Function and Biology

N-TERMINAL SH3 DOMAIN OF CMS (CD2AP HUMAN HOMOLOG) BOUND TO CBL-B PEPTIDE

Source organism: Homo sapiens
Biochemical function: not assigned
Biological process: not assigned
Cellular component: not assigned

EC 2.3.2.27: RING-type E3 ubiquitin transferase

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Systematic name:
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein]-L-lysine ubiquitin transferase (isopeptide bond-forming; RING-type)
Alternative Name(s):
  • RING E3 ligase
  • Ubiquitin transferase RING E3

GO terms

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Sequence family

Pfam Protein family (Pfam)
PF14604
Domain description: Variant SH3 domain
Occurring in:
  1. CD2-associated protein
1 copy of Pfam domain PF14604 (Variant SH3 domain) in CD2-associated protein in PDB 2j6f.

InterPro InterPro annotations
IPR001452
Domain description: SH3 domain
Occurring in:
  1. CD2-associated protein
IPR035775
Domain description: CD2-associated protein, first SH3 domain
Occurring in:
  1. CD2-associated protein
IPR036028
Domain description: SH3-like domain superfamily
Occurring in:
  1. CD2-associated protein
IPR028445
Domain description: CD2-associated protein
Occurring in:
  1. CD2-associated protein

Structure domain

CATH CATH domain
2.30.30.40
Class: Mainly Beta
Architecture: Roll
Topology: SH3 type barrels.
Homology: SH3 Domains
Occurring in:
  1. CD2-associated protein
1 copy of CATH domain 2.30.30.40 (SH3 type barrels.) in CD2-associated protein in PDB 2j6f.