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Q9Y4H2

- IRS2_HUMAN

UniProt

Q9Y4H2 - IRS2_HUMAN

Protein

Insulin receptor substrate 2

Gene

IRS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (29 Mar 2005)
      Previous versions | rss
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    Functioni

    May mediate the control of various cellular processes by insulin.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. signal transducer activity Source: ProtInc

    GO - Biological processi

    1. brain development Source: Ensembl
    2. cell proliferation Source: Ensembl
    3. cellular response to glucose stimulus Source: Ensembl
    4. cellular response to insulin stimulus Source: BHF-UCL
    5. epidermal growth factor receptor signaling pathway Source: Reactome
    6. Fc-epsilon receptor signaling pathway Source: Reactome
    7. fibroblast growth factor receptor signaling pathway Source: Reactome
    8. glucose metabolic process Source: ProtInc
    9. innate immune response Source: Reactome
    10. insulin receptor signaling pathway Source: BHF-UCL
    11. JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
    12. lipid homeostasis Source: BHF-UCL
    13. mammary gland development Source: Ensembl
    14. negative regulation of B cell apoptotic process Source: BHF-UCL
    15. negative regulation of kinase activity Source: BHF-UCL
    16. negative regulation of plasma membrane long-chain fatty acid transport Source: BHF-UCL
    17. neurotrophin TRK receptor signaling pathway Source: Reactome
    18. phosphatidylinositol-mediated signaling Source: Reactome
    19. positive regulation of B cell proliferation Source: BHF-UCL
    20. positive regulation of cell migration Source: Ensembl
    21. positive regulation of cell proliferation Source: BHF-UCL
    22. positive regulation of fatty acid beta-oxidation Source: BHF-UCL
    23. positive regulation of glucose import Source: BHF-UCL
    24. positive regulation of glucose metabolic process Source: BHF-UCL
    25. positive regulation of glycogen biosynthetic process Source: BHF-UCL
    26. positive regulation of insulin secretion Source: BHF-UCL
    27. positive regulation of mesenchymal cell proliferation Source: Ensembl
    28. regulation of lipid metabolic process Source: BHF-UCL
    29. response to glucose Source: BHF-UCL
    30. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Transducer

    Enzyme and pathway databases

    ReactomeiREACT_111133. Growth hormone receptor signaling.
    REACT_12464. PI3K/AKT activation.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_150203. IRS-related events triggered by IGF1R.
    REACT_169118. Signaling by Leptin.
    REACT_508. Signal attenuation.
    REACT_524. SOS-mediated signalling.
    REACT_570. IRS activation.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_976. PI3K Cascade.
    SignaLinkiQ9Y4H2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Insulin receptor substrate 2
    Short name:
    IRS-2
    Gene namesi
    Name:IRS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:6126. IRS2.

    Subcellular locationi

    Cytoplasmcytosol By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA375.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13381338Insulin receptor substrate 2PRO_0000084239Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei306 – 3061Phosphoserine3 Publications
    Modified residuei346 – 3461Phosphoserine1 Publication
    Modified residuei350 – 3501Phosphothreonine2 Publications
    Modified residuei365 – 3651Phosphoserine1 Publication
    Modified residuei384 – 3841Phosphoserine1 Publication
    Modified residuei388 – 3881Phosphoserine4 Publications
    Modified residuei391 – 3911Phosphoserine5 Publications
    Modified residuei523 – 5231Phosphoserine1 Publication
    Modified residuei527 – 5271Phosphothreonine2 Publications
    Modified residuei540 – 5401Phosphotyrosine; by INSRBy similarity
    Modified residuei560 – 5601Phosphoserine3 Publications
    Modified residuei577 – 5771Phosphoserine1 Publication
    Modified residuei579 – 5791Phosphothreonine1 Publication
    Modified residuei580 – 5801Phosphothreonine1 Publication
    Modified residuei594 – 5941Phosphoserine2 Publications
    Modified residuei608 – 6081Phosphoserine1 Publication
    Modified residuei620 – 6201Phosphoserine1 Publication
    Modified residuei653 – 6531Phosphotyrosine; by INSR
    Modified residuei675 – 6751Phosphotyrosine; by INSR1 Publication
    Modified residuei679 – 6791Phosphoserine1 Publication
    Modified residuei735 – 7351Phosphoserine1 Publication
    Modified residuei736 – 7361Phosphoserine2 Publications
    Modified residuei770 – 7701Phosphoserine1 Publication
    Modified residuei779 – 7791Phosphothreonine1 Publication
    Modified residuei828 – 8281Phosphoserine1 Publication
    Modified residuei915 – 9151Phosphoserine5 Publications
    Modified residuei919 – 9191Phosphotyrosine; by INSRBy similarity
    Modified residuei973 – 9731Phosphoserine2 Publications
    Modified residuei978 – 9781Phosphotyrosine; by INSRBy similarity
    Modified residuei1100 – 11001Phosphoserine1 Publication
    Modified residuei1159 – 11591Phosphothreonine1 Publication
    Modified residuei1162 – 11621Phosphoserine1 Publication
    Modified residuei1174 – 11741Phosphoserine1 Publication
    Modified residuei1176 – 11761Phosphoserine3 Publications
    Modified residuei1203 – 12031Phosphoserine1 Publication
    Modified residuei1253 – 12531Phosphotyrosine; by INSRBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y4H2.
    PaxDbiQ9Y4H2.
    PRIDEiQ9Y4H2.

    PTM databases

    PhosphoSiteiQ9Y4H2.

    Miscellaneous databases

    PMAP-CutDBQ9Y4H2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y4H2.
    BgeeiQ9Y4H2.
    CleanExiHS_IRS2.
    GenevestigatoriQ9Y4H2.

    Organism-specific databases

    HPAiCAB016944.

    Interactioni

    Subunit structurei

    Interacts with PHIP.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PIK3R1P279862EBI-1049582,EBI-79464
    SIRT1Q96EB62EBI-1049582,EBI-1802965

    Protein-protein interaction databases

    BioGridi114209. 31 interactions.
    IntActiQ9Y4H2. 10 interactions.
    MINTiMINT-156306.
    STRINGi9606.ENSP00000365016.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FQWX-ray1.93C1097-1105[»]
    3FQXX-ray1.70C1097-1105[»]
    ProteinModelPortaliQ9Y4H2.
    SMRiQ9Y4H2. Positions 31-303.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y4H2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 144129PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini194 – 298105IRS-type PTBPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi540 – 5434YXXM motif 1
    Motifi598 – 6014YXXM motif 2
    Motifi653 – 6564YXXM motif 3
    Motifi675 – 6784YXXM motif 4
    Motifi742 – 7454YXXM motif 5
    Motifi823 – 8264YXXM motif 6
    Motifi1072 – 10754YXXM motif 7

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi19 – 2810Poly-Asn
    Compositional biasi371 – 38010Poly-Ala
    Compositional biasi447 – 4526Poly-Ser
    Compositional biasi460 – 4678Poly-Pro
    Compositional biasi533 – 5375Poly-Gly
    Compositional biasi642 – 6454Poly-Ser
    Compositional biasi694 – 7018Poly-Ala
    Compositional biasi944 – 9474Poly-Ser
    Compositional biasi1031 – 10388Poly-Pro
    Compositional biasi1265 – 127814Poly-ProAdd
    BLAST

    Sequence similaritiesi

    Contains 1 IRS-type PTB domain.PROSITE-ProRule annotation
    Contains 1 PH domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG81285.
    HOVERGENiHBG000542.
    InParanoidiQ9Y4H2.
    KOiK07187.
    OMAiDSCLNIN.
    OrthoDBiEOG7XM2X6.
    PhylomeDBiQ9Y4H2.
    TreeFamiTF325994.

    Family and domain databases

    Gene3Di2.30.29.30. 2 hits.
    InterProiIPR002404. Insln_rcpt_S1.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PfamiPF02174. IRS. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view]
    PRINTSiPR00628. INSULINRSI.
    SMARTiSM00233. PH. 1 hit.
    SM00310. PTBI. 1 hit.
    [Graphical view]
    PROSITEiPS51064. IRS_PTB. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y4H2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASPPRHGPP GPASGDGPNL NNNNNNNNHS VRKCGYLRKQ KHGHKRFFVL     50
    RGPGAGGDEA TAGGGSAPQP PRLEYYESEK KWRSKAGAPK RVIALDCCLN 100
    INKRADAKHK YLIALYTKDE YFAVAAENEQ EQEGWYRALT DLVSEGRAAA 150
    GDAPPAAAPA ASCSASLPGA LGGSAGAAGA EDSYGLVAPA TAAYREVWQV 200
    NLKPKGLGQS KNLTGVYRLC LSARTIGFVK LNCEQPSVTL QLMNIRRCGH 250
    SDSFFFIEVG RSAVTGPGEL WMQADDSVVA QNIHETILEA MKALKELFEF 300
    RPRSKSQSSG SSATHPISVP GARRHHHLVN LPPSQTGLVR RSRTDSLAAT 350
    PPAAKCSSCR VRTASEGDGG AAAGAAAAGA RPVSVAGSPL SPGPVRAPLS 400
    RSHTLSGGCG GRGSKVALLP AGGALQHSRS MSMPVAHSPP AATSPGSLSS 450
    SSGHGSGSYP PPPGPHPPLP HPLHHGPGQR PSSGSASASG SPSDPGFMSL 500
    DEYGSSPGDL RAFCSHRSNT PESIAETPPA RDGGGGGEFY GYMTMDRPLS 550
    HCGRSYRRVS GDAAQDLDRG LRKRTYSLTT PARQRPVPQP SSASLDEYTL 600
    MRATFSGSAG RLCPSCPASS PKVAYHPYPE DYGDIEIGSH RSSSSNLGAD 650
    DGYMPMTPGA ALAGSGSGSC RSDDYMPMSP ASVSAPKQIL QPRAAAAAAA 700
    AVPSAGPAGP APTSAAGRTF PASGGGYKAS SPAESSPEDS GYMRMWCGSK 750
    LSMEHADGKL LPNGDYLNVS PSDAVTTGTP PDFFSAALHP GGEPLRGVPG 800
    CCYSSLPRSY KAPYTCGGDS DQYVLMSSPV GRILEEERLE PQATPGPSQA 850
    ASAFGAGPTQ PPHPVVPSPV RPSGGRPEGF LGQRGRAVRP TRLSLEGLPS 900
    LPSMHEYPLP PEPKSPGEYI NIDFGEPGAR LSPPAPPLLA SAASSSSLLS 950
    ASSPASSLGS GTPGTSSDSR QRSPLSDYMN LDFSSPKSPK PGAPSGHPVG 1000
    SLDGLLSPEA SSPYPPLPPR PSASPSSSLQ PPPPPPAPGE LYRLPPASAV 1050
    ATAQGPGAAS SLSSDTGDNG DYTEMAFGVA ATPPQPIAAP PKPEAARVAS 1100
    PTSGVKRLSL MEQVSGVEAF LQASQPPDPH RGAKVIRADP QGGRRRHSSE 1150
    TFSSTTTVTP VSPSFAHNPK RHNSASVENV SLRKSSEGGV GVGPGGGDEP 1200
    PTSPRQLQPA PPLAPQGRPW TPGQPGGLVG CPGSGGSPMR RETSAGFQNG 1250
    LNYIAIDVRE EPGLPPQPQP PPPPLPQPGD KSSWGRTRSL GGLISAVGVG 1300
    STGGGCGGPG PGALPPANTY ASIDFLSHHL KEATIVKE 1338
    Length:1,338
    Mass (Da):137,334
    Last modified:March 29, 2005 - v2
    Checksum:i58E569E8BDBAF3D7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281N → NN in AAD21531. (PubMed:10077005)Curated
    Sequence conflicti39 – 413KQK → NEE in AAD21531. (PubMed:10077005)Curated
    Sequence conflicti59 – 591E → K in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti81 – 811K → N in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti107 – 1071A → P in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti171 – 1711L → V in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti371 – 3711A → R in AAD21531. (PubMed:10077005)Curated
    Sequence conflicti379 – 3824GARP → AQRL in AAD21531. (PubMed:10077005)Curated
    Sequence conflicti406 – 4061S → I in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti410 – 41910GGRGSKVALL → RAAGTKWHCF in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti424 – 4241A → G in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti436 – 4383AHS → EHL in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti453 – 4531G → D in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti456 – 4561S → W in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti468 – 4681P → L in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti662 – 6621L → F in AAD21531. (PubMed:10077005)Curated
    Sequence conflicti704 – 7041S → F in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti714 – 7141S → F in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti848 – 8481S → T in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti872 – 8721P → R in AAD21531. (PubMed:10077005)Curated
    Sequence conflicti875 – 8784GRPE → RRS in AAD21531. (PubMed:10077005)Curated
    Sequence conflicti956 – 9561S → L in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti1252 – 12521N → K in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti1303 – 13031G → R in BAA24500. (PubMed:9312143)Curated
    Sequence conflicti1314 – 133825LPPAN…TIVKE → PAPCPTTYAQH in BAA24500. (PubMed:9312143)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti789 – 7891H → Y.
    Corresponds to variant rs35223808 [ dbSNP | Ensembl ].
    VAR_033992
    Natural varianti879 – 8791G → S.1 Publication
    VAR_021557
    Natural varianti882 – 8821G → A.1 Publication
    VAR_021558
    Natural varianti999 – 9991V → M.
    Corresponds to variant rs35927012 [ dbSNP | Ensembl ].
    VAR_033993
    Natural varianti1057 – 10571G → D.1 Publication
    Corresponds to variant rs1805097 [ dbSNP | Ensembl ].
    VAR_014857

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000732 Genomic DNA. Translation: BAA24500.1.
    AF073310 mRNA. Translation: AAD21531.1.
    AF322115, AF322114 Genomic DNA. Translation: AAG50013.1.
    AL162497 Genomic DNA. Translation: CAH72369.1.
    AF288517 Genomic DNA. Translation: AAK83053.1.
    CCDSiCCDS9510.1.
    RefSeqiNP_003740.2. NM_003749.2.
    UniGeneiHs.442344.

    Genome annotation databases

    EnsembliENST00000375856; ENSP00000365016; ENSG00000185950.
    GeneIDi8660.
    KEGGihsa:8660.
    UCSCiuc001vqv.3. human.

    Polymorphism databases

    DMDMi62298062.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000732 Genomic DNA. Translation: BAA24500.1 .
    AF073310 mRNA. Translation: AAD21531.1 .
    AF322115 , AF322114 Genomic DNA. Translation: AAG50013.1 .
    AL162497 Genomic DNA. Translation: CAH72369.1 .
    AF288517 Genomic DNA. Translation: AAK83053.1 .
    CCDSi CCDS9510.1.
    RefSeqi NP_003740.2. NM_003749.2.
    UniGenei Hs.442344.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FQW X-ray 1.93 C 1097-1105 [» ]
    3FQX X-ray 1.70 C 1097-1105 [» ]
    ProteinModelPortali Q9Y4H2.
    SMRi Q9Y4H2. Positions 31-303.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114209. 31 interactions.
    IntActi Q9Y4H2. 10 interactions.
    MINTi MINT-156306.
    STRINGi 9606.ENSP00000365016.

    PTM databases

    PhosphoSitei Q9Y4H2.

    Polymorphism databases

    DMDMi 62298062.

    Proteomic databases

    MaxQBi Q9Y4H2.
    PaxDbi Q9Y4H2.
    PRIDEi Q9Y4H2.

    Protocols and materials databases

    DNASUi 8660.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375856 ; ENSP00000365016 ; ENSG00000185950 .
    GeneIDi 8660.
    KEGGi hsa:8660.
    UCSCi uc001vqv.3. human.

    Organism-specific databases

    CTDi 8660.
    GeneCardsi GC13M110406.
    HGNCi HGNC:6126. IRS2.
    HPAi CAB016944.
    MIMi 600797. gene.
    neXtProti NX_Q9Y4H2.
    PharmGKBi PA375.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG81285.
    HOVERGENi HBG000542.
    InParanoidi Q9Y4H2.
    KOi K07187.
    OMAi DSCLNIN.
    OrthoDBi EOG7XM2X6.
    PhylomeDBi Q9Y4H2.
    TreeFami TF325994.

    Enzyme and pathway databases

    Reactomei REACT_111133. Growth hormone receptor signaling.
    REACT_12464. PI3K/AKT activation.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_150203. IRS-related events triggered by IGF1R.
    REACT_169118. Signaling by Leptin.
    REACT_508. Signal attenuation.
    REACT_524. SOS-mediated signalling.
    REACT_570. IRS activation.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_976. PI3K Cascade.
    SignaLinki Q9Y4H2.

    Miscellaneous databases

    ChiTaRSi IRS2. human.
    EvolutionaryTracei Q9Y4H2.
    GeneWikii IRS2.
    GenomeRNAii 8660.
    NextBioi 32479.
    PMAP-CutDB Q9Y4H2.
    PROi Q9Y4H2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y4H2.
    Bgeei Q9Y4H2.
    CleanExi HS_IRS2.
    Genevestigatori Q9Y4H2.

    Family and domain databases

    Gene3Di 2.30.29.30. 2 hits.
    InterProi IPR002404. Insln_rcpt_S1.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF02174. IRS. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view ]
    PRINTSi PR00628. INSULINRSI.
    SMARTi SM00233. PH. 1 hit.
    SM00310. PTBI. 1 hit.
    [Graphical view ]
    PROSITEi PS51064. IRS_PTB. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "14-3-3 protein binds to insulin receptor substrate-1, one of the binding sites of which is in the phosphotyrosine binding domain."
      Ogihara T., Isobe T., Ichimura T., Taoka M., Funaki M., Sakoda H., Onishi Y., Inukai K., Anai M., Fukushima Y., Kikuchi M., Yazaki Y., Oka Y., Asano T.
      J. Biol. Chem. 272:25267-25274(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Human insulin receptor substrate-2 (IRS-2) is a primary progesterone response gene."
      Vassen L., Wegrzyn W., Klein-Hitpass L.
      Mol. Endocrinol. 13:485-494(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Insulin receptor substrate 2 gene sequence."
      Heyne B.
      Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Two missense mutations in insulin receptor substrate 2 (G879S and G882A)."
      Heyne B., Gehrisch S., Jaross W.
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE OF 1-1337, VARIANTS SER-879 AND ALA-882.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388; SER-391 AND SER-560, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-350 AND THR-527, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-915, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388; SER-391 AND SER-915, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-346; THR-350; SER-365; SER-384; SER-388; SER-391; SER-523; THR-527; SER-577; THR-579; THR-580; SER-594; SER-608; SER-620; SER-679; SER-735; SER-736; SER-770; THR-779; SER-828; SER-915; SER-973; SER-1100; THR-1159; SER-1162; SER-1174; SER-1176 AND SER-1203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-388; SER-391; SER-560; SER-594; TYR-675; SER-736; SER-915 AND SER-1176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-560; SER-915; SER-973 AND SER-1176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Complex haplotypes of IRS2 gene are associated with severe obesity and reveal heterogeneity in the effect of Gly1057Asp mutation."
      Lautier C., El Mkadem S.A., Renard E., Brun J.F., Gris J.-C., Bringer J., Grigorescu F.
      Hum. Genet. 113:34-43(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASP-1057.

    Entry informationi

    Entry nameiIRS2_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y4H2
    Secondary accession number(s): Q96RR2, Q9BZG0, Q9Y6I5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3