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Suppressor of cytokine signaling 3 (SOCS-3) (Cytokine-inducible SH2 protein 3) (CIS-3) (Protein EF-10)

 SOCS3_MOUSE             Reviewed;         225 AA.
O35718; P97803; Q3U7X5;
16-APR-2002, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
16-OCT-2019, entry version 177.
RecName: Full=Suppressor of cytokine signaling 3;
Short=SOCS-3;
AltName: Full=Cytokine-inducible SH2 protein 3;
Short=CIS-3;
AltName: Full=Protein EF-10;
Name=Socs3; Synonyms=Cis3, Cish3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung, and Thymus;
PubMed=9202125; DOI=10.1038/43206;
Starr R., Willson T.A., Viney E.M., Murray L.J.L., Rayner J.R.,
Jenkins B.J., Gonda T.J., Alexander W.S., Metcalf D., Nicola N.A.,
Hilton D.J.;
"A family of cytokine-inducible inhibitors of signaling.";
Nature 387:917-921(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Le Provost F., Henninghausen L.;
"Murine SOCS3 gene structure.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Cerebellum, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; 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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
STRAIN=ICR X Swiss Webster;
PubMed=10359822; DOI=10.1073/pnas.96.12.6964;
Auernhammer C.J., Bousquet C., Melmed S.;
"Autoregulation of pituitary corticotroph SOCS-3 expression:
characterization of the murine SOCS-3 promoter.";
Proc. Natl. Acad. Sci. U.S.A. 96:6964-6969(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 221-225.
STRAIN=BALB/cJ;
PubMed=9032278; DOI=10.1128/mcb.17.3.1503;
Fu X., Kamps M.P.;
"E2a-Pbx1 induces aberrant expression of tissue-specific and
developmentally regulated genes when expressed in NIH 3T3
fibroblasts.";
Mol. Cell. Biol. 17:1503-1512(1997).
[7]
FUNCTION IN LIF AND IL6 SIGNALING.
PubMed=9889194; DOI=10.1093/emboj/18.2.375;
Nicholson S.E., Willson T.A., Farley A., Starr R., Zhang J.-G.,
Baca M., Alexander W.S., Metcalf D., Hilton D.J., Nicola N.A.;
"Mutational analyses of the SOCS proteins suggest a dual domain
requirement but distinct mechanisms for inhibition of LIF and IL-6
signal transduction.";
EMBO J. 18:375-385(1999).
[8]
FUNCTION IN INHIBITION OF INSR KINASE ACTIVITY, AND INTERACTION WITH
INSR.
PubMed=10821852; DOI=10.1074/jbc.275.21.15985;
Emanuelli B., Peraldi P., Filloux C., Sawka-Verhelle D., Hilton D.,
Van Obberghen E.;
"SOCS-3 is an insulin-induced negative regulator of insulin
signaling.";
J. Biol. Chem. 275:15985-15991(2000).
[9]
INTERACTION WITH EPOR AND JAK2, AND MUTAGENESIS OF LEU-22; PHE-25;
GLY-45 AND ARG-71.
PubMed=10882725; DOI=10.1074/jbc.m003456200;
Sasaki A., Yasukawa H., Shouda T., Kitamura T., Dikic I.,
Yoshimura A.;
"CIS3/SOCS-3 suppresses erythropoietin (EPO) signaling by binding the
EPO receptor and JAK2.";
J. Biol. Chem. 275:29338-29347(2000).
[10]
TISSUE SPECIFICITY.
PubMed=12242343; DOI=10.1073/pnas.202477099;
Seki Y., Hayashi K., Matsumoto A., Seki N., Tsukada J., Ransom J.,
Naka T., Kishimoto T., Yoshimura A., Kubo M.;
"Expression of the suppressor of cytokine signaling-5 (SOCS5)
negatively regulates IL-4-dependent STAT6 activation and Th2
differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 99:13003-13008(2002).
[11]
FUNCTION IN ERYTHROPOIESIS.
PubMed=10490101; DOI=10.1016/s0092-8674(00)80049-5;
Marine J.-C., McKay C., Wang D., Topham D.J., Parganas E.,
Nakajima H., Pendeville H., Yasukawa H., Sasaki A., Yoshimura A.,
Ihle J.N.;
"SOCS3 is essential in the regulation of fetal liver erythropoiesis.";
Cell 98:617-627(1999).
[12]
ROLE IN IL-6 SIGNALING.
PubMed=12754505; DOI=10.1038/ni931;
Croker B.A., Krebs D.L., Zhang J.-G., Wormald S., Willson T.A.,
Stanley E.G., Robb L., Greenhalgh C.J., Foerster I., Clausen B.E.,
Nicola N.A., Metcalf D., Hilton D.J., Roberts A.W., Alexander W.S.;
"SOCS3 negatively regulates IL-6 signaling in vivo.";
Nat. Immunol. 4:540-545(2003).
[13]
ROLE IN ALLERGIC RESPONSE, AND INDUCTION BY IL-4.
PubMed=12847520; DOI=10.1038/nm896;
Seki Y., Inoue H., Nagata N., Hayashi K., Fukuyama S., Matsumoto K.,
Komine O., Hamano S., Himeno K., Inagaki-Ohara K., Cacalano N.,
O'Garra A., Oshida T., Saito H., Johnston J.A., Yoshimura A., Kubo M.;
"SOCS-3 regulates onset and maintenance of T(H)2-mediated allergic
responses.";
Nat. Med. 9:1047-1054(2003).
[14]
INTERACTION WITH BCL10.
PubMed=15213237; DOI=10.1074/jbc.m400241200;
Liu Y., Dong W., Chen L., Xiang R., Xiao H., De G., Wang Z., Qi Y.;
"BCL10 mediates lipopolysaccharide/toll-like receptor-4 signaling
through interaction with Pellino2.";
J. Biol. Chem. 279:37436-37444(2004).
[15]
INTERACTION WITH NOD2.
PubMed=23019338; DOI=10.1074/jbc.m112.410027;
Lee K.H., Biswas A., Liu Y.J., Kobayashi K.S.;
"Proteasomal degradation of Nod2 protein mediates tolerance to
bacterial cell wall components.";
J. Biol. Chem. 287:39800-39811(2012).
[16]
STRUCTURE BY NMR OF 22-185.
PubMed=16630890; DOI=10.1016/j.molcel.2006.03.024;
Babon J.J., McManus E.J., Yao S., DeSouza D.P., Mielke L.A.,
Sprigg N.S., Willson T.A., Hilton D.J., Nicola N.A., Baca M.,
Nicholson S.E., Norton R.S.;
"The structure of SOCS3 reveals the basis of the extended SH2 domain
function and identifies an unstructured insertion that regulates
stability.";
Mol. Cell 22:205-216(2006).
[17]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 15-185 IN COMPLEX WITH
PHOSPHORYLATED IL6ST.
PubMed=16905102; DOI=10.1016/j.str.2006.06.011;
Bergamin E., Wu J., Hubbard S.R.;
"Structural basis for phosphotyrosine recognition by suppressor of
cytokine signaling-3.";
Structure 14:1285-1292(2006).
-!- FUNCTION: SOCS family proteins form part of a classical negative
feedback system that regulates cytokine signal transduction. SOCS3
is involved in negative regulation of cytokines that signal
through the JAK/STAT pathway. Inhibits cytokine signal
transduction by binding to tyrosine kinase receptors including
gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin
receptors. Binding to JAK2 inhibits its kinase activity.
Suppresses fetal liver erythropoiesis. Regulates onset and
maintenance of allergic responses mediated by T-helper type 2
cells. Regulates IL-6 signaling in vivo. Probable 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 (By similarity). Seems to recognize IL6ST.
{ECO:0000250, ECO:0000269|PubMed:10490101,
ECO:0000269|PubMed:10821852, ECO:0000269|PubMed:12754505,
ECO:0000269|PubMed:12847520, ECO:0000269|PubMed:9889194}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with multiple activated proteins of the
tyrosine kinase signaling pathway including IGF1 receptor, insulin
receptor and JAK2. Binding to JAK2 is mediated through the KIR and
SH2 domains to a phosphorylated tyrosine residue within the JAK2
JH1 domain (By similarity). Binds specific activated tyrosine
residues of the leptin, EPO, IL12, GSCF and gp130 receptors
(PubMed:10882725). Interaction with CSNK1E stabilizes SOCS3
protein (By similarity). Component of the probable ECS(SOCS3) E3
ubiquitin-protein ligase complex which contains CUL5, RNF7/RBX2,
elongin BC complex and SOCS3 (By similarity). Interacts with CUL5,
RNF7, ELOB and ELOC (By similarity). Interacts with FGFR3 (By
similarity). Interacts with INSR (PubMed:10821852). Interacts with
BCL10; this interaction may interfere with BCL10-binding with
PELI2 (PubMed:15213237). Interacts with NOD2 (via CARD domain);
the interaction promotes NOD2 degradation (PubMed:23019338).
{ECO:0000250|UniProtKB:O14543, ECO:0000269|PubMed:10821852,
ECO:0000269|PubMed:10882725, ECO:0000269|PubMed:15213237,
ECO:0000269|PubMed:16905102, ECO:0000269|PubMed:23019338}.
-!- INTERACTION:
Q00560:Il6st; NbExp=2; IntAct=EBI-2659360, EBI-3862992;
-!- TISSUE SPECIFICITY: Low expression in lung, spleen and thymus.
Expressed in Th2 but not TH1 cells. {ECO:0000269|PubMed:12242343}.
-!- DEVELOPMENTAL STAGE: In the developing brain, expressed at low
levels from 10 dpc stages to young adulthood (P25) with peak
levels from 14 dpc to P8. In the cortex, first expressed uniformly
in all cells at 14 dpc. Not expressed in the retina. Highly
expressed in fetal liver progenitors at 12.5 dpc.
-!- INDUCTION: By a subset of cytokines including EPO, leptin, LIF,
IL-2, IL-3, IL-4, IGF1, growth hormone and prolactin.
{ECO:0000269|PubMed:12847520}.
-!- DOMAIN: The ESS and SH2 domains are required for JAK
phosphotyrosine binding. Further interaction with the KIR domain
is necessary for signal and kinase inhibition.
-!- DOMAIN: The SOCS box domain mediates the interaction with the
Elongin BC complex, an adapter module in different E3 ubiquitin
ligase complexes. {ECO:0000250}.
-!- PTM: Phosphorylated on tyrosine residues after stimulation by the
cytokines, IL-2, EPO or IGF1. {ECO:0000250}.
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EMBL; U88328; AAB62403.1; -; mRNA.
EMBL; AF314501; AAK60601.1; -; Genomic_DNA.
EMBL; AK047165; BAC32977.1; -; mRNA.
EMBL; AK139241; BAE23929.1; -; mRNA.
EMBL; AK152468; BAE31244.1; -; mRNA.
EMBL; AK152514; BAE31277.1; -; mRNA.
EMBL; AK157708; BAE34161.1; -; mRNA.
EMBL; AK159395; BAE35049.1; -; mRNA.
EMBL; AK170406; BAE41773.1; -; mRNA.
EMBL; AK172399; BAE42985.1; -; mRNA.
EMBL; BC052031; AAH52031.1; -; mRNA.
EMBL; AF117732; AAD18024.1; -; Genomic_DNA.
EMBL; U72673; AAB51035.1; ALT_SEQ; mRNA.
CCDS; CCDS25697.1; -.
RefSeq; NP_031733.1; NM_007707.3.
RefSeq; XP_011247009.1; XM_011248707.2.
PDB; 2BBU; NMR; -; A=22-185.
PDB; 2HMH; X-ray; 2.00 A; A=15-185.
PDB; 2JZ3; NMR; -; A=186-225.
PDB; 4GL9; X-ray; 3.90 A; E/F/G/H=22-128, E/F/G/H=163-185.
PDBsum; 2BBU; -.
PDBsum; 2HMH; -.
PDBsum; 2JZ3; -.
PDBsum; 4GL9; -.
SMR; O35718; -.
BioGrid; 198718; 14.
DIP; DIP-29137N; -.
IntAct; O35718; 11.
MINT; O35718; -.
STRING; 10090.ENSMUSP00000059129; -.
iPTMnet; O35718; -.
PhosphoSitePlus; O35718; -.
PaxDb; O35718; -.
PRIDE; O35718; -.
DNASU; 12702; -.
Ensembl; ENSMUST00000054002; ENSMUSP00000059129; ENSMUSG00000053113.
GeneID; 12702; -.
KEGG; mmu:12702; -.
UCSC; uc007moi.2; mouse.
CTD; 9021; -.
MGI; MGI:1201791; Socs3.
eggNOG; KOG4566; Eukaryota.
eggNOG; ENOG4111V4J; LUCA.
GeneTree; ENSGT00940000159620; -.
HOGENOM; HOG000236320; -.
InParanoid; O35718; -.
KO; K04696; -.
OMA; VTHSKFD; -.
OrthoDB; 1135696at2759; -.
PhylomeDB; O35718; -.
TreeFam; TF321368; -.
Reactome; R-MMU-1059683; Interleukin-6 signaling.
Reactome; R-MMU-877300; Interferon gamma signaling.
Reactome; R-MMU-877312; Regulation of IFNG signaling.
Reactome; R-MMU-8849474; PTK6 Activates STAT3.
Reactome; R-MMU-8951664; Neddylation.
Reactome; R-MMU-909733; Interferon alpha/beta signaling.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
EvolutionaryTrace; O35718; -.
PRO; PR:O35718; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000053113; Expressed in 250 organ(s), highest expression level in islet of Langerhans.
Genevisible; O35718; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IBA:GO_Central.
GO; GO:0001784; F:phosphotyrosine residue binding; IMP:CAFA.
GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IMP:MGI.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
GO; GO:0050728; P:negative regulation of inflammatory response; IGI:MGI.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:MGI.
GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
GO; GO:0009968; P:negative regulation of signal transduction; IGI:MGI.
GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
GO; GO:0046854; P:phosphatidylinositol phosphorylation; IBA:GO_Central.
GO; GO:0060674; P:placenta blood vessel development; IMP:MGI.
GO; GO:0045597; P:positive regulation of cell differentiation; IDA:MGI.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISO:MGI.
GO; GO:0045595; P:regulation of cell differentiation; IMP:MGI.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0001932; P:regulation of protein phosphorylation; IDA:MGI.
GO; GO:0007165; P:signal transduction; ISO:MGI.
GO; GO:0060708; P:spongiotrophoblast differentiation; IMP:MGI.
GO; GO:0060707; P:trophoblast giant cell differentiation; IMP:MGI.
CDD; cd10384; SH2_SOCS3; 1.
DisProt; DP00446; -.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR028414; SOCS3.
InterPro; IPR035863; SOCS3_SH2.
InterPro; IPR001496; SOCS_box.
InterPro; IPR036036; SOCS_box-like_dom_sf.
PANTHER; PTHR10155:SF11; PTHR10155:SF11; 1.
Pfam; PF00017; SH2; 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;
3D-structure; Complete proteome; Growth regulation; Phosphoprotein;
Reference proteome; SH2 domain; Signal transduction inhibitor;
Ubl conjugation pathway.
CHAIN 1 225 Suppressor of cytokine signaling 3.
/FTId=PRO_0000181244.
DOMAIN 46 142 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 177 224 SOCS box. {ECO:0000255|PROSITE-
ProRule:PRU00194}.
REGION 22 33 Kinase inhibitory region (KIR).
REGION 34 45 Extended SH2 subdomain (ESS).
MUTAGEN 22 22 L->A: No effect on LIF-induced signal
transduction suppression.
{ECO:0000269|PubMed:10882725}.
MUTAGEN 22 22 L->D: Abolishes binding to JAK2. No
effect on binding to EPOR.
{ECO:0000269|PubMed:10882725}.
MUTAGEN 25 25 F->A: Loss of LIF/EPO-induced signal
transduction suppression. Abolishes
binding to JAK2 and to EPOR.
{ECO:0000269|PubMed:10882725}.
MUTAGEN 30 30 E->R: No effect on LIF-induced signal
transduction suppression.
MUTAGEN 45 45 G->A: Abolishes binding to EPOR. No
effect on binding to JAK2.
{ECO:0000269|PubMed:10882725}.
MUTAGEN 71 71 R->K: Little effect on LIF-induced signal
transduction suppression. Loss of EPO-
induced signal transduction suppression.
Abolishes binding to JAK2 and EPOR.
{ECO:0000269|PubMed:10882725}.
HELIX 32 43 {ECO:0000244|PDB:2HMH}.
STRAND 45 48 {ECO:0000244|PDB:2HMH}.
HELIX 53 61 {ECO:0000244|PDB:2HMH}.
STRAND 67 72 {ECO:0000244|PDB:2HMH}.
STRAND 79 86 {ECO:0000244|PDB:2HMH}.
STRAND 89 96 {ECO:0000244|PDB:2HMH}.
HELIX 98 100 {ECO:0000244|PDB:2HMH}.
STRAND 102 104 {ECO:0000244|PDB:2HMH}.
STRAND 117 119 {ECO:0000244|PDB:2HMH}.
HELIX 120 126 {ECO:0000244|PDB:2HMH}.
STRAND 137 139 {ECO:0000244|PDB:2BBU}.
STRAND 165 167 {ECO:0000244|PDB:2HMH}.
STRAND 174 176 {ECO:0000244|PDB:2HMH}.
HELIX 189 199 {ECO:0000244|PDB:2JZ3}.
SEQUENCE 225 AA; 24776 MW; CD3859561D4CCDED CRC64;
MVTHSKFPAA GMSRPLDTSL RLKTFSSKSE YQLVVNAVRK LQESGFYWSA VTGGEANLLL
SAEPAGTFLI RDSSDQRHFF TLSVKTQSGT KNLRIQCEGG SFSLQSDPRS TQPVPRFDCV
LKLVHHYMPP PGTPSFSLPP TEPSSEVPEQ PPAQALPGST PKRAYYIYSG GEKIPLVLSR
PLSSNVATLQ HLCRKTVNGH LDSYEKVTQL PGPIREFLDQ YDAPL


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EIAAB07442 CIS,Cis,CIS-1,Cish,Cytokine-inducible SH2-containing protein,Mouse,Mus musculus,SOCS,Suppressor of cytokine signaling
EIAAB39200 Cish5,Cytokine-inducible SH2-containing protein 5,Mouse,Mus musculus,Socs5,SOCS-5,Suppressor of cytokine signaling 5
EIAAB39191 Cish2,Cytokine-inducible SH2 protein 2,Rat,Rattus norvegicus,Socs2,SOCS-2,Suppressor of cytokine signaling 2
EIAAB07441 CIS,CIS-1,CISH,Cytokine-inducible SH2-containing protein,G18,Homo sapiens,Human,Protein G18,SOCS,Suppressor of cytokine signaling
E1684r ELISA Cish3,Cytokine-inducible SH2 protein 3,Rat,Rattus norvegicus,Socs3,SOCS-3,Suppressor of cytokine signaling 3 96T
U1684r CLIA Cish3,Cytokine-inducible SH2 protein 3,Rat,Rattus norvegicus,Socs3,SOCS-3,Suppressor of cytokine signaling 3 96T
E1684r ELISA kit Cish3,Cytokine-inducible SH2 protein 3,Rat,Rattus norvegicus,Socs3,SOCS-3,Suppressor of cytokine signaling 3 96T
EIAAB39193 Cis2,CIS-2,Cish2,Cytokine-inducible SH2 protein 2,Mouse,Mus musculus,Socs2,SOCS-2,Suppressor of cytokine signaling 2
E1684m ELISA Cis3,CIS-3,Cish3,Cytokine-inducible SH2 protein 3,Mouse,Mus musculus,Protein EF-10,Socs3,SOCS-3,Suppressor of cytokine signaling 3 96T
U1684m CLIA Cis3,CIS-3,Cish3,Cytokine-inducible SH2 protein 3,Mouse,Mus musculus,Protein EF-10,Socs3,SOCS-3,Suppressor of cytokine signaling 3 96T
E1684m ELISA kit Cis3,CIS-3,Cish3,Cytokine-inducible SH2 protein 3,Mouse,Mus musculus,Protein EF-10,Socs3,SOCS-3,Suppressor of cytokine signaling 3 96T
EIAAB07444 Chicken,CIS,CIS,CIS-1,CISH,Cytokine-inducible SH2-containing protein,Gallus gallus,SOCS,Suppressor of cytokine signaling
E1684h ELISA kit CIS3,CIS-3,Cytokine-inducible SH2 protein 3,Homo sapiens,Human,SOCS3,SOCS-3,SSI3,SSI-3,STAT-induced STAT inhibitor 3,Suppressor of cytokine signaling 3 96T
E1684h ELISA CIS3,CIS-3,Cytokine-inducible SH2 protein 3,Homo sapiens,Human,SOCS3,SOCS-3,SSI3,SSI-3,STAT-induced STAT inhibitor 3,Suppressor of cytokine signaling 3 96T
U1684h CLIA CIS3,CIS-3,Cytokine-inducible SH2 protein 3,Homo sapiens,Human,SOCS3,SOCS-3,SSI3,SSI-3,STAT-induced STAT inhibitor 3,Suppressor of cytokine signaling 3 96T
EIAAB39195 CIS2,CIS-2,Cytokine-inducible SH2 protein 2,Homo sapiens,Human,SOCS2,SOCS-2,SSI2,SSI-2,STATI2,STAT-induced STAT inhibitor 2,Suppressor of cytokine signaling 2
EIAAB39198 Homo sapiens,Human,SOCS4,SOCS-4,SOCS7,SOCS-7,Suppressor of cytokine signaling 4,Suppressor of cytokine signaling 7
EIAAB39196 Mouse,Mus musculus,Socs4,SOCS-4,Socs7,SOCS-7,Suppressor of cytokine signaling 4,Suppressor of cytokine signaling 7
29-704 SOCS1 is a member of the STAT-induced STAT inhibitor (SSI), also known as suppressor of cytokine signaling (SOCS), family. SSI family members are cytokine-inducible negative regulators of cytokine sig 0.1 mg
bs-0113P Peptides: Socs 1 (suppressor of cytokine signaling 1) Protein Length:12-25 amino acids. 200ug lyophilized
bs-0580P Peptides: Socs 3 (suppressor of cytokine signaling 3) Protein Length:12-25 amino acids. 200ug lyophilized
Pathways :
WP2292: Chemokine signaling pathway
WP2272: Pathogenic Escherichia coli infection
WP1165: G Protein Signaling Pathways
WP232: G Protein Signaling Pathways
WP2203: TSLP Signaling Pathway
WP1371: G Protein Signaling Pathways
WP1049: G Protein Signaling Pathways
WP35: G Protein Signaling Pathways
WP211: BMP signaling pathway
WP931: G Protein Signaling Pathways
WP73: G Protein Signaling Pathways
WP813: G Protein Signaling Pathways
WP2032: TSH signaling pathway
WP1665: Limonene and pinene degradation
WP1675: Nitrogen metabolism
WP1616: ABC transporters
WP1685: Peptidoglycan biosynthesis
WP1692: Protein export
WP1644: DNA replication
WP1657: Glycerolipid metabolism
WP1502: Mitochondrial biogenesis
WP1714: Tyrosine metabolism
WP1663: Homologous recombination
WP1909: Signal regulatory protein (SIRP) family interactions
WP1531: Vitamin D synthesis

Related Genes :
[Socs3 Cis3 Cish3] Suppressor of cytokine signaling 3 (SOCS-3) (Cytokine-inducible SH2 protein 3) (CIS-3) (Protein EF-10)
[SOCS3 CIS3 SSI3] Suppressor of cytokine signaling 3 (SOCS-3) (Cytokine-inducible SH2 protein 3) (CIS-3) (STAT-induced STAT inhibitor 3) (SSI-3)
[Socs3 Cish3] Suppressor of cytokine signaling 3 (SOCS-3) (Cytokine-inducible SH2 protein 3)
[SOCS7 NAP4 SOCS6] Suppressor of cytokine signaling 7 (SOCS-7) (Nck, Ash and phospholipase C gamma-binding protein) (Nck-associated protein 4) (NAP-4)
[Socs7 Cish7 Nap4] Suppressor of cytokine signaling 7 (SOCS-7)
[SOCS3] Suppressor of cytokine signaling 3 (SOCS-3)
[GRB2 ASH] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (Protein Ash) (SH2/SH3 adapter GRB2)
[Ccl1 Scya1 Tca3] C-C motif chemokine 1 (P500) (SIS-epsilon) (Small-inducible cytokine A1) (T-cell activation protein 3) (TCA-3) (TCA3)
[SHC1 SHC SHCA] SHC-transforming protein 1 (SHC-transforming protein 3) (SHC-transforming protein A) (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1)
[Flt3 Flk-2 Flt-3] Receptor-type tyrosine-protein kinase FLT3 (EC 2.7.10.1) (FL cytokine receptor) (Fetal liver kinase 2) (FLK-2) (Fms-like tyrosine kinase 3) (FLT-3) (Tyrosine-protein kinase receptor flk-2) (CD antigen CD135)
[FLT3 CD135 FLK2 STK1] Receptor-type tyrosine-protein kinase FLT3 (EC 2.7.10.1) (FL cytokine receptor) (Fetal liver kinase-2) (FLK-2) (Fms-like tyrosine kinase 3) (FLT-3) (Stem cell tyrosine kinase 1) (STK-1) (CD antigen CD135)
[Sh2b1 Sh2bpsm1] SH2B adapter protein 1 (Pro-rich, PH and SH2 domain-containing signaling mediator) (PSM) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1)
[CCL3 G0S19-1 MIP1A SCYA3] C-C motif chemokine 3 (G0/G1 switch regulatory protein 19-1) (Macrophage inflammatory protein 1-alpha) (MIP-1-alpha) (PAT 464.1) (SIS-beta) (Small-inducible cytokine A3) (Tonsillar lymphocyte LD78 alpha protein) [Cleaved into: MIP-1-alpha(4-69) (LD78-alpha(4-69))]
[INPP5D SHIP SHIP1] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC 3.1.3.86) (Inositol polyphosphate-5-phosphatase D) (EC 3.1.3.56) (Inositol polyphosphate-5-phosphatase of 145 kDa) (SIP-145) (Phosphatidylinositol 4,5-bisphosphate 5-phosphatase) (EC 3.1.3.36) (SH2 domain-containing inositol 5'-phosphatase 1) (SH2 domain-containing inositol phosphatase 1) (SHIP-1) (p150Ship) (hp51CN)
[PLK3 CNK FNK PRK] Serine/threonine-protein kinase PLK3 (EC 2.7.11.21) (Cytokine-inducible serine/threonine-protein kinase) (FGF-inducible kinase) (Polo-like kinase 3) (PLK-3) (Proliferation-related kinase)
[INPPL1 SHIP2] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) (Inositol polyphosphate phosphatase-like protein 1) (INPPL-1) (Protein 51C) (SH2 domain-containing inositol 5'-phosphatase 2) (SH2 domain-containing inositol phosphatase 2) (SHIP-2)
[Sh2b1 Sh2-b Sh2bpsm1] SH2B adapter protein 1 (FceRI gamma-chain-interacting protein SH2-B) (SH2 domain-containing protein 1B) (SH2-B PH domain-containing signaling mediator 1)
[SH2B1 KIAA1299 SH2B] SH2B adapter protein 1 (Pro-rich, PH and SH2 domain-containing signaling mediator) (PSM) (SH2 domain-containing protein 1B)
[CCL15 MIP5 NCC3 SCYA15] C-C motif chemokine 15 (Chemokine CC-2) (HCC-2) (Leukotactin-1) (LKN-1) (MIP-1 delta) (Macrophage inflammatory protein 5) (MIP-5) (Mrp-2b) (NCC-3) (Small-inducible cytokine A15) [Cleaved into: CCL15(22-92); CCL15(25-92); CCL15(29-92)]
[CCL4 LAG1 MIP1B SCYA4] C-C motif chemokine 4 (G-26 T-lymphocyte-secreted protein) (HC21) (Lymphocyte activation gene 1 protein) (LAG-1) (MIP-1-beta(1-69)) (Macrophage inflammatory protein 1-beta) (MIP-1-beta) (PAT 744) (Protein H400) (SIS-gamma) (Small-inducible cytokine A4) (T-cell activation protein 2) (ACT-2) [Cleaved into: MIP-1-beta(3-69)]
[Grb2] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (SH2/SH3 adapter GRB2)
[CCL3L1 D17S1718 G0S19-2 SCYA3L1; CCL3L3] C-C motif chemokine 3-like 1 (G0/G1 switch regulatory protein 19-2) (LD78-beta(1-70)) (PAT 464.2) (Small-inducible cytokine A3-like 1) (Tonsillar lymphocyte LD78 beta protein) [Cleaved into: LD78-beta(3-70); LD78-beta(5-70)]
[Cxcl10 Crg2 Ifi10 Inp10 Scyb10] C-X-C motif chemokine 10 (10 kDa interferon gamma-induced protein) (Gamma-IP10) (IP-10) (C7) (Interferon-gamma induced protein CRG-2) (Small-inducible cytokine B10)
[Ccl2 Je Mcp1 Scya2] C-C motif chemokine 2 (Monocyte chemoattractant protein 1) (Monocyte chemotactic protein 1) (MCP-1) (Platelet-derived growth factor-inducible protein JE) (Small-inducible cytokine A2)
[CCL20 LARC MIP3A SCYA20] C-C motif chemokine 20 (Beta-chemokine exodus-1) (CC chemokine LARC) (Liver and activation-regulated chemokine) (Macrophage inflammatory protein 3 alpha) (MIP-3-alpha) (Small-inducible cytokine A20) [Cleaved into: CCL20(1-67); CCL20(1-64); CCL20(2-70)]
[Ctr9 Kiaa0155 Sh2bp1] RNA polymerase-associated protein CTR9 homolog (SH2 domain-binding protein 1) (Tetratricopeptide repeat-containing, SH2-binding phosphoprotein of 150 kDa) (TPR-containing, SH2-binding phosphoprotein of 150 kDa) (p150TSP)
[NCK1 NCK] Cytoplasmic protein NCK1 (NCK adaptor protein 1) (Nck-1) (SH2/SH3 adaptor protein NCK-alpha)
[Cx3cl1 Cx3c Fkn Scyd1] Fractalkine (C-X3-C motif chemokine 1) (CX3C membrane-anchored chemokine) (Neurotactin) (Small-inducible cytokine D1) [Cleaved into: Processed fractalkine]
[CX3CL1 FKN NTT SCYD1 A-152E5.2] Fractalkine (C-X3-C motif chemokine 1) (CX3C membrane-anchored chemokine) (Neurotactin) (Small-inducible cytokine D1) [Cleaved into: Processed fractalkine]
[PPBP CTAP3 CXCL7 SCYB7 TGB1 THBGB1] Platelet basic protein (PBP) (C-X-C motif chemokine 7) (Leukocyte-derived growth factor) (LDGF) (Macrophage-derived growth factor) (MDGF) (Small-inducible cytokine B7) [Cleaved into: Connective tissue-activating peptide III (CTAP-III) (LA-PF4) (Low-affinity platelet factor IV); TC-2; Connective tissue-activating peptide III(1-81) (CTAP-III(1-81)); Beta-thromboglobulin (Beta-TG); Neutrophil-activating peptide 2(74) (NAP-2(74)); Neutrophil-activating peptide 2(73) (NAP-2(73)); Neutrophil-activating peptide 2 (NAP-2); TC-1; Neutrophil-activating peptide 2(1-66) (NAP-2(1-66)); Neutrophil-activating peptide 2(1-63) (NAP-2(1-63))]

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