zinc finger protein 185 isoform X1 [Mus musculus]
Protein Classification
LIM domain-containing protein( domain architecture ID 10639037)
LIM (LIN-11, Isl1 and MEC-3) domain-containing protein; LIM is a small protein-protein interaction domain containing two zinc fingers; similar to mammalian sciellin and zinc finger protein 185
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| LIM | smart00132 | Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ... |
425-481 | 5.17e-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: 57.78 E-value: 5.17e-11
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| Name | Accession | Description | Interval | E-value | ||
| LIM | smart00132 | Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ... |
425-481 | 5.17e-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: 57.78 E-value: 5.17e-11
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| LIM | cd08368 | LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ... |
426-482 | 4.10e-07 | ||
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: 46.54 E-value: 4.10e-07
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| LIM | pfam00412 | LIM domain; This family represents two copies of the LIM structural domain. |
426-486 | 5.63e-06 | ||
LIM domain; This family represents two copies of the LIM structural domain. Pssm-ID: 395333 [Multi-domain] Cd Length: 57 Bit Score: 43.48 E-value: 5.63e-06
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| Name | Accession | Description | Interval | E-value | ||
| LIM | smart00132 | Zinc-binding domain present in Lin-11, Isl-1, Mec-3; Zinc-binding domain family. Some LIM ... |
425-481 | 5.17e-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: 57.78 E-value: 5.17e-11
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| LIM | cd08368 | LIM is a small protein-protein interaction domain, containing two zinc fingers; LIM domains ... |
426-482 | 4.10e-07 | ||
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: 46.54 E-value: 4.10e-07
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| LIM | pfam00412 | LIM domain; This family represents two copies of the LIM structural domain. |
426-486 | 5.63e-06 | ||
LIM domain; This family represents two copies of the LIM structural domain. Pssm-ID: 395333 [Multi-domain] Cd Length: 57 Bit Score: 43.48 E-value: 5.63e-06
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| LIM1_Testin_like | cd09340 | The first LIM domain of Testin-like family; The first LIM domain of Testin_like family: This ... |
426-482 | 7.22e-05 | ||
The first LIM domain of Testin-like family; The first 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: 188726 Cd Length: 58 Bit Score: 40.66 E-value: 7.22e-05
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| LIM2_FHL | cd09345 | The second LIM domain of Four and a half LIM domains protein (FHL); The second LIM domain of ... |
441-482 | 1.25e-04 | ||
The second LIM domain of Four and a half LIM domains protein (FHL); The second 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: 188731 [Multi-domain] Cd Length: 54 Bit Score: 39.58 E-value: 1.25e-04
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| LIM2_FHL1 | cd09424 | The second LIM domain of Four and a half LIM domains protein 1 (FHL1); The second LIM domain ... |
440-486 | 3.04e-04 | ||
The second LIM domain of Four and a half LIM domains protein 1 (FHL1); The second LIM domain of Four and a half LIM domains protein 1 (FHL1): FHL1 is heavily expressed in skeletal and cardiac muscles. It plays important roles in muscle growth, differentiation, and sarcomere assembly by acting as a modulator of transcription factors. Defects in FHL1 gene are responsible for a number of Muscular dystrophy-like muscle disorders. It has been detected that FHL1 binds to Myosin-binding protein C, regulating myosin filament formation and sarcomere assembly. 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: 188808 Cd Length: 58 Bit Score: 38.59 E-value: 3.04e-04
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| LIM1_Prickle_1 | cd09483 | The first LIM domain of Prickle 1; The first LIM domain of Prickle 1. Prickle contains three ... |
445-480 | 1.69e-03 | ||
The first LIM domain of Prickle 1; The first LIM domain of Prickle 1. 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. Four forms of prickles have been identified: prickle 1-4. The best characterized is prickle 1 and prickle 2 which are differentially expressed. While prickle 1 is expressed in fetal heart and hematological malignancies, prickle 2 is found in mainly expressed in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. In addition, Prickle 1 regulates cell movements during gastrulation and neuronal migration through interaction with the noncanonical Wnt11/Wnt5 pathway in zebrafish. Mutations in prickle 1 have been linked to progressive myoclonus epilepsy. 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: 188867 Cd Length: 59 Bit Score: 36.82 E-value: 1.69e-03
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| LIM1_Prickle | cd09415 | The first LIM domain of Prickle; The first LIM domain of Prickle: Prickle contains three ... |
445-480 | 8.52e-03 | ||
The first LIM domain of Prickle; The first 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. Four forms of prickles have been identified: prickle 1-4. The best characterized is prickle 1 and prickle 2 which 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. Mutations in prickle 1 have been linked to progressive myoclonus epilepsy. 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: 188799 Cd Length: 59 Bit Score: 34.54 E-value: 8.52e-03
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