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Conserved domains on  [gi|578813549|ref|XP_006715809|]
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anillin isoform X1 [Homo sapiens]

Protein Classification

Anillin and PH_anillin domain-containing protein( domain architecture ID 11240350)

protein containing domains Anillin_N, Anillin, and PH_anillin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PH_anillin cd01263
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
1001-1128 3.19e-64

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: 212.91  E-value: 3.19e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549 1001 SVEERGFLTIFEDVSGFGAWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRQIEPANREFCARRNTFELITVR 1080
Cdd:cd01263     1 SVEYRGFLTVFEDVSGLGAWHRRWCVLRGGYLSFWKYPDDEEKKKPIGSIDLTKCITEKVEPAPRELCARPNTFLLETLR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 578813549 1081 PQREDDREtlvsqcrDTLCVTKNWLSADTKEERDLWMQKLNQVLVDIR 1128
Cdd:cd01263    81 PAEDDDRD-------DTNEKIRVLLSADTKEERIEWLSALNQTLADLR 121
Anillin pfam08174
Cell division protein anillin; Anillin is a protein involved in septin organisation during ...
800-953 4.74e-43

Cell division protein anillin; Anillin is a protein involved in septin organisation during cell division. It is an actin binding protein that is localized to the cleavage furrow, and it maintains the localization of active myosin, which ensures the spatial control of concerted contraction during cytokinesis.


:

Pssm-ID: 429861  Cd Length: 139  Bit Score: 153.19  E-value: 4.74e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549   800 SKGSVTLSEIRLPLKADFVCSTVQKPDAANYYYLIILKAGaENMVATPLASTSNSLNGDALTFTTTFTLQDVSNDFEINI 879
Cdd:pfam08174    1 CKGKVTISDIRLPLKWKDVDHFKNKGESRRFAVFCLLKYG-TEIYATDLVSTVDRTDGTDLCFPDPIVFSNVPPDFEITV 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578813549   880 EVYSLVQKKDPSGLdkkkktskskAITPKRLltsittKSNIHSSVMASPGGLSAV--RTSNFALVGSYTLSLSSVG 953
Cdd:pfam08174   80 EVYSLCALEEDLSS----------ASTPKKL------KSKLSSSLGRSPGKKLAVavRGPKFKLLGSLTLTLSSVG 139
Anillin_N pfam16018
Anillin N-terminus; This domain is found towards the N-terminus of anillin. In mammalian ...
142-229 1.77e-41

Anillin N-terminus; This domain is found towards the N-terminus of anillin. In mammalian anillin this domain is repeated. This domain overlaps with the region responsible for nuclear localization of anillin.


:

Pssm-ID: 435074 [Multi-domain]  Cd Length: 86  Bit Score: 146.71  E-value: 1.77e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549   142 VKTRMQKLAEQRRRWDNDDMTDDIPESSLFSPMPSEEKAASPPRPllSNASATPVGRRGRLANLAATICSWEDDVNHSFA 221
Cdd:pfam16018    1 VKSRMQKLAEQRRRWDNDDWSDDVPESSPVSPLKSEAEAASPPKP--ITSSETPVGRRGRLANLAATIGSWEDDLSHPSI 78

                   ....*...
gi 578813549   222 KQNSVQEQ 229
Cdd:pfam16018   79 PQNPAQEK 86
Anillin_N super family cl24550
Anillin N-terminus; This domain is found towards the N-terminus of anillin. In mammalian ...
428-505 1.96e-08

Anillin N-terminus; This domain is found towards the N-terminus of anillin. In mammalian anillin this domain is repeated. This domain overlaps with the region responsible for nuclear localization of anillin.


The actual alignment was detected with superfamily member pfam16018:

Pssm-ID: 435074 [Multi-domain]  Cd Length: 86  Bit Score: 52.34  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549   428 KQERQKELACLRGRFDKgNIWSAEKGGNSKSKQLETKQE-------THCQSTPLKKHQGVSKTQSLPVT--EKVTENQIP 498
Cdd:pfam16018    1 VKSRMQKLAEQRRRWDN-DDWSDDVPESSPVSPLKSEAEaasppkpITSSETPVGRRGRLANLAATIGSweDDLSHPSIP 79

                   ....*..
gi 578813549   499 AKNSSTE 505
Cdd:pfam16018   80 QNPAQEK 86
 
Name Accession Description Interval E-value
PH_anillin cd01263
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
1001-1128 3.19e-64

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: 212.91  E-value: 3.19e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549 1001 SVEERGFLTIFEDVSGFGAWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRQIEPANREFCARRNTFELITVR 1080
Cdd:cd01263     1 SVEYRGFLTVFEDVSGLGAWHRRWCVLRGGYLSFWKYPDDEEKKKPIGSIDLTKCITEKVEPAPRELCARPNTFLLETLR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 578813549 1081 PQREDDREtlvsqcrDTLCVTKNWLSADTKEERDLWMQKLNQVLVDIR 1128
Cdd:cd01263    81 PAEDDDRD-------DTNEKIRVLLSADTKEERIEWLSALNQTLADLR 121
Anillin pfam08174
Cell division protein anillin; Anillin is a protein involved in septin organisation during ...
800-953 4.74e-43

Cell division protein anillin; Anillin is a protein involved in septin organisation during cell division. It is an actin binding protein that is localized to the cleavage furrow, and it maintains the localization of active myosin, which ensures the spatial control of concerted contraction during cytokinesis.


Pssm-ID: 429861  Cd Length: 139  Bit Score: 153.19  E-value: 4.74e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549   800 SKGSVTLSEIRLPLKADFVCSTVQKPDAANYYYLIILKAGaENMVATPLASTSNSLNGDALTFTTTFTLQDVSNDFEINI 879
Cdd:pfam08174    1 CKGKVTISDIRLPLKWKDVDHFKNKGESRRFAVFCLLKYG-TEIYATDLVSTVDRTDGTDLCFPDPIVFSNVPPDFEITV 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578813549   880 EVYSLVQKKDPSGLdkkkktskskAITPKRLltsittKSNIHSSVMASPGGLSAV--RTSNFALVGSYTLSLSSVG 953
Cdd:pfam08174   80 EVYSLCALEEDLSS----------ASTPKKL------KSKLSSSLGRSPGKKLAVavRGPKFKLLGSLTLTLSSVG 139
Anillin_N pfam16018
Anillin N-terminus; This domain is found towards the N-terminus of anillin. In mammalian ...
142-229 1.77e-41

Anillin N-terminus; This domain is found towards the N-terminus of anillin. In mammalian anillin this domain is repeated. This domain overlaps with the region responsible for nuclear localization of anillin.


Pssm-ID: 435074 [Multi-domain]  Cd Length: 86  Bit Score: 146.71  E-value: 1.77e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549   142 VKTRMQKLAEQRRRWDNDDMTDDIPESSLFSPMPSEEKAASPPRPllSNASATPVGRRGRLANLAATICSWEDDVNHSFA 221
Cdd:pfam16018    1 VKSRMQKLAEQRRRWDNDDWSDDVPESSPVSPLKSEAEAASPPKP--ITSSETPVGRRGRLANLAATIGSWEDDLSHPSI 78

                   ....*...
gi 578813549   222 KQNSVQEQ 229
Cdd:pfam16018   79 PQNPAQEK 86
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
1005-1124 7.02e-17

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  Cd Length: 102  Bit Score: 77.20  E-value: 7.02e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549   1005 RGFLTIFEDvSGFGAWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRqiEPANREFCARRNTFELITvrpqre 1084
Cdd:smart00233    4 EGWLYKKSG-GGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLSGCTVR--EAPDPDSSKKPHCFEIKT------ 74
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 578813549   1085 DDRETLVsqcrdtlcvtknwLSADTKEERDLWMQKLNQVL 1124
Cdd:smart00233   75 SDRKTLL-------------LQAESEEEREKWVEALRKAI 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
1005-1124 1.71e-13

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 395117 [Multi-domain]  Cd Length: 105  Bit Score: 67.59  E-value: 1.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549  1005 RGFLTIFEDVSGFGaWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRQIEPANREfcARRNTFELITVRPQRe 1084
Cdd:pfam00169    4 EGWLLKKGGGKKKS-WKKRYFVLFDGSLLYYKDDKSKKSKEPKGSISLSGCEVVEVVASDSP--KRKFCFELRTGERTG- 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 578813549  1085 ddRETLVsqcrdtlcvtknwLSADTKEERDLWMQKLNQVL 1124
Cdd:pfam00169   80 --KRTYL-------------LQAESEEERKDWIKAIQSAI 104
Anillin_N pfam16018
Anillin N-terminus; This domain is found towards the N-terminus of anillin. In mammalian ...
428-505 1.96e-08

Anillin N-terminus; This domain is found towards the N-terminus of anillin. In mammalian anillin this domain is repeated. This domain overlaps with the region responsible for nuclear localization of anillin.


Pssm-ID: 435074 [Multi-domain]  Cd Length: 86  Bit Score: 52.34  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549   428 KQERQKELACLRGRFDKgNIWSAEKGGNSKSKQLETKQE-------THCQSTPLKKHQGVSKTQSLPVT--EKVTENQIP 498
Cdd:pfam16018    1 VKSRMQKLAEQRRRWDN-DDWSDDVPESSPVSPLKSEAEaasppkpITSSETPVGRRGRLANLAATIGSweDDLSHPSIP 79

                   ....*..
gi 578813549   499 AKNSSTE 505
Cdd:pfam16018   80 QNPAQEK 86
 
Name Accession Description Interval E-value
PH_anillin cd01263
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
1001-1128 3.19e-64

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: 212.91  E-value: 3.19e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549 1001 SVEERGFLTIFEDVSGFGAWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRQIEPANREFCARRNTFELITVR 1080
Cdd:cd01263     1 SVEYRGFLTVFEDVSGLGAWHRRWCVLRGGYLSFWKYPDDEEKKKPIGSIDLTKCITEKVEPAPRELCARPNTFLLETLR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 578813549 1081 PQREDDREtlvsqcrDTLCVTKNWLSADTKEERDLWMQKLNQVLVDIR 1128
Cdd:cd01263    81 PAEDDDRD-------DTNEKIRVLLSADTKEERIEWLSALNQTLADLR 121
Anillin pfam08174
Cell division protein anillin; Anillin is a protein involved in septin organisation during ...
800-953 4.74e-43

Cell division protein anillin; Anillin is a protein involved in septin organisation during cell division. It is an actin binding protein that is localized to the cleavage furrow, and it maintains the localization of active myosin, which ensures the spatial control of concerted contraction during cytokinesis.


Pssm-ID: 429861  Cd Length: 139  Bit Score: 153.19  E-value: 4.74e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549   800 SKGSVTLSEIRLPLKADFVCSTVQKPDAANYYYLIILKAGaENMVATPLASTSNSLNGDALTFTTTFTLQDVSNDFEINI 879
Cdd:pfam08174    1 CKGKVTISDIRLPLKWKDVDHFKNKGESRRFAVFCLLKYG-TEIYATDLVSTVDRTDGTDLCFPDPIVFSNVPPDFEITV 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578813549   880 EVYSLVQKKDPSGLdkkkktskskAITPKRLltsittKSNIHSSVMASPGGLSAV--RTSNFALVGSYTLSLSSVG 953
Cdd:pfam08174   80 EVYSLCALEEDLSS----------ASTPKKL------KSKLSSSLGRSPGKKLAVavRGPKFKLLGSLTLTLSSVG 139
Anillin_N pfam16018
Anillin N-terminus; This domain is found towards the N-terminus of anillin. In mammalian ...
142-229 1.77e-41

Anillin N-terminus; This domain is found towards the N-terminus of anillin. In mammalian anillin this domain is repeated. This domain overlaps with the region responsible for nuclear localization of anillin.


Pssm-ID: 435074 [Multi-domain]  Cd Length: 86  Bit Score: 146.71  E-value: 1.77e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549   142 VKTRMQKLAEQRRRWDNDDMTDDIPESSLFSPMPSEEKAASPPRPllSNASATPVGRRGRLANLAATICSWEDDVNHSFA 221
Cdd:pfam16018    1 VKSRMQKLAEQRRRWDNDDWSDDVPESSPVSPLKSEAEAASPPKP--ITSSETPVGRRGRLANLAATIGSWEDDLSHPSI 78

                   ....*...
gi 578813549   222 KQNSVQEQ 229
Cdd:pfam16018   79 PQNPAQEK 86
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
1005-1124 7.02e-17

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  Cd Length: 102  Bit Score: 77.20  E-value: 7.02e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549   1005 RGFLTIFEDvSGFGAWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRqiEPANREFCARRNTFELITvrpqre 1084
Cdd:smart00233    4 EGWLYKKSG-GGKKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKGSIDLSGCTVR--EAPDPDSSKKPHCFEIKT------ 74
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 578813549   1085 DDRETLVsqcrdtlcvtknwLSADTKEERDLWMQKLNQVL 1124
Cdd:smart00233   75 SDRKTLL-------------LQAESEEEREKWVEALRKAI 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
1005-1124 1.71e-13

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 395117 [Multi-domain]  Cd Length: 105  Bit Score: 67.59  E-value: 1.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549  1005 RGFLTIFEDVSGFGaWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRQIEPANREfcARRNTFELITVRPQRe 1084
Cdd:pfam00169    4 EGWLLKKGGGKKKS-WKKRYFVLFDGSLLYYKDDKSKKSKEPKGSISLSGCEVVEVVASDSP--KRKFCFELRTGERTG- 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 578813549  1085 ddRETLVsqcrdtlcvtknwLSADTKEERDLWMQKLNQVL 1124
Cdd:pfam00169   80 --KRTYL-------------LQAESEEERKDWIKAIQSAI 104
PH_GRP1-like cd01252
General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 ...
1020-1124 3.85e-13

General Receptor for Phosphoinositides-1-like Pleckstrin homology (PH) domain; GRP1/cytohesin3 and the related proteins ARNO (ARF nucleotide-binding site opener)/cytohesin-2 and cytohesin-1 are ARF exchange factors that contain a pleckstrin homology (PH) domain thought to target these proteins to cell membranes through binding polyphosphoinositides. The PH domains of all three proteins exhibit relatively high affinity for PtdIns(3,4,5)P3. Within the Grp1 family, diglycine (2G) and triglycine (3G) splice variants, differing only in the number of glycine residues in the PH domain, strongly influence the affinity and specificity for phosphoinositides. The 2G variants selectively bind PtdIns(3,4,5)P3 with high affinity,the 3G variants bind PtdIns(3,4,5)P3 with about 30-fold lower affinity and require the polybasic region for plasma membrane targeting. These ARF-GEFs share a common, tripartite structure consisting of an N-terminal coiled-coil domain, a central domain with homology to the yeast protein Sec7, a PH domain, and a C-terminal polybasic region. The Sec7 domain is autoinhibited by conserved elements proximal to the PH domain. GRP1 binds to the DNA binding domain of certain nuclear receptors (TRalpha, TRbeta, AR, ER, but not RXR), and can repress thyroid hormone receptor (TR)-mediated transactivation by decreasing TR-complex formation on thyroid hormone response elements. ARNO promotes sequential activation of Arf6, Cdc42 and Rac1 and insulin secretion. Cytohesin acts as a PI 3-kinase effector mediating biological responses including cell spreading and adhesion, chemotaxis, protein trafficking, and cytoskeletal rearrangements, only some of which appear to depend on their ability to activate ARFs. 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: 269954  Cd Length: 119  Bit Score: 66.95  E-value: 3.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549 1020 WHRRWCVLSGNCISYWTYPDDekrKNPIGRINLANCTSRQIEPANREFCarrntFELITvrpqreDDRETLVSQCR---D 1096
Cdd:cd01252    19 WKRRWFILTDNCLYYFEYTTD---KEPRGIIPLENLSVREVEDKKKPFC-----FELYS------PSNGQVIKACKtdsD 84
                          90       100       110
                  ....*....|....*....|....*....|..
gi 578813549 1097 TLCVTKN----WLSADTKEERDLWMQKLNQVL 1124
Cdd:cd01252    85 GKVVEGNhtvyRISAASEEERDEWIKSIKASI 116
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
1006-1120 4.32e-12

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: 63.33  E-value: 4.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549 1006 GFLTIFEDVSGFGaWHRRWCVLSGNCISYwTYPDDEKRKNPIGRINLANCTSrqIEPANREfcARRNTFELITvrpqreD 1085
Cdd:cd00821     3 GYLLKRGGGGLKS-WKKRWFVLFEGVLLY-YKSKKDSSYKPKGSIPLSGILE--VEEVSPK--ERPHCFELVT------P 70
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 578813549 1086 DRETLVsqcrdtlcvtknwLSADTKEERDLWMQKL 1120
Cdd:cd00821    71 DGRTYY-------------LQADSEEERQEWLKAL 92
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
996-1122 1.18e-08

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. 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: 270068  Cd Length: 104  Bit Score: 53.82  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549  996 CQVNSSVEERGFLTIfEDVSGFGAWHRRWCVLSGNCISYWTYPDDEKrknPIGRINLAnctSRQIEPANREFCA-RRNTF 1074
Cdd:cd13248     1 RDPNAPVVMSGWLHK-QGGSGLKNWRKRWFVLKDNCLYYYKDPEEEK---ALGSILLP---SYTISPAPPSDEIsRKFAF 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 578813549 1075 ELitvrpQREDDRetlvsqcrdtlcvtKNWLSADTKEERDLWMQKLNQ 1122
Cdd:cd13248    74 KA-----EHANMR--------------TYYFAADTAEEMEQWMNAMSL 102
Anillin_N pfam16018
Anillin N-terminus; This domain is found towards the N-terminus of anillin. In mammalian ...
428-505 1.96e-08

Anillin N-terminus; This domain is found towards the N-terminus of anillin. In mammalian anillin this domain is repeated. This domain overlaps with the region responsible for nuclear localization of anillin.


Pssm-ID: 435074 [Multi-domain]  Cd Length: 86  Bit Score: 52.34  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549   428 KQERQKELACLRGRFDKgNIWSAEKGGNSKSKQLETKQE-------THCQSTPLKKHQGVSKTQSLPVT--EKVTENQIP 498
Cdd:pfam16018    1 VKSRMQKLAEQRRRWDN-DDWSDDVPESSPVSPLKSEAEaasppkpITSSETPVGRRGRLANLAATIGSweDDLSHPSIP 79

                   ....*..
gi 578813549   499 AKNSSTE 505
Cdd:pfam16018   80 QNPAQEK 86
PH_ACAP cd13250
ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP ...
1015-1121 2.26e-08

ArfGAP with coiled-coil, ankyrin repeat and PH domains Pleckstrin homology (PH) domain; ACAP (also called centaurin beta) functions both as a Rab35 effector and as an Arf6-GTPase-activating protein (GAP) by which it controls actin remodeling and membrane trafficking. ACAP contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain, a phospholipid-binding domain, a PH domain, a GAP domain, and four ankyrin repeats. The AZAPs constitute a family of Arf GAPs that are characterized by an NH2-terminal pleckstrin homology (PH) domain and a central Arf GAP domain followed by two or more ankyrin repeats. On the basis of sequence and domain organization, the AZAP family is further subdivided into four subfamilies: 1) the ACAPs contain an NH2-terminal bin/amphiphysin/Rvs (BAR) domain (a phospholipid-binding domain that is thought to sense membrane curvature), a single PH domain followed by the GAP domain, and four ankyrin repeats; 2) the ASAPs also contain an NH2-terminal BAR domain, the tandem PH domain/GAP domain, three ankyrin repeats, two proline-rich regions, and a COOH-terminal Src homology 3 domain; 3) the AGAPs contain an NH2-terminal GTPase-like domain (GLD), a split PH domain, and the GAP domain followed by four ankyrin repeats; and 4) the ARAPs contain both an Arf GAP domain and a Rho GAP domain, as well as an NH2-terminal sterile-a motif (SAM), a proline-rich region, a GTPase-binding domain, and five PH domains. PMID 18003747 and 19055940 Centaurin can bind to phosphatidlyinositol (3,4,5)P3. 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: 270070  Cd Length: 98  Bit Score: 52.61  E-value: 2.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549 1015 SGFGAWHRRWCVLSGNCISYwtYPDDEKRKNPIGRINLANCTSRQIEPANREFCarrntFELITvrPQReddreTLVsqc 1094
Cdd:cd13250    11 NAFKTWKRRWFSLQNGQLYY--QKRDKKDEPTVMVEDLRLCTVKPTEDSDRRFC-----FEVIS--PTK-----SYM--- 73
                          90       100
                  ....*....|....*....|....*..
gi 578813549 1095 rdtlcvtknwLSADTKEERDLWMQKLN 1121
Cdd:cd13250    74 ----------LQAESEEDRQAWIQAIQ 90
PH_Ses cd13288
Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 ...
999-1120 9.26e-07

Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 mammalian members: Ses1 and Ses2, which are also callled 7 kDa inositol polyphosphate phosphatase-interacting protein 1 and 2. They play a role in endocytic trafficking and are required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. Members of this family form homodimers and heterodimers. Sesquipedalian interacts with inositol polyphosphate 5-phosphatase OCRL-1 (INPP5F) also known as Lowe oculocerebrorenal syndrome protein, a phosphatase enzyme that is involved in actin polymerization and is found in the trans-Golgi network and INPP5B. Sesquipedalian contains a single 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: 270105 [Multi-domain]  Cd Length: 120  Bit Score: 48.77  E-value: 9.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549  999 NSSVEERGFLtiFEDVSGFGAWHRRWCVLSGNCISYWTYPDDekrKNPIGRINLANCTsrqIEPANrefCARRNTFELIT 1078
Cdd:cd13288     5 NSPVDKEGYL--WKKGERNTSYQKRWFVLKGNLLFYFEKKGD---REPLGVIVLEGCT---VELAE---DAEPYAFAIRF 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 578813549 1079 vrpQREDDReTLVsqcrdtlcvtknwLSADTKEERDLWMQKL 1120
Cdd:cd13288    74 ---DGPGAR-SYV-------------LAAENQEDMESWMKAL 98
PH_Btk cd01238
Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of ...
1020-1123 1.23e-06

Bruton's tyrosine kinase pleckstrin homology (PH) domain; Btk is a member of the Tec family of cytoplasmic protein tyrosine kinases that includes BMX, IL2-inducible T-cell kinase (Itk) and Tec. Btk plays a role in the maturation of B cells. Tec proteins general have an N-terminal PH domain, followed by a Tek homology (TH) domain, a SH3 domain, a SH2 domain and a kinase domain. The Btk PH domain binds phosphatidylinositol 3,4,5-trisphosphate and responds to signalling via phosphatidylinositol 3-kinase. The PH domain is also involved in membrane anchoring which is confirmed by the discovery of a mutation of a critical arginine residue in the BTK PH domain. This results in severe human immunodeficiency known as X-linked agammaglobulinemia (XLA) in humans and a related disorder is mice.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: 269944 [Multi-domain]  Cd Length: 140  Bit Score: 49.15  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549 1020 WHRRWCVLSGNCISYWTYpDDEKRKNPIGRINLANCTSrqIEPA-NREFCARRNTFElitvrpqreddretlVSQCRDTL 1098
Cdd:cd01238    20 YKERWFVLTKSSLSYYEG-DGEKRGKEKGSIDLSKVRC--VEEVkDEAFFERKYPFQ---------------VVYDDYTL 81
                          90       100
                  ....*....|....*....|....*
gi 578813549 1099 CVtknwlSADTKEERDLWMQKLNQV 1123
Cdd:cd01238    82 YV-----FAPSEEDRDEWIAALRKV 101
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
1006-1126 1.11e-05

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: 45.45  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549 1006 GFLTIFEDVSGFGAWHRRWCVLSGNCIS-YWTYPDDEKRKNPIGRINLANCTsrQIEPANREFCARRNTFELITVRPqre 1084
Cdd:cd13249     6 GYLSQQQSVEGLQSWTRLYCVLKGGNLLcYYSPEEIEAKVEPLLTIPINKET--RIRAVEKDSKGRASSLSIINPYS--- 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 578813549 1085 DDRETLVsqcrdtlcvtknwLSADTKEERDLWMQKLNQVLVD 1126
Cdd:cd13249    81 GEEVTHV-------------LSADSREELQKWMEALWQHFYD 109
PH_RhoGap25-like cd13263
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ...
1020-1124 1.69e-05

Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; RhoGAP25 (also called ArhGap25) like other RhoGaps are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. This hierarchy contains RhoGAP22, RhoGAP24, and RhoGAP25. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) 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: 270083  Cd Length: 114  Bit Score: 45.07  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549 1020 WHRRWCVLSGNCISYWTYPDDEKrknPIGRINLANCTSRQIePANREfCARRNTFELItvrPQREDDRETlvsQCRDTlC 1099
Cdd:cd13263    19 WQQRWFVLRGDQLYYYKDEDDTK---PQGTIPLPGNKVKEV-PFNPE-EPGKFLFEII---PGGGGDRMT---SNHDS-Y 86
                          90       100
                  ....*....|....*....|....*
gi 578813549 1100 VtknwLSADTKEERDLWMQKLNQVL 1124
Cdd:cd13263    87 L----LMANSQAEMEEWVKVIRRVI 107
PH_Bem3 cd13277
Bud emergence protein 3 (Bem3) Pleckstrin homology (PH) domain; Bud emergence in Saccharomyces ...
1015-1124 2.09e-05

Bud emergence protein 3 (Bem3) Pleckstrin homology (PH) domain; Bud emergence in Saccharomyces cerevisiae involves cell cycle-regulated reorganizations of cortical cytoskeletal elements and requires the action of the Rho-type GTPase Cdc42. Bem3 contains a RhoGAP domain and a PH domain. Though Bem3 and Bem2 both contain a RhoGAP, but only Bem3 is able to stimulate the hydrolysis of GTP on Cdc42. Bem3 is thought to be the GAP for Cdc42. 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: 270096  Cd Length: 111  Bit Score: 44.58  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549 1015 SGFGAWHRRWCVLSGNCISYWtypddEKRKNP-IGRINLANCTSRQIEPANREFCARRNTFeLITvrpqrEDDRETLVSQ 1093
Cdd:cd13277    18 GSTGGWKLRYGVLDGNILELY-----ESRGGQlLESIKLRNAQIERQPNLPDDKYGTRHGF-LIN-----EHKKSGLSST 86
                          90       100       110
                  ....*....|....*....|....*....|.
gi 578813549 1094 CRDTLCvtknwlsADTKEERDLWMQKLNQVL 1124
Cdd:cd13277    87 TKYYLC-------AETDKERDEWVSALSEYI 110
PH1_PLEKHH1_PLEKHH2 cd13282
Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 ...
1006-1124 2.88e-05

Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 (PLEKHH1) PH domain, repeat 1; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. 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: 241436  Cd Length: 96  Bit Score: 43.83  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549 1006 GFLTifeDVSG-FGAWHRRWCVLSGNCISYWTYPDDEKRKnPIGRINLAncTSRQIEPANREfcarrNTFELITvrpqre 1084
Cdd:cd13282     3 GYLT---KLGGkVKTWKRRWFVLKNGELFYYKSPNDVIRK-PQGQIALD--GSCEIARAEGA-----QTFEIVT------ 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 578813549 1085 dDRETLVsqcrdtlcvtknwLSADTKEERDLWMQKLNQVL 1124
Cdd:cd13282    66 -EKRTYY-------------LTADSENDLDEWIRVIQNVL 91
PH-GRAM1_AGT26 cd13215
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
981-1078 5.50e-05

Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, repeat 1; ATG26 (also called UGT51/UDP-glycosyltransferase 51), a member of the glycosyltransferase 28 family, resulting in the biosynthesis of sterol glucoside. ATG26 in decane metabolism and autophagy. There are 32 known autophagy-related (ATG) proteins, 17 are components of the core autophagic machinery essential for all autophagy-related pathways and 15 are the additional components required only for certain pathways or species. The core autophagic machinery includes 1) the ATG9 cycling system (ATG1, ATG2, ATG9, ATG13, ATG18, and ATG27), 2) the phosphatidylinositol 3-kinase complex (ATG6/VPS30, ATG14, VPS15, and ATG34), and 3) the ubiquitin-like protein system (ATG3, ATG4, ATG5, ATG7, ATG8, ATG10, ATG12, and ATG16). Less is known about how the core machinery is adapted or modulated with additional components to accommodate the nonselective sequestration of bulk cytosol (autophagosome formation) or selective sequestration of specific cargos (Cvt vesicle, pexophagosome, or bacteria-containing autophagosome formation). The pexophagosome-specific additions include the ATG30-ATG11-ATG17 receptor-adaptors complex, the coiled-coil protein ATG25, and the sterol glucosyltransferase ATG26. ATG26 is necessary for the degradation of medium peroxisomes. It contains 2 GRAM domains and a single PH domain. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but 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: 275402  Cd Length: 116  Bit Score: 43.76  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549  981 PFLSSLEGHIylkIKCqvnssveerGFLTIFEDVSGFgaWHRRWCVLSGNCISYwtYPDDEKRKNPIGRINLANCTSRQI 1060
Cdd:cd13215    12 AYLPKRSGAV---IKS---------GYLSKRSKRTLR--YTRYWFVLKGDTLSW--YNSSTDLYFPAGTIDLRYATSIEL 75
                          90
                  ....*....|....*...
gi 578813549 1061 EPANREfcaRRNTFELIT 1078
Cdd:cd13215    76 SKSNGE---ATTSFKIVT 90
PH_M-RIP cd13275
Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed ...
1018-1107 1.76e-04

Myosin phosphatase-RhoA Interacting Protein Pleckstrin homology (PH) domain; M-RIP is proposed to play a role in myosin phosphatase regulation by RhoA. M-RIP contains 2 PH domains followed by a Rho binding domain (Rho-BD), and a C-terminal myosin binding subunit (MBS) binding domain (MBS-BD). The amino terminus of M-RIP with its adjacent PH domains and polyproline motifs mediates binding to both actin and Galpha. M-RIP brings RhoA and MBS into close proximity where M-RIP can target RhoA to the myosin phosphatase complex to regulate the myosin phosphorylation state. M-RIP does this via its C-terminal coiled-coil domain which interacts with the MBS leucine zipper domain of myosin phosphatase, while its Rho-BD, directly binds RhoA in a nucleotide-independent manner. 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: 270094  Cd Length: 104  Bit Score: 41.93  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549 1018 GAWHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSRQIEPANREFcarrnTFELITvrpqREDDRETLVSQcrdT 1097
Cdd:cd13275    13 GEWSKHWFVLRGAALKYYRDPSAEEAGELDGVIDLSSCTEVTELPVSRNY-----GFQVKT----WDGKVYVLSAM---T 80
                          90
                  ....*....|
gi 578813549 1098 LCVTKNWLSA 1107
Cdd:cd13275    81 SGIRTNWIQA 90
PH_AtPH1 cd13276
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ...
1020-1078 6.02e-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: 40.38  E-value: 6.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 578813549 1020 WHRRWCVLSGNCISYWTYPDDEKRKNPIGRINLANCTSrqIEPANREFcARRNTFELIT 1078
Cdd:cd13276    15 WRRRWFVLKQGKLFWFKEPDVTPYSKPRGVIDLSKCLT--VKSAEDAT-NKENAFELST 70
PH3_ARAP cd13256
ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, ...
1022-1110 1.72e-03

ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, repeat 3; ARAP proteins (also called centaurin delta) are phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating proteins that modulate actin cytoskeleton remodeling by regulating ARF and RHO family members. They bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding. There are 3 mammalian ARAP proteins: ARAP1, ARAP2, and ARAP3. All ARAP proteins contain a N-terminal SAM (sterile alpha motif) domain, 5 PH domains, an ArfGAP domain, 2 ankyrin domain, A RhoGap domain, and a Ras-associating domain. This hierarchy contains the third PH domain in ARAP. 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: 270076  Cd Length: 110  Bit Score: 39.36  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549 1022 RRWCVLSGNCISYWtypDDEKRKNPIGRINLANCTSRQIEPANREFCAR-RNTFELITvrpqrEDDRETLVSQcrDTLCV 1100
Cdd:cd13256    29 RRWCVLEDGFLSYY---ESERSPEPNGEIDVSEIVCLAVSPPDTHPGDGfPFTFELYL-----ESERLYLFGL--ETAEA 98
                          90
                  ....*....|
gi 578813549 1101 TKNWLSADTK 1110
Cdd:cd13256    99 LHEWVKAIAK 108
PH_DAPP1 cd10573
Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; ...
1020-1121 2.93e-03

Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; DAPP1 (also known as PHISH/3' phosphoinositide-interacting SH2 domain-containing protein or Bam32) plays a role in B-cell activation and has potential roles in T-cell and mast cell function. DAPP1 promotes B cell receptor (BCR) induced activation of Rho GTPases Rac1 and Cdc42, which feed into mitogen-activated protein kinases (MAPK) activation pathways and affect cytoskeletal rearrangement. DAPP1can also regulate BCR-induced activation of extracellular signal-regulated kinase (ERK), and c-jun NH2-terminal kinase (JNK). DAPP1 contains an N-terminal SH2 domain and a C-terminal pleckstrin homology (PH) domain with a single tyrosine phosphorylation site located centrally. DAPP1 binds strongly to both PtdIns(3,4,5)P3 and PtdIns(3,4)P2. The PH domain is essential for plasma membrane recruitment of PI3K upon cell activation. 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: 269977 [Multi-domain]  Cd Length: 96  Bit Score: 38.07  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549 1020 WHRRWCVLSGNCISYWTYPDDEKrknPIGRINLANCTSRQIEPAnrefCARRNTFELitVRPQREddretlvsqcrdtlc 1099
Cdd:cd10573    19 WKTRWFVLRRNELKYFKTRGDTK---PIRVLDLRECSSVQRDYS----QGKVNCFCL--VFPERT--------------- 74
                          90       100
                  ....*....|....*....|..
gi 578813549 1100 vtkNWLSADTKEERDLWMQKLN 1121
Cdd:cd10573    75 ---FYMYANTEEEADEWVKLLK 93
PH_Skap1 cd13380
Src kinase-associated phosphoprotein 1 Pleckstrin homology (PH) domain; Adaptor protein Skap1 ...
1013-1078 5.17e-03

Src kinase-associated phosphoprotein 1 Pleckstrin homology (PH) domain; Adaptor protein Skap1 (also called Skap55/Src kinase-associated phosphoprotein of 55 kDa) and its partner, ADAP (adhesion and degranulation promoting adapter protein) help reorganize the cytoskeleton and/or promote integrin-mediated adhesion upon immunoreceptor activation. Skap1 is also involved in T Cell Receptor (TCR)-induced RapL-Rap1 complex formation and LFA-1 activation. Skap1 has an N-terminal coiled-coil conformation which is proposed to be involved in homodimer formation, a central PH domain and a C-terminal SH3 domain that associates with ADAP. The Skap1 PH domain plays a role in controlling integrin function via recruitment of ADAP-SKAP complexes to integrins as well as in controlling the ability of ADAP to interact with the CBM signalosome and regulate NF-kappaB. SKAP1 is necessary for RapL binding to membranes in a PH domain-dependent manner and the PI3K pathway. Skap adaptor proteins couple receptors to cytoskeletal rearrangements. Skap55/Skap1, Skap2, and Skap-homology (Skap-hom) have an N-terminal coiled-coil conformation, a central PH domain and a C-terminal SH3 domain. Their PH domains bind 3'-phosphoinositides as well as directly affecting targets such as in Skap55 where it directly affecting integrin regulation by ADAP and NF-kappaB activation or in Skap-hom where the dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch that controls ruffle formation. 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: 270180  Cd Length: 106  Bit Score: 37.91  E-value: 5.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578813549 1013 DVSGFGA-WHRRWCVLSGNCISYWTypdDEKRKNPIGRINLANCtSRQIEPANREFCARRNTFELIT 1078
Cdd:cd13380    13 DHSFFGSeWQKRWCVLTNRAFYYYA---SEKSKQPKGGFLIKGY-SAQMAPHLRKDSRRDSCFELTT 75
PH1_ARAP cd13253
ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, ...
1020-1124 7.04e-03

ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, repeat 1; ARAP proteins (also called centaurin delta) are phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating proteins that modulate actin cytoskeleton remodeling by regulating ARF and RHO family members. They bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding. There are 3 mammalian ARAP proteins: ARAP1, ARAP2, and ARAP3. All ARAP proteins contain a N-terminal SAM (sterile alpha motif) domain, 5 PH domains, an ArfGAP domain, 2 ankyrin domain, A RhoGap domain, and a Ras-associating domain. This hierarchy contains the first PH domain in ARAP. 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: 270073  Cd Length: 94  Bit Score: 36.98  E-value: 7.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549 1020 WHRRWCVLSGNCISYWtypDDEKRKNPIGRINLAnCTSRQIEPANrefcarrNTFELITVrpQReddreTLVsqcrdtlc 1099
Cdd:cd13253    18 FQKRWVVFDGLSLRYF---DSEKDAYSKRIIPLS-AISTVRAVGD-------NKFELVTT--NR-----TFV-------- 71
                          90       100
                  ....*....|....*....|....*
gi 578813549 1100 vtknwLSADTKEERDLWMQKLNQVL 1124
Cdd:cd13253    72 -----FRAESDDERNLWCSTLQAAI 91
PH_evt cd13265
Evectin Pleckstrin homology (PH) domain; There are 2 members of the evectin family (also ...
1020-1123 9.42e-03

Evectin Pleckstrin homology (PH) domain; There are 2 members of the evectin family (also called pleckstrin homology domain containing, family B): evt-1 (also called PLEKHB1) and evt-2 (also called PLEKHB2). evt-1 is specific to the nervous system, where it is expressed in photoreceptors and myelinating glia. evt-2 is widely expressed in both neural and nonneural tissues. Evectins possess a single N-terminal PH domain and a C-terminal hydrophobic region. evt-1 is thought to function as a mediator of post-Golgi trafficking in cells that produce large membrane-rich organelles. It is a candidate gene for the inherited human retinopathy autosomal dominant familial exudative vitreoretinopathy and a susceptibility gene for multiple sclerosis. evt-2 is essential for retrograde endosomal membrane transport from the plasma membrane (PM) to the Golgi. Two membrane trafficking pathways pass through recycling endosomes: a recycling pathway and a retrograde pathway that links the PM to the Golgi/ER. Its PH domain that is unique in that it specifically recognizes phosphatidylserine (PS), but not polyphosphoinositides. PS is an anionic phospholipid class in eukaryotic biomembranes, is highly enriched in the PM, and plays key roles in various physiological processes such as the coagulation cascade, recruitment and activation of signaling molecules, and clearance of apoptotic cells. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. 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: 270085  Cd Length: 108  Bit Score: 36.90  E-value: 9.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578813549 1020 WHRRWCVLSGN-CISYWtypDDEKRKNPIGRINL-ANCtsRQIEPANREfcarRNtfelitVRPQREDDRETLVS-QCRD 1096
Cdd:cd13265    19 WKKNWFVLYGDgNLVYY---EDETRREVEGRINMpREC--RNIRVGLEC----RD------VQPPEGRSRDCLLQiVLRD 83
                          90       100
                  ....*....|....*....|....*...
gi 578813549 1097 tlcvTKNW-LSADTKEERDLWMQKLNQV 1123
Cdd:cd13265    84 ----GSTLfLCAESADDALAWKLALQDA 107
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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