Reviewed, UniProtKB/Swiss-Prot Q9Y4H2 (IRS2_HUMAN)

Names and origin

Protein names

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

Gene names

Name:

IRS2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May mediate the control of various cellular processes by insulin.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Sequence similarities	Contains 1 IRS-type PTB domain. Contains 1 PH domain.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Molecular function	Transducer
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	glucose metabolic process Traceable author statement. Source: ProtInc insulin receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB lipid homeostasis Traceable author statement. Source: UniProtKB negative regulation of plasma membrane long-chain fatty acid transport Inferred from mutant phenotype. Source: UniProtKB positive regulation of fatty acid beta-oxidation Inferred from mutant phenotype. Source: UniProtKB positive regulation of glucose import Inferred from mutant phenotype. Source: UniProtKB positive regulation of glucose metabolic process Inferred from mutant phenotype. Source: UniProtKB positive regulation of glycogen biosynthetic process Inferred from mutant phenotype. Source: UniProtKB
Cellular component	plasma membrane Inferred from Experiment. Source: Reactome
Molecular function	signal transducer activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
YWHAB	P31946	1	EBI-1049582,EBI-359815
YWHAG	P61981	1	EBI-1049582,EBI-359832
YWHAQ	P27348	1	EBI-1049582,EBI-359854

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	75	1	Phosphotyrosine Ref.9
	Modified residue	306	1	Phosphoserine Ref.13
	Modified residue	309	1	Phosphoserine Ref.7
	Modified residue	334	1	Phosphoserine Ref.10
	Modified residue	346	1	Phosphoserine Ref.8 Ref.13
	Modified residue	350	1	Phosphothreonine Ref.8 Ref.13
	Modified residue	365	1	Phosphoserine Ref.13
	Modified residue	384	1	Phosphoserine Ref.13
	Modified residue	388	1	Phosphoserine Ref.7 Ref.11 Ref.13
	Modified residue	391	1	Phosphoserine Ref.7 Ref.11 Ref.13
	Modified residue	520	1	Phosphothreonine Ref.6 Ref.13
	Modified residue	523	1	Phosphoserine Ref.13
	Modified residue	527	1	Phosphothreonine Ref.8 Ref.13
	Modified residue	540	1	Phosphotyrosine; by INSR By similarity
	Modified residue	560	1	Phosphoserine Ref.7 Ref.13
	Modified residue	577	1	Phosphoserine Ref.8 Ref.13
	Modified residue	579	1	Phosphothreonine Ref.13
	Modified residue	580	1	Phosphothreonine Ref.8 Ref.13
	Modified residue	594	1	Phosphoserine Ref.13
	Modified residue	608	1	Phosphoserine Ref.11 Ref.13
	Modified residue	620	1	Phosphoserine Ref.13
	Modified residue	653	1	Phosphotyrosine; by INSR Ref.9
	Modified residue	675	1	Phosphotyrosine; by INSR Ref.9
	Modified residue	679	1	Phosphoserine Ref.13
	Modified residue	713	1	Phosphothreonine Ref.12
	Modified residue	731	1	Phosphoserine Ref.13
	Modified residue	735	1	Phosphoserine Ref.13
	Modified residue	736	1	Phosphoserine Ref.13
	Modified residue	742	1	Phosphotyrosine Ref.9
	Modified residue	770	1	Phosphoserine Ref.12 Ref.13
	Modified residue	772	1	Phosphoserine Ref.12
	Modified residue	779	1	Phosphothreonine Ref.13
	Modified residue	823	1	Phosphotyrosine Ref.9
	Modified residue	828	1	Phosphoserine Ref.13
	Modified residue	894	1	Phosphoserine Ref.13
	Modified residue	915	1	Phosphoserine Ref.6 Ref.11 Ref.12 Ref.13
	Modified residue	919	1	Phosphotyrosine; by INSR By similarity
	Modified residue	973	1	Phosphoserine Ref.13
	Modified residue	978	1	Phosphotyrosine; by INSR By similarity
	Modified residue	1100	1	Phosphoserine Ref.6 Ref.8 Ref.11 Ref.13
	Modified residue	1103	1	Phosphoserine Ref.13
	Modified residue	1148	1	Phosphoserine Ref.13
	Modified residue	1149	1	Phosphoserine Ref.13
	Modified residue	1159	1	Phosphothreonine Ref.13
	Modified residue	1162	1	Phosphoserine Ref.13
	Modified residue	1174	1	Phosphoserine Ref.13
	Modified residue	1176	1	Phosphoserine Ref.7 Ref.12 Ref.13
	Modified residue	1203	1	Phosphoserine Ref.6 Ref.13
	Modified residue	1253	1	Phosphotyrosine; by INSR By similarity
Natural variations
	Natural variant	789	1	H → Y: dbSNP rs35223808.		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: dbSNP rs35927012.		VAR_033993
	Natural variant	1057	1	G → D: dbSNP rs1805097. Ref.15		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 Ref.2
	Sequence conflict	875 – 878	4	GRPE → RRS 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)
	Q9Y4H2-1 [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: 9312143] [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: 10077005] [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: 15057823] [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]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-520; SER-915; SER-1100 AND SER-1203, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309; SER-388; SER-391; SER-560 AND SER-1176, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346; THR-350; THR-527; SER-577; THR-580 AND SER-1100, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-75; TYR-653; TYR-675; TYR-742 AND TYR-823, MASS SPECTROMETRY.
[10]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, MASS SPECTROMETRY.
[11]	"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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388; SER-391; SER-608; SER-915 AND SER-1100, MASS SPECTROMETRY. Tissue: Platelet.
[12]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-713; SER-770; SER-772; SER-915 AND SER-1176, MASS SPECTROMETRY.
[13]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-346; THR-350; SER-365; SER-384; SER-388; SER-391; THR-520; SER-523; THR-527; SER-560; SER-577; THR-579; THR-580; SER-594; SER-608; SER-620; SER-679; SER-731; SER-735; SER-736; SER-770; THR-779; SER-828; SER-894; SER-915; SER-973; SER-1100; SER-1103; SER-1148; SER-1149; THR-1159; SER-1162; SER-1174; SER-1176 AND SER-1203, MASS SPECTROMETRY.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], 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: 12687350] [Abstract] Cited for: VARIANT ASP-1057.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

UniGene

Hs.442344

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y4H2. 4 interactions.

PTM databases

PhosphoSite

Q9Y4H2.

Proteomic databases

PRIDE

Q9Y4H2.

Genome annotation databases

Ensembl

ENSG00000185950. Homo sapiens. [Contig view]

GeneID

8660.

KEGG

hsa:8660.

UCSC

uc001vqv.1. human.

Organism-specific databases

GeneCards

GC13M109204.

HGNC

HGNC:6126. IRS2.

HPA

CAB016944.

MIM

600797. gene.

PharmGKB

PA375.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9Y4H2.

OMA

Q9Y4H2. CLNINKR.

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_11061. Signalling by NGF.
REACT_498. Signaling by Insulin receptor.
REACT_508. Signal attenuation.

Gene expression databases

ArrayExpress

Q9Y4H2.

Bgee

Q9Y4H2.

CleanEx

HS_IRS2.

GermOnline

ENSG00000185950. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:2.30.29.30. PH_type. 2 hits.

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 Resources

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:	July 7, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)