Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y4H2 (IRS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Insulin receptor substrate 2

Short name=IRS-2
Gene names
Name:IRS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1338 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May mediate the control of various cellular processes by insulin.

Subunit structure

Interacts with PHIP By similarity.

Subcellular location

Cytoplasmcytosol By similarity.

Sequence similarities

Contains 1 IRS-type PTB domain.

Contains 1 PH domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   Molecular functionTransducer
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

JAK-STAT cascade involved in growth hormone signaling pathway

Traceable author statement. Source: Reactome

brain development

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to insulin stimulus

Inferred from mutant phenotype PubMed 16814735. Source: BHF-UCL

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

glucose metabolic process

Traceable author statement PubMed 9495343. Source: ProtInc

innate immune response

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

lipid homeostasis

Traceable author statement PubMed 16814735. Source: BHF-UCL

mammary gland development

Inferred from electronic annotation. Source: Ensembl

negative regulation of B cell apoptotic process

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of kinase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of plasma membrane long-chain fatty acid transport

Inferred from mutant phenotype PubMed 16814735. Source: BHF-UCL

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

positive regulation of B cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Non-traceable author statement PubMed 17925406. Source: BHF-UCL

positive regulation of fatty acid beta-oxidation

Inferred from mutant phenotype PubMed 16814735. Source: BHF-UCL

positive regulation of glucose import

Inferred from mutant phenotype PubMed 16814735. Source: BHF-UCL

positive regulation of glucose metabolic process

Inferred from mutant phenotype PubMed 16814735. Source: BHF-UCL

positive regulation of glycogen biosynthetic process

Inferred from mutant phenotype PubMed 16814735. Source: BHF-UCL

positive regulation of insulin secretion

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of mesenchymal cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of lipid metabolic process

Traceable author statement PubMed 16814735. Source: BHF-UCL

response to glucose

Inferred from sequence or structural similarity. Source: BHF-UCL

signal transduction

Traceable author statement PubMed 7675087. Source: ProtInc

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 17901049PubMed 21241768PubMed 23617393. Source: IntAct

signal transducer activity

Traceable author statement PubMed 7675087PubMed 9495343. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PIK3R1P279862EBI-1049582,EBI-79464
SIRT1Q96EB62EBI-1049582,EBI-1802965

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13381338Insulin receptor substrate 2
PRO_0000084239

Regions

Domain16 – 144129PH
Domain194 – 298105IRS-type PTB
Motif540 – 5434YXXM motif 1
Motif598 – 6014YXXM motif 2
Motif653 – 6564YXXM motif 3
Motif675 – 6784YXXM motif 4
Motif742 – 7454YXXM motif 5
Motif823 – 8264YXXM motif 6
Motif1072 – 10754YXXM motif 7
Compositional bias19 – 2810Poly-Asn
Compositional bias371 – 38010Poly-Ala
Compositional bias447 – 4526Poly-Ser
Compositional bias460 – 4678Poly-Pro
Compositional bias533 – 5375Poly-Gly
Compositional bias642 – 6454Poly-Ser
Compositional bias694 – 7018Poly-Ala
Compositional bias944 – 9474Poly-Ser
Compositional bias1031 – 10388Poly-Pro
Compositional bias1265 – 127814Poly-Pro

Amino acid modifications

Modified residue3061Phosphoserine Ref.10 Ref.13 Ref.15
Modified residue3461Phosphoserine Ref.10
Modified residue3501Phosphothreonine Ref.7 Ref.10
Modified residue3651Phosphoserine Ref.10
Modified residue3841Phosphoserine Ref.10
Modified residue3881Phosphoserine Ref.6 Ref.9 Ref.10 Ref.13
Modified residue3911Phosphoserine Ref.6 Ref.9 Ref.10 Ref.12 Ref.13
Modified residue5231Phosphoserine Ref.10
Modified residue5271Phosphothreonine Ref.7 Ref.10
Modified residue5401Phosphotyrosine; by INSR By similarity
Modified residue5601Phosphoserine Ref.6 Ref.13 Ref.15
Modified residue5771Phosphoserine Ref.10
Modified residue5791Phosphothreonine Ref.10
Modified residue5801Phosphothreonine Ref.10
Modified residue5941Phosphoserine Ref.10 Ref.13
Modified residue6081Phosphoserine Ref.10
Modified residue6201Phosphoserine Ref.10
Modified residue6531Phosphotyrosine; by INSR
Modified residue6751Phosphotyrosine; by INSR Ref.13
Modified residue6791Phosphoserine Ref.10
Modified residue7351Phosphoserine Ref.10
Modified residue7361Phosphoserine Ref.10 Ref.13
Modified residue7701Phosphoserine Ref.10
Modified residue7791Phosphothreonine Ref.10
Modified residue8281Phosphoserine Ref.10
Modified residue9151Phosphoserine Ref.8 Ref.9 Ref.10 Ref.13 Ref.15
Modified residue9191Phosphotyrosine; by INSR By similarity
Modified residue9731Phosphoserine Ref.10 Ref.15
Modified residue9781Phosphotyrosine; by INSR By similarity
Modified residue11001Phosphoserine Ref.10
Modified residue11591Phosphothreonine Ref.10
Modified residue11621Phosphoserine Ref.10
Modified residue11741Phosphoserine Ref.10
Modified residue11761Phosphoserine Ref.10 Ref.13 Ref.15
Modified residue12031Phosphoserine Ref.10
Modified residue12531Phosphotyrosine; by INSR By similarity

Natural variations

Natural variant7891H → Y.
Corresponds to variant rs35223808 [ dbSNP | Ensembl ].
VAR_033992
Natural variant8791G → S. Ref.5
VAR_021557
Natural variant8821G → A. Ref.5
VAR_021558
Natural variant9991V → M.
Corresponds to variant rs35927012 [ dbSNP | Ensembl ].
VAR_033993
Natural variant10571G → D. Ref.16
Corresponds to variant rs1805097 [ dbSNP | Ensembl ].
VAR_014857

Experimental info

Sequence conflict281N → NN in AAD21531. Ref.2
Sequence conflict39 – 413KQK → NEE in AAD21531. Ref.2
Sequence conflict591E → K in BAA24500. Ref.1
Sequence conflict811K → N in BAA24500. Ref.1
Sequence conflict1071A → P in BAA24500. Ref.1
Sequence conflict1711L → V in BAA24500. Ref.1
Sequence conflict3711A → R in AAD21531. Ref.2
Sequence conflict379 – 3824GARP → AQRL in AAD21531. Ref.2
Sequence conflict4061S → I in BAA24500. Ref.1
Sequence conflict410 – 41910GGRGSKVALL → RAAGTKWHCF in BAA24500. Ref.1
Sequence conflict4241A → G in BAA24500. Ref.1
Sequence conflict436 – 4383AHS → EHL in BAA24500. Ref.1
Sequence conflict4531G → D in BAA24500. Ref.1
Sequence conflict4561S → W in BAA24500. Ref.1
Sequence conflict4681P → L in BAA24500. Ref.1
Sequence conflict6621L → F in AAD21531. Ref.2
Sequence conflict7041S → F in BAA24500. Ref.1
Sequence conflict7141S → F in BAA24500. Ref.1
Sequence conflict8481S → T in BAA24500. Ref.1
Sequence conflict8721P → R in AAD21531. Ref.2
Sequence conflict875 – 8784GRPE → RRS in AAD21531. Ref.2
Sequence conflict9561S → L in BAA24500. Ref.1
Sequence conflict12521N → K in BAA24500. Ref.1
Sequence conflict13031G → R in BAA24500. Ref.1
Sequence conflict1314 – 133825LPPAN…TIVKE → PAPCPTTYAQH in BAA24500. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Y4H2 [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: 58E569E8BDBAF3D7

FASTA1,338137,334
        10         20         30         40         50         60 
MASPPRHGPP GPASGDGPNL NNNNNNNNHS VRKCGYLRKQ KHGHKRFFVL RGPGAGGDEA 

        70         80         90        100        110        120 
TAGGGSAPQP PRLEYYESEK KWRSKAGAPK RVIALDCCLN INKRADAKHK YLIALYTKDE 

       130        140        150        160        170        180 
YFAVAAENEQ EQEGWYRALT DLVSEGRAAA GDAPPAAAPA ASCSASLPGA LGGSAGAAGA 

       190        200        210        220        230        240 
EDSYGLVAPA TAAYREVWQV NLKPKGLGQS KNLTGVYRLC LSARTIGFVK LNCEQPSVTL 

       250        260        270        280        290        300 
QLMNIRRCGH SDSFFFIEVG RSAVTGPGEL WMQADDSVVA QNIHETILEA MKALKELFEF 

       310        320        330        340        350        360 
RPRSKSQSSG SSATHPISVP GARRHHHLVN LPPSQTGLVR RSRTDSLAAT PPAAKCSSCR 

       370        380        390        400        410        420 
VRTASEGDGG AAAGAAAAGA RPVSVAGSPL SPGPVRAPLS RSHTLSGGCG GRGSKVALLP 

       430        440        450        460        470        480 
AGGALQHSRS MSMPVAHSPP AATSPGSLSS SSGHGSGSYP PPPGPHPPLP HPLHHGPGQR 

       490        500        510        520        530        540 
PSSGSASASG SPSDPGFMSL DEYGSSPGDL RAFCSHRSNT PESIAETPPA RDGGGGGEFY 

       550        560        570        580        590        600 
GYMTMDRPLS HCGRSYRRVS GDAAQDLDRG LRKRTYSLTT PARQRPVPQP SSASLDEYTL 

       610        620        630        640        650        660 
MRATFSGSAG RLCPSCPASS PKVAYHPYPE DYGDIEIGSH RSSSSNLGAD DGYMPMTPGA 

       670        680        690        700        710        720 
ALAGSGSGSC RSDDYMPMSP ASVSAPKQIL QPRAAAAAAA AVPSAGPAGP APTSAAGRTF 

       730        740        750        760        770        780 
PASGGGYKAS SPAESSPEDS GYMRMWCGSK LSMEHADGKL LPNGDYLNVS PSDAVTTGTP 

       790        800        810        820        830        840 
PDFFSAALHP GGEPLRGVPG CCYSSLPRSY KAPYTCGGDS DQYVLMSSPV GRILEEERLE 

       850        860        870        880        890        900 
PQATPGPSQA ASAFGAGPTQ PPHPVVPSPV RPSGGRPEGF LGQRGRAVRP TRLSLEGLPS 

       910        920        930        940        950        960 
LPSMHEYPLP PEPKSPGEYI NIDFGEPGAR LSPPAPPLLA SAASSSSLLS ASSPASSLGS 

       970        980        990       1000       1010       1020 
GTPGTSSDSR QRSPLSDYMN LDFSSPKSPK PGAPSGHPVG SLDGLLSPEA SSPYPPLPPR 

      1030       1040       1050       1060       1070       1080 
PSASPSSSLQ PPPPPPAPGE LYRLPPASAV ATAQGPGAAS SLSSDTGDNG DYTEMAFGVA 

      1090       1100       1110       1120       1130       1140 
ATPPQPIAAP PKPEAARVAS PTSGVKRLSL MEQVSGVEAF LQASQPPDPH RGAKVIRADP 

      1150       1160       1170       1180       1190       1200 
QGGRRRHSSE TFSSTTTVTP VSPSFAHNPK RHNSASVENV SLRKSSEGGV GVGPGGGDEP 

      1210       1220       1230       1240       1250       1260 
PTSPRQLQPA PPLAPQGRPW TPGQPGGLVG CPGSGGSPMR RETSAGFQNG LNYIAIDVRE 

      1270       1280       1290       1300       1310       1320 
EPGLPPQPQP PPPPLPQPGD KSSWGRTRSL GGLISAVGVG STGGGCGGPG PGALPPANTY 

      1330 
ASIDFLSHHL KEATIVKE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388; SER-391 AND SER-915, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9510.1.
RefSeqNP_003740.2. NM_003749.2.
UniGeneHs.442344.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FQWX-ray1.93C1097-1105[»]
3FQXX-ray1.70C1097-1105[»]
ProteinModelPortalQ9Y4H2.
SMRQ9Y4H2. Positions 31-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114209. 31 interactions.
IntActQ9Y4H2. 10 interactions.
MINTMINT-156306.
STRING9606.ENSP00000365016.

PTM databases

PhosphoSiteQ9Y4H2.

Polymorphism databases

DMDM62298062.

Proteomic databases

MaxQBQ9Y4H2.
PaxDbQ9Y4H2.
PRIDEQ9Y4H2.

Protocols and materials databases

DNASU8660.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375856; ENSP00000365016; ENSG00000185950.
GeneID8660.
KEGGhsa:8660.
UCSCuc001vqv.3. human.

Organism-specific databases

CTD8660.
GeneCardsGC13M110406.
HGNCHGNC:6126. IRS2.
HPACAB016944.
MIM600797. gene.
neXtProtNX_Q9Y4H2.
PharmGKBPA375.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG81285.
HOVERGENHBG000542.
InParanoidQ9Y4H2.
KOK07187.
OMADSCLNIN.
OrthoDBEOG7XM2X6.
PhylomeDBQ9Y4H2.
TreeFamTF325994.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkQ9Y4H2.

Gene expression databases

ArrayExpressQ9Y4H2.
BgeeQ9Y4H2.
CleanExHS_IRS2.
GenevestigatorQ9Y4H2.

Family and domain databases

Gene3D2.30.29.30. 2 hits.
InterProIPR002404. Insln_rcpt_S1.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF02174. IRS. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSPR00628. INSULINRSI.
SMARTSM00233. PH. 1 hit.
SM00310. PTBI. 1 hit.
[Graphical view]
PROSITEPS51064. IRS_PTB. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIRS2. human.
EvolutionaryTraceQ9Y4H2.
GeneWikiIRS2.
GenomeRNAi8660.
NextBio32479.
PMAP-CutDBQ9Y4H2.
PROQ9Y4H2.
SOURCESearch...

Entry information

Entry nameIRS2_HUMAN
AccessionPrimary (citable) accession number: Q9Y4H2
Secondary accession number(s): Q96RR2, Q9BZG0, Q9Y6I5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: March 29, 2005
Last modified: July 9, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM