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Conserved domains on  [gi|2462554275|ref|XP_054171609|]
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WW domain-binding protein 2 isoform X1 [Homo sapiens]

Protein Classification

GRAM domain-containing protein( domain architecture ID 10192315)

GRAM domain-containing protein is a membrane-associated protein; similar to Homo sapiens WW domain-binding protein 2, which acts as a transcriptional coactivator of estrogen and progesterone receptors (ESR1 and PGR) upon hormone activation

CATH:  2.30.29.30
Gene Ontology:  GO:0003713|GO:0031490
PubMed:  11050430|18201690
SCOP:  4000903

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-GRAM_WBP2 cd13214
WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 8-109 2.48e-52

WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; WBP2 plays a number of roles including: acting as a tyrosine kinase substrate, activation of estrogen receptor alpha (ERalpha)/progesterone receptor (PR) transcription, and playing a role in breast cancer. WBP2 contain a N-terminal PH-GRAM domain and a C-terminal WWbp domain. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The WWbp domain is characterized by several short PY and PT-like motifs of the PPPPY form and binds to WW domains. WW domains contain two highly conserved tryptophans that are spaced 20-23 residues apart. They bind proline-rich peptide motifs [AP]-P-P-[AP]-Y, and/or phosphoserine- phosphothreonine-containing motifs.


:

Pssm-ID: 275401  Cd Length: 103  Bit Score: 164.65  E-value: 2.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554275   8 LTFNDMKNVPEAFKGTKKGTVYLTPYRVIFLS-KGKDAMQSFMMPFYLMKDCEIKQPVFGANYIKGTVKAEAGGGWEGSA 86
Cdd:cd13214     1 VESVKGKGAPPFFKGSKKGTIYLTNQRLIFVSsKPTDNFQSFSMPLLNIRDVKFEQPVFGANYLKGKVKPVPGGGWPGEA 80

                          90       100
                  ....*....|....*....|...
gi 2462554275  87 SYKLTFTAGGAIEFGQRMLQVAS 109
Cdd:cd13214    81 EFKLTFKDGGAIEFGQAFLRLAE 103
 
Name Accession Description Interval E-value
PH-GRAM_WBP2 cd13214
WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 8-109 2.48e-52

WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; WBP2 plays a number of roles including: acting as a tyrosine kinase substrate, activation of estrogen receptor alpha (ERalpha)/progesterone receptor (PR) transcription, and playing a role in breast cancer. WBP2 contain a N-terminal PH-GRAM domain and a C-terminal WWbp domain. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The WWbp domain is characterized by several short PY and PT-like motifs of the PPPPY form and binds to WW domains. WW domains contain two highly conserved tryptophans that are spaced 20-23 residues apart. They bind proline-rich peptide motifs [AP]-P-P-[AP]-Y, and/or phosphoserine- phosphothreonine-containing motifs.


Pssm-ID: 275401  Cd Length: 103  Bit Score: 164.65  E-value: 2.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554275   8 LTFNDMKNVPEAFKGTKKGTVYLTPYRVIFLS-KGKDAMQSFMMPFYLMKDCEIKQPVFGANYIKGTVKAEAGGGWEGSA 86
Cdd:cd13214     1 VESVKGKGAPPFFKGSKKGTIYLTNQRLIFVSsKPTDNFQSFSMPLLNIRDVKFEQPVFGANYLKGKVKPVPGGGWPGEA 80

                          90       100
                  ....*....|....*....|...
gi 2462554275  87 SYKLTFTAGGAIEFGQRMLQVAS 109
Cdd:cd13214    81 EFKLTFKDGGAIEFGQAFLRLAE 103
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 21-110 1.10e-18

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 78.56  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554275  21 KGTKKGTVYLTPYRVIFLSKGKDAMQSFMMPFYLMKdcEIKQPVFGANYIKGTVKAEAGGGWEgsASYKLTFTAGGAIEF 100
Cdd:pfam02893  27 GGPVQGRLYLTNYRLCFRSLPKGWSTKVVIPLVDIE--EIEKLKGGANLFPNGIQVETGSNDK--FSFAGFVTRDEAIEF 102

                          90
                  ....*....|
gi 2462554275 101 GQRMLQVASQ 110
Cdd:pfam02893 103 ILALLKNAHP 112
 
Name Accession Description Interval E-value
PH-GRAM_WBP2 cd13214
WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ...
 8-109 2.48e-52

WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; WBP2 plays a number of roles including: acting as a tyrosine kinase substrate, activation of estrogen receptor alpha (ERalpha)/progesterone receptor (PR) transcription, and playing a role in breast cancer. WBP2 contain a N-terminal PH-GRAM domain and a C-terminal WWbp domain. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The WWbp domain is characterized by several short PY and PT-like motifs of the PPPPY form and binds to WW domains. WW domains contain two highly conserved tryptophans that are spaced 20-23 residues apart. They bind proline-rich peptide motifs [AP]-P-P-[AP]-Y, and/or phosphoserine- phosphothreonine-containing motifs.


Pssm-ID: 275401  Cd Length: 103  Bit Score: 164.65  E-value: 2.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554275   8 LTFNDMKNVPEAFKGTKKGTVYLTPYRVIFLS-KGKDAMQSFMMPFYLMKDCEIKQPVFGANYIKGTVKAEAGGGWEGSA 86
Cdd:cd13214     1 VESVKGKGAPPFFKGSKKGTIYLTNQRLIFVSsKPTDNFQSFSMPLLNIRDVKFEQPVFGANYLKGKVKPVPGGGWPGEA 80

                          90       100
                  ....*....|....*....|...
gi 2462554275  87 SYKLTFTAGGAIEFGQRMLQVAS 109
Cdd:cd13214    81 EFKLTFKDGGAIEFGQAFLRLAE 103
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 21-110 1.10e-18

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 78.56  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554275  21 KGTKKGTVYLTPYRVIFLSKGKDAMQSFMMPFYLMKdcEIKQPVFGANYIKGTVKAEAGGGWEgsASYKLTFTAGGAIEF 100
Cdd:pfam02893  27 GGPVQGRLYLTNYRLCFRSLPKGWSTKVVIPLVDIE--EIEKLKGGANLFPNGIQVETGSNDK--FSFAGFVTRDEAIEF 102

                          90
                  ....*....|
gi 2462554275 101 GQRMLQVASQ 110
Cdd:pfam02893 103 ILALLKNAHP 112
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 12-107 1.28e-11

Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275393  Cd Length: 94  Bit Score: 59.32  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462554275  12 DMKNVPEAFKGTKK------GTVYLTPYRVIFLSKGKDAMQSFMMPFYLMKDCEIKQPV-FGANYIKGTVKAeagggweg 84
Cdd:cd10570     1 IEKLGVRFCCALRPrklpleGTLYLSTYRLIFSSKADGDETKLVIPLVDITDVEKIAGAsFLPSGLIITCKD-------- 72

                          90       100
                  ....*....|....*....|...
gi 2462554275  85 SASYKLTFTagGAIEFGQRMLQV 107
Cdd:cd10570    73 FRTIKFSFD--SEDEAVKVIARV 93
 
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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