLFCKEDFF 174
Cdd:cd09381   2 CSSCGLEIVDKYLLKVNDLCWHVRCLSCSVCRTSLgrHTSCYIKDKDIFCKLDYF 56
LIM2_Lhx7_Lhx8 cd09383
The second LIM domain of Lhx7 and Lhx8; The second LIM domain of Lhx7 and Lhx8: Lhx7 and Lhx8 ...
181-236 2.81e-10

The second LIM domain of Lhx7 and Lhx8; The second LIM domain of Lhx7 and Lhx8: Lhx7 and Lhx8 belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs such as the pituitary gland and the pancreas. Studies using mutant mice have revealed roles for Lhx7 and Lhx8 in the development of cholinergic neurons in the telencephalon and in basal forebrain development. Mice lacking alleles of the LIM-homeobox gene Lhx7 or Lhx8 display dramatically reduced number of forebrain cholinergic neurons. In addition, Lhx7 mutation affects male and female mice differently, with females appearing more affected than males. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188769  Cd Length: 55  Bit Score: 55.81  E-value: 2.81e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDRkLICKRDY 236
Cdd:cd09383   1 CSRCGRHIHSTDWVRRAKGNVYHLACFACFSCKRQLSTGEEFALVEEK-VLCRVHY 55
LIM cd08368
LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ...
181-236 2.92e-10

LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains are identified in a diverse group of proteins with wide variety of biological functions, including gene expression regulation, cell fate determination, cytoskeleton organization, tumor formation and development. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes. They perform their functions through interactions with other protein partners. LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. The consensus sequence of LIM domain has been defined as C-x(2)-C-x(16,23)-H-x(2)-[CH]-x(2)-C-x(2)-C-x(16,21)-C-x(2,3)-[CHD] (where X denotes any amino acid).


Pssm-ID: 259829 [Multi-domain]  Cd Length: 53  Bit Score: 55.79  E-value: 2.92e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPtQVVRRAQDNVYHLQCFLCAMCSRTLntGDEFYLMEDRKLICKRDY 236
Cdd:cd08368   1 CAGCGKPIEG-RELLRALGKKWHPECFKCAECGKPL--GGDSFYEKDGKPYCEKCY 53
LIM1_LIMK2 cd09463
The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain ...
122-173 4.43e-10

The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, altering the rate of actin depolymerization. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188847 [Multi-domain]  Cd Length: 53  Bit Score: 55.26  E-value: 4.43e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFARNGQLFCKEDF 173
Cdd:cd09463   1 CTGCGGRIQDSFHYRVVQEAWHNSCFQCSVCQDLLTNWYYEKDGKLYCHKHY 52
LIM2_LMO1_LMO3 cd09389
The second LIM domain of LMO1 and LMO3 (LIM domain only protein 1 and 3); The second LIM ...
181-236 4.89e-10

The second LIM domain of LMO1 and LMO3 (LIM domain only protein 1 and 3); The second LIM domain of LMO1 and LMO3 (LIM domain only protein 1 and 3): LMO1 and LMO3 are highly homologous and belong to the LMO protein family. LMO1 and LMO3 are nuclear protein that plays important roles in transcriptional regulation and development. As LIM domains lack intrinsic DNA-binding activity, nuclear LMOs are involved in transcriptional regulation by forming complexes with other transcription factors or cofactors. For example, LMO1 interacts with the the bHLH domain of bHLH transcription factor, TAL1 (T-cell acute leukemia1)/SCL (stem cell leukemia) . LMO1 inhibits the expression of TAL1/SCL target genes. LMO3 facilitates p53 binding to its response elements, which suggests that LMO3 acts as a co-repressor of p53, suppressing p53-dependent transcriptional regulation. In addition, LMO3 interacts with neuronal transcription factor, HEN2, and acts as an oncogene in neuroblastoma. Another binding partner of LMO3 is calcium- and integrin-binding protein CIB, which binds via the second LIM domain (LIM2) of LMO3. One role of the CIB/LMO3 complex is to inhibit cell proliferation. Although LMO1 and LMO3 are highly homologous proteins, they play different roles in the regulation of the pituitary glycoprotein hormone alpha-subunit (alpha GSU) gene. Alpha GSU promoter activity was markedly repressed by LMO1 but activated by LMO3. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188775  Cd Length: 55  Bit Score: 55.05  E-value: 4.89e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLmEDRKLICKRDY 236
Cdd:cd09389   1 CAACSKLIPAFEMVMRAKDNVYHLDCFACQLCNQRFCVGDKFFL-KNNMILCQMDY 55
LIM1_LIMK1 cd09462
The first LIM domain of LIMK1 (LIM domain Kinase 1); The first LIM domain of LIMK1 (LIM domain ...
119-174 7.07e-10

The first LIM domain of LIMK1 (LIM domain Kinase 1); The first LIM domain of LIMK1 (LIM domain Kinase 1): LIMK1 belongs to the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerization. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK1 is expressed in all tissues and is localized to focal adhesions in the cell. LIMK1 can form homodimers upon binding of HSP90 and is activated by Rho effector Rho kinase and MAPKAPK2. LIMK1 is important for normal central nervous system development, and its deletion has been implicated in the development of the human genetic disorder Williams syndrome. Moreover, LIMK1 up-regulates the promoter activity of urokinase type plasminogen activator and induces its mRNA and protein expression in breast cancer cells. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188846 [Multi-domain]  Cd Length: 74  Bit Score: 55.28  E-value: 7.07e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 119 IPKCGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFARNGQLFCKEDFF 174
Cdd:cd09462  19 LPVCASCGQSIYDGQYLQALNSDWHADCFRCCECGASLSHWYYEKDGRLFCKKDYW 74
LIM1_Lhx6 cd09380
The first LIM domain of Lhx6; The first LIM domain of Lhx6. Lhx6 is a member of LHX protein ...
122-173 2.95e-09

The first LIM domain of Lhx6; The first LIM domain of Lhx6. Lhx6 is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs such as the pituitary gland and the pancreas. Lhx6 functions in the brain and nervous system. It is expressed at high levels in several regions of the embryonic mouse CNS, including the telencephalon and hypothalamus, and the first branchial arch. Lhx6 is proposed to have a role in patterning of the mandible and maxilla, and in signaling during odontogenesis. In brain sections, knockdown of Lhx6 gene blocks the normal migration of neurons to the cortex. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188766 [Multi-domain]  Cd Length: 54  Bit Score: 53.10  E-value: 2.95e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQL--NDKCFARNGQLFCKEDF 173
Cdd:cd09380   1 CSSCGLEILDRYLLKVNNLIWHVRCLECSVCRTSLrqHNSCYIKNKEIFCKMDY 54
LIM2_Lhx9 cd09475
The second LIM domain of Lhx9; The second LIM domain of Lhx9: Lhx9 belongs to the LHX protein ...
180-227 3.01e-09

The second LIM domain of Lhx9; The second LIM domain of Lhx9: Lhx9 belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx9 is highly homologous to Lhx2. It is expressed in several regions of the developing mouse brain, the spinal cord, the pancreas, in limb mesenchyme, and in the urogenital region. Lhx9 plays critical roles in gonad development. Homozygous mice lacking functional Lhx9 alleles exhibit numerous urogenital defects, such as gonadal agenesis, infertility, and undetectable levels of testosterone and estradiol coupled with high FSH levels. Lhx9 null mice have reduced levels of the Sf1 nuclear receptor that is required for gonadogenesis, and recent studies have shown that Lhx9 is able to activate the Sf1/FtzF1 gene. Lhx9 null mice are phenotypically female, even those that are genotypically male. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188859  Cd Length: 59  Bit Score: 53.17  E-value: 3.01e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 24585132 180 KCSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMED 227
Cdd:cd09475   4 RCARCHLGISASEMVMRARESVYHLSCFTCTTCNKTLTTGDHFGMKDN 51
LIM1_Lhx2 cd09469
The first LIM domain of Lhx2; The first LIM domain of Lhx2: Lhx2 belongs to the LHX protein ...
122-173 3.88e-09

The first LIM domain of Lhx2; The first LIM domain of Lhx2: Lhx2 belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. In animals, Lhx2 plays important roles in eye, cerebral cortex, limb, the olfactory organs, and erythrocyte development. Lhx2 gene knockout mice exhibit impaired patterning of the cortical hem and the telencephalon of the developing brain, and a lack of development in olfactory structures. The Lhx2 protein has been shown to bind to the mouse M71 olfactory receptor promoter. Similar to other LIM domains, this domain family is 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188853  Cd Length: 64  Bit Score: 53.09  E-value: 3.88e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDK--CFARNGQLFCKEDF 173
Cdd:cd09469  11 CAGCGGKISDRYYLLAVDKQWHMRCLKCCECKLNLESEltCFSKDGSIYCKEDY 64
LIM1_Lhx9 cd09470
The first LIM domain of Lhx9; The first LIM domain of Lhx9: Lhx9 belongs to the LHX protein ...
122-173 4.81e-09

The first LIM domain of Lhx9; The first LIM domain of Lhx9: Lhx9 belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Lhx9 is highly homologous to Lhx2. It is expressed in several regions of the developing mouse brain, the spinal cord, the pancreas, in limb mesenchyme, and in the urogenital region. Lhx9 plays critical roles in gonad development. Homozygous mice lacking functional Lhx9 alleles exhibit numerous urogenital defects, such as gonadal agenesis, infertility, and undetectable levels of testosterone and estradiol coupled with high FSH levels. Lhx9 null mice have reduced levels of the Sf1 nuclear receptor that is required for gonadogenesis, and recent studies have shown that Lhx9 is able to activate the Sf1/FtzF1 gene. Lhx9 null mice are phenotypically female, even those that are genotypically male. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188854  Cd Length: 54  Bit Score: 52.36  E-value: 4.81e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDK--CFARNGQLFCKEDF 173
Cdd:cd09470   1 CAGCGGKISDRYYLLAVDKQWHLRCLKCCECKLALESEltCFAKDGSIYCKEDY 54
LIM2_Lhx2 cd09474
The second LIM domain of Lhx2; The second LIM domain of Lhx2: Lhx2 belongs to the LHX protein ...
180-233 9.60e-09

The second LIM domain of Lhx2; The second LIM domain of Lhx2: Lhx2 belongs to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. In animals, Lhx2 plays important roles in eye, cerebral cortex, limb, the olfactory organs, and erythrocyte development. Lhx2 gene knockout mice exhibit impaired patterning of the cortical hem and the telencephalon of the developing brain, and a lack of development in olfactory structures. The Lhx2 protein has been shown to bind to the mouse M71 olfactory receptor promoter. Similar to other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188858  Cd Length: 59  Bit Score: 51.62  E-value: 9.60e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 24585132 180 KCSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYlMEDRKLICK 233
Cdd:cd09474   4 RCARCHLGISASEMVMRARDLVYHLNCFTCTTCNKMLTTGDHFG-MKDNLVYCR 56
LIM2_Lhx6 cd09382
The second LIM domain of Lhx6; The second LIM domain of Lhx6. Lhx6 is a member of LHX protein ...
181-236 1.00e-08

The second LIM domain of Lhx6; The second LIM domain of Lhx6. Lhx6 is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs such as the pituitary gland and the pancreas. Lhx6 functions in brain and nervous system. It is expressed at high levels in several regions of the embryonic mouse CNS, including the telencephalon and hypothalamus, and the first branchial arch. Lhx6 is proposed to have a role in patterning of the mandible and maxilla, and in signaling during odontogenesis. In brain sections, knockdown of Lhx6 gene blocks the normal migration of neurons to the cortex. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188768  Cd Length: 55  Bit Score: 51.63  E-value: 1.00e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDrKLICKRDY 236
Cdd:cd09382   1 CARCGRQIYASDWVRRARGNAYHLACFACFSCKRQLSTGEEFGLVEE-KVLCRIHY 55
LIM1_LMO1_LMO3 cd09388
The first LIM domain of LMO1 and LMO3 (LIM domain only protein 1 and 3); The first LIM domain ...
122-173 2.22e-08

The first LIM domain of LMO1 and LMO3 (LIM domain only protein 1 and 3); The first LIM domain of LMO1 and LMO3 (LIM domain only protein 1 and 3): LMO1 and LMO3 are highly homologous and belong to the LMO protein family. LMO1 and LMO3 are nuclear protein that plays important roles in transcriptional regulation and development. As LIM domains lack intrinsic DNA-binding activity, nuclear LMOs are involved in transcriptional regulation by forming complexes with other transcription factors or cofactors. For example, LMO1 interacts with the the bHLH domain of bHLH transcription factor, TAL1 (T-cell acute leukemia1)/SCL (stem cell leukemia) . LMO1 inhibits the expression of TAL1/SCL target genes. LMO3 facilitates p53 binding to its response elements, which suggests that LMO3 acts as a co-repressor of p53, suppressing p53-dependent transcriptional regulation. In addition, LMO3 interacts with neuronal transcription factor, HEN2, and acts as an oncogene in neuroblastoma. Another binding partner of LMO3 is calcium- and integrin-binding protein CIB, which binds via the second LIM domain (LIM2) of LMO3. One role of the CIB/LMO3 complex is to inhibit cell proliferation. Although LMO1 and LMO3 are highly homologous proteins, they play different roles in the regulation of the pituitary glycoprotein hormone alpha-subunit (alpha GSU) gene. Alpha GSU promoter activity was markedly repressed by LMO1 but activated by LMO3. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188774  Cd Length: 55  Bit Score: 50.63  E-value: 2.22e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECH---GQLNDKCFARNGQLFCKEDF 173
Cdd:cd09388   1 CAGCNRKIKDRYLLKALDQYWHEDCLKCACCDcrlGEVGSTLYTKANLILCRRDY 55
LIM3_abLIM cd09329
The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin ...
122-173 4.32e-08

The third LIM domain of actin binding LIM (abLIM) proteins; The third LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188715 [Multi-domain]  Cd Length: 52  Bit Score: 49.62  E-value: 4.32e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFARNGQLFCKEDF 173
Cdd:cd09329   1 CAGCGQEIKNGQALLALDKQWHVWCFKCKECGKVLTGEYMGKDGKPYCERDY 52
LIM1_LMO2 cd09384
The first LIM domain of LMO2 (LIM domain only protein 2); The first LIM domain of LMO2 (LIM ...
122-174 9.12e-08

The first LIM domain of LMO2 (LIM domain only protein 2); The first LIM domain of LMO2 (LIM domain only protein 2): LMO2 is a nuclear protein that plays important roles in transcriptional regulation and development. The two tandem LIM domains of LMO2 support the assembly of a crucial cell-regulatory complex by interacting with both the TAL1-E47 and GATA1 transcription factors to form a DNA-binding complex that is capable of transcriptional activation. LMOs have also been shown to be involved in oncogenesis. LMO1 and LMO2 are activated in T-cell acute lymphoblastic leukemia by distinct chromosomal translocations. LMO2 was also shown to be involved in erythropoiesis and is required for the hematopoiesis in the adult animals. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188770  Cd Length: 56  Bit Score: 48.69  E-value: 9.12e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECH---GQLNDKCFARNGQLFCKEDFF 174
Cdd:cd09384   1 CGGCQQNIGDRYFLKAIDQYWHEDCLSCDLCGcrlGEVGRRLYYKLGRKLCRRDYL 56
LIM2_LMO2 cd09385
The second LIM domain of LMO2 (LIM domain only protein 2); The second LIM domain of LMO2 (LIM ...
181-235 1.38e-06

The second LIM domain of LMO2 (LIM domain only protein 2); The second LIM domain of LMO2 (LIM domain only protein 2): LMO2 is a nuclear protein that plays important roles in transcriptional regulation and development. The two tandem LIM domains of LMO2 support the assembly of a crucial cell-regulatory complex by interacting with both the TAL1-E47 and GATA1 transcription factors to form a DNA-binding complex that is capable of transcriptional activation. LMOs have also been shown to be involved in oncogenesis. LMO1 and LMO2 are activated in T-cell acute lymphoblastic leukemia by distinct chromosomal translocations. LMO2 was also shown to be involved in erythropoiesis and is required for the hematopoiesis in the adult animals. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188771  Cd Length: 56  Bit Score: 45.39  E-value: 1.38e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEfYLMEDRKLICKRD 235
Cdd:cd09385   1 CASCDKRIRAYEMTMRVKDKVYHLECFKCAACQKHFCVGDR-YLLINSDIVCEQD 54
LIM2_PINCH cd09332
The second LIM domain of protein PINCH; The second LIM domain of protein PINCH: PINCH plays a ...
122-171 2.18e-06

The second LIM domain of protein PINCH; The second LIM domain of protein PINCH: PINCH plays a pivotal role in the assembly of focal adhesions (FAs), regulating diverse functions in cell adhesion, growth, and differentiation through LIM-mediated protein-protein interactions. PINCH comprises an array of five LIM domains that interact with integrin-linked kinase (ILK), Nck2 (also called Nckbeta or Grb4) and other interaction partners. These interactions are essential for triggering the FA assembly and for relaying diverse mechanical and biochemical signals between Cell-extracellular matrix and the actin cytoskeleton. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188718 [Multi-domain]  Cd Length: 52  Bit Score: 44.63  E-value: 2.18e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 24585132 122 CGGCHELILDRFIlKVLERTWHAKCLQCSECHGQLNDKCFARN-GQLFCKE 171
Cdd:cd09332   1 CGKCGEFVIGRVI-KAMNNNWHPDCFRCEICNKELADIGFVKNaGRALCHP 50
LIM2_Lmx1a_Lmx1b cd09378
The second LIM domain of Lmx1a and Lmx1b; The second LIM domain of Lmx1a and Lmx1b: Lmx1a and ...
122-173 2.67e-06

The second LIM domain of Lmx1a and Lmx1b; The second LIM domain of Lmx1a and Lmx1b: Lmx1a and Lmx1b belong to the LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Members of LHX family are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs such as the pituitary gland and the pancreas. Mouse Lmx1a is expressed in multiple tissues, including the roof plate of the neural tube, the developing brain, the otic vesicles, the notochord, and the pancreas. In mouse, mutations in Lmx1a result in failure of the roof plate to develop. Lmx1a may act upstream of other roof plate markers such as MafB, Gdf7, Bmp6, and Bmp7. Further characterization of these mice reveals numerous defects including disorganized cerebellum, hippocampus, and cortex; altered pigmentation; female sterility, skeletal defects, and behavioral abnormalities. In the mouse, Lmx1b functions in the developing limbs and eyes, the kidneys, the brain, and in cranial mesenchyme. The disruption of Lmx1b gene results kidney and limb defects. In the brain, Lmx1b is important for generation of mesencephalic dopamine neurons and the differentiation of serotonergic neurons. In the mouse eye, Lmx1b regulates anterior segment (cornea, iris, ciliary body, trabecular meshwork, and lens) development. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188764  Cd Length: 55  Bit Score: 44.75  E-value: 2.67e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24585132 122 CGGCHELIL-DRFILKVLERTWHAKCLQCSECHGQLN--DKCFARNGQLFCKEDF 173
Cdd:cd09378   1 CSGCLEKIApSELVMRALENVYHLRCFCCCVCERQLQkgDEFVLKEGQLLCKSDY 55
LIM2_Paxillin_like cd09337
The second LIM domain of the paxillin like protein family; The second LIM domain of the ...
122-173 4.61e-06

The second LIM domain of the paxillin like protein family; The second LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188723 [Multi-domain]  Cd Length: 52  Bit Score: 43.92  E-value: 4.61e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 24585132 122 CGGCHELILDRfILKVLERTWHAKCLQCSECHGQLNDKCF-ARNGQLFCKEDF 173
Cdd:cd09337   1 CAYCNGPILDK-CVTALDKTWHPEHFFCAQCGKPFGDEGFhEKDGKPYCREDY 52
LIM1_Lrg1p_like cd09391
The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM ...
181-236 4.92e-06

The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The first LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188777  Cd Length: 57  Bit Score: 43.83  E-value: 4.92e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24585132 181 CSACDMGIPPTQVvrRAQDNVYHLQCFLCAMCSRTLNTgdEFYLMEDRK-----LICKRDY 236
Cdd:cd09391   1 CAKCGKPITGQFV--RALGDVYHLDCFTCHDCGKPVAS--KFFPVDDPDtseqvPLCETDY 57
LIM1_PINCH cd09331
The first LIM domain of protein PINCH; The first LIM domain of paxillin: Paxillin is an ...
181-236 8.77e-06

The first LIM domain of protein PINCH; The first LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188717  Cd Length: 59  Bit Score: 43.09  E-value: 8.77e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGdEFYLMEDRKLiCKRDY 236
Cdd:cd09331   1 CERCREGFEPDEKIVNSNGELYHEQCFVCAQCFQPFPDG-LFYEFEGRKY-CEHDF 54
LIM2_FBLP-1 cd09372
The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1); The second LIM domain of ...
122-173 9.91e-06

The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1); The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1): Fblp-1 contains a proline-rich domain near its N terminus and two LIM domains at its C terminus. FBLP-1 mRNA was detected in a variety of tissues and cells including platelets and endothelial cells. FBLP-1 binds to Filamins. The association between filamin B and FBLP-1 may play an unknown role in cytoskeletal function, cell adhesion, and cell motility. As in other LIM domains, this domain family is 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188758 [Multi-domain]  Cd Length: 53  Bit Score: 42.80  E-value: 9.91e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 24585132 122 CGGCHELILDRfILKVLERTWHAKCLQCSECHGQLNDKCFARN--GQLFCKEDF 173
Cdd:cd09372   1 CAKCQGVITEH-IIRALGKGYHPPCFTCVTCGRRIGDESFAVDeqNEVYCLDDY 53
LIM1_abLIM cd09327
The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin ...
194-236 1.19e-05

The first LIM domain of actin binding LIM (abLIM) proteins; The first LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188713 [Multi-domain]  Cd Length: 52  Bit Score: 42.63  E-value: 1.19e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24585132 194 VRRAQDNVYHLQCFLCAMCSRTLNTGDefYLMEDRKLICKRDY 236
Cdd:cd09327  12 VLRVQDKYFHIKCFTCKVCGCDLAQGG--FFVKEGEYYCTDDY 52
LIM1_Ajuba_like cd09352
The first LIM domain of Ajuba-like proteins; The first LIM domain of Ajuba-like proteins: ...
181-236 1.41e-05

The first LIM domain of Ajuba-like proteins; The first LIM domain of Ajuba-like proteins: Ajuba like LIM protein family includes three highly homologous proteins Ajuba, Limd1, and WTIP. Members of the family contain three tandem C-terminal LIM domains and a proline-rich N-terminal region. This family of proteins functions as scaffolds, participating in the assembly of numerous protein complexes. In the cytoplasm, Ajuba binds Grb2 to modulate serum-stimulated ERK activation. Ajuba also recruits the TNF receptor-associated factor 6 (TRAF6) to p62 and activates PKCKappa activity. Ajuba interacts with alpha-catenin and F-actin to contribute to the formation or stabilization of adheren junctions by linking adhesive receptors to the actin cytoskeleton. Although Ajuba is a cytoplasmic protein, it can shuttle into the nucleus. In nucleus, Ajuba functions as a corepressor for the zinc finger-protein Snail. It binds to the SNAG repression domain of Snail through its LIM region. Arginine methyltransferase-5 (Prmt5), a protein in the complex, is recruited to Snai l through an interaction with Ajuba. This ternary complex functions to repress E-cadherin, a Snail target gene. In addition, Ajuba contains functional nuclear-receptor interacting motifs and selectively interacts with retinoic acid receptors (RARs) and rexinoid receptor (RXRs) to negatively regulate retinoic acid signaling. Wtip, the Wt1-interacting protein, was originally identified as an interaction partner of the Wilms tumour protein 1 (WT1). Wtip is involved in kidney and neural crest development. Wtip interacts with the receptor tyrosine kinase Ror2 and inhibits canonical Wnt signaling. LIMD1 was reported to inhibit cell growth and metastases. The inhibition may be mediated through an interaction with the protein barrier-to-autointegration (BAF), a component of SWI/SNF chromatin-remodeling protein; or through the interaction with retinoblastoma protein (pRB), resulting in inhibition of E2F-mediated transcription, and expression of the majority of genes with E2F1- responsive elements. Recently, Limd1 was shown to interact with the p62/sequestosome protein and influence IL-1 and RANKL signaling by facilitating the assembly of a p62/TRAF6/a-PKC multi-protein complex. The Limd1-p62 interaction affects both NF-kappaB and AP-1 activity in epithelial cells and osteoclasts. Moreover, LIMD1 functions as tumor repressor to block lung tumor cell line in vitro and in vivo. Recent studies revealed that LIM proteins Wtip, LIMD1 and Ajuba interact with components of RNA induced silencing complexes (RISC) as well as eIF4E and the mRNA m7GTP cap-protein complex and are required for microRNA-mediated gene silencing. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188738  Cd Length: 54  Bit Score: 42.42  E-value: 1.41e-05
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gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNtGDEFYLMEDrKLICKRDY 236
Cdd:cd09352   1 CVKCGKGVYGASQACQAMGNLYHTNCFTCCSCGRTLR-GKAFYNVNG-KVYCEEDY 54
LIM1_Paxillin_like cd09336
The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin ...
122-174 1.96e-05

The first LIM domain of the paxillin like protein family; The first LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 259830 [Multi-domain]  Cd Length: 53  Bit Score: 41.99  E-value: 1.96e-05
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gi 24585132 122 CGGCHELILDRFIlKVLERTWHAKCLQCSECHGQLNDKCF-ARNGQLFCKEDFF 174
Cdd:cd09336   1 CAACNKPIVGQVV-TALGKTWHPEHFVCVHCQTELGTSNFfERDGKPYCEKDYH 53
LIM2_LMO4 cd09387
The second LIM domain of LMO4 (LIM domain only protein 4); The second LIM domain of LMO4 (LIM ...
122-173 2.88e-05

The second LIM domain of LMO4 (LIM domain only protein 4); The second LIM domain of LMO4 (LIM domain only protein 4): LMO4 is a nuclear protein that plays important roles in transcriptional regulation and development. LMO4 is involved in various functions in tumorigenesis and cellular differentiation. LMO4 proteins regulate gene expression by interacting with a wide variety of transcription factors and cofactors to form large transcription complexes. It can interact with Smad proteins, and associate with the promoter of the PAI-1 (plasminogen activator inhibitor-1) gene in a TGFbeta (transforming growth factor beta)-dependent manner. LMO4 can also form a complex with transcription regulator CREB (cAMP response element-binding protein) and interact with CLIM1 and CLIM2. In breast tissue, LMO4 interacts with multiple proteins, including the cofactor CtIP [CtBP (C-terminal binding protein)-interacting protein], the breast and ovarian tumor suppressor BRCA1 (breast-cancer susceptibility gene 1) and the LIM-domain-binding protein LDB1. Functionally, LMO4 is shown to repress BRCA1-mediated transcription activation, thus invoking a potential role for LMO4 as a negative regulator of BRCA1 in sporadic breast cancer. LMO4 also forms complex to both ERa (oestrogen receptor alpha), MTA1 (metastasis tumor antigen 1), and HDACs (histone deacetylases), implying that LMO4 is also a component of the MTA1 corepressor complex. Over-expressed LMO4 represses ERa transactivation functions in an HDAC-dependent manner, and contributes to the process of breast cancer progression by allowing the development of Era-negative phenotypes. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188773  Cd Length: 55  Bit Score: 41.70  E-value: 2.88e-05
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gi 24585132 122 CGGCHELI-LDRFILKVLERTWHAKCLQCSECHGQL--NDKCFARNGQLFCKEDF 173
Cdd:cd09387   1 CSACGQSIpASELVMRAQGNVYHLKCFTCSTCHNQLvpGDRFHYVNGSLFCEHDR 55
LIM1_LIMK cd09364
The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain ...
181-236 8.82e-05

The first LIM domain of LIMK (LIM domain Kinase ); The first LIM domain of LIMK (LIM domain Kinase ): LIMK protein family is comprised of two members LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerisation. LIMKs can function in both cytoplasm and nucleus and are expressed in all tissues. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. However, LIMK1 and LIMk2 have different cellular locations. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The LIM domains of LIMK have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188750 [Multi-domain]  Cd Length: 53  Bit Score: 40.17  E-value: 8.82e-05
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gi 24585132 181 CSACDMGIPPTQVVRRAQDNvYHLQCFLCAMCSRTLNTgdeFYLMEDRKLICKRDY 236
Cdd:cd09364   1 CAGCRGKILDSQYVQALNQD-WHCDCFRCSVCSDSLSN---WYFEKDGKLYCRKDY 52
LIM3_Leupaxin cd09410
The third LIM domain of Leupaxin; The third LIM domain of Leupaxin: Leupaxin is a cytoskeleton ...
122-173 1.02e-04

The third LIM domain of Leupaxin; The third LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188794 [Multi-domain]  Cd Length: 53  Bit Score: 40.19  E-value: 1.02e-04
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gi 24585132 122 CGGCHELILDRFiLKVLERTWHAKCLQCSECHGQLNDKCFAR-NGQLFCKEDF 173
Cdd:cd09410   1 CSGCGRPVKENY-LSAANGVWHPECFVCSDCLKPFTDGSFFElDGRPLCELHY 52
LIM2_ENH cd09457
The second LIM domain of the Enigma Homolog (ENH) family; The second LIM domain of the Enigma ...
122-173 2.10e-04

The second LIM domain of the Enigma Homolog (ENH) family; The second LIM domain of the Enigma Homolog (ENH) family: ENH was initially identified in rat brain. Same as enigma, it contains three LIM domains at the C-terminus and a PDZ domain at N-terminus. ENH is implicated in signal transduction processes involving protein kinases. It has also been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ENH is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188841 [Multi-domain]  Cd Length: 52  Bit Score: 39.24  E-value: 2.10e-04
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gi 24585132 122 CGGCHELILDRfILKVLERTWHAKCLQCSECHGQLNDKCF-ARNGQLFCKEDF 173
Cdd:cd09457   1 CGRCQRKILGE-VINALKQTWHVSCFVCVACHNPIRNNVFhLEDGEPYCETDY 52
LIM2_Testin_like cd09341
The second LIM domain of Testin-like family; The second LIM domain of Testin-like family: This ...
120-169 2.35e-04

The second LIM domain of Testin-like family; The second LIM domain of Testin-like family: This family includes testin, prickle, dyxin and LIMPETin. Structurally, testin and prickle proteins contain three LIM domains at C-terminal; LIMPETin has six LIM domains; and dyxin presents only two LIM domains. However, all members of the family contain a PET protein-protein interaction domain. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell-cell-contact areas, and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and it is involved in cell motility and adhesion events. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). Dyxin involves in lung and heart development by interaction with GATA6 and blocking GATA6 activated target genes. LIMPETin might be the recombinant product of genes coding testin and four and half LIM proteins and its function is not well understood. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188727  Cd Length: 56  Bit Score: 39.13  E-value: 2.35e-04
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gi 24585132 120 PKCGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCF-ARNGQLFC 169
Cdd:cd09341   1 PRCAACDELIFSGEYTQAEGKNWHLKHFCCFQCDEPLGGQRYvLREGKPYC 51
LIM1_Leupaxin cd09406
The first LIM domain of Leupaxin; The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton ...
122-173 2.47e-04

The first LIM domain of Leupaxin; The first LIM domain of Leupaxin: Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. Leupaxin belongs to the paxillin focal adhesion protein family. Same as other members of the family, it has four leucine-rich LD-motifs in the N-terminus and four LIM domains in the C-terminus. It may function in cell type-specific signaling by associating with interaction partners PYK2, FAK, PEP and p95PKL. When expressed in human leukocytic cells, leupaxin significantly suppressed integrin-mediated cell adhesion to fibronectin and the tyrosine phosphorylation of paxillin. These findings indicate that leupaxin may negatively regulate the functions of paxillin during integrin signaling. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188790 [Multi-domain]  Cd Length: 55  Bit Score: 39.08  E-value: 2.47e-04
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gi 24585132 122 CGGCHELILDRFILkVLERTWHAKCLQCSECHGQLNDKCF-ARNGQLFCKEDF 173
Cdd:cd09406   3 CASCQKPIAGQVVT-ALGQTWHPEHFVCCQCGKELGSRPFfERNGQAYCEEDY 54
LIM1_FHL cd09343
The first LIM domain of Four and a half LIM domains protein (FHL); The first LIM domain of ...
122-171 2.65e-04

The first LIM domain of Four and a half LIM domains protein (FHL); The first LIM domain of Four and a half LIM domains protein (FHL): LIM-only protein family consists of five members, designated FHL1, FHL2, FHL3, FHL5 and LIMPETin. The first four members are composed of four complete LIM domains arranged in tandem and an N-terminal single zinc finger domain with a consensus sequence equivalent to the C-terminal half of a LIM domain. LIMPETin is an exception, containing six LIM domains. FHL1, 2 and 3 are predominantly expressed in muscle tissues, and FHL5 is highly expressed in male germ cells. FHL proteins exert their roles as transcription co-activators or co-repressors through a wide array of interaction partners. For example, FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. FHL2 has shown to interact with more than 50 different proteins, including receptors, structural proteins, transcription factors and cofactors, signal transducers, splicing factors, DNA replication and repair enzymes, and metabolic enzymes. FHL3 int eracts with many transcription factors, such as CREB, BKLF/KLF3, CtBP2, MyoD, and MZF_1. FHL5 is a tissue-specific coactivator of CREB/CREM family transcription factors. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188729  Cd Length: 59  Bit Score: 38.96  E-value: 2.65e-04
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gi 24585132 122 CGGCHELI-LDRFILKVLERTWHAKCLQCSECHGQLNDKCFA-RNGQLFCKE 171
Cdd:cd09343   5 CEECKKKIgCDSKDLSYKDRHWHEGCFKCFKCQRSLVDKPFAaKDEDLLCTE 56
LIM1_Zyxin cd09349
The first LIM domain of Zyxin; The first LIM domain of Zyxin: Zyxin exhibits three copies of ...
181-236 2.76e-04

The first LIM domain of Zyxin; The first LIM domain of Zyxin: Zyxin exhibits three copies of the LIM domain, an extensive proline-rich domain and a nuclear export signal. Localized at sites of cell substratum adhesion in fibroblasts, Zyxin interacts with alpha-actinin, members of the cysteine-rich protein (CRP) family, proteins that display Src homology 3 (SH3) domains and Ena/VASP family members. Zyxin and its partners have been implicated in the spatial control of actin filament assembly as well as in pathways important for cell differentiation. In addition to its functions at focal adhesion plaques, recent work has shown that zyxin moves from the sites of cell contacts to the nucleus, where it directly participates in the regulation of gene expression. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188735 [Multi-domain]  Cd Length: 87  Bit Score: 39.84  E-value: 2.76e-04
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gi 24585132 181 CSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNtGDEFYLMEDRKLiCKRDY 236
Cdd:cd09349  34 CGICGQPLSRTQPAVRALGHLFHVTCFTCHQCEQQLQ-GQQFYSLEGKPY-CEECY 87
LIM3_Paxillin_like cd09338
The third LIM domain of the paxillin like protein family; The third LIM domain of the paxillin ...
122-170 3.23e-04

The third LIM domain of the paxillin like protein family; The third LIM domain of the paxillin like protein family: This family consists of paxillin, leupaxin, Hic-5 (ARA55), and other related proteins. There are four LIM domains in the C-terminal of the proteins and leucine-rich LD-motifs in the N-terminal region. Members of this family are adaptor proteins to recruit key components of signal-transduction machinery to specific sub-cellular locations. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. Paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. Leupaxin is a cytoskeleton adaptor protein, which is preferentially expressed in hematopoietic cells. It associates with focal adhesion kinases PYK2 and pp125FAK and identified to be a component of the osteoclast pososomal signaling complex. Hic-5 controls cell proliferation, migration and senescence by functioning as coactivator for steroid receptors such as androgen receptor, glucocorticoid receptor and progesterone receptor. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188724 [Multi-domain]  Cd Length: 53  Bit Score: 38.47  E-value: 3.23e-04
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gi 24585132 122 CGGCHELILDRFIlKVLERTWHAKCLQCSECHGQLNDKCF-ARNGQLFCK 170
Cdd:cd09338   1 CGGCNKPILENYI-SALNTQWHPECFVCRECHKPFINGSFfEHEGLPYCE 49
LIM3_Paxillin cd09409
The third LIM domain of paxillin; The third LIM domain of paxillin: Paxillin is an adaptor ...
122-173 5.07e-04

The third LIM domain of paxillin; The third LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188793 [Multi-domain]  Cd Length: 53  Bit Score: 38.28  E-value: 5.07e-04
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gi 24585132 122 CGGCHELILDRFIlKVLERTWHAKCLQCSECHGQL-NDKCFARNGQLFCKEDF 173
Cdd:cd09409   1 CGGCARAILENYI-SALNTLWHPECFVCRECFTPFvNGSFFEHDGQPYCEAHY 52
LIM3_Zyxin_like cd09357
The third LIM domain of Zyxin-like family; The third LIM domain of Zyxin like family: This ...
122-170 5.12e-04

The third LIM domain of Zyxin-like family; The third LIM domain of Zyxin like family: This family includes Ajuba, Limd1, WTIP, Zyxin, LPP, and Trip6 LIM proteins. Members of Zyxin family contain three tandem C-terminal LIM domains, and a proline-rich N-terminal region. Zyxin proteins are detected primarily in focal adhesion plaques. They function as scaffolds, participating in the assembly of multiple interactions and signal transduction networks, which regulate cell adhesion, spreading, and motility. They can also shuffle into nucleus. In nucleus, zyxin proteins affect gene transcription by interaction with a variety of nuclear proteins, including several transcription factors, playing regulating roles in cell proliferation, differentiation and apoptosis. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188743  Cd Length: 63  Bit Score: 38.56  E-value: 5.12e-04
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gi 24585132 122 CGGCHELILDR------FILKVLERTWHAKCLQCSECHGQLNDK-----CFARNGQLFCK 170
Cdd:cd09357   1 CSVCGEPIMPEpgqdetVRIVALDRSFHVNCYKCEDCGMLLSSEdegqgCYPLDGHLLCK 60
LIM2_Enigma cd09456
The second LIM domain of Enigma; The second LIM domain of Enigma: Enigma was initially ...
181-236 5.26e-04

The second LIM domain of Enigma; The second LIM domain of Enigma: Enigma was initially characterized in humans as a protein containing three LIM domains at the C-terminus and a PDZ domain at N-terminus. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. Enigma is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188840 [Multi-domain]  Cd Length: 52  Bit Score: 38.05  E-value: 5.26e-04
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gi 24585132 181 CSACDMGIppTQVVRRAQDNVYHLQCFLCAMCsRTLNTGDEFYlMEDRKLICKRDY 236
Cdd:cd09456   1 CAKCKKKI--TGEIMHALKMTWHVHCFTCAAC-KTPIRNRAFY-MEEGAPYCERDY 52
LIM1_Enigma_like cd09361
The first LIM domain of Enigma-like family; The first LIM domain of Enigma-like family: The ...
122-169 8.44e-04

The first LIM domain of Enigma-like family; The first LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone, and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188747 [Multi-domain]  Cd Length: 52  Bit Score: 37.34  E-value: 8.44e-04
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gi 24585132 122 CGGCHELILDRFILkVLERTWHAKCLQCSECHGQLNDKCFA-RNGQLFC 169
Cdd:cd09361   1 CAHCNQVIRGPFLV-ALGRSWHPEEFTCSHCHCSLAEIGFVeEKGSLYC 48
LIM_TLP_like cd09401
The LIM domains of thymus LIM protein (TLP); The LIM domain of thymus LIM protein (TLP) like ...
122-170 1.01e-03

The LIM domains of thymus LIM protein (TLP); The LIM domain of thymus LIM protein (TLP) like proteins: This family includes the LIM domains of TLP and CRIP (Cysteine-Rich Intestinal Protein). TLP is the distant member of the CRP family of proteins. TLP has two isomers (TLP-A and TLP-B) and sharing approximately 30% with each of the three other CRPs. Like CRP1, CRP2 and CRP3/MLP, TLP has two LIM domains, connected by a flexible linker region. Unlike the CRPs, TLP lacks the nuclear targeting signal (K/R-K/R-Y-G-P-K) and is localized solely in the cytoplasm. TLP is specifically expressed in the thymus in a subset of cortical epithelial cells. TLP has a role in development of normal thymus and in controlling the development and differentiation of thymic epithelial cells. CRIP is a short LIM protein with only one LIM domain. CRIP gene is developmentally regulated and can be induced by glucocorticoid hormones during the first three postnatal weeks. The domain shows close sequence homology to LIM domain of thymus LIM protein. However, unlike the TLP proteins which have two LIM domains, the members of this family have only one LIM domain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188785 [Multi-domain]  Cd Length: 53  Bit Score: 37.32  E-value: 1.01e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24585132 122 CGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFA-RNGQLFCK 170
Cdd:cd09401   1 CPKCGKPVYFAEKKTSLGRDWHKPCLRCEKCKKTLTPGQHSeHEGKPYCN 50
LIM2_Enigma_like cd09362
The second LIM domain of Enigma-like family; The second LIM domain of Enigma-like family: The ...
122-173 1.30e-03

The second LIM domain of Enigma-like family; The second LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188748 [Multi-domain]  Cd Length: 52  Bit Score: 37.07  E-value: 1.30e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 24585132 122 CGGCHELILDRfILKVLERTWHAKCLQCSECHGQLNDKCF-ARNGQLFCKEDF 173
Cdd:cd09362   1 CARCHKKILGE-VMHALKQTWHVSCFVCAACKQPIGNSLFhMEDGEPYCEKDY 52
LIM2_Zyxin cd09353
The second LIM domain of Zyxin; The second LIM domain of Zyxin: Zyxin exhibits three copies of ...
181-241 1.37e-03

The second LIM domain of Zyxin; The second LIM domain of Zyxin: Zyxin exhibits three copies of the LIM domain, an extensive proline-rich domain and a nuclear export signal. Localized at sites of cellsubstratum adhesion in fibroblasts, Zyxin interacts with alpha-actinin, members of the cysteine-rich protein (CRP) family, proteins that display Src homology 3 (SH3) domains and Ena/VASP family members. Zyxin and its partners have been implicated in the spatial control of actin filament assembly as well as in pathways important for cell differentiation. In addition to its functions at focal adhesion plaques, recent work has shown that zyxin moves from the sites of cell contacts to the nucleus, where it directly participates in the regulation of gene expression. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors o r scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188739 [Multi-domain]  Cd Length: 60  Bit Score: 37.22  E-value: 1.37e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24585132 181 CSACDMGIppTQVVRRAQDNVYHLQCFLCAMCSRTLNtGDEFYLMEDRKLICKRDYEEAKA 241
Cdd:cd09353   1 CAVCDQKI--TDRMLKATGKSYHPQCFTCVVCKCPLE-GESFIVDQANQPHCVNDYHRRYA 58
LIM1_LIMK2 cd09463
The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain ...
181-236 1.47e-03

The first LIM domain of LIMK2 (LIM domain Kinase 2); The first LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, altering the rate of actin depolymerization. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188847 [Multi-domain]  Cd Length: 53  Bit Score: 36.77  E-value: 1.47e-03
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                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPTQVVRRAQDnVYHLQCFLCAMCSRTLNTgdeFYLMEDRKLICKRDY 236
Cdd:cd09463   1 CTGCGGRIQDSFHYRVVQE-AWHNSCFQCSVCQDLLTN---WYYEKDGKLYCHKHY 52
LIM1_Paxillin cd09405
The first LIM domain of paxillin; The first LIM domain of paxillin: Paxillin is an adaptor ...
122-173 1.67e-03

The first LIM domain of paxillin; The first LIM domain of paxillin: Paxillin is an adaptor protein, which recruits key components of the signal-transduction machinery to specific sub-cellular locations to respond to environmental changes rapidly. The C-terminal region of paxillin contains four LIM domains which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal of paxillin is leucine-rich LD-motifs. Paxillin is found at the interface between the plasma membrane and the actin cytoskeleton. The binding partners of paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization. Paxillin recruits these proteins to their function sites to control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight cons erved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188789 [Multi-domain]  Cd Length: 54  Bit Score: 36.52  E-value: 1.67e-03
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                ....*....|....*....|....*....|....*....|....*....|...
gi 24585132 122 CGGCHELILDRfILKVLERTWHAKCLQCSECHGQLNDK-CFARNGQLFCKEDF 173
Cdd:cd09405   2 CGACKKPIAGQ-VVTAMGKTWHPEHFVCTHCQEEIGSRnFFERDGQPYCEKDY 53
LIM2_TRIP6 cd09356
The second LIM domain of Thyroid receptor-interacting protein 6 (TRIP6); The second LIM domain ...
122-173 1.67e-03

The second LIM domain of Thyroid receptor-interacting protein 6 (TRIP6); The second LIM domain of Thyroid receptor-interacting protein 6 (TRIP6): TRIP6 is a member of the zyxin LIM protein family and contains three LIM zinc-binding domains at the C-terminal. TRIP6 protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid (LPA)-dependent manner. TRIP6 recruits a number of molecules involved in actin assembly, cell motility, survival and transcriptional control. The function of TRIP6 in cell motility is regulated by Src-dependent phosphorylation at a Tyr residue. The phosphorylation activates the coupling to the Crk SH2 domain, which is required for the function of TRIP6 in promoting lysophosphatidic acid (LPA)-induced cell migration. TRIP6 can shuttle to the nucleus to serve as a coactivator of AP-1 and NF-kappaB transcriptional factors. Moreover, TRIP6 can form a ternary complex with the NHERF2 PDZ protein and LPA2 receptor to regulate LPA-induced activation of ERK and AKT, rendering cells resistant to chemotherapy. Recent evidence shows that TRIP6 antagonizes Fas-Induced apoptosis by enhancing the antiapoptotic effect of LPA in cells. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188742  Cd Length: 53  Bit Score: 36.77  E-value: 1.67e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 24585132 122 CGGCHELILDRfILKVLERTWHAKCLQCSECHGQLNDKCFA--RNGQLFCKEDF 173
Cdd:cd09356   1 CSVCSKPIMER-ILRATGKAYHPHCFTCVVCHRSLDGIPFTvdATGQIHCIEDF 53
LIM2_LIMK2 cd09465
The second LIM domain of LIMK2 (LIM domain Kinase 2); The second LIM domain of LIMK2 (LIM ...
176-236 2.16e-03

The second LIM domain of LIMK2 (LIM domain Kinase 2); The second LIM domain of LIMK2 (LIM domain Kinase 2): LIMK2 is a member of the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, altering the rate of actin depolymerisation. LIMK activity is activated by phosphorylation of a threonine residue within the activation loop of the kinase by p21-activated kinases 1 and 4 and by Rho kinase. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK2 is expressed in all tissues. While LIMK1 localizes mainly at focal adhesions, LIMK2 is found in cytoplasmic punctae, suggesting that they may have different cellular functions. The activity of LIM kinase 2 to regulate cofilin phosphorylation is inhibited by the direct binding of Par-3. LIMK2 activation promotes cell cycle progression. The phenotype of Limk2 knockout mice shows a defect in spermatogenesis. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188849 [Multi-domain]  Cd Length: 59  Bit Score: 36.45  E-value: 2.16e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24585132 176 RYGTKCSACDMGIppTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDRKLICKRDY 236
Cdd:cd09465   1 KFGELCHGCSLLM--TGPAMVAGEYKYHPECFACMSCKVIIEDGDTYALVQHTTLYCGKCH 59
LIM2_FBLP-1 cd09372
The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1); The second LIM domain of ...
181-236 2.89e-03

The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1); The second LIM domain of the filamin-binding LIM protein-1 (FBLP-1): Fblp-1 contains a proline-rich domain near its N terminus and two LIM domains at its C terminus. FBLP-1 mRNA was detected in a variety of tissues and cells including platelets and endothelial cells. FBLP-1 binds to Filamins. The association between filamin B and FBLP-1 may play an unknown role in cytoskeletal function, cell adhesion, and cell motility. As in other LIM domains, this domain family is 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188758 [Multi-domain]  Cd Length: 53  Bit Score: 35.86  E-value: 2.89e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24585132 181 CSACDMGIppTQVVRRAQDNVYHLQCFLCAMCSRTLntGDE-FYLMEDRKLICKRDY 236
Cdd:cd09372   1 CAKCQGVI--TEHIIRALGKGYHPPCFTCVTCGRRI--GDEsFAVDEQNEVYCLDDY 53
LIM2_Enigma_like cd09362
The second LIM domain of Enigma-like family; The second LIM domain of Enigma-like family: The ...
181-236 3.06e-03

The second LIM domain of Enigma-like family; The second LIM domain of Enigma-like family: The Enigma LIM domain family is comprised of three members: Enigma, ENH, and Cypher (mouse)/ZASP (human). These subfamily members contain a single PDZ domain at the N-terminus and three LIM domains at the C-terminus. Enigma was initially characterized in humans and is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes, such as mitogenic activity, insulin related actin organization, and glucose metabolism. The second member, ENH protein, was first identified in rat brain. It has been shown that ENH interacts with protein kinase D1 (PKD1) via its LIM domains and forms a complex with PKD1 and the alpha1C subunit of cardiac L-type voltage-gated calcium channel in rat neonatal cardiomyocytes. The N-terminal PDZ domain interacts with alpha-actinin at the Z-line. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188748 [Multi-domain]  Cd Length: 52  Bit Score: 35.92  E-value: 3.06e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIppTQVVRRAQDNVYHLQCFLCAMCSRTLntGDEFYLMEDRKLICKRDY 236
Cdd:cd09362   1 CARCHKKI--LGEVMHALKQTWHVSCFVCAACKQPI--GNSLFHMEDGEPYCEKDY 52
LIM2_Isl cd09374
The second LIM domain of Isl, a member of LHX protein family; The second LIM domain of Isl: ...
120-172 3.86e-03

The second LIM domain of Isl, a member of LHX protein family; The second LIM domain of Isl: Isl is a member of LHX protein family, which features two tandem N-terminal LIM domains and a C-terminal DNA binding homeodomain. Isl1 and Isl2 are the two conserved members of this family. Proteins in this group are found in the nucleus and act as transcription factors or cofactors. LHX proteins are critical for the development of specialized cells in multiple tissue types, including the nervous system, skeletal muscle, the heart, the kidneys, and endocrine organs, such as the pituitary gland and the pancreas. Isl-1 is one of the LHX proteins isolated originally by virtue of its ability to bind DNA sequences from the 5'-flanking region of the rat insulin gene in pancreatic insulin-producing cells. Mice deficient in Isl-1 fail to form the dorsal exocrine pancreas and islet cells fail to differentiate. On the other hand, Isl-1 takes part in the pituitary development by activating the gonadotropin-releasing hormone receptor gene together with LHX3 and steroidogenic factor 1. Mouse Isl2 is expressed in the retinal ganglion cells and the developing spinal cord where it plays a role in motor neuron development. Same as Isl1, Isl2 may also be able to bind to the insulin gene enhancer to promote gene activation. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188760  Cd Length: 55  Bit Score: 35.49  E-value: 3.86e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24585132 120 PKCGGCheLILDRFILKVLERTWHAKCLQCSECHGQL--NDKCFARNGQLFCKED 172
Cdd:cd09374   2 AKCQQS--FSKNDFVMRARTKIYHIECFRCSACSRQLipGDEFALRDDGLFCKAD 54
LIM1_ZASP_Cypher cd09454
The first LIM domain of ZASP/Cypher family; The first LIM domain of ZASP/Cypher family: ZASP ...
122-161 5.19e-03

The first LIM domain of ZASP/Cypher family; The first LIM domain of ZASP/Cypher family: ZASP was identified in human heart and skeletal muscle and Cypher is a mice ortholog of ZASP. ZASP/Cyppher contains three LIM domains at the C-terminus and a PDZ domain at N-terminus. ZASP/Cypher is required for maintenance of Z-line structure during muscle contraction, but not required for Z-line assembly. In heart, Cypher/ZASP plays a structural role through its interaction with cytoskeletal Z-line proteins. In addition, there is increasing evidence that Cypher/ZASP also performs signaling functions. Studies reveal that Cypher/ZASP interacts with and directs PKC to the Z-line, where PKC phosphorylates downstream signaling targets. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188838 [Multi-domain]  Cd Length: 52  Bit Score: 35.34  E-value: 5.19e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24585132 122 CGGCHELILDRFILkVLERTWHAKCLQCSECHGQLNDKCF 161
Cdd:cd09454   1 CGHCNNIIRGPFLV-ALGRSWHPEEFTCHYCHTSLADVSF 39
LIM2_abLIM cd09328
The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin ...
121-152 5.33e-03

The second LIM domain on actin binding LIM (abLIM) proteins; The second LIM domain of actin binding LIM (abLIM) proteins: Three homologous members of the abLIM protein family have been identified; abLIM-1, abLIM-2 and abLIM-3. The N-terminal of abLIM consists of four tandem repeats of LIM domains and the C-terminal of acting binding LIM protein is a villin headpiece domain, which has strong actin binding activity. The abLIM-1, which is expressed in retina, brain, and muscle tissue, has been indicated to function as a tumor suppressor. AbLIM-2 and -3, mainly expressed in muscle and neuronal tissue, bind to F-actin strongly. They may serve as a scaffold for signaling modules of the actin cytoskeleton and thereby modulate transcription. It has shown that LIM domains of abLIMs interact with STARS (striated muscle activator of Rho signaling), which directly binds actin and stimulates serum-response factor (SRF)-dependent transcription. All LIM domains are 50-60 amino acids in size and share two characteristic highly conserved zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188714  Cd Length: 56  Bit Score: 35.40  E-value: 5.33e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 24585132 121 KCGGCHELILDRFILkVLERTWHAKCLQCSEC 152
Cdd:cd09328   3 KCDSCQDFVEGEVVS-ALGKTYHPKCFVCSVC 33
LIM1_Enigma cd09452
The first LIM domain of Enigma; The first LIM domain of Enigma: Enigma was initially ...
122-169 5.93e-03

The first LIM domain of Enigma; The first LIM domain of Enigma: Enigma was initially characterized in humans as a protein containing three LIM domains at the C-terminus and a PDZ domain at N-terminus. The third LIM domain specifically interacts with the insulin receptor and the second LIM domain interacts with the receptor tyrosine kinase Ret and the adaptor protein APS. Thus Enigma is implicated in signal transduction processes such as mitogenic activity, insulin related actin organization, and glucose metabolism. Enigma is expressed in multiple tissues, such as skeletal muscle, heart, bone and brain. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188836 [Multi-domain]  Cd Length: 52  Bit Score: 35.16  E-value: 5.93e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 24585132 122 CGGCHELILDRFILkVLERTWHAKCLQCSECHGQLND-KCFARNGQLFC 169
Cdd:cd09452   1 CAQCNKIIRGRYLV-ALGRSYHPEEFTCSQCKKVLDEgGFFEEKGSIFC 48
LIM2_Prickle cd09418
The second LIM domain of Prickle; The second LIM domain of Prickle: Prickle contains three ...
120-169 7.26e-03

The second LIM domain of Prickle; The second LIM domain of Prickle: Prickle contains three C-terminal LIM domains and a N-terminal PET domain. Prickles have been implicated in roles of regulating tissue polarity or planar cell polarity (PCP). PCP establishment requires the conserved Frizzled/Dishevelled PCP pathway. Prickle interacts with Dishevelled, thereby modulating Frizzled/Dishevelled activity and PCP signaling. Two forms of prickles have been identified; namely prickle 1 and prickle 2. Prickle 1 and prickle 2 are differentially expressed. While prickle 1 is expressed in fetal heart and hematological malignancies, prickle 2 is found in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188802  Cd Length: 56  Bit Score: 35.10  E-value: 7.26e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 24585132 120 PKCGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCF-ARNGQLFC 169
Cdd:cd09418   1 PRCSACDEIIFADECTEAEGRHWHMKHFCCFECECQLGGQRYiMREGRPYC 51
LIM2_Zyxin cd09353
The second LIM domain of Zyxin; The second LIM domain of Zyxin: Zyxin exhibits three copies of ...
122-180 8.26e-03

The second LIM domain of Zyxin; The second LIM domain of Zyxin: Zyxin exhibits three copies of the LIM domain, an extensive proline-rich domain and a nuclear export signal. Localized at sites of cellsubstratum adhesion in fibroblasts, Zyxin interacts with alpha-actinin, members of the cysteine-rich protein (CRP) family, proteins that display Src homology 3 (SH3) domains and Ena/VASP family members. Zyxin and its partners have been implicated in the spatial control of actin filament assembly as well as in pathways important for cell differentiation. In addition to its functions at focal adhesion plaques, recent work has shown that zyxin moves from the sites of cell contacts to the nucleus, where it directly participates in the regulation of gene expression. As in other LIM domains, this domain family is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors o r scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188739 [Multi-domain]  Cd Length: 60  Bit Score: 34.91  E-value: 8.26e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24585132 122 CGGCHELILDRfILKVLERTWHAKCLQCSECHGQLNDKCFA--RNGQLFCKEDFFKRYGTK 180
Cdd:cd09353   1 CAVCDQKITDR-MLKATGKSYHPQCFTCVVCKCPLEGESFIvdQANQPHCVNDYHRRYAPR 60
LIM2_LIMK1 cd09464
The second LIM domain of LIMK1 (LIM domain Kinase 1); The second LIM domain of LIMK1 (LIM ...
181-236 9.54e-03

The second LIM domain of LIMK1 (LIM domain Kinase 1); The second LIM domain of LIMK1 (LIM domain Kinase 1): LIMK1 belongs to the LIMK protein family, which comprises LIMK1 and LIMK2. LIMK contains two LIM domains, a PDZ domain, and a kinase domain. LIMK is involved in the regulation of actin polymerization and microtubule disassembly. LIMK influences architecture of the actin cytoskeleton by regulating the activity of the cofilin family proteins cofilin1, cofilin2, and destrin. The mechanism of the activation is to phosphorylates cofilin on serine 3 and inactivates its actin-severing activity, and altering the rate of actin depolymerization. LIMKs can function in both cytoplasm and nucleus. Both LIMK1 and LIMK2 can act in the nucleus to suppress Rac/Cdc42-dependent cyclin D1 expression. LIMK1 is expressed in all tissues and is localized to focal adhesions in the cell. LIMK1 can form homodimers upon binding of HSP90 and is activated by Rho effector Rho kinase and MAPKAPK2. LIMK1 is important for normal central nervous system development, and its deletion has been implicated in the development of the human genetic disorder Williams syndrome. Moreover, LIMK1 up-regulates the promoter activity of urokinase type plasminogen activator and induces its mRNA and protein expression in breast cancer cells. The LIM domains have been shown to play an important role in regulating kinase activity and likely also contribute to LIMK function by acting as sites of protein-to-protein interactions. All LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188848  Cd Length: 55  Bit Score: 34.46  E-value: 9.54e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPpTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDRKLICKRDY 236
Cdd:cd09464   1 CHGCSETIT-TGLVMVAGEQKYHPECFSCLRCGAFIGDGDTYALVEHSKLYCGHCY 55
LIM2_Lrg1p_like cd09392
The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM ...
181-236 9.80e-03

The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein; The second LIM domain of Lrg1p, a LIM and RhoGap domain containing protein: The members of this family contain three tandem repeats of LIM domains and a Rho-type GTPase activating protein (RhoGap) domain. Lrg1p is a Rho1 GTPase-activating protein required for efficient cell fusion in yeast. Lrg1p-GAP domain strongly and specifically stimulates the GTPase activity of Rho1p, a regulator of beta (1-3)-glucan synthase in vitro. The LIM domain is 50-60 amino acids in size and shares two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein.


Pssm-ID: 188778 [Multi-domain]  Cd Length: 53  Bit Score: 34.64  E-value: 9.80e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24585132 181 CSACDMGIPPTQVVrrAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDrKLICKRDY 236
Cdd:cd09392   1 CFKCGGALRGSYIT--ALGRKYHVEHFTCSVCPTVFGPNDSYYEHEG-KIYCHYHY 53
LIM1_FHL2 cd09422
The first LIM domain of Four and a half LIM domains protein 2 (FHL2); The first LIM domain of ...
139-177 9.83e-03

The first LIM domain of Four and a half LIM domains protein 2 (FHL2); The first LIM domain of Four and a half LIM domains protein 2 (FHL2): FHL2 is one of the best studied FHL proteins. FHL2 expression is most abundant in the heart, and in brain, liver and lung at lesser extent. FHL2 participates in a wide range of cellular processes, such as transcriptional regulation, signal transduction, and cell survival by binding to various protein partners. FHL2 has shown to interact with more than 50 different proteins, including receptors, structural proteins, transcription factors and cofactors, signal transducers, splicing factors, DNA replication and repair enzymes, and metabolic enzymes. Although FHL2 is abundantly expressed in heart, the fhl2 null mice are viable and had no detectable abnormal cardiac phenotype. LIM domains are 50-60 amino acids in size and share two characteristic zinc finger motifs. The two zinc fingers contain eight conserved residues, mostly cysteines and histidines, which coordinately bond to two zinc atoms. LIM domains function as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 188806  Cd Length: 62  Bit Score: 34.88  E-value: 9.83e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24585132 139 ERTWHAKCLQCSECHGQLNDKCFA-RNGQLFCKEDFFKRY 177
Cdd:cd09422  23 DRHWHESCFHCFQCKNSLVDKPFAaKEEHLLCTECYSNEY 62
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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