SOCS2
entrez
8835
canonical
uniprot
O14508
canonical
ensembl
ENSG00000120833
resolver
ensp
ENSP00000339428
resolver
ensp
ENSP00000442898
resolver
ensp
ENSP00000447161
resolver
ensp
ENSP00000448815
resolver
ensp
ENSP00000449227
resolver
ensp
ENSP00000481249
resolver
ensp
ENSP00000532949
resolver
ensp
ENSP00000532950
resolver
ensp
ENSP00000532951
resolver
ensp
ENSP00000532952
resolver
ensp
ENSP00000532953
resolver
ensp
ENSP00000592493
resolver
ensp
ENSP00000592494
resolver
ensp
ENSP00000592495
resolver
ensp
ENSP00000592496
resolver
ensp
ENSP00000592497
resolver
ensp
ENSP00000592498
resolver
ensp
ENSP00000638902
resolver
ensp
ENSP00000788189
resolver
enst
ENST00000340600
resolver
enst
ENST00000536696
resolver
enst
ENST00000549122
resolver
enst
ENST00000549206
resolver
enst
ENST00000551556
resolver
enst
ENST00000622746
resolver
enst
ENST00000862890
resolver
enst
ENST00000862891
resolver
enst
ENST00000862892
resolver
enst
ENST00000862893
resolver
enst
ENST00000862894
resolver
enst
ENST00000922434
resolver
enst
ENST00000922435
resolver
enst
ENST00000922436
resolver
enst
ENST00000922437
resolver
enst
ENST00000922438
resolver
enst
ENST00000922439
resolver
enst
ENST00000968843
resolver
genesymbol
SOCS2
resolver
genesymbol_syn
CIS2
resolver
genesymbol_syn
SSI2
resolver
genesymbol_syn
STATI2
resolver
hgnc
HGNC:19382
resolver
uniprot
A8K3D1
resolver
uniprot
O14542
resolver
uniprot
O95102
resolver
uniprot
Q9UKS5
resolver
uniprot_entry
SOCS2_HUMAN
resolver
uniprot_sec
A8K3D1
resolver
uniprot_sec
O14542
resolver
uniprot_sec
O95102
resolver
uniprot_sec
Q9UKS5
resolver
activity_regulation
ACTIVITY REGULATION: Substrate-binding is prevented by the covalent inhibitor MN551 that cross-links with Cys-111 (PubMed:37816714). Also inhibited by a MN551 derivative, MN714, which contains a pivaloyloxymethyl that allows cell permeability (PubMed:37816714). {ECO:0000269|PubMed:37816714}.
uniprot
proteins
amino_acid_sequence
MTLRCLEPSGNGGEGTRSQWGTAGSAEEPSPQAARLAKALRELGQTGWYWGSMTVNEAKEKLKEAPEGTFLIRDSSHSDYLLTISVKTSAGPTNLRIEYQDGKFRLDSIICVKSKLKQFDSVVHLIDYYVQMCKDKRTGPEAPRNGTVHLYLTKPLYTSAPSLQHLCRLTINKCTGAIWGLPLPTRLKDYLEEYKFQV
uniprot
proteins
function
FUNCTION: Substrate-recognition component of a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex, also named CRL5 complex), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as EPOR and GHR (PubMed:11781573, PubMed:21980433, PubMed:25505247, PubMed:31182716, PubMed:34857742). Specifically recognizes and binds phosphorylated proteins via its SH2 domain, promoting their ubiquitination (PubMed:21980433, PubMed:25505247, PubMed:31182716, PubMed:34857742, PubMed:37816714). The ECS(SOCS2) complex acts as a key regulator of growth hormone receptor (GHR) levels by mediating ubiquitination and degradation of GHR, following GHR phosphorylation by JAK2 (PubMed:21980433, PubMed:25505247, PubMed:34857742). The ECS(SOCS2) also catalyzes ubiquitination and degradation of JAK2-phosphorylated EPOR (PubMed:11781573). {ECO:0000269|PubMed:11781573, ECO:0000269|PubMed:21980433, ECO:0000269|PubMed:25505247, ECO:0000269|PubMed:31182716, ECO:0000269|PubMed:34857742, ECO:0000269|PubMed:37816714}.
uniprot
proteins
mass_dalton
22172
uniprot
proteins
mutagenesis
MUTAGEN 73; /note="R->E: Impaired ability to mediate ubiquitination of GHR."; /evidence="ECO:0000269|PubMed:21980433"; MUTAGEN 87; /note="K->R: No effect on protein half-life."; /evidence="ECO:0000269|PubMed:31578312"; MUTAGEN 154; /note="K->R: No effect on protein half-life."; /evidence="ECO:0000269|PubMed:31578312"; MUTAGEN 163; /note="L->P: Abolished interaction with ELOB and ELOC, preventing formation of the ECS(SOCS2) complex."; /evidence="ECO:0000269|PubMed:21980433"; MUTAGEN 167; /note="C->F: Abolished interaction with ELOB and ELOC, preventing formation of the ECS(SOCS2) complex."; /evidence="ECO:0000269|PubMed:21980433"; MUTAGEN 173; /note="K->R: Increased protein half-life."; /evidence="ECO:0000269|PubMed:31578312
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:11781573, ECO:0000269|PubMed:21980433, ECO:0000269|PubMed:25505247, ECO:0000269|PubMed:31182716, ECO:0000269|PubMed:34857742}.
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated; mediated by AREL1 and leading to its subsequent proteasomal degradation (PubMed:31578312). Ubiquitination is dependent on its phosphorylation at Ser-52, by PKC (PubMed:31578312). Ubiquitination is stimulated by LPS (By similarity). {ECO:0000250|UniProtKB:O35717, ECO:0000269|PubMed:31578312}.; PTM: Phosphorylation at Ser-52 by PKC facilitates its ubiquitination and proteasomal degradation. {ECO:0000269|PubMed:31578312}.
uniprot
proteins
pubmed
10512686
uniprot
proteins
pubmed
11781573
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16675548
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21980433
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23401859
uniprot
proteins
pubmed
23897481
uniprot
proteins
pubmed
25505247
uniprot
proteins
pubmed
31182716
uniprot
proteins
pubmed
31578312
uniprot
proteins
pubmed
34857742
uniprot
proteins
pubmed
37816714
uniprot
proteins
pubmed
9266833
uniprot
proteins
pubmed
9344848
uniprot
proteins
pubmed
9727029
uniprot
proteins
sequence_length
198
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9727029}.
uniprot
proteins