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Protein

Suppressor of cytokine signaling 3

Gene

Socs3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity5 Publications

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

GO - Biological processi

  • aging Source: Ensembl
  • branching involved in labyrinthine layer morphogenesis Source: MGI
  • cytokine-mediated signaling pathway Source: GO_Central
  • JAK-STAT cascade Source: InterPro
  • negative regulation of apoptotic process Source: InterPro
  • negative regulation of inflammatory response Source: MGI
  • negative regulation of insulin receptor signaling pathway Source: MGI
  • negative regulation of JAK-STAT cascade Source: GO_Central
  • negative regulation of protein kinase activity Source: GO_Central
  • negative regulation of signal transduction Source: MGI
  • organ regeneration Source: Ensembl
  • placenta blood vessel development Source: MGI
  • positive regulation of cell differentiation Source: MGI
  • protein ubiquitination Source: UniProtKB-UniPathway
  • regulation of cell differentiation Source: MGI
  • regulation of growth Source: UniProtKB-KW
  • regulation of protein phosphorylation Source: MGI
  • response to drug Source: Ensembl
  • response to estradiol Source: Ensembl
  • response to food Source: Ensembl
  • response to gamma radiation Source: Ensembl
  • response to glucocorticoid Source: Ensembl
  • response to heat Source: Ensembl
  • response to hypoxia Source: Ensembl
  • response to insulin Source: Ensembl
  • response to lipopolysaccharide Source: Ensembl
  • response to progesterone Source: Ensembl
  • spongiotrophoblast differentiation Source: MGI
  • trophoblast giant cell differentiation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Keywords - Biological processi

Growth regulation, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_169390. Signaling by Leptin.
REACT_289967. Regulation of IFNG signaling.
REACT_301070. Interleukin-6 signaling.
REACT_317434. Growth hormone receptor signaling.
REACT_323806. Signaling by Leptin.
REACT_336467. Interferon alpha/beta signaling.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_349056. Interferon gamma signaling.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Suppressor of cytokine signaling 3
Short name:
SOCS-3
Alternative name(s):
Cytokine-inducible SH2 protein 3
Short name:
CIS-3
Protein EF-10
Gene namesi
Name:Socs3
Synonyms:Cis3, Cish3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1201791. Socs3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221L → A: No effect on LIF-induced signal transduction suppression. 1 Publication
Mutagenesisi22 – 221L → D: Abolishes binding to JAK2. No effect on binding to EPOR. 1 Publication
Mutagenesisi25 – 251F → A: Loss of LIF/EPO-induced signal transduction suppression. Abolishes binding to JAK2 and to EPOR. 1 Publication
Mutagenesisi30 – 301E → R: No effect on LIF-induced signal transduction suppression.
Mutagenesisi45 – 451G → A: Abolishes binding to EPOR. No effect on binding to JAK2. 1 Publication
Mutagenesisi71 – 711R → K: Little effect on LIF-induced signal transduction suppression. Loss of EPO-induced signal transduction suppression. Abolishes binding to JAK2 and EPOR. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 225225Suppressor of cytokine signaling 3PRO_0000181244Add
BLAST

Post-translational modificationi

Phosphorylated on tyrosine residues after stimulation by the cytokines, IL-2, EPO or IGF1.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiO35718.

PTM databases

PhosphoSiteiO35718.

Expressioni

Tissue specificityi

Low expression in lung, spleen and thymus. Expressed in Th2 but not TH1 cells.1 Publication

Developmental stagei

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.

Inductioni

By a subset of cytokines including EPO, leptin, LIF, IL-2, IL-3, IL-4, IGF1, growth hormone and prolactin.1 Publication

Gene expression databases

BgeeiO35718.
CleanExiMM_SOCS3.
GenevisibleiO35718. MM.

Interactioni

Subunit structurei

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, TCEB1 and TCEB2 (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).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Il6stQ005603EBI-2659360,EBI-3862992

Protein-protein interaction databases

BioGridi198718. 13 interactions.
DIPiDIP-29137N.
IntActiO35718. 9 interactions.
MINTiMINT-2569503.
STRINGi10090.ENSMUSP00000059129.

Structurei

Secondary structure

1
225
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 4312Combined sources
Beta strandi45 – 484Combined sources
Helixi53 – 619Combined sources
Beta strandi67 – 726Combined sources
Beta strandi79 – 868Combined sources
Beta strandi89 – 968Combined sources
Helixi98 – 1003Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi117 – 1193Combined sources
Helixi120 – 1267Combined sources
Beta strandi137 – 1393Combined sources
Beta strandi165 – 1673Combined sources
Beta strandi174 – 1763Combined sources
Helixi189 – 19911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BBUNMR-A22-185[»]
2HMHX-ray2.00A15-185[»]
2JZ3NMR-A186-225[»]
4GL9X-ray3.90E/F/G/H38-128[»]
E/F/G/H182-185[»]
DisProtiDP00446.
ProteinModelPortaliO35718.
SMRiO35718. Positions 30-185.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35718.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 14297SH2PROSITE-ProRule annotationAdd
BLAST
Domaini177 – 22448SOCS boxPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 3312Kinase inhibitory region (KIR)Add
BLAST
Regioni34 – 4512Extended SH2 subdomain (ESS)Add
BLAST

Domaini

The ESS and SH2 domains are required for JAK phosphotyrosine binding. Further interaction with the KIR domain is necessary for signal and kinase inhibition.
The SOCS box domain mediates the interaction with the Elongin BC complex, an adapter module in different E3 ubiquitin ligase complexes.By similarity

Sequence similaritiesi

Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SOCS box domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiNOG281730.
GeneTreeiENSGT00760000119136.
HOGENOMiHOG000236320.
HOVERGENiHBG105645.
InParanoidiO35718.
KOiK04696.
OMAiKRTYYIY.
OrthoDBiEOG7TXKHR.
PhylomeDBiO35718.
TreeFamiTF321368.

Family and domain databases

Gene3Di3.30.505.10. 2 hits.
InterProiIPR000980. SH2.
IPR028413. SOCS.
IPR028414. SOCS3.
IPR001496. SOCS_C.
[Graphical view]
PANTHERiPTHR10385. PTHR10385. 1 hit.
PTHR10385:SF4. PTHR10385:SF4. 1 hit.
PfamiPF00017. SH2. 1 hit.
PF07525. SOCS_box. 1 hit.
[Graphical view]
SMARTiSM00252. SH2. 1 hit.
SM00253. SOCS. 1 hit.
SM00969. SOCS_box. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
PS50225. SOCS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35718-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTHSKFPAA GMSRPLDTSL RLKTFSSKSE YQLVVNAVRK LQESGFYWSA
60 70 80 90 100
VTGGEANLLL SAEPAGTFLI RDSSDQRHFF TLSVKTQSGT KNLRIQCEGG
110 120 130 140 150
SFSLQSDPRS TQPVPRFDCV LKLVHHYMPP PGTPSFSLPP TEPSSEVPEQ
160 170 180 190 200
PPAQALPGST PKRAYYIYSG GEKIPLVLSR PLSSNVATLQ HLCRKTVNGH
210 220
LDSYEKVTQL PGPIREFLDQ YDAPL
Length:225
Mass (Da):24,776
Last modified:January 1, 1998 - v1
Checksum:iCD3859561D4CCDED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88328 mRNA. Translation: AAB62403.1.
AF314501 Genomic DNA. Translation: AAK60601.1.
AK047165 mRNA. Translation: BAC32977.1.
AK139241 mRNA. Translation: BAE23929.1.
AK152468 mRNA. Translation: BAE31244.1.
AK152514 mRNA. Translation: BAE31277.1.
AK157708 mRNA. Translation: BAE34161.1.
AK159395 mRNA. Translation: BAE35049.1.
AK170406 mRNA. Translation: BAE41773.1.
AK172399 mRNA. Translation: BAE42985.1.
BC052031 mRNA. Translation: AAH52031.1.
AF117732 Genomic DNA. Translation: AAD18024.1.
U72673 mRNA. Translation: AAB51035.1. Sequence problems.
CCDSiCCDS25697.1.
RefSeqiNP_031733.1. NM_007707.3.
XP_011247009.1. XM_011248707.1.
UniGeneiMm.3468.

Genome annotation databases

EnsembliENSMUST00000054002; ENSMUSP00000059129; ENSMUSG00000053113.
GeneIDi12702.
KEGGimmu:12702.
UCSCiuc007moi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88328 mRNA. Translation: AAB62403.1.
AF314501 Genomic DNA. Translation: AAK60601.1.
AK047165 mRNA. Translation: BAC32977.1.
AK139241 mRNA. Translation: BAE23929.1.
AK152468 mRNA. Translation: BAE31244.1.
AK152514 mRNA. Translation: BAE31277.1.
AK157708 mRNA. Translation: BAE34161.1.
AK159395 mRNA. Translation: BAE35049.1.
AK170406 mRNA. Translation: BAE41773.1.
AK172399 mRNA. Translation: BAE42985.1.
BC052031 mRNA. Translation: AAH52031.1.
AF117732 Genomic DNA. Translation: AAD18024.1.
U72673 mRNA. Translation: AAB51035.1. Sequence problems.
CCDSiCCDS25697.1.
RefSeqiNP_031733.1. NM_007707.3.
XP_011247009.1. XM_011248707.1.
UniGeneiMm.3468.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BBUNMR-A22-185[»]
2HMHX-ray2.00A15-185[»]
2JZ3NMR-A186-225[»]
4GL9X-ray3.90E/F/G/H38-128[»]
E/F/G/H182-185[»]
DisProtiDP00446.
ProteinModelPortaliO35718.
SMRiO35718. Positions 30-185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198718. 13 interactions.
DIPiDIP-29137N.
IntActiO35718. 9 interactions.
MINTiMINT-2569503.
STRINGi10090.ENSMUSP00000059129.

PTM databases

PhosphoSiteiO35718.

Proteomic databases

PRIDEiO35718.

Protocols and materials databases

DNASUi12702.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000054002; ENSMUSP00000059129; ENSMUSG00000053113.
GeneIDi12702.
KEGGimmu:12702.
UCSCiuc007moi.2. mouse.

Organism-specific databases

CTDi9021.
MGIiMGI:1201791. Socs3.

Phylogenomic databases

eggNOGiNOG281730.
GeneTreeiENSGT00760000119136.
HOGENOMiHOG000236320.
HOVERGENiHBG105645.
InParanoidiO35718.
KOiK04696.
OMAiKRTYYIY.
OrthoDBiEOG7TXKHR.
PhylomeDBiO35718.
TreeFamiTF321368.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_169390. Signaling by Leptin.
REACT_289967. Regulation of IFNG signaling.
REACT_301070. Interleukin-6 signaling.
REACT_317434. Growth hormone receptor signaling.
REACT_323806. Signaling by Leptin.
REACT_336467. Interferon alpha/beta signaling.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_349056. Interferon gamma signaling.

Miscellaneous databases

EvolutionaryTraceiO35718.
NextBioi281958.
PROiO35718.
SOURCEiSearch...

Gene expression databases

BgeeiO35718.
CleanExiMM_SOCS3.
GenevisibleiO35718. MM.

Family and domain databases

Gene3Di3.30.505.10. 2 hits.
InterProiIPR000980. SH2.
IPR028413. SOCS.
IPR028414. SOCS3.
IPR001496. SOCS_C.
[Graphical view]
PANTHERiPTHR10385. PTHR10385. 1 hit.
PTHR10385:SF4. PTHR10385:SF4. 1 hit.
PfamiPF00017. SH2. 1 hit.
PF07525. SOCS_box. 1 hit.
[Graphical view]
SMARTiSM00252. SH2. 1 hit.
SM00253. SOCS. 1 hit.
SM00969. SOCS_box. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
PS50225. SOCS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung and Thymus.
  2. "Murine SOCS3 gene structure."
    Le Provost F., Henninghausen L.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Cerebellum and Spleen.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain.
  5. "Autoregulation of pituitary corticotroph SOCS-3 expression: characterization of the murine SOCS-3 promoter."
    Auernhammer C.J., Bousquet C., Melmed S.
    Proc. Natl. Acad. Sci. U.S.A. 96:6964-6969(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
    Strain: ICR X Swiss Webster.
  6. "E2a-Pbx1 induces aberrant expression of tissue-specific and developmentally regulated genes when expressed in NIH 3T3 fibroblasts."
    Fu X., Kamps M.P.
    Mol. Cell. Biol. 17:1503-1512(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 221-225.
    Strain: BALB/c.
  7. "Mutational analyses of the SOCS proteins suggest a dual domain requirement but distinct mechanisms for inhibition of LIF and IL-6 signal transduction."
    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.
    EMBO J. 18:375-385(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN LIF AND IL6 SIGNALING.
  8. "SOCS-3 is an insulin-induced negative regulator of insulin signaling."
    Emanuelli B., Peraldi P., Filloux C., Sawka-Verhelle D., Hilton D., Van Obberghen E.
    J. Biol. Chem. 275:15985-15991(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INHIBITION OF INSR KINASE ACTIVITY, INTERACTION WITH INSR.
  9. "CIS3/SOCS-3 suppresses erythropoietin (EPO) signaling by binding the EPO receptor and JAK2."
    Sasaki A., Yasukawa H., Shouda T., Kitamura T., Dikic I., Yoshimura A.
    J. Biol. Chem. 275:29338-29347(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPOR AND JAK2, MUTAGENESIS OF LEU-22; PHE-25; GLY-45 AND ARG-71.
  10. "Expression of the suppressor of cytokine signaling-5 (SOCS5) negatively regulates IL-4-dependent STAT6 activation and Th2 differentiation."
    Seki Y., Hayashi K., Matsumoto A., Seki N., Tsukada J., Ransom J., Naka T., Kishimoto T., Yoshimura A., Kubo M.
    Proc. Natl. Acad. Sci. U.S.A. 99:13003-13008(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. Cited for: FUNCTION IN ERYTHROPOIESIS.
  12. Cited for: ROLE IN IL-6 SIGNALING.
  13. Cited for: ROLE IN ALLERGIC RESPONSE, INDUCTION BY IL-4.
  14. "BCL10 mediates lipopolysaccharide/toll-like receptor-4 signaling through interaction with Pellino2."
    Liu Y., Dong W., Chen L., Xiang R., Xiao H., De G., Wang Z., Qi Y.
    J. Biol. Chem. 279:37436-37444(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCL10.
  15. "Proteasomal degradation of Nod2 protein mediates tolerance to bacterial cell wall components."
    Lee K.H., Biswas A., Liu Y.J., Kobayashi K.S.
    J. Biol. Chem. 287:39800-39811(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOD2.
  16. "The structure of SOCS3 reveals the basis of the extended SH2 domain function and identifies an unstructured insertion that regulates stability."
    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.
    Mol. Cell 22:205-216(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 22-185.
  17. "Structural basis for phosphotyrosine recognition by suppressor of cytokine signaling-3."
    Bergamin E., Wu J., Hubbard S.R.
    Structure 14:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 15-185 IN COMPLEX WITH PHOSPHORYLATED IL6ST.

Entry informationi

Entry nameiSOCS3_MOUSE
AccessioniPrimary (citable) accession number: O35718
Secondary accession number(s): P97803, Q3U7X5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: January 1, 1998
Last modified: July 22, 2015
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.