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Protein

Insulin receptor substrate 1

Gene

IRS1

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. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains such as phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • cellular response to insulin stimulus Source: BHF-UCL
  • glucose homeostasis Source: BHF-UCL
  • insulin-like growth factor receptor signaling pathway Source: UniProtKB
  • insulin receptor signaling pathway Source: UniProtKB
  • MAPK cascade Source: Reactome
  • negative regulation of insulin receptor signaling pathway Source: BHF-UCL
  • negative regulation of insulin secretion Source: BHF-UCL
  • phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  • phosphatidylinositol-mediated signaling Source: Reactome
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of fatty acid beta-oxidation Source: BHF-UCL
  • positive regulation of glucose import Source: BHF-UCL
  • positive regulation of glucose import in response to insulin stimulus Source: BHF-UCL
  • positive regulation of glucose metabolic process Source: BHF-UCL
  • positive regulation of glycogen biosynthetic process Source: BHF-UCL
  • positive regulation of insulin receptor signaling pathway Source: BHF-UCL
  • positive regulation of phosphatidylinositol 3-kinase activity Source: BHF-UCL
  • regulation of phosphatidylinositol 3-kinase signaling Source: Reactome
  • response to insulin Source: BHF-UCL
  • response to peptide hormone Source: BHF-UCL
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Enzyme and pathway databases

BioCyciZFISH:ENSG00000169047-MONOMER.
ReactomeiR-HSA-109704. PI3K Cascade.
R-HSA-112412. SOS-mediated signalling.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-198203. PI3K/AKT activation.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-2428928. IRS-related events triggered by IGF1R.
R-HSA-2586552. Signaling by Leptin.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-74713. IRS activation.
R-HSA-74749. Signal attenuation.
R-HSA-982772. Growth hormone receptor signaling.
SignaLinkiP35568.
SIGNORiP35568.

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin receptor substrate 1
Short name:
IRS-1
Gene namesi
Name:IRS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:6125. IRS1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Diabetes mellitus, non-insulin-dependent (NIDDM)3 Publications
The gene represented in this entry may be involved in disease pathogenesis.
Disease descriptionA multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.
See also OMIM:125853
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_005301723Missing in NIDDM. 1 Publication1
Natural variantiVAR_0053021043S → Y in NIDDM. 1 Publication1
Natural variantiVAR_0053031095C → Y in NIDDM. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi307S → A: Impaired degradation by the Cul7-RING(FBXW8) complex; when associated with A-312; A-527; A-636 and A-639. 1 Publication1
Mutagenesisi312S → A: Impaired degradation by the Cul7-RING(FBXW8) complex; when associated with A-307; A-527; A-636 and A-639. 1 Publication1
Mutagenesisi527S → A: Impaired degradation by the Cul7-RING(FBXW8) complex; when associated with A-307; A-312; A-636 and A-639. 1 Publication1
Mutagenesisi636S → A: Impaired degradation by the Cul7-RING(FBXW8) complex; when associated with A-307; A-312; A-527 and A-639. 1 Publication1
Mutagenesisi639S → A: Impaired degradation by the Cul7-RING(FBXW8) complex; when associated with A-307; A-312; A-527 and A-636. 1 Publication1
Mutagenesisi794S → A: Loss of phosphorylation by SIK2. 1 Publication1

Keywords - Diseasei

Diabetes mellitus, Disease mutation

Organism-specific databases

DisGeNETi3667.
MalaCardsiIRS1.
MIMi125853. phenotype.
OpenTargetsiENSG00000169047.
PharmGKBiPA203.

Polymorphism and mutation databases

BioMutaiIRS1.
DMDMi547738.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000842361 – 1242Insulin receptor substrate 1Add BLAST1242

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3PhosphoserineBy similarity1
Modified residuei99Phosphoserine; by CK2By similarity1
Modified residuei270Phosphoserine; by RPS6KB11 Publication1
Modified residuei307Phosphoserine; by RPS6KB12 Publications1
Modified residuei312Phosphoserine; by IKKB, MAPK8 and RPS6KB12 Publications1
Modified residuei323PhosphoserineCombined sources1
Modified residuei330PhosphoserineBy similarity1
Modified residuei345PhosphoserineBy similarity1
Modified residuei348PhosphoserineCombined sources1
Modified residuei419PhosphoserineBy similarity1
Modified residuei446PhosphothreonineBy similarity1
Modified residuei453PhosphothreonineCombined sources1
Modified residuei465Phosphotyrosine; by INSRBy similarity1
Modified residuei527Phosphoserine; by RPS6KB1Combined sources1 Publication1
Modified residuei612Phosphotyrosine; by INSR1 Publication1
Modified residuei629PhosphoserineCombined sources1
Modified residuei632Phosphotyrosine; by INSR1 Publication1
Modified residuei636Phosphoserine; by RPS6KB1Combined sources2 Publications1
Modified residuei662PhosphotyrosineCombined sources1
Modified residuei794Phosphoserine; by AMPK and SIK21 Publication1
Modified residuei892PhosphoserineBy similarity1
Modified residuei896Phosphotyrosine; by INSRBy similarity1
Modified residuei941Phosphotyrosine; by INSR1 Publication1
Modified residuei989Phosphotyrosine; by INSRBy similarity1
Modified residuei1100PhosphoserineBy similarity1
Modified residuei1101Phosphoserine; by RPS6KB1 and PKC/PRKCQ2 Publications1
Modified residuei1179Phosphotyrosine; by INSRBy similarity1
Modified residuei1229Phosphotyrosine; by INSRBy similarity1

Post-translational modificationi

Serine phosphorylation of IRS1 is a mechanism for insulin resistance. Ser-312 phosphorylation inhibits insulin action through disruption of IRS1 interaction with the insulin receptor (By similarity). Phosphorylation of Tyr-896 is required for GRB2-binding (By similarity). Phosphorylated by ALK. Phosphorylated at Ser-270, Ser-307, Ser-636 and Ser-1101 by RPS6KB1; phosphorylation induces accelerated degradation of IRS1.By similarity4 Publications
Ubiquitinated by the Cul7-RING(FBXW8) complex in a mTOR-dependent manner, leading to its degradation: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2).1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP35568.
MaxQBiP35568.
PaxDbiP35568.
PeptideAtlasiP35568.
PRIDEiP35568.

PTM databases

iPTMnetiP35568.
PhosphoSitePlusiP35568.

Miscellaneous databases

PMAP-CutDBP35568.

Expressioni

Gene expression databases

BgeeiENSG00000169047.
CleanExiHS_IRS1.
ExpressionAtlasiP35568. baseline and differential.
GenevisibleiP35568. HS.

Organism-specific databases

HPAiCAB005261.

Interactioni

Subunit structurei

Interacts with UBTF and PIK3CA (By similarity). Interacts (via phosphorylated YXXM motifs) with PIK3R1 (By similarity). Interacts with ROCK1 and FER (By similarity). Interacts (via PH domain) with PHIP (By similarity). Interacts with GRB2 (By similarity). Interacts with SOCS7. Interacts (via IRS-type PTB domain) with IGF1R and INSR (via the tyrosine-phosphorylated NPXY motif). Interacts with ALK. Interacts with EIF2AK2/PKR (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
P030702EBI-517592,EBI-617698From a different organism.
BCAR3O758153EBI-517592,EBI-702336
ERBB2P046262EBI-517592,EBI-641062
INSRP062133EBI-517592,EBI-475899
NSP034952EBI-517592,EBI-2548993From a different organism.
PABPC1P119402EBI-517592,EBI-81531
PIK3CAP4233620EBI-517592,EBI-2116585
PIK3R1P2798612EBI-517592,EBI-79464
PIK3R1P27986-23EBI-517592,EBI-9090282
PIK3R3Q925694EBI-517592,EBI-79893
PTPN11Q061243EBI-517592,EBI-297779

GO - Molecular functioni

  • insulin-like growth factor receptor binding Source: UniProtKB
  • insulin receptor binding Source: UniProtKB
  • phosphatidylinositol 3-kinase binding Source: UniProtKB
  • protein kinase C binding Source: BHF-UCL
  • SH2 domain binding Source: UniProtKB
  • transmembrane receptor protein tyrosine kinase adaptor activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi109874. 59 interactors.
DIPiDIP-523N.
IntActiP35568. 25 interactors.
MINTiMINT-149537.
STRINGi9606.ENSP00000304895.

Structurei

Secondary structure

11242
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 20Combined sources8
Turni22 – 24Combined sources3
Beta strandi27 – 33Combined sources7
Turni37 – 39Combined sources3
Beta strandi40 – 49Combined sources10
Helixi50 – 54Combined sources5
Beta strandi61 – 65Combined sources5
Helixi66 – 68Combined sources3
Beta strandi69 – 75Combined sources7
Beta strandi81 – 90Combined sources10
Beta strandi92 – 96Combined sources5
Helixi100 – 113Combined sources14
Beta strandi161 – 172Combined sources12
Helixi173 – 176Combined sources4
Beta strandi181 – 187Combined sources7
Beta strandi189 – 196Combined sources8
Beta strandi203 – 207Combined sources5
Helixi208 – 210Combined sources3
Beta strandi211 – 217Combined sources7
Beta strandi220 – 225Combined sources6
Beta strandi233 – 239Combined sources7
Helixi243 – 258Combined sources16
Helixi259 – 261Combined sources3
Beta strandi897 – 901Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IRSNMR-A157-267[»]
1K3AX-ray2.10B891-902[»]
1QQGX-ray2.30A/B4-267[»]
2Z8CX-ray3.25B731-736[»]
ProteinModelPortaliP35568.
SMRiP35568.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35568.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 115PHPROSITE-ProRule annotationAdd BLAST104
Domaini160 – 264IRS-type PTBPROSITE-ProRule annotationAdd BLAST105

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni3 – 137Mediates interaction with PHIPBy similarityAdd BLAST135
Regioni896 – 898GRB2-bindingBy similarity3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi465 – 468YXXM motif 14
Motifi551 – 554YXXM motif 24
Motifi612 – 615YXXM motif 34
Motifi632 – 635YXXM motif 44
Motifi662 – 665YXXM motif 54
Motifi732 – 735YXXM motif 64
Motifi941 – 944YXXM motif 74
Motifi989 – 992YXXM motif 84
Motifi1012 – 1015YXXM motif 94

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi128 – 134Poly-Gly7
Compositional biasi268 – 444Ser-richAdd BLAST177
Compositional biasi680 – 686Poly-Ser7
Compositional biasi807 – 815Poly-Ser9
Compositional biasi877 – 882Poly-Gln6
Compositional biasi1192 – 1210Pro-richAdd BLAST19

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IXEK. Eukaryota.
ENOG410Z9EP. LUCA.
GeneTreeiENSGT00530000063420.
HOGENOMiHOG000113103.
HOVERGENiHBG000542.
InParanoidiP35568.
KOiK16172.
OMAiHALPHPK.
OrthoDBiEOG091G02EF.
PhylomeDBiP35568.
TreeFamiTF325994.

Family and domain databases

CDDicd01204. PTB_IRS. 1 hit.
Gene3Di2.30.29.30. 2 hits.
InterProiIPR002404. IRS_PTB.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF02174. IRS. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSiPR00628. INSULINRSI.
SMARTiSM00233. PH. 1 hit.
SM00310. PTBI. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 2 hits.
PROSITEiPS51064. IRS_PTB. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35568-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASPPESDGF SDVRKVGYLR KPKSMHKRFF VLRAASEAGG PARLEYYENE
60 70 80 90 100
KKWRHKSSAP KRSIPLESCF NINKRADSKN KHLVALYTRD EHFAIAADSE
110 120 130 140 150
AEQDSWYQAL LQLHNRAKGH HDGAAALGAG GGGGSCSGSS GLGEAGEDLS
160 170 180 190 200
YGDVPPGPAF KEVWQVILKP KGLGQTKNLI GIYRLCLTSK TISFVKLNSE
210 220 230 240 250
AAAVVLQLMN IRRCGHSENF FFIEVGRSAV TGPGEFWMQV DDSVVAQNMH
260 270 280 290 300
ETILEAMRAM SDEFRPRSKS QSSSNCSNPI SVPLRRHHLN NPPPSQVGLT
310 320 330 340 350
RRSRTESITA TSPASMVGGK PGSFRVRASS DGEGTMSRPA SVDGSPVSPS
360 370 380 390 400
TNRTHAHRHR GSARLHPPLN HSRSIPMPAS RCSPSATSPV SLSSSSTSGH
410 420 430 440 450
GSTSDCLFPR RSSASVSGSP SDGGFISSDE YGSSPCDFRS SFRSVTPDSL
460 470 480 490 500
GHTPPARGEE ELSNYICMGG KGPSTLTAPN GHYILSRGGN GHRCTPGTGL
510 520 530 540 550
GTSPALAGDE AASAADLDNR FRKRTHSAGT SPTITHQKTP SQSSVASIEE
560 570 580 590 600
YTEMMPAYPP GGGSGGRLPG HRHSAFVPTR SYPEEGLEMH PLERRGGHHR
610 620 630 640 650
PDSSTLHTDD GYMPMSPGVA PVPSGRKGSG DYMPMSPKSV SAPQQIINPI
660 670 680 690 700
RRHPQRVDPN GYMMMSPSGG CSPDIGGGPS SSSSSSNAVP SGTSYGKLWT
710 720 730 740 750
NGVGGHHSHV LPHPKPPVES SGGKLLPCTG DYMNMSPVGD SNTSSPSDCY
760 770 780 790 800
YGPEDPQHKP VLSYYSLPRS FKHTQRPGEP EEGARHQHLR LSTSSGRLLY
810 820 830 840 850
AATADDSSSS TSSDSLGGGY CGARLEPSLP HPHHQVLQPH LPRKVDTAAQ
860 870 880 890 900
TNSRLARPTR LSLGDPKAST LPRAREQQQQ QQPLLHPPEP KSPGEYVNIE
910 920 930 940 950
FGSDQSGYLS GPVAFHSSPS VRCPSQLQPA PREEETGTEE YMKMDLGPGR
960 970 980 990 1000
RAAWQESTGV EMGRLGPAPP GAASICRPTR AVPSSRGDYM TMQMSCPRQS
1010 1020 1030 1040 1050
YVDTSPAAPV SYADMRTGIA AEEVSLPRAT MAAASSSSAA SASPTGPQGA
1060 1070 1080 1090 1100
AELAAHSSLL GGPQGPGGMS AFTRVNLSPN RNQSAKVIRA DPQGCRRRHS
1110 1120 1130 1140 1150
SETFSSTPSA TRVGNTVPFG AGAAVGGGGG SSSSSEDVKR HSSASFENVW
1160 1170 1180 1190 1200
LRPGELGGAP KEPAKLCGAA GGLENGLNYI DLDLVKDFKQ CPQECTPEPQ
1210 1220 1230 1240
PPPPPPPHQP LGSGESSSTR RSSEDLSAYA SISFQKQPED RQ
Length:1,242
Mass (Da):131,591
Last modified:June 1, 1994 - v1
Checksum:i3C0EFD9E32B3E64A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti134G → GG in AAB21608 (PubMed:1311924).Curated1
Sequence conflicti362S → R in AAB21608 (PubMed:1311924).Curated1
Sequence conflicti384P → R in AAB21608 (PubMed:1311924).Curated1

Polymorphismi

The Arg-971 polymorphism impairs the ability of insulin to stimulate glucose transport, glucose transporter translocation, and glycogen synthesis by affecting the PI3K/AKT1/GSK3 signaling pathway. The polymorphism at Arg-971 may contribute to the in vivo insulin resistance observed in carriers of this variant. Arg-971 could contribute to the risk for atherosclerotic cardiovascular diseases associated with non-insulin-dependent diabetes mellitus (NIDDM) by producing a cluster of insulin resistance-related metabolic abnormalities. In insulin-stimulated human endothelial cells from carriers of the Arg-971 polymorphism, genetic impairment of the IRS1/PI3K/PDPK1/AKT1 insulin signaling cascade results in impaired insulin-stimulated nitric oxide (NO) release and suggested that this may be a mechanism through which the Arg-971 polymorphism contributes to the genetic predisposition to develop endothelial dysfunction and cardiovascular disease. The Arg-971 polymorphism not only reduces phosphorylation of the substrate but allows IRS1 to act as an inhibitor of PI3K, producing global insulin resistance.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_014853158P → R.Corresponds to variant rs1801108dbSNPEnsembl.1
Natural variantiVAR_014854209M → T.Corresponds to variant rs1801118dbSNPEnsembl.1
Natural variantiVAR_005299512A → P.1 PublicationCorresponds to variant rs1801276dbSNPEnsembl.1
Natural variantiVAR_025320608T → R May contribute to insulin resistance by impairing metabolic signaling through PI3K-dependent pathways. 1 PublicationCorresponds to variant rs104893642dbSNPEnsembl.1
Natural variantiVAR_005301723Missing in NIDDM. 1 Publication1
Natural variantiVAR_014855809S → F.Corresponds to variant rs1801120dbSNPEnsembl.1
Natural variantiVAR_014856892S → G.Corresponds to variant rs1801277dbSNPEnsembl.1
Natural variantiVAR_005300971G → R.5 PublicationsCorresponds to variant rs1801278dbSNPEnsembl.1
Natural variantiVAR_0053021043S → Y in NIDDM. 1 Publication1
Natural variantiVAR_0053031095C → Y in NIDDM. 1 Publication1
Natural variantiVAR_0218371137D → N.Corresponds to variant rs3731594dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S85963 Genomic DNA. Translation: AAB21608.1.
S62539 mRNA. Translation: AAB27175.1.
BC053895 mRNA. Translation: AAH53895.1.
CCDSiCCDS2463.1.
PIRiI53160. JS0670.
RefSeqiNP_005535.1. NM_005544.2.
UniGeneiHs.471508.

Genome annotation databases

EnsembliENST00000305123; ENSP00000304895; ENSG00000169047.
GeneIDi3667.
KEGGihsa:3667.
UCSCiuc002voh.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S85963 Genomic DNA. Translation: AAB21608.1.
S62539 mRNA. Translation: AAB27175.1.
BC053895 mRNA. Translation: AAH53895.1.
CCDSiCCDS2463.1.
PIRiI53160. JS0670.
RefSeqiNP_005535.1. NM_005544.2.
UniGeneiHs.471508.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IRSNMR-A157-267[»]
1K3AX-ray2.10B891-902[»]
1QQGX-ray2.30A/B4-267[»]
2Z8CX-ray3.25B731-736[»]
ProteinModelPortaliP35568.
SMRiP35568.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109874. 59 interactors.
DIPiDIP-523N.
IntActiP35568. 25 interactors.
MINTiMINT-149537.
STRINGi9606.ENSP00000304895.

PTM databases

iPTMnetiP35568.
PhosphoSitePlusiP35568.

Polymorphism and mutation databases

BioMutaiIRS1.
DMDMi547738.

Proteomic databases

EPDiP35568.
MaxQBiP35568.
PaxDbiP35568.
PeptideAtlasiP35568.
PRIDEiP35568.

Protocols and materials databases

DNASUi3667.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000305123; ENSP00000304895; ENSG00000169047.
GeneIDi3667.
KEGGihsa:3667.
UCSCiuc002voh.5. human.

Organism-specific databases

CTDi3667.
DisGeNETi3667.
GeneCardsiIRS1.
HGNCiHGNC:6125. IRS1.
HPAiCAB005261.
MalaCardsiIRS1.
MIMi125853. phenotype.
147545. gene.
neXtProtiNX_P35568.
OpenTargetsiENSG00000169047.
PharmGKBiPA203.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IXEK. Eukaryota.
ENOG410Z9EP. LUCA.
GeneTreeiENSGT00530000063420.
HOGENOMiHOG000113103.
HOVERGENiHBG000542.
InParanoidiP35568.
KOiK16172.
OMAiHALPHPK.
OrthoDBiEOG091G02EF.
PhylomeDBiP35568.
TreeFamiTF325994.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000169047-MONOMER.
ReactomeiR-HSA-109704. PI3K Cascade.
R-HSA-112412. SOS-mediated signalling.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-198203. PI3K/AKT activation.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-2428928. IRS-related events triggered by IGF1R.
R-HSA-2586552. Signaling by Leptin.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-74713. IRS activation.
R-HSA-74749. Signal attenuation.
R-HSA-982772. Growth hormone receptor signaling.
SignaLinkiP35568.
SIGNORiP35568.

Miscellaneous databases

ChiTaRSiIRS1. human.
EvolutionaryTraceiP35568.
GeneWikiiIRS1.
GenomeRNAii3667.
PMAP-CutDBP35568.
PROiP35568.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000169047.
CleanExiHS_IRS1.
ExpressionAtlasiP35568. baseline and differential.
GenevisibleiP35568. HS.

Family and domain databases

CDDicd01204. PTB_IRS. 1 hit.
Gene3Di2.30.29.30. 2 hits.
InterProiIPR002404. IRS_PTB.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF02174. IRS. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSiPR00628. INSULINRSI.
SMARTiSM00233. PH. 1 hit.
SM00310. PTBI. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 2 hits.
PROSITEiPS51064. IRS_PTB. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIRS1_HUMAN
AccessioniPrimary (citable) accession number: P35568
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 30, 2016
This is version 185 of the entry and version 1 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 2
    Human chromosome 2: 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

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 one 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.