WW domain binding protein 2, isoform CRA_a [Homo sapiens]
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
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 ... |
30-131 | 2.75e-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: 165.43 E-value: 2.75e-52
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Name | Accession | Description | Interval | E-value | |||
PH-GRAM_WBP2 | cd13214 | WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ... |
30-131 | 2.75e-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: 165.43 E-value: 2.75e-52
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GRAM | pfam02893 | GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ... |
43-132 | 1.67e-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: 1.67e-18
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Name | Accession | Description | Interval | E-value | |||
PH-GRAM_WBP2 | cd13214 | WW binding protein 2 (WB2) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase ... |
30-131 | 2.75e-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: 165.43 E-value: 2.75e-52
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GRAM | pfam02893 | GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ... |
43-132 | 1.67e-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: 1.67e-18
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PH-GRAM | cd10570 | Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ... |
34-129 | 1.67e-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: 1.67e-11
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Blast search parameters | ||||
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