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Protein

Insulin receptor substrate 2

Gene

IRS2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May mediate the control of various cellular processes by insulin.

GO - Molecular functioni

  1. insulin receptor binding Source: GO_Central
  2. phosphatidylinositol 3-kinase binding Source: GO_Central
  3. 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
Complete GO annotation...

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: GO_Central
  2. plasma membrane Source: GO_Central
Complete GO annotation...

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 – 5941Phosphoserine3 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 – 9151Phosphoserine6 Publications
Modified residuei919 – 9191Phosphotyrosine; by INSRBy similarity
Modified residuei973 – 9731Phosphoserine2 Publications
Modified residuei978 – 9781Phosphotyrosine; by INSRBy similarity
Modified residuei1082 – 10821Phosphothreonine1 Publication
Modified residuei1100 – 11001Phosphoserine2 Publications
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

BgeeiQ9Y4H2.
CleanExiHS_IRS2.
ExpressionAtlasiQ9Y4H2. baseline and differential.
GenevestigatoriQ9Y4H2.

Organism-specific databases

HPAiCAB016944.
HPA054664.

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. 33 interactions.
IntActiQ9Y4H2. 10 interactions.
MINTiMINT-156306.
STRINGi9606.ENSP00000365016.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00530000063420.
HOVERGENiHBG000542.
InParanoidiQ9Y4H2.
KOiK07187.
OMAiTRRHLNN.
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

        10         20         30         40         50
MASPPRHGPP GPASGDGPNL NNNNNNNNHS VRKCGYLRKQ KHGHKRFFVL
60 70 80 90 100
RGPGAGGDEA TAGGGSAPQP PRLEYYESEK KWRSKAGAPK RVIALDCCLN
110 120 130 140 150
INKRADAKHK YLIALYTKDE YFAVAAENEQ EQEGWYRALT DLVSEGRAAA
160 170 180 190 200
GDAPPAAAPA ASCSASLPGA LGGSAGAAGA EDSYGLVAPA TAAYREVWQV
210 220 230 240 250
NLKPKGLGQS KNLTGVYRLC LSARTIGFVK LNCEQPSVTL QLMNIRRCGH
260 270 280 290 300
SDSFFFIEVG RSAVTGPGEL WMQADDSVVA QNIHETILEA MKALKELFEF
310 320 330 340 350
RPRSKSQSSG SSATHPISVP GARRHHHLVN LPPSQTGLVR RSRTDSLAAT
360 370 380 390 400
PPAAKCSSCR VRTASEGDGG AAAGAAAAGA RPVSVAGSPL SPGPVRAPLS
410 420 430 440 450
RSHTLSGGCG GRGSKVALLP AGGALQHSRS MSMPVAHSPP AATSPGSLSS
460 470 480 490 500
SSGHGSGSYP PPPGPHPPLP HPLHHGPGQR PSSGSASASG SPSDPGFMSL
510 520 530 540 550
DEYGSSPGDL RAFCSHRSNT PESIAETPPA RDGGGGGEFY GYMTMDRPLS
560 570 580 590 600
HCGRSYRRVS GDAAQDLDRG LRKRTYSLTT PARQRPVPQP SSASLDEYTL
610 620 630 640 650
MRATFSGSAG RLCPSCPASS PKVAYHPYPE DYGDIEIGSH RSSSSNLGAD
660 670 680 690 700
DGYMPMTPGA ALAGSGSGSC RSDDYMPMSP ASVSAPKQIL QPRAAAAAAA
710 720 730 740 750
AVPSAGPAGP APTSAAGRTF PASGGGYKAS SPAESSPEDS GYMRMWCGSK
760 770 780 790 800
LSMEHADGKL LPNGDYLNVS PSDAVTTGTP PDFFSAALHP GGEPLRGVPG
810 820 830 840 850
CCYSSLPRSY KAPYTCGGDS DQYVLMSSPV GRILEEERLE PQATPGPSQA
860 870 880 890 900
ASAFGAGPTQ PPHPVVPSPV RPSGGRPEGF LGQRGRAVRP TRLSLEGLPS
910 920 930 940 950
LPSMHEYPLP PEPKSPGEYI NIDFGEPGAR LSPPAPPLLA SAASSSSLLS
960 970 980 990 1000
ASSPASSLGS GTPGTSSDSR QRSPLSDYMN LDFSSPKSPK PGAPSGHPVG
1010 1020 1030 1040 1050
SLDGLLSPEA SSPYPPLPPR PSASPSSSLQ PPPPPPAPGE LYRLPPASAV
1060 1070 1080 1090 1100
ATAQGPGAAS SLSSDTGDNG DYTEMAFGVA ATPPQPIAAP PKPEAARVAS
1110 1120 1130 1140 1150
PTSGVKRLSL MEQVSGVEAF LQASQPPDPH RGAKVIRADP QGGRRRHSSE
1160 1170 1180 1190 1200
TFSSTTTVTP VSPSFAHNPK RHNSASVENV SLRKSSEGGV GVGPGGGDEP
1210 1220 1230 1240 1250
PTSPRQLQPA PPLAPQGRPW TPGQPGGLVG CPGSGGSPMR RETSAGFQNG
1260 1270 1280 1290 1300
LNYIAIDVRE EPGLPPQPQP PPPPLPQPGD KSSWGRTRSL GGLISAVGVG
1310 1320 1330
STGGGCGGPG PGALPPANTY ASIDFLSHHL KEATIVKE
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi114209. 33 interactions.
IntActiQ9Y4H2. 10 interactions.
MINTiMINT-156306.
STRINGi9606.ENSP00000365016.

PTM databases

PhosphoSiteiQ9Y4H2.

Polymorphism databases

DMDMi62298062.

Proteomic databases

MaxQBiQ9Y4H2.
PaxDbiQ9Y4H2.
PRIDEiQ9Y4H2.

Protocols and materials databases

DNASUi8660.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8660.
GeneCardsiGC13M110406.
HGNCiHGNC:6126. IRS2.
HPAiCAB016944.
HPA054664.
MIMi600797. gene.
neXtProtiNX_Q9Y4H2.
PharmGKBiPA375.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG81285.
GeneTreeiENSGT00530000063420.
HOVERGENiHBG000542.
InParanoidiQ9Y4H2.
KOiK07187.
OMAiTRRHLNN.
OrthoDBiEOG7XM2X6.
PhylomeDBiQ9Y4H2.
TreeFamiTF325994.

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.

Miscellaneous databases

ChiTaRSiIRS2. human.
EvolutionaryTraceiQ9Y4H2.
GeneWikiiIRS2.
GenomeRNAii8660.
NextBioi32479.
PMAP-CutDBQ9Y4H2.
PROiQ9Y4H2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y4H2.
CleanExiHS_IRS2.
ExpressionAtlasiQ9Y4H2. baseline and differential.
GenevestigatoriQ9Y4H2.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 AND SER-1176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594; SER-915; SER-973; THR-1082 AND SER-1100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "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: March 4, 2015
This is version 131 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

Similar proteinsi

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