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SOCS5_BOVIN
ID   SOCS5_BOVIN             Reviewed;         536 AA.
AC   Q29RN6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Suppressor of cytokine signaling 5;
DE            Short=SOCS-5;
GN   Name=SOCS5;
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 [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-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. May be a
CC       substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-
CC       SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates
CC       the ubiquitination and subsequent proteasomal degradation of target
CC       proteins. Inhibits for instance EGF signaling by mediating the
CC       degradation of the EGF receptor/EGFR. Involved in the regulation of T-
CC       helper cell differentiation by inhibiting of the IL4 signaling pathway
CC       which promotes differentiation into the Th2 phenotype. Can also
CC       partially inhibit IL6 and LIF signaling (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with EGFR. Interacts with ELOB and ELOC; mediates
CC       EGFR ubiquitination and degradation. Interacts with IL4R; inhibits IL4
CC       signaling (By similarity). {ECO:0000250}.
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: Phosphorylated. Phosphorylation is induced by EGF (By similarity).
CC       {ECO:0000250}.
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DR   EMBL; BC114096; AAI14097.1; -; mRNA.
DR   RefSeq; NP_001039647.1; NM_001046182.1.
DR   AlphaFoldDB; Q29RN6; -.
DR   BMRB; Q29RN6; -.
DR   SMR; Q29RN6; -.
DR   STRING; 9913.ENSBTAP00000011826; -.
DR   PaxDb; Q29RN6; -.
DR   PRIDE; Q29RN6; -.
DR   GeneID; 514773; -.
DR   KEGG; bta:514773; -.
DR   CTD; 9655; -.
DR   eggNOG; KOG4566; Eukaryota.
DR   InParanoid; Q29RN6; -.
DR   OrthoDB; 722019at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; ISS:UniProtKB.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEA:InterPro.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   CDD; cd03739; SOCS_SOCS5; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR022252; SOCS4/SOCS5_dom.
DR   InterPro; IPR028420; SOCS5.
DR   InterPro; IPR037343; SOCS5_SOCS.
DR   InterPro; IPR001496; SOCS_box.
DR   InterPro; IPR036036; SOCS_box-like_dom_sf.
DR   PANTHER; PTHR10155:SF15; PTHR10155:SF15; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF12610; SOCS; 1.
DR   Pfam; PF07525; SOCS_box; 1.
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; Reference proteome; SH2 domain;
KW   Signal transduction inhibitor; Ubl conjugation pathway.
FT   CHAIN           1..536
FT                   /note="Suppressor of cytokine signaling 5"
FT                   /id="PRO_0000244382"
FT   DOMAIN          381..476
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          471..520
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT   REGION          1..50
FT                   /note="Required for interaction with IL4R"
FT                   /evidence="ECO:0000250"
FT   REGION          115..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   536 AA;  61172 MW;  64AEAFB80EE6BB71 CRC64;
     MDKVGKMWNN FKYRCQNLFG HEGGSRSENV DMNSNRCLSV KKKNISLGDS APQQQSSPLR
     ENVALQLGLS PSKNSSRRNQ NCAAEIPQIV EISIEKDNDS CVTPGTRLAR RDSYSRHAPW
     GGKKKHSCST KTQSSLDTDK KFGRTRSGLQ RRERRYGVSS VHDMDSVSSR TVGSRSLRQR
     LQDTVGLCFP MRTYSKQSKP LFSNKRKIHL SELMLEKCPF PAGSDLAQKW HLIKQHTAPV
     SPHSTFFDTF DPSLVSTEDE EDRLRERRRL SIEEGVDPPP NAQIHTFEAT AQVNPLYKLG
     PKLAPGMTEV NGDSCAVPQA NCDSEEDTTT LCLQSRRQKQ RQVSGDSHAH VSRQGAWKVH
     TQIDYIHCLV PDLLQITGNP CYWGVMDRYE AEALLEGKPE GTFLLRDSAQ EDYLFSVSFR
     RYNRSLHARI EQWNHNFSFD AHDPCVFHSS TVTGLLEHYK DPSSCMFFEP LLTISLNRTF
     PFSLQYICRA VICRCTTYDG IDGLPLPSML QDFLKEYHYK QKVRVRWLER EPVKAK
 
 
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