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Conserved domains on  [gi|1958757274|ref|XP_038954681|]
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rhotekin-2 isoform X3 [Rattus norvegicus]

Protein Classification

RTKN2 family PH domain-containing protein( domain architecture ID 10192577)

RTKN2 family PH (pleckstrin homology) domain-containing protein similar to PH region of rhotekin-2 (RTKN2) that may play an important role in lymphopoiesis

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  22728242|17233582|15766521
SCOP:  4002395

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 58-167 7.33e-48

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 270069  Cd Length: 111  Bit Score: 157.93  E-value: 7.33e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757274  58 EDAFAGFLNEQQTGKGLVGWRRLYCALRGGKLRCFYGPEEIEAKVEPTLVIPVDKETRIQAMEKDSK-KMHCFSVLTTAA 136
Cdd:cd13249     1 QEMMSGYLSQQQSVEGLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSKgRASSLSIINPYS 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958757274 137 GRAVSHIFAADGLGDFQEWMDAFRQHRFDLS 167
Cdd:cd13249    81 GEEVTHVLSADSREELQKWMEALWQHFYDMS 111
 
Name Accession Description Interval E-value
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 58-167 7.33e-48

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270069  Cd Length: 111  Bit Score: 157.93  E-value: 7.33e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757274  58 EDAFAGFLNEQQTGKGLVGWRRLYCALRGGKLRCFYGPEEIEAKVEPTLVIPVDKETRIQAMEKDSK-KMHCFSVLTTAA 136
Cdd:cd13249     1 QEMMSGYLSQQQSVEGLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSKgRASSLSIINPYS 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958757274 137 GRAVSHIFAADGLGDFQEWMDAFRQHRFDLS 167
Cdd:cd13249    81 GEEVTHVLSADSREELQKWMEALWQHFYDMS 111
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 63-162 5.78e-11

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 58.71  E-value: 5.78e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757274   63 GFLnEQQTGKGLVGWRRLYCALRGGKLrCFYGPEEIEAKVEPTLVIPVDKET-RIQAMEKDSKKMHCFSVLTtaaGRAVS 141
Cdd:smart00233   5 GWL-YKKSGGGKKSWKKRYFVLFNSTL-LYYKSKKDKKSYKPKGSIDLSGCTvREAPDPDSSKKPHCFEIKT---SDRKT 79

                           90       100
                   ....*....|....*....|.
gi 1958757274  142 HIFAADGLGDFQEWMDAFRQH 162
Cdd:smart00233  80 LLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 63-161 1.97e-10

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 57.57  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757274  63 GFLNEQqTGKGLVGWRRLYCALRGGKLrCFYGPEEIEAKVEPTLVIPVDKETRIQAMEKDS-KKMHCFSVLTTAAGRAVS 141
Cdd:pfam00169   5 GWLLKK-GGGKKKSWKKRYFVLFDGSL-LYYKDDKSGKSKEPKGSISLSGCEVVEVVASDSpKRKFCFELRTGERTGKRT 82

                          90       100
                  ....*....|....*....|
gi 1958757274 142 HIFAADGLGDFQEWMDAFRQ 161
Cdd:pfam00169  83 YLLQAESEEERKDWIKAIQS 102
 
Name Accession Description Interval E-value
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 58-167 7.33e-48

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270069  Cd Length: 111  Bit Score: 157.93  E-value: 7.33e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757274  58 EDAFAGFLNEQQTGKGLVGWRRLYCALRGGKLRCFYGPEEIEAKVEPTLVIPVDKETRIQAMEKDSK-KMHCFSVLTTAA 136
Cdd:cd13249     1 QEMMSGYLSQQQSVEGLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSKgRASSLSIINPYS 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958757274 137 GRAVSHIFAADGLGDFQEWMDAFRQHRFDLS 167
Cdd:cd13249    81 GEEVTHVLSADSREELQKWMEALWQHFYDMS 111
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 63-162 5.78e-11

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 58.71  E-value: 5.78e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757274   63 GFLnEQQTGKGLVGWRRLYCALRGGKLrCFYGPEEIEAKVEPTLVIPVDKET-RIQAMEKDSKKMHCFSVLTtaaGRAVS 141
Cdd:smart00233   5 GWL-YKKSGGGKKSWKKRYFVLFNSTL-LYYKSKKDKKSYKPKGSIDLSGCTvREAPDPDSSKKPHCFEIKT---SDRKT 79

                           90       100
                   ....*....|....*....|.
gi 1958757274  142 HIFAADGLGDFQEWMDAFRQH 162
Cdd:smart00233  80 LLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 63-161 1.97e-10

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 57.57  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757274  63 GFLNEQqTGKGLVGWRRLYCALRGGKLrCFYGPEEIEAKVEPTLVIPVDKETRIQAMEKDS-KKMHCFSVLTTAAGRAVS 141
Cdd:pfam00169   5 GWLLKK-GGGKKKSWKKRYFVLFDGSL-LYYKDDKSGKSKEPKGSISLSGCEVVEVVASDSpKRKFCFELRTGERTGKRT 82

                          90       100
                  ....*....|....*....|
gi 1958757274 142 HIFAADGLGDFQEWMDAFRQ 161
Cdd:pfam00169  83 YLLQAESEEERKDWIKAIQS 102
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 62-159 1.13e-08

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 52.16  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757274  62 AGFLnEQQTGKGLVGWRRLYCALRGGKLRCFYGPEEieAKVEPTLVIPVDKETRIQAMEKDSKKmHCFSvLTTAAGRavS 141
Cdd:cd00821     2 EGYL-LKRGGGGLKSWKKRWFVLFEGVLLYYKSKKD--SSYKPKGSIPLSGILEVEEVSPKERP-HCFE-LVTPDGR--T 74

                          90
                  ....*....|....*...
gi 1958757274 142 HIFAADGLGDFQEWMDAF 159
Cdd:cd00821    75 YYLQADSEEERQEWLKAL 92
PH_anillin cd01263
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 61-166 1.92e-08

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269964  Cd Length: 121  Bit Score: 52.28  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757274  61 FAGFLNEQQTGKGLVGWRRLYCALRGGKLRCFYGPEEiEAKVEPTLVI----PVDKETRIQAMEKDSkKMHCFSVLTTAA 136
Cdd:cd01263     4 YRGFLTVFEDVSGLGAWHRRWCVLRGGYLSFWKYPDD-EEKKKPIGSIdltkCITEKVEPAPRELCA-RPNTFLLETLRP 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958757274 137 GRAVS---------HIFAADGLGDFQEWMDAFRQHRFDL 166
Cdd:cd01263    82 AEDDDrddtnekirVLLSADTKEERIEWLSALNQTLADL 120
PH_RASA1 cd13260
RAS p21 protein activator (GTPase activating protein) 1 Pleckstrin homology (PH) domain; RASA1 ...
 60-161 4.21e-05

RAS p21 protein activator (GTPase activating protein) 1 Pleckstrin homology (PH) domain; RASA1 (also called RasGap1 or p120) is a member of the RasGAP family of GTPase-activating proteins. RASA1 contains N-terminal SH2-SH3-SH2 domains, followed by two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. Splice variants lack the N-terminal domains. It is a cytosolic vertebrate protein that acts as a suppressor of RAS via its C-terminal GAP domain function, enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation. Additionally, it is involved in mitogenic signal transmission towards downstream interacting partners through its N-terminal SH2-SH3-SH2 domains. RASA1 interacts with a number of proteins including: G3BP1, SOCS3, ANXA6, Huntingtin, KHDRBS1, Src, EPHB3, EPH receptor B2, Insulin-like growth factor 1 receptor, PTK2B, DOK1, PDGFRB, HCK, Caveolin 2, DNAJA3, HRAS, GNB2L1 and NCK1. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270080  Cd Length: 103  Bit Score: 42.33  E-value: 4.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757274  60 AFAGFLNEQqtGKGLVGWRRLYCALRGGKLR-CFYgpeEIEAKVEPTLVIPVdKETRIQAMEkDS--KKMHCFSVLTTAA 136
Cdd:cd13260     4 DKKGYLLKK--GGKNKKWKNLYFVLEGKEQHlYFF---DNEKRTKPKGLIDL-SYCSLYPVH-DSlfGRPNCFQIVVRAL 76

                          90       100
                  ....*....|....*....|....*
gi 1958757274 137 GRAVSHIFAADGLGDFQEWMDAFRQ 161
Cdd:cd13260    77 NESTITYLCADTAELAQEWMRALRA 101
PH_AtPH1 cd13276
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ...
 61-158 6.18e-04

Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all plant tissue and is proposed to be the plant homolog of human pleckstrin. Pleckstrin consists of two PH domains separated by a linker region, while AtPH has a single PH domain with a short N-terminal extension. AtPH1 binds PtdIns3P specifically and is thought to be an adaptor molecule since it has no obvious catalytic functions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270095  Cd Length: 106  Bit Score: 38.84  E-value: 6.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757274  61 FAGFLNEQqtGKGLVGWRRLYCALRGGKLRCFYGPEEIEAKVePTLVIPVDKETRIQAMEKDSKKMHCFSVLTTAAgrav 140
Cdd:cd13276     1 KAGWLEKQ--GEFIKTWRRRWFVLKQGKLFWFKEPDVTPYSK-PRGVIDLSKCLTVKSAEDATNKENAFELSTPEE---- 73

                          90
                  ....*....|....*...
gi 1958757274 141 SHIFAADGLGDFQEWMDA 158
Cdd:cd13276    74 TFYFIADNEKEKEEWIGA 91
PH_PLEKHJ1 cd13258
Pleckstrin homology domain containing, family J member 1 Pleckstrin homology (PH) domain; ...
 47-162 1.87e-03

Pleckstrin homology domain containing, family J member 1 Pleckstrin homology (PH) domain; PLEKHJ1 (also called GNRPX2/Guanine nucleotide-releasing protein x ). It contains a single PH domain. Very little information is known about PLEKHJ1. PLEKHJ1 has been shown to interact with IKBKG (inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma) and KRT33B (keratin 33B). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270078  Cd Length: 123  Bit Score: 38.07  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958757274  47 CRLVAQPACMaEDAFAGflNEQQTGKGLVGWRRLYCALRGGKLrcFY-GPEEIEAKVEPTLVIpVDKETRIQaMEKDSKK 125
Cdd:cd13258     9 AALSSQPAEK-EGKIAE--RQMGGPKKSEVFKERWFKLKGNLL--FYfRTNEFGDCSEPIGAI-VLENCRVQ-MEEITEK 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958757274 126 MHCFSV--LTTAAGRavsHIFAADGLGDFQEWMDAFRQH 162
Cdd:cd13258    82 PFAFSIvfNDEPEKK---YIFSCRSEEQCEQWIEALRQA 117
 
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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