Q9Y4H2 (IRS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Insulin receptor substrate 2
Short name=IRS-2

Gene names

Name:

IRS2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1338 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytosol By similarity.
Sequence similarities	Contains 1 IRS-type PTB domain. Contains 1 PH domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Transducer
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JAK-STAT cascade involved in growth hormone signaling pathway Traceable author statement. Source: Reactome brain development Inferred from electronic annotation. Source: Compara cell proliferation Inferred from electronic annotation. Source: Compara glucose metabolic process Traceable author statement PubMed 9495343. Source: ProtInc 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: Compara 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 nerve growth factor 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: Compara 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 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: Compara response to glucose stimulus Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	cytosol Traceable author statement. Source: Reactome plasma membrane Traceable author statement. Source: Reactome
Molecular_function	phospholipid binding Inferred from electronic annotation. Source: InterPro signal transducer activity Traceable author statement PubMed 7675087PubMed 9495343. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SIRT1	Q96EB6	2	EBI-1049582,EBI-1802965

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1338	1338	Insulin receptor substrate 2		PRO_0000084239
Regions
	Domain	16 – 144	129	PH
	Domain	194 – 298	105	IRS-type PTB
	Motif	540 – 543	4	YXXM motif 1
	Motif	598 – 601	4	YXXM motif 2
	Motif	653 – 656	4	YXXM motif 3
	Motif	675 – 678	4	YXXM motif 4
	Motif	742 – 745	4	YXXM motif 5
	Motif	823 – 826	4	YXXM motif 6
	Motif	1072 – 1075	4	YXXM motif 7
	Compositional bias	19 – 28	10	Poly-Asn
	Compositional bias	371 – 380	10	Poly-Ala
	Compositional bias	447 – 452	6	Poly-Ser
	Compositional bias	460 – 467	8	Poly-Pro
	Compositional bias	533 – 537	5	Poly-Gly
	Compositional bias	642 – 645	4	Poly-Ser
	Compositional bias	694 – 701	8	Poly-Ala
	Compositional bias	944 – 947	4	Poly-Ser
	Compositional bias	1031 – 1038	8	Poly-Pro
	Compositional bias	1265 – 1278	14	Poly-Pro
Amino acid modifications
	Modified residue	306	1	Phosphoserine Ref.10 Ref.12 Ref.14
	Modified residue	346	1	Phosphoserine Ref.10
	Modified residue	350	1	Phosphothreonine Ref.7 Ref.10
	Modified residue	365	1	Phosphoserine Ref.10
	Modified residue	384	1	Phosphoserine Ref.10
	Modified residue	388	1	Phosphoserine Ref.6 Ref.9 Ref.10 Ref.12
	Modified residue	391	1	Phosphoserine Ref.6 Ref.9 Ref.10 Ref.11 Ref.12
	Modified residue	523	1	Phosphoserine Ref.10
	Modified residue	527	1	Phosphothreonine Ref.7 Ref.10
	Modified residue	540	1	Phosphotyrosine; by INSR By similarity
	Modified residue	560	1	Phosphoserine Ref.6 Ref.12 Ref.14
	Modified residue	577	1	Phosphoserine Ref.10
	Modified residue	579	1	Phosphothreonine Ref.10
	Modified residue	580	1	Phosphothreonine Ref.10
	Modified residue	594	1	Phosphoserine Ref.10 Ref.12
	Modified residue	608	1	Phosphoserine Ref.10
	Modified residue	620	1	Phosphoserine Ref.10
	Modified residue	653	1	Phosphotyrosine; by INSR
	Modified residue	675	1	Phosphotyrosine; by INSR Ref.12
	Modified residue	679	1	Phosphoserine Ref.10
	Modified residue	735	1	Phosphoserine Ref.10
	Modified residue	736	1	Phosphoserine Ref.10 Ref.12
	Modified residue	770	1	Phosphoserine Ref.10
	Modified residue	779	1	Phosphothreonine Ref.10
	Modified residue	828	1	Phosphoserine Ref.10
	Modified residue	915	1	Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12 Ref.14
	Modified residue	919	1	Phosphotyrosine; by INSR By similarity
	Modified residue	973	1	Phosphoserine Ref.10 Ref.14
	Modified residue	978	1	Phosphotyrosine; by INSR By similarity
	Modified residue	1100	1	Phosphoserine Ref.10
	Modified residue	1159	1	Phosphothreonine Ref.10
	Modified residue	1162	1	Phosphoserine Ref.10
	Modified residue	1174	1	Phosphoserine Ref.10
	Modified residue	1176	1	Phosphoserine Ref.10 Ref.12 Ref.14
	Modified residue	1203	1	Phosphoserine Ref.10
	Modified residue	1253	1	Phosphotyrosine; by INSR By similarity
Natural variations
	Natural variant	789	1	H → Y. Corresponds to variant rs35223808 [ dbSNP | Ensembl ].		VAR_033992
	Natural variant	879	1	G → S. Ref.5		VAR_021557
	Natural variant	882	1	G → A. Ref.5		VAR_021558
	Natural variant	999	1	V → M. Corresponds to variant rs35927012 [ dbSNP | Ensembl ].		VAR_033993
	Natural variant	1057	1	G → D. Ref.15 Corresponds to variant rs1805097 [ dbSNP | Ensembl ].		VAR_014857
Experimental info
	Sequence conflict	28	1	N → NN in AAD21531. Ref.2
	Sequence conflict	39 – 41	3	KQK → NEE in AAD21531. Ref.2
	Sequence conflict	59	1	E → K in BAA24500. Ref.1
	Sequence conflict	81	1	K → N in BAA24500. Ref.1
	Sequence conflict	107	1	A → P in BAA24500. Ref.1
	Sequence conflict	171	1	L → V in BAA24500. Ref.1
	Sequence conflict	371	1	A → R in AAD21531. Ref.2
	Sequence conflict	379 – 382	4	GARP → AQRL in AAD21531. Ref.2
	Sequence conflict	406	1	S → I in BAA24500. Ref.1
	Sequence conflict	410 – 419	10	GGRGSKVALL → RAAGTKWHCF in BAA24500. Ref.1
	Sequence conflict	424	1	A → G in BAA24500. Ref.1
	Sequence conflict	436 – 438	3	AHS → EHL in BAA24500. Ref.1
	Sequence conflict	453	1	G → D in BAA24500. Ref.1
	Sequence conflict	456	1	S → W in BAA24500. Ref.1
	Sequence conflict	468	1	P → L in BAA24500. Ref.1
	Sequence conflict	662	1	L → F in AAD21531. Ref.2
	Sequence conflict	704	1	S → F in BAA24500. Ref.1
	Sequence conflict	714	1	S → F in BAA24500. Ref.1
	Sequence conflict	848	1	S → T in BAA24500. Ref.1
	Sequence conflict	872	1	P → R in AAD21531. Ref.2
	Sequence conflict	875 – 878	4	GRPE → RRS in AAD21531. Ref.2
	Sequence conflict	956	1	S → L in BAA24500. Ref.1
	Sequence conflict	1252	1	N → K in BAA24500. Ref.1
	Sequence conflict	1303	1	G → R in BAA24500. Ref.1
	Sequence conflict	1314 – 1338	25	LPPAN…TIVKE → PAPCPTTYAQH in BAA24500. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9Y4H2 [UniParc]. Last modified March 29, 2005. Version 2. Checksum: 58E569E8BDBAF3D7	FASTA	1,338	137,334
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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, MASS SPECTROMETRY.
[12]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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].
[14]	"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, MASS SPECTROMETRY.
[15]	"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.

IPI

IPI00464978.

RefSeq

NP_003740.2. NM_003749.2.

UniGene

Hs.442344.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FQW	X-ray	1.93	C	1097-1105	[»]
3FQX	X-ray	1.70	C	1097-1105	[»]

ProteinModelPortal

Q9Y4H2.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y4H2. 4 interactions.

MINT

MINT-156306.

STRING

9606.ENSP00000365016.

PTM databases

PhosphoSite

Q9Y4H2.

Polymorphism databases

DMDM

62298062.

Proteomic databases

PaxDb

Q9Y4H2.

PRIDE

Q9Y4H2.

Protocols and materials databases

DNASU

8660.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375856; ENSP00000365016; ENSG00000185950.

GeneID

8660.

KEGG

hsa:8660.

UCSC

uc001vqv.3. human.

Organism-specific databases

CTD

8660.

GeneCards

GC13M110406.

HGNC

HGNC:6126. IRS2.

HPA

CAB016944.

MIM

600797. gene.

neXtProt

NX_Q9Y4H2.

PharmGKB

PA375.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG81285.

HOVERGEN

HBG000542.

InParanoid

Q9Y4H2.

KO

K07187.

OMA

DSCLNIN.

OrthoDB

EOG44MXTG.

PhylomeDB

Q9Y4H2.

Enzyme and pathway databases

Pathway_Interaction_DB

epopathway. EPO signaling pathway.
igf1_pathway. IGF1 pathway.
il2_1pathway. IL2-mediated signaling events.
il4_2pathway. IL4-mediated signaling events.
ret_pathway. Signaling events regulated by Ret tyrosine kinase.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q9Y4H2.

Bgee

Q9Y4H2.

CleanEx

HS_IRS2.

Genevestigator

Q9Y4H2.

GermOnline

ENSG00000185950. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 2 hits.

InterPro

IPR002404. Insln_rcpt_S1.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]

Pfam

PF02174. IRS. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]

PRINTS

PR00628. INSULINRSI.

SMART

SM00233. PH. 1 hit.
SM00310. PTBI. 1 hit.
[Graphical view]

PROSITE

PS51064. IRS_PTB. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

IRS2. human.

EvolutionaryTrace

Q9Y4H2.

GenomeRNAi

8660.

NextBio

32479.

PMAP-CutDB

Q9Y4H2.

SOURCE

Search...

Entry information

Entry name

IRS2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.