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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.
27-SEP-2017, entry version 162.
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=3; 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 E10 stages to young adulthood (P25) with peak levels
from E14 to P8. In the cortex, first expressed uniformly in all
cells at E14. Not expressed in the retina. Highly expressed in
fetal liver progenitors at E12.5.
-!- 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.
UniGene; Mm.3468; -.
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=179-185.
PDBsum; 2BBU; -.
PDBsum; 2HMH; -.
PDBsum; 2JZ3; -.
PDBsum; 4GL9; -.
DisProt; DP00446; -.
ProteinModelPortal; O35718; -.
SMR; O35718; -.
BioGrid; 198718; 13.
DIP; DIP-29137N; -.
IntAct; O35718; 9.
MINT; MINT-2569503; -.
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; ENSGT00760000119136; -.
HOGENOM; HOG000236320; -.
HOVERGEN; HBG105645; -.
InParanoid; O35718; -.
KO; K04696; -.
OMA; KRTYYIY; -.
OrthoDB; EOG091G0NEU; -.
PhylomeDB; O35718; -.
TreeFam; TF321368; -.
Reactome; R-MMU-2586551; Signaling by Leptin.
Reactome; R-MMU-2586552; Signaling by Leptin.
Reactome; R-MMU-6783589; Interleukin-6 family 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-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes.
Reactome; R-MMU-8951664; Neddylation.
Reactome; R-MMU-909733; Interferon alpha/beta signaling.
Reactome; R-MMU-982772; Growth hormone receptor signaling.
UniPathway; UPA00143; -.
EvolutionaryTrace; O35718; -.
PRO; PR:O35718; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000053113; -.
CleanEx; MM_SOCS3; -.
Genevisible; O35718; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0001784; F:phosphotyrosine residue binding; IMP:CAFA.
GO; GO:0004860; F:protein kinase inhibitor activity; IBA:GO_Central.
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:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; TAS:Reactome.
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 JAK-STAT cascade; ISO:MGI.
GO; GO:0006469; P:negative regulation of protein kinase activity; IBA:GO_Central.
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: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:0045595; P:regulation of cell differentiation; IMP:MGI.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0045616; P:regulation of keratinocyte differentiation; TAS:Reactome.
GO; GO:0001932; P:regulation of protein phosphorylation; IDA:MGI.
GO; GO:0060708; P:spongiotrophoblast differentiation; IMP:MGI.
GO; GO:0060707; P:trophoblast giant cell differentiation; IMP:MGI.
CDD; cd10384; SH2_SOCS3; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR000980; SH2.
InterPro; IPR028414; SOCS3.
InterPro; IPR035863; SOCS3_SH2.
InterPro; IPR001496; SOCS_box.
PANTHER; PTHR24369:SF110; PTHR24369:SF110; 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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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


 

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