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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475765  30 LTFNDMKNVPEAFKGTKKGTVYLTPYRVIFLS-KGKDAMQSFMMPFYLMKDCEIKQPVFGANYIKGTVKAEAGGGWEGSA 108
Cdd:cd13214    1 VESVKGKGAPPFFKGSKKGTIYLTNQRLIFVSsKPTDNFQSFSMPLLNIRDVKFEQPVFGANYLKGKVKPVPGGGWPGEA 80

                         90       100
                 ....*....|....*....|...
gi 384475765 109 SYKLTFTAGGAIEFGQRMLQVAS 131
Cdd:cd13214   81 EFKLTFKDGGAIEFGQAFLRLAE 103

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475765  30 LTFNDMKNVPEAFKGTKKGTVYLTPYRVIFLS-KGKDAMQSFMMPFYLMKDCEIKQPVFGANYIKGTVKAEAGGGWEGSA 108
Cdd:cd13214    1 VESVKGKGAPPFFKGSKKGTIYLTNQRLIFVSsKPTDNFQSFSMPLLNIRDVKFEQPVFGANYLKGKVKPVPGGGWPGEA 80

                         90       100
                 ....*....|....*....|...
gi 384475765 109 SYKLTFTAGGAIEFGQRMLQVAS 131
Cdd:cd13214   81 EFKLTFKDGGAIEFGQAFLRLAE 103

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475765  30 LTFNDMKNVPEAFKGTKKGTVYLTPYRVIFLS-KGKDAMQSFMMPFYLMKDCEIKQPVFGANYIKGTVKAEAGGGWEGSA 108
Cdd:cd13214    1 VESVKGKGAPPFFKGSKKGTIYLTNQRLIFVSsKPTDNFQSFSMPLLNIRDVKFEQPVFGANYLKGKVKPVPGGGWPGEA 80

                         90       100
                 ....*....|....*....|...
gi 384475765 109 SYKLTFTAGGAIEFGQRMLQVAS 131
Cdd:cd13214   81 EFKLTFKDGGAIEFGQAFLRLAE 103

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475765  34 DMKNVPEAFKGTKK------GTVYLTPYRVIFLSKGKDAMQSFMMPFYLMKDCEIKQPV-FGANYIKGTVKAeagggweg 106
Cdd:cd10570    1 IEKLGVRFCCALRPrklpleGTLYLSTYRLIFSSKADGDETKLVIPLVDITDVEKIAGAsFLPSGLIITCKD-------- 72

                         90       100
                 ....*....|....*....|...
gi 384475765 107 SASYKLTFTagGAIEFGQRMLQV 129
Cdd:cd10570   73 FRTIKFSFD--SEDEAVKVIARV 93