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O35718

- SOCS3_MOUSE

UniProt

O35718 - SOCS3_MOUSE

Protein

Suppressor of cytokine signaling 3

Gene

Socs3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. branching involved in labyrinthine layer morphogenesis Source: MGI
    2. JAK-STAT cascade Source: InterPro
    3. negative regulation of apoptotic process Source: InterPro
    4. negative regulation of insulin receptor signaling pathway Source: MGI
    5. negative regulation of signal transduction Source: MGI
    6. placenta blood vessel development Source: MGI
    7. positive regulation of cell differentiation Source: MGI
    8. protein ubiquitination Source: UniProtKB-UniPathway
    9. regulation of cell differentiation Source: MGI
    10. regulation of growth Source: UniProtKB-KW
    11. regulation of protein phosphorylation Source: MGI
    12. spongiotrophoblast differentiation Source: MGI
    13. trophoblast giant cell differentiation Source: MGI

    Keywords - Molecular functioni

    Signal transduction inhibitor

    Keywords - Biological processi

    Growth regulation, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_169390. Signaling by Leptin.
    REACT_188529. Signaling by Leptin.
    REACT_198614. Growth hormone receptor signaling.
    REACT_198627. Regulation of IFNA signaling.
    REACT_198645. Regulation of IFNG signaling.
    REACT_198660. Interferon gamma signaling.
    REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_199118. Interleukin-6 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: Chromosome 11

    Organism-specific databases

    MGIiMGI:1201791. Socs3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    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.
    GenevestigatoriO35718.

    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. Binds specific activated tyrosine residues of the leptin, EPO, IL12, GSCF and gp130 receptors. Interaction with CSNK1E stabilizes SOCS3 protein. Component of the probable ECS(SOCS3) E3 ubiquitin-protein ligase complex which contains CUL5, RNF7/RBX2, elongin BC complex and SOCS3. Interacts with CUL5, RNF7, TCEB1 and TCEB2. Interacts with FGFR3 By similarity. Interacts with INSR. Interacts with BCL10; this interaction may interfere with BCL10-binding with PELI2.By similarity4 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi198718. 11 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 – 4312
    Beta strandi45 – 484
    Helixi53 – 619
    Beta strandi67 – 726
    Beta strandi79 – 868
    Beta strandi89 – 968
    Helixi98 – 1003
    Beta strandi102 – 1043
    Beta strandi117 – 1193
    Helixi120 – 1267
    Beta strandi137 – 1393
    Beta strandi165 – 1673
    Beta strandi174 – 1763
    Helixi189 – 19911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    GeneTreeiENSGT00740000115151.
    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

    MVTHSKFPAA GMSRPLDTSL RLKTFSSKSE YQLVVNAVRK LQESGFYWSA    50
    VTGGEANLLL SAEPAGTFLI RDSSDQRHFF TLSVKTQSGT KNLRIQCEGG 100
    SFSLQSDPRS TQPVPRFDCV LKLVHHYMPP PGTPSFSLPP TEPSSEVPEQ 150
    PPAQALPGST PKRAYYIYSG GEKIPLVLSR PLSSNVATLQ HLCRKTVNGH 200
    LDSYEKVTQL PGPIREFLDQ YDAPL 225
    Length:225
    Mass (Da):24,776
    Last modified:January 1, 1998 - v1
    Checksum:iCD3859561D4CCDED
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_006532173.1. XM_006532110.1.
    UniGeneiMm.3468.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS25697.1.
    RefSeqi NP_031733.1. NM_007707.3.
    XP_006532173.1. XM_006532110.1.
    UniGenei Mm.3468.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BBU NMR - A 22-185 [» ]
    2HMH X-ray 2.00 A 15-185 [» ]
    2JZ3 NMR - A 186-225 [» ]
    4GL9 X-ray 3.90 E/F/G/H 38-128 [» ]
    E/F/G/H 182-185 [» ]
    DisProti DP00446.
    ProteinModelPortali O35718.
    SMRi O35718. Positions 30-185.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198718. 11 interactions.
    DIPi DIP-29137N.
    IntActi O35718. 9 interactions.
    MINTi MINT-2569503.
    STRINGi 10090.ENSMUSP00000059129.

    PTM databases

    PhosphoSitei O35718.

    Proteomic databases

    PRIDEi O35718.

    Protocols and materials databases

    DNASUi 12702.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000054002 ; ENSMUSP00000059129 ; ENSMUSG00000053113 .
    GeneIDi 12702.
    KEGGi mmu:12702.
    UCSCi uc007moi.2. mouse.

    Organism-specific databases

    CTDi 9021.
    MGIi MGI:1201791. Socs3.

    Phylogenomic databases

    eggNOGi NOG281730.
    GeneTreei ENSGT00740000115151.
    HOGENOMi HOG000236320.
    HOVERGENi HBG105645.
    InParanoidi O35718.
    KOi K04696.
    OMAi KRTYYIY.
    OrthoDBi EOG7TXKHR.
    PhylomeDBi O35718.
    TreeFami TF321368.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_169390. Signaling by Leptin.
    REACT_188529. Signaling by Leptin.
    REACT_198614. Growth hormone receptor signaling.
    REACT_198627. Regulation of IFNA signaling.
    REACT_198645. Regulation of IFNG signaling.
    REACT_198660. Interferon gamma signaling.
    REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_199118. Interleukin-6 signaling.

    Miscellaneous databases

    EvolutionaryTracei O35718.
    NextBioi 281958.
    PROi O35718.
    SOURCEi Search...

    Gene expression databases

    Bgeei O35718.
    CleanExi MM_SOCS3.
    Genevestigatori O35718.

    Family and domain databases

    Gene3Di 3.30.505.10. 2 hits.
    InterProi IPR000980. SH2.
    IPR028413. SOCS.
    IPR028414. SOCS3.
    IPR001496. SOCS_C.
    [Graphical view ]
    PANTHERi PTHR10385. PTHR10385. 1 hit.
    PTHR10385:SF4. PTHR10385:SF4. 1 hit.
    Pfami PF00017. SH2. 1 hit.
    PF07525. SOCS_box. 1 hit.
    [Graphical view ]
    SMARTi SM00252. SH2. 1 hit.
    SM00253. SOCS. 1 hit.
    SM00969. SOCS_box. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55550. SSF55550. 1 hit.
    PROSITEi PS50001. SH2. 1 hit.
    PS50225. SOCS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    16. "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: October 1, 2014
    This is version 133 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