SOCS2_BOVIN
ID SOCS2_BOVIN Reviewed; 198 AA.
AC Q861R0; Q1RMX0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Suppressor of cytokine signaling 2;
DE Short=SOCS-2;
GN Name=SOCS2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Smith T.P.L., Nonneman D.J., Farber C.R., Wong M.S., Bennett G.L.,
RA Harhay G.P., Snelling W.C., Rohrer G.A., Page B.T., Medrano J.F.;
RT "Comparative genome analysis of the murine high-growth locus in cattle and
RT swine.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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; AY183451; AAO45009.1; -; Genomic_DNA.
DR EMBL; AY183452; AAO45010.1; -; mRNA.
DR EMBL; BC114662; AAI14663.1; -; mRNA.
DR RefSeq; NP_803489.1; NM_177523.2.
DR RefSeq; XP_005206158.1; XM_005206101.3.
DR RefSeq; XP_005206159.1; XM_005206102.3.
DR RefSeq; XP_010803126.1; XM_010804824.2.
DR RefSeq; XP_015326402.1; XM_015470916.1.
DR AlphaFoldDB; Q861R0; -.
DR SMR; Q861R0; -.
DR STRING; 9913.ENSBTAP00000015929; -.
DR PaxDb; Q861R0; -.
DR PRIDE; Q861R0; -.
DR Ensembl; ENSBTAT00000015929; ENSBTAP00000015929; ENSBTAG00000012007.
DR Ensembl; ENSBTAT00000071024; ENSBTAP00000065158; ENSBTAG00000012007.
DR GeneID; 338437; -.
DR KEGG; bta:338437; -.
DR CTD; 8835; -.
DR VEuPathDB; HostDB:ENSBTAG00000012007; -.
DR VGNC; VGNC:35120; SOCS2.
DR eggNOG; KOG4566; Eukaryota.
DR GeneTree; ENSGT00940000157983; -.
DR HOGENOM; CLU_079452_4_0_1; -.
DR InParanoid; Q861R0; -.
DR OrthoDB; 1135696at2759; -.
DR TreeFam; TF321368; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000012007; Expressed in myometrium and 102 other tissues.
DR ExpressionAtlas; Q861R0; baseline and differential.
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:0005159; F:insulin-like growth factor receptor binding; IEA:InterPro.
DR GO; GO:0008269; F:JAK pathway signal transduction adaptor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0001558; P:regulation of cell growth; IEA:InterPro.
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_0000236239"
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 6..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 6..25
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"
FT CONFLICT 35
FT /note="R -> P (in Ref. 2; AAI14663)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 22214 MW; E1AA26CF2CE7485A CRC64;
MTLRCLESSG NGAEGAQSQW GTAGSAEEPS PEAARLAKAL RELSHTGWYW GSMTVNEAKE
KLKEAPEGTF LIRDSSHSDY LLTISVKTSA GPTNLRIEYQ DGKFRLDSII CVKSKLKQFD
SVVHLIDYYV QMCKDKRTGP EAPRNGTVHL YLTKPLYTSA PPLQHLCRLT INKCTSTVWG
LPLPTRLKDY LEEYKFQV
