SOCS2_RAT
ID SOCS2_RAT Reviewed; 198 AA.
AC O88582;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Suppressor of cytokine signaling 2;
DE Short=SOCS-2;
DE AltName: Full=Cytokine-inducible SH2 protein 2;
GN Name=Socs2; Synonyms=Cish2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=10579313; DOI=10.1210/endo.140.12.7212;
RA Mao Y., Ling P.R., Fitzgibbons T.P., McCowen K.C., Frick G.P.,
RA Bistrian B.R., Smith R.J.;
RT "Endotoxin-induced inhibition of growth hormone receptor signaling in rat
RT liver in vivo.";
RL Endocrinology 140:5505-5515(1999).
CC -!- FUNCTION: SOCS family proteins form part of a classical negative
CC feedback system that regulates cytokine signal transduction. SOCS2
CC appears to be a negative regulator in the growth hormone/IGF1 signaling
CC pathway. Probable substrate recognition component of a SCF-like ECS
CC (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which
CC mediates the ubiquitination and subsequent proteasomal degradation of
CC target proteins (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with IGF1R (By similarity). Associates with the
CC Elongin BC complex (By similarity). Interacts with AREL1 and PRKCA (By
CC similarity). Interacts with DCUN1D1 (By similarity).
CC {ECO:0000250|UniProtKB:O14508, ECO:0000250|UniProtKB:O35717}.
CC -!- DOMAIN: The SOCS box domain mediates the interaction with the Elongin
CC BC complex, an adapter module in different E3 ubiquitin ligase
CC complexes. {ECO:0000250}.
CC -!- PTM: Ubiquitinated; mediated by AREL1 and leading to its subsequent
CC proteasomal degradation. Ubiquitination is dependent on phosphorylation
CC at Ser-52, by PKC and is stimulated by LPS.
CC {ECO:0000250|UniProtKB:O35717}.
CC -!- PTM: Phosphorylation at Ser-52 by PKC facilitates its ubiquitination
CC and proteosomal degradation. {ECO:0000250|UniProtKB:O35717}.
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DR EMBL; AF075382; AAC26222.1; -; mRNA.
DR RefSeq; NP_478115.1; NM_058208.1.
DR RefSeq; XP_017450626.1; XM_017595137.1.
DR AlphaFoldDB; O88582; -.
DR SMR; O88582; -.
DR BioGRID; 250034; 4.
DR STRING; 10116.ENSRNOP00000011948; -.
DR PaxDb; O88582; -.
DR GeneID; 84607; -.
DR KEGG; rno:84607; -.
DR UCSC; RGD:69273; rat.
DR CTD; 8835; -.
DR RGD; 69273; Socs2.
DR eggNOG; KOG4566; Eukaryota.
DR HOGENOM; CLU_079452_4_0_1; -.
DR InParanoid; O88582; -.
DR OrthoDB; 1135696at2759; -.
DR PhylomeDB; O88582; -.
DR TreeFam; TF321368; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-9706369; Negative regulation of FLT3.
DR UniPathway; UPA00143; -.
DR PRO; PR:O88582; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; O88582; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IBA:GO_Central.
DR GO; GO:0005131; F:growth hormone receptor binding; ISO:RGD.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0008269; F:JAK pathway signal transduction adaptor activity; IEA:InterPro.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0032870; P:cellular response to hormone stimulus; ISO:RGD.
DR GO; GO:0060396; P:growth hormone receptor signaling pathway; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0007595; P:lactation; ISO:RGD.
DR GO; GO:0060749; P:mammary gland alveolus development; ISO:RGD.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; ISO:RGD.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0001558; P:regulation of cell growth; IEA:InterPro.
DR GO; GO:0040014; P:regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; ISO:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR CDD; cd10383; SH2_SOCS2; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR028410; SOCS2.
DR InterPro; IPR035862; SOCS2_SH2.
DR InterPro; IPR001496; SOCS_box.
DR InterPro; IPR036036; SOCS_box-like_dom_sf.
DR PANTHER; PTHR10155:SF7; PTHR10155:SF7; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF07525; SOCS_box; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00253; SOCS; 1.
DR SMART; SM00969; SOCS_box; 1.
DR SUPFAM; SSF158235; SSF158235; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50225; SOCS; 1.
PE 2: Evidence at transcript level;
KW Growth regulation; Isopeptide bond; Phosphoprotein; Reference proteome;
KW SH2 domain; Signal transduction inhibitor; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..198
FT /note="Suppressor of cytokine signaling 2"
FT /id="PRO_0000181240"
FT DOMAIN 48..156
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 151..197
FT /note="SOCS box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT REGION 1..75
FT /note="Interaction with AREL1"
FT /evidence="ECO:0000250|UniProtKB:O14508"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14508"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14508"
FT CROSSLNK 173
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O14508"
SQ SEQUENCE 198 AA; 22380 MW; DD6160D3899122E6 CRC64;
MTLRCLEPSG NGADRTRSQW GTAGSPEDQS PEAARLAKAL RELSQTGWYW GSMTVNEAKE
KLKEAPEGTF LIRDSSHSDY LLTISVKTSA GPTNLRIEYQ DGKFRLDSII CVKSKLKQFD
SVVHLIDYYV QMCKDKRTGP EAPRNGTVHL YLTKPLYTSA PTLQHFCRLS INKCTGTIRG
LPLPTRLKDY LEEYKFQV
