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Protein

Suppressor of cytokine signaling 1

Gene

Socs1

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. SOCS1 is involved in negative regulation of cytokines that signal through the JAK/STAT3 pathway. Through binding to JAKs, inhibits their kinase activity. In vitro, also suppresses Tec protein-tyrosine activity (By similarity). Appears to be a major regulator of signaling by interleukin 6 (IL6) and leukemia inhibitory factor (LIF). Regulates interferon-gamma mediated sensory neuron survival. Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Seems to recognize JAK2 (By similarity). SOCS1 appears to be a negative regulator in IGF1R signaling pathway (By similarity).By similarity2 Publications

Pathwayi: protein 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

  • cellular response to amino acid stimulus Source: MGI
  • cellular response to cytokine stimulus Source: MGI
  • cellular response to organic cyclic compound Source: MGI
  • cytokine-mediated signaling pathway Source: MGI
  • fat cell differentiation Source: MGI
  • JAK-STAT cascade Source: MGI
  • negative regulation of insulin receptor signaling pathway Source: MGI
  • negative regulation of JAK-STAT cascade Source: MGI
  • negative regulation of tyrosine phosphorylation of Stat3 protein Source: MGI
  • organ regeneration Source: Ensembl
  • protein ubiquitination Source: UniProtKB-UniPathway
  • regulation of activation of JAK2 kinase activity Source: MGI
  • regulation of cytokine secretion Source: MGI
  • regulation of growth Source: UniProtKB-KW
  • regulation of interferon-gamma-mediated signaling pathway Source: InterPro
  • regulation of JAK-STAT cascade Source: MGI
  • regulation of protein phosphorylation Source: MGI
  • regulation of tyrosine phosphorylation of Stat1 protein Source: MGI
  • response to drug Source: Ensembl
  • response to estradiol Source: Ensembl
  • response to lipopolysaccharide Source: Ensembl
  • response to peptide hormone Source: Ensembl
  • response to progesterone Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Keywords - Biological processi

Growth regulation, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-MMU-877300. Interferon gamma signaling.
R-MMU-877312. Regulation of IFNG signaling.
R-MMU-909733. Interferon alpha/beta signaling.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SABIO-RKO35716.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Suppressor of cytokine signaling 1
Short name:
SOCS-1
Alternative name(s):
JAK-binding protein
Short name:
JAB
STAT-induced STAT inhibitor 1
Short name:
SSI-1
Gene namesi
Name:Socs1
Synonyms:Cish1, Ssi1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1354910. Socs1.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasmic vesicle By similarity

  • Note: Detected in perinuclear cytoplasmic vesicles upon interaction with FGFR3.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice exhibit lymphocyte deficiency and degeneration of the liver parenchyma. Animals die within 3 weeks of age.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi51 – 511P → A: No effect on LIF signal transduction suppression.
Mutagenesisi52 – 521G → A: No effect on LIF signal transduction suppression.
Mutagenesisi53 – 531D → A or R: No effect on LIF signal transduction suppression.
Mutagenesisi54 – 541T → A: No effect on LIF signal transduction suppression.
Mutagenesisi55 – 551H → A or D: No effect on JAK signal transduction suppression. 1 Publication
Mutagenesisi56 – 561F → A, S or D: Loss of JAK signal transduction suppression. 1 Publication
Mutagenesisi56 – 561F → E or S: Reduced binding to JH1. 1 Publication
Mutagenesisi56 – 561F → L: No effect on JAK signal transduction inhibition nor on binding to JH1. 1 Publication
Mutagenesisi57 – 571R → A or E: No effect on JAK signal transduction suppression. 1 Publication
Mutagenesisi58 – 581T → A: No effect on JAK signal transduction suppression. 1 Publication
Mutagenesisi59 – 591F → A or E: Loss of JAK signal transduction suppression. Reduced binding to JH1. 2 Publications
Mutagenesisi59 – 591F → D: Loss of JAK signal transduction suppression. Destabilization of SOCS1. 2 Publications
Mutagenesisi59 – 591F → L: No effect on JAK signal transduction suppression nor on binding to JH1. 2 Publications
Mutagenesisi60 – 601R → A: No effect on LIF signal transduction suppression. 1 Publication
Mutagenesisi61 – 611S → E: No effect on JAK signal transduction suppression. 1 Publication
Mutagenesisi62 – 621H → E: No effect on JAK signal transduction suppression. 1 Publication
Mutagenesisi64 – 641D → R: Loss of JAK signal transduction suppression. Reduced binding to JH1. 1 Publication
Mutagenesisi65 – 651Y → A: Some loss of JAK signal transduction signaling. Reduced binding to JH1. 1 Publication
Mutagenesisi68 – 681I → E: Loss of binding to JH1/Y-1007 of JAK2 and loss of signal transduction suppression.
Mutagenesisi70 – 701R → E: No effect on LIF signal transduction suppression.
Mutagenesisi75 – 751L → E: Loss of binding to JH1/Y-1007 of JAK2 and loss of signal transduction suppression.
Mutagenesisi105 – 1051R → K: Loss of LIF signal transduction suppression. Loss of binding to KIT. No effect on binding to VAV. 1 Publication
Mutagenesisi105 – 1051R → Q: Loss of IL-6 signal transduction suppression. No effect on binding to TYK2. 1 Publication
Mutagenesisi175 – 1751L → P: Abolishes interaction with elongin BC complex; when associated with F-179. 1 Publication
Mutagenesisi179 – 1791C → F: Abolishes interaction with elongin BC complex; when associated with P-175. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 212212Suppressor of cytokine signaling 1PRO_0000181236Add
BLAST

Proteomic databases

EPDiO35716.
PaxDbiO35716.
PRIDEiO35716.

PTM databases

iPTMnetiO35716.

Expressioni

Tissue specificityi

High expression in thymus. Lower expression in lung and spleen. Expressed in both Th1 and Th2 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, expression first observed at E14 uniformly in all cells. Also expressed in the innermost layers of the developing retina. Levels of expression remain unchanged from P8 until adulthood. In the peripheral nervous system, high levels found in virtually all neurons of the dorsal root ganglion.

Inductioni

By a subset of cytokines including those belonging to the interferon, interleukin and colony-stimulating factor families.

Gene expression databases

BgeeiO35716.
CleanExiMM_SOCS1.
GenevisibleiO35716. MM.

Interactioni

Subunit structurei

Interacts with multiple activated proteins of the tyrosine kinase signaling pathway including JAK family kinases, TEC, KIT, GRB2 and VAV. Binding to JAKs is mediated through the KIR and SH2 domain to a phosphorylated tyrosine residue within the JAK JH1 domain. Binds the SH3 domain of GRB2 via diproline determinants in the N-terminus, and the N-terminal regulatory domain of VAV. Interacts with the Elongin BC complex (TCEB1 and TCEB2). Component of an ECS CBC(SOCS1) E3 ubiquitin-protein ligase complex which contains Elongin BC, CUL5, RBX1 and SOCS1. Interacts (via SH2 domain and SOCS box) with TRIM8. Interacts with CUL2. Interacts with AXL and FGFR3 (By similarity). Interacts with INSR.By similarity4 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198719. 32 interactions.
IntActiO35716. 6 interactions.
MINTiMINT-84865.
STRINGi10090.ENSMUSP00000038121.

Structurei

3D structure databases

ProteinModelPortaliO35716.
SMRiO35716. Positions 56-212.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini80 – 17596SH2PROSITE-ProRule annotationAdd
BLAST
Domaini162 – 21150SOCS boxPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni56 – 6712Kinase inhibitory region (KIR)Add
BLAST
Regioni68 – 7912Extended SH2 subdomain (ESS)Add
BLAST
Regioni174 – 18310Interaction with Elongin BC complex

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi26 – 338Poly-Ser

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. The Elongin BC complex binding domain is also known as BC-box with the consensus [APST]-L-x(3)-C-x(3)-[AILV] and is part of the SOCS box.

Sequence similaritiesi

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

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiKOG4566. Eukaryota.
ENOG4111V4J. LUCA.
GeneTreeiENSGT00760000119136.
HOGENOMiHOG000236320.
HOVERGENiHBG002457.
InParanoidiO35716.
KOiK04694.
OMAiETFDCLF.
OrthoDBiEOG7TMZSZ.
PhylomeDBiO35716.
TreeFamiTF321368.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000980. SH2.
IPR028411. SOCS1.
IPR001496. SOCS_box.
[Graphical view]
PANTHERiPTHR24369:SF72. PTHR24369:SF72. 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]
SUPFAMiSSF158235. SSF158235. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
PS50225. SOCS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35716-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVARNQVAAD NAISPAAEPR RRSEPSSSSS SSSPAAPVRP RPCPAVPAPA
60 70 80 90 100
PGDTHFRTFR SHSDYRRITR TSALLDACGF YWGPLSVHGA HERLRAEPVG
110 120 130 140 150
TFLVRDSRQR NCFFALSVKM ASGPTSIRVH FQAGRFHLDG SRETFDCLFE
160 170 180 190 200
LLEHYVAAPR RMLGAPLRQR RVRPLQELCR QRIVAAVGRE NLARIPLNPV
210
LRDYLSSFPF QI
Length:212
Mass (Da):23,715
Last modified:January 1, 1998 - v1
Checksum:i4621E05DC3D44C69
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411S → N in BAA21538 (PubMed:9202126).Curated
Sequence conflicti141 – 1411S → N in BAA21539 (PubMed:9202127).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88325 mRNA. Translation: AAB62400.1.
AB000677 mRNA. Translation: BAA21538.1.
AB000710 mRNA. Translation: BAA21539.1.
AF120490 mRNA. Translation: AAD24777.1.
AF180302 mRNA. Translation: AAD53324.1.
AK028632 mRNA. Translation: BAC26040.1.
AK154706 mRNA. Translation: BAE32775.1.
BC132366 mRNA. Translation: AAI32367.1.
BC132368 mRNA. Translation: AAI32369.1.
CCDSiCCDS27952.1.
RefSeqiNP_001258532.1. NM_001271603.1.
NP_034026.1. NM_009896.2.
UniGeneiMm.130.

Genome annotation databases

EnsembliENSMUST00000038099; ENSMUSP00000038121; ENSMUSG00000038037.
GeneIDi12703.
KEGGimmu:12703.
UCSCiuc007yed.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88325 mRNA. Translation: AAB62400.1.
AB000677 mRNA. Translation: BAA21538.1.
AB000710 mRNA. Translation: BAA21539.1.
AF120490 mRNA. Translation: AAD24777.1.
AF180302 mRNA. Translation: AAD53324.1.
AK028632 mRNA. Translation: BAC26040.1.
AK154706 mRNA. Translation: BAE32775.1.
BC132366 mRNA. Translation: AAI32367.1.
BC132368 mRNA. Translation: AAI32369.1.
CCDSiCCDS27952.1.
RefSeqiNP_001258532.1. NM_001271603.1.
NP_034026.1. NM_009896.2.
UniGeneiMm.130.

3D structure databases

ProteinModelPortaliO35716.
SMRiO35716. Positions 56-212.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198719. 32 interactions.
IntActiO35716. 6 interactions.
MINTiMINT-84865.
STRINGi10090.ENSMUSP00000038121.

PTM databases

iPTMnetiO35716.

Proteomic databases

EPDiO35716.
PaxDbiO35716.
PRIDEiO35716.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038099; ENSMUSP00000038121; ENSMUSG00000038037.
GeneIDi12703.
KEGGimmu:12703.
UCSCiuc007yed.1. mouse.

Organism-specific databases

CTDi8651.
MGIiMGI:1354910. Socs1.

Phylogenomic databases

eggNOGiKOG4566. Eukaryota.
ENOG4111V4J. LUCA.
GeneTreeiENSGT00760000119136.
HOGENOMiHOG000236320.
HOVERGENiHBG002457.
InParanoidiO35716.
KOiK04694.
OMAiETFDCLF.
OrthoDBiEOG7TMZSZ.
PhylomeDBiO35716.
TreeFamiTF321368.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-877300. Interferon gamma signaling.
R-MMU-877312. Regulation of IFNG signaling.
R-MMU-909733. Interferon alpha/beta signaling.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SABIO-RKO35716.

Miscellaneous databases

NextBioi281962.
PROiO35716.
SOURCEiSearch...

Gene expression databases

BgeeiO35716.
CleanExiMM_SOCS1.
GenevisibleiO35716. MM.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000980. SH2.
IPR028411. SOCS1.
IPR001496. SOCS_box.
[Graphical view]
PANTHERiPTHR24369:SF72. PTHR24369:SF72. 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]
SUPFAMiSSF158235. SSF158235. 1 hit.
SSF55550. 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: Thymus.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Thymus.
  4. "SOCS-1 binds to multiple signaling proteins and suppresses Steel factor-dependent proliferation."
    De Sepulveda P., Okkenhaug K., La Rose J., Hawley R.G., Dubreuil P., Rottapel R.
    EMBO J. 18:904-915(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Hematopoietic.
  5. "Regulation of SOCS-1 expression by translational repression."
    Gregorieff A., Pyronnet S., Sonenberg N., Veillette A.
    J. Biol. Chem. 275:21596-21604(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. "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: Skin.
  7. "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].
    Tissue: Lung.
  8. "The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families."
    Kamura T., Sato S., Haque D., Liu L., Kaelin W.G. Jr., Conaway R.C., Conaway J.W.
    Genes Dev. 12:3872-3881(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ELONGIN BC COMPLEX, MUTAGENESIS OF LEU-175 AND CYS-179.
  9. "The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation."
    Zhang J.-G., Farley A., Nicholson S.E., Willson T.A., Zugaro L.M., Simpson R.J., Moritz R.L., Cary D., Richardson R., Hausmann G., Kile B.J., Kent S.B.H., Alexander W.S., Metcalf D., Hilton D.J., Nicola N.A., Baca M.
    Proc. Natl. Acad. Sci. U.S.A. 96:2071-2076(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ELONGIN BC COMPLEX.
  10. Cited for: INTERACTION WITH TRIM8.
  11. "Three distinct domains of SSI-1/SOCS-1/JAB protein are required for its suppression of interleukin 6 signaling."
    Narazaki M., Fujimoto M., Matsumoto T., Morita Y., Saito H., Kajita T., Yoshizaki K., Naka T., Kishimoto T.
    Proc. Natl. Acad. Sci. U.S.A. 95:13130-13134(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  12. "Liver degeneration and lymphoid deficiencies in mice lacking suppressor of cytokine signaling-1."
    Starr R., Metcalf D., Elefanty A.G., Brysha M., Willson T.A., Nicola N.A., Hilton D.J., Alexander W.S.
    Proc. Natl. Acad. Sci. U.S.A. 95:14395-14399(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  13. "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: MUTAGENESIS.
  14. "The JAK-binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loop."
    Yasukawa H., Misawa H., Sakamoto H., Masuhara M., Sasaki A., Wakioka T., Ohtsuka S., Imaizumi T., Matsuda T., Ihle J.N., Yoshimura A.
    EMBO J. 18:1309-1320(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INHIBITION OF JAK2 KINASE ACTIVITY, MUTAGENESIS OF HIS-55; PHE-56; ARG-57; THR-58; PHE-59; ARG-60; SER-61; HIS-62; ASP-64; TYR-65 AND ARG-105.
  15. "A mutant form of JAB/SOCS1 augments the cytokine-induced JAK/STAT pathway by accelerating degradation of wild-type JAB/CIS family proteins through the SOCS-box."
    Hanada T., Yoshida T., Kinjyo I., Minoguchi S., Yasukawa H., Kato S., Mimata H., Nomura Y., Seki Y., Kubo M., Yoshimura A.
    J. Biol. Chem. 276:40746-40754(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PHE-59.
  16. "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.
  17. "Suppressor of cytokine signaling 1 (SOCS-1) and SOCS-3 cause insulin resistance through inhibition of tyrosine phosphorylation of insulin receptor substrate proteins by discrete mechanisms."
    Ueki K., Kondo T., Kahn C.R.
    Mol. Cell. Biol. 24:5434-5446(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INHIBITION OF INSR KINASE ACTIVITY, INTERACTION WITH INSR.

Entry informationi

Entry nameiSOCS1_MOUSE
AccessioniPrimary (citable) accession number: O35716
Secondary accession number(s): A2RT46, O35960, Q3U3L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 142 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

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. SIMILARITY comments
    Index of protein domains and families

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 one 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.