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signal transducing adapter molecule 2; STAM-2; Hrs-binding protein (STAM2, HBP)
Function:
- role in intracellular signal transduction mediated by cytokines & growth factors
- upon IL-2 & GM-CSL stimulation, plays a role in signaling leading to DNA synthesis & MYC induction
- may also play a role in T-cell development
- role in down-regulation of receptor tyrosine kinase via multivesicular body when complexed with HGS (ESCRT-0 complex)
- phosphorylated in response to IL-2, GM-CSF, EGF & PDGF
- component of the ESCRT-0 complex
- interacts with JAK2 & JAK3
- interacts with ubiquitinated proteins & the deubiquitinating enzyme USP8/UBPY (putative)
- interacts (via the via the PxVxL motif) with CBX5
- interacts with VPS37C
- interacts with ubiquitin
Structure:
- the VHS & UIM domains mediate the interaction with ubiquitinated proteins
- the SH3 domain mediates the interaction with USP8
- contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains
- this motif requires additional residues -7, -6, +4 & +5 of the central Val which contact the chromoshadow domain
- belongs to the STAM family
- contains 1 ITAM domain
- contains 1 SH3 domain
- contains 1 UIM (ubiquitin-interacting motif) repeat
- contains 1 VHS domain
Compartment:
- cytoplasm (putative)
- early endosome membrane
- peripheral membrane, cytoplasmic side
Alternative splicing: named isoforms=2
Expression: ubiquitously expressed
General
phosphoprotein
Properties
SIZE: entity length = 525 aa
MW = 58 kD
COMPARTMENT: cytoplasm
MOTIF: VHS domain {16-144}
MOTIF: PxVxL {54-67}
UIM {165-184}
Tyr phosphorylation site {Y192}
src homology 3 [SH3] domain
SITE: 202-261
MOTIF: USP8 interaction {219-220}
Tyr phosphorylation site {Y291}
HGS interaction {334-368}
ITAM {360-377}
MOTIF: Tyr phosphorylation site {Y371}
Tyr phosphorylation site {Y374}
Database Correlations
OMIM 606244
UniProt O75886
PFAM correlations
Entrez Gene 10254
Kegg hsa:10254
References
UniProt :accession O75886
Component-of
ESCRT-0 complex; STAM1/STAM2-HGS complex