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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.
17-JUN-2020, entry version 181.
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:
O35718; 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; -.
Antibodypedia; 3206; 777 antibodies.
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; CLU_079452_3_0_1; -.
InParanoid; O35718; -.
KO; K04696; -.
OMA; PKRTYYI; -.
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; -.
BioGRID-ORCS; 12702; 4 hits in 13 CRISPR screens.
EvolutionaryTrace; O35718; -.
PRO; PR:O35718; -.
Proteomes; UP000000589; Chromosome 11.
RNAct; O35718; protein.
Bgee; ENSMUSG00000053113; Expressed in islet of Langerhans and 249 other tissues.
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.
IDEAL; IID50193; -.
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; Growth regulation; Phosphoprotein; Reference proteome;
SH2 domain; Signal transduction inhibitor; Ubl conjugation pathway.
CHAIN 1..225
/note="Suppressor of cytokine signaling 3"
/id="PRO_0000181244"
DOMAIN 46..142
/note="SH2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
DOMAIN 177..224
/note="SOCS box"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
REGION 22..33
/note="Kinase inhibitory region (KIR)"
REGION 34..45
/note="Extended SH2 subdomain (ESS)"
MUTAGEN 22
/note="L->A: No effect on LIF-induced signal transduction
suppression."
/evidence="ECO:0000269|PubMed:10882725"
MUTAGEN 22
/note="L->D: Abolishes binding to JAK2. No effect on
binding to EPOR."
/evidence="ECO:0000269|PubMed:10882725"
MUTAGEN 25
/note="F->A: Loss of LIF/EPO-induced signal transduction
suppression. Abolishes binding to JAK2 and to EPOR."
/evidence="ECO:0000269|PubMed:10882725"
MUTAGEN 30
/note="E->R: No effect on LIF-induced signal transduction
suppression."
MUTAGEN 45
/note="G->A: Abolishes binding to EPOR. No effect on
binding to JAK2."
/evidence="ECO:0000269|PubMed:10882725"
MUTAGEN 71
/note="R->K: Little effect on LIF-induced signal
transduction suppression. Loss of EPO-induced signal
transduction suppression. Abolishes binding to JAK2 and
EPOR."
/evidence="ECO:0000269|PubMed:10882725"
HELIX 32..43
/evidence="ECO:0000244|PDB:2HMH"
STRAND 45..48
/evidence="ECO:0000244|PDB:2HMH"
HELIX 53..61
/evidence="ECO:0000244|PDB:2HMH"
STRAND 67..72
/evidence="ECO:0000244|PDB:2HMH"
STRAND 79..86
/evidence="ECO:0000244|PDB:2HMH"
STRAND 89..96
/evidence="ECO:0000244|PDB:2HMH"
HELIX 98..100
/evidence="ECO:0000244|PDB:2HMH"
STRAND 102..104
/evidence="ECO:0000244|PDB:2HMH"
STRAND 117..119
/evidence="ECO:0000244|PDB:2HMH"
HELIX 120..126
/evidence="ECO:0000244|PDB:2HMH"
STRAND 137..139
/evidence="ECO:0000244|PDB:2BBU"
STRAND 165..167
/evidence="ECO:0000244|PDB:2HMH"
STRAND 174..176
/evidence="ECO:0000244|PDB:2HMH"
HELIX 189..199
/evidence="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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EIAAB39203 Cis4,CIS-4,Cish4,Cytokine-inducible SH2 protein 4,Mouse,Mus musculus,Socs4,SOCS-4,Socs6,SOCS-6,Suppressor of cytokine signaling 4,Suppressor of cytokine signaling 6
EIAAB39201 CIS6,CIS-6,CISH5,CISH6,Cytokine-inducible SH2 protein 6,Cytokine-inducible SH2-containing protein 5,Homo sapiens,Human,KIAA0671,SOCS5,SOCS-5,Suppressor of cytokine signaling 5
EIAAB07443 CIS,CIS-1,Cish,Cytokine-inducible SH2-containing protein,Rat,Rattus norvegicus,SOCS,Suppressor of cytokine signaling
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
WP211: BMP signaling pathway
WP35: G Protein Signaling Pathways
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
WP525: Mitochondrial Unfolded-Protein Response
WP1663: Homologous recombination
WP1909: Signal regulatory protein (SIRP) family interactions

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)
[GRB2 ASH] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (Protein Ash) (SH2/SH3 adapter GRB2)
[SOCS3] Suppressor of cytokine signaling 3 (SOCS-3)
[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)
[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)
[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))]
[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 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)
[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)]
[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)
[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)
[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)]
[NCK1 NCK] Cytoplasmic protein NCK1 (NCK adaptor protein 1) (Nck-1) (SH2/SH3 adaptor protein NCK-alpha)
[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)
[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]
[Cx3cl1 Acc1 Fkn Scyd1] Fractalkine (C-X3-C motif chemokine 1) (CX3C membrane-anchored chemokine) (Neurotactin) (Small-inducible cytokine D1) [Cleaved into: Processed fractalkine]

Bibliography :