Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
BSCOP2B SuperfamilyEF-hand 8039549 3001983 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyN-terminal domain of cbl (N-cbl) 8039550 3000373 SCOP2B (2022-06-29)
BSCOP2B SuperfamilySH2 domain 8039553 3000197 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BCbl_N2e3bumB1 A: alpha arraysX: EF-handH: EF-hand-relatedT: EF-handF: Cbl_N2ECOD (1.6)
BCbl_Ne3bumB2 A: alpha bundlesX: N-cbl likeH: N-terminal domain of cbl (N-cbl) (From Topology)T: N-terminal domain of cbl (N-cbl)F: Cbl_NECOD (1.6)
BCbl_N3e3bumB3 A: a+b two layersX: SH2 (From Topology)H: SH2 (From Topology)T: SH2F: Cbl_N3ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
B1.20.930.20 Mainly Alpha Up-down Bundle Transcription Elongation Factor S-II Chain ACATH (4.3.0)
B1.10.238.10 Mainly Alpha Orthogonal Bundle Recoverin domain 1CATH (4.3.0)
B3.30.505.10 Alpha Beta 2-Layer Sandwich SHC Adaptor Protein SH2 domainCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF02262CBL proto-oncogene N-terminal domain 1 (Cbl_N)CBL proto-oncogene N-terminal domain 1Cbl is an adaptor protein that binds EGF receptors (or other tyrosine kinases) and SH3 domains, functioning as a negative regulator of many signaling pathways. The N-terminal domain is evolutionarily conserved, and is known to bind to phosphorylated ...Cbl is an adaptor protein that binds EGF receptors (or other tyrosine kinases) and SH3 domains, functioning as a negative regulator of many signaling pathways. The N-terminal domain is evolutionarily conserved, and is known to bind to phosphorylated tyrosine residues. Cbl_N is comprised of 3 structural domains of which this is the first - a four helix bundle.
Domain
PF02762CBL proto-oncogene N-terminus, SH2-like domain (Cbl_N3)CBL proto-oncogene N-terminus, SH2-like domainCbl is an adaptor protein that binds EGF receptors (or other tyrosine kinases) and SH3 domains, functioning as a negative regulator of many signaling pathways. The N-terminal domain is evolutionarily conserved, and is known to bind to phosphorylated ...Cbl is an adaptor protein that binds EGF receptors (or other tyrosine kinases) and SH3 domains, functioning as a negative regulator of many signaling pathways. The N-terminal domain is evolutionarily conserved, and is known to bind to phosphorylated tyrosine residues. The so called N-terminal domain is actually 3 structural domains, of which this is the C-terminal SH2 domain.
Domain
PF02761CBL proto-oncogene N-terminus, EF hand-like domain (Cbl_N2)CBL proto-oncogene N-terminus, EF hand-like domainCbl is an adaptor protein that binds EGF receptors (or other tyrosine kinases) and SH3 domains, functioning as a negative regulator of many signaling pathways. The N-terminal domain is evolutionarily conserved, and is known to bind to phosphorylated ...Cbl is an adaptor protein that binds EGF receptors (or other tyrosine kinases) and SH3 domains, functioning as a negative regulator of many signaling pathways. The N-terminal domain is evolutionarily conserved, and is known to bind to phosphorylated tyrosine residues. The so called N-terminal domain is actually 3 structural domains, of which this is the central EF hand domain.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
Protein sprouty homolog 2
E3 ubiquitin-protein ligase CBL

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
PharosO43597
PharosP22681

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
PTR Parent Component: TYR

RESIDAA0039

PSI-MOD :  O4'-phospho-L-tyrosine MOD:00048