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Suppressor of cytokine signaling 5 (SOCS-5) (Cytokine-inducible SH2 protein 6) (CIS-6) (Cytokine-inducible SH2-containing protein 5)

 SOCS5_HUMAN             Reviewed;         536 AA.
O75159; Q53SD4; Q8IYZ4;
16-APR-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
22-NOV-2017, entry version 156.
RecName: Full=Suppressor of cytokine signaling 5;
Short=SOCS-5;
AltName: Full=Cytokine-inducible SH2 protein 6;
Short=CIS-6;
AltName: Full=Cytokine-inducible SH2-containing protein 5;
Name=SOCS5; Synonyms=CIS6, CISH5, CISH6, KIAA0671;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=10773671;
Magrangeas F., Apiou F., Denis S., Weidle U., Jacques Y.,
Minvielle S.;
"Cloning and expression of CIS6, chromosomal assignment to 3p22 and
2p21 by in situ hybridization.";
Cytogenet. Cell Genet. 88:78-81(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:169-176(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION IN EGFR DEGRADATION, INDUCTION BY EGF, PHOSPHORYLATION,
MUTAGENESIS OF ARG-406; LEU-484 AND CYS-488, AND INTERACTION WITH
EGFR; ELOB AND ELOC.
PubMed=15590694; DOI=10.1074/jbc.M408575200;
Kario E., Marmor M.D., Adamsky K., Citri A., Amit I., Amariglio N.,
Rechavi G., Yarden Y.;
"Suppressors of cytokine signaling 4 and 5 regulate epidermal growth
factor receptor signaling.";
J. Biol. Chem. 280:7038-7048(2005).
-!- FUNCTION: SOCS family proteins form part of a classical negative
feedback system that regulates cytokine signal transduction. May
be a substrate-recognition component of a SCF-like ECS (Elongin
BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex
which mediates the ubiquitination and subsequent proteasomal
degradation of target proteins. Inhibits for instance EGF
signaling by mediating the degradation of the EGF receptor/EGFR.
Involved in the regulation of T-helper cell differentiation by
inhibiting of the IL4 signaling pathway which promotes
differentiation into the Th2 phenotype. Can also partially inhibit
IL6 and LIF signaling. {ECO:0000269|PubMed:15590694}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with IL4R; inhibits IL4 signaling (By
similarity). Interacts with EGFR. Interacts with ELOB and ELOC;
mediates EGFR ubiquitination and degradation. {ECO:0000250,
ECO:0000269|PubMed:15590694}.
-!- INTERACTION:
P08581:MET; NbExp=2; IntAct=EBI-970130, EBI-1039152;
-!- INDUCTION: Up-regulated by EGF (at protein level).
{ECO:0000269|PubMed:15590694}.
-!- DOMAIN: The SOCS box domain mediates the interaction with the
Elongin BC complex, an adapter module in different E3 ubiquitin
ligase complexes.
-!- PTM: Phosphorylated. Phosphorylation is induced by EGF.
{ECO:0000269|PubMed:15590694}.
-!- SEQUENCE CAUTION:
Sequence=BAA31646.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF073958; AAD40484.1; -; mRNA.
EMBL; AB014571; BAA31646.2; ALT_INIT; mRNA.
EMBL; AL136896; CAB66830.1; -; mRNA.
EMBL; AK290194; BAF82883.1; -; mRNA.
EMBL; AC020604; AAY24289.1; -; Genomic_DNA.
EMBL; CH471053; EAX00236.1; -; Genomic_DNA.
EMBL; CH471053; EAX00237.1; -; Genomic_DNA.
EMBL; BC032862; AAH32862.1; -; mRNA.
CCDS; CCDS1830.1; -.
PIR; T46499; T46499.
RefSeq; NP_054730.1; NM_014011.4.
RefSeq; NP_659198.1; NM_144949.2.
UniGene; Hs.468426; -.
ProteinModelPortal; O75159; -.
SMR; O75159; -.
BioGrid; 115013; 10.
IntAct; O75159; 6.
MINT; MINT-2835826; -.
STRING; 9606.ENSP00000305133; -.
iPTMnet; O75159; -.
PhosphoSitePlus; O75159; -.
BioMuta; SOCS5; -.
EPD; O75159; -.
PaxDb; O75159; -.
PeptideAtlas; O75159; -.
PRIDE; O75159; -.
DNASU; 9655; -.
Ensembl; ENST00000306503; ENSP00000305133; ENSG00000171150.
Ensembl; ENST00000394861; ENSP00000378330; ENSG00000171150.
GeneID; 9655; -.
KEGG; hsa:9655; -.
UCSC; uc002rvf.4; human.
CTD; 9655; -.
DisGeNET; 9655; -.
EuPathDB; HostDB:ENSG00000171150.7; -.
GeneCards; SOCS5; -.
HGNC; HGNC:16852; SOCS5.
HPA; CAB025510; -.
HPA; HPA020884; -.
MIM; 607094; gene.
neXtProt; NX_O75159; -.
OpenTargets; ENSG00000171150; -.
PharmGKB; PA134884627; -.
eggNOG; KOG4566; Eukaryota.
eggNOG; ENOG4111V4J; LUCA.
GeneTree; ENSGT00760000119136; -.
HOGENOM; HOG000027791; -.
HOVERGEN; HBG054138; -.
InParanoid; O75159; -.
KO; K04698; -.
OMA; QVSGDSH; -.
OrthoDB; EOG091G0EQ0; -.
PhylomeDB; O75159; -.
TreeFam; TF321368; -.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-8951664; Neddylation.
SignaLink; O75159; -.
UniPathway; UPA00143; -.
GeneWiki; SOCS5; -.
GenomeRNAi; 9655; -.
PRO; PR:O75159; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000171150; -.
CleanEx; HS_SOCS5; -.
Genevisible; O75159; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:Ensembl.
GO; GO:0004860; F:protein kinase inhibitor activity; IBA:GO_Central.
GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
GO; GO:0016049; P:cell growth; NAS:UniProtKB.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0007259; P:JAK-STAT cascade; IEA:InterPro.
GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; IDA:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IBA:GO_Central.
GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IEA:Ensembl.
GO; GO:0009968; P:negative regulation of signal transduction; NAS:UniProtKB.
GO; GO:0045629; P:negative regulation of T-helper 2 cell differentiation; ISS:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; ISS:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0097699; P:vascular endothelial cell response to fluid shear stress; IEA:Ensembl.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR022252; SOCS4/SOCS5_dom.
InterPro; IPR028420; SOCS5.
InterPro; IPR001496; SOCS_box.
InterPro; IPR036036; SOCS_box-like_dom_sf.
PANTHER; PTHR44282:SF3; PTHR44282:SF3; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF12610; SOCS; 1.
Pfam; PF07525; SOCS_box; 1.
SMART; SM00252; SH2; 1.
SMART; SM00253; SOCS; 1.
SMART; SM00969; SOCS_box; 1.
SUPFAM; SSF158235; SSF158235; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50225; SOCS; 1.
1: Evidence at protein level;
Complete proteome; Growth regulation; Reference proteome; SH2 domain;
Signal transduction inhibitor; Ubl conjugation pathway.
CHAIN 1 536 Suppressor of cytokine signaling 5.
/FTId=PRO_0000181249.
DOMAIN 381 476 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 471 520 SOCS box. {ECO:0000255|PROSITE-
ProRule:PRU00194}.
REGION 1 50 Required for interaction with IL4R.
{ECO:0000250}.
MUTAGEN 406 406 R->K: Abrogates the ability to induce
EGFR degradation.
{ECO:0000269|PubMed:15590694}.
MUTAGEN 484 484 L->P: Abrogates the interaction with ELOB
and ELOC and the ability to suppress EGFR
signaling; when associated with F-488.
{ECO:0000269|PubMed:15590694}.
MUTAGEN 488 488 C->F: Abrogates the interaction with ELOB
and ELOC and the ability to suppress EGFR
signaling; when associated with P-484.
{ECO:0000269|PubMed:15590694}.
CONFLICT 478 478 R -> M (in Ref. 7; AAH32862).
{ECO:0000305}.
SEQUENCE 536 AA; 61246 MW; 0629CDCF2A97E9D8 CRC64;
MDKVGKMWNN FKYRCQNLFG HEGGSRSENV DMNSNRCLSV KEKNISIGDS TPQQQSSPLR
ENIALQLGLS PSKNSSRRNQ NCATEIPQIV EISIEKDNDS CVTPGTRLAR RDSYSRHAPW
GGKKKHSCST KTQSSLDADK KFGRTRSGLQ RRERRYGVSS VHDMDSVSSR TVGSRSLRQR
LQDTVGLCFP MRTYSKQSKP LFSNKRKIHL SELMLEKCPF PAGSDLAQKW HLIKQHTAPV
SPHSTFFDTF DPSLVSTEDE EDRLRERRRL SIEEGVDPPP NAQIHTFEAT AQVNPLYKLG
PKLAPGMTEI SGDSSAIPQA NCDSEEDTTT LCLQSRRQKQ RQISGDSHTH VSRQGAWKVH
TQIDYIHCLV PDLLQITGNP CYWGVMDRYE AEALLEGKPE GTFLLRDSAQ EDYLFSVSFR
RYNRSLHARI EQWNHNFSFD AHDPCVFHSS TVTGLLEHYK DPSSCMFFEP LLTISLNRTF
PFSLQYICRA VICRCTTYDG IDGLPLPSML QDFLKEYHYK QKVRVRWLER EPVKAK


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