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O14654 (IRS4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 4

Short name=IRS-4
Alternative name(s):
160 kDa phosphotyrosine protein
Short name=py160
Phosphoprotein of 160 kDa
Short name=pp160
Gene names
Name:IRS4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1257 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as an interface between multiple growth factor receptors possessing tyrosine kinase activity, such as insulin receptor, IGF1R and FGFR1, and a complex network of intracellular signaling molecules containing SH2 domains. Involved in the IGF1R mitogenic signaling pathway. Promotes the AKT1 signaling pathway and BAD phosphorylation during insulin stimulation without activation of RPS6KB1 or the inhibition of apoptosis. Interaction with GRB2 enhances insulin-stimulated mitogen-activated protein kinase activity. May be involved in nonreceptor tyrosine kinase signaling in myoblasts. Plays a pivotal role in the proliferation/differentiation of hepatoblastoma cell through EPHB2 activation upon IGF1 stimulation. May play a role in the signal transduction in response to insulin and to a lesser extent in response to IL4 and GH on mitogenesis. Plays a role in growth, reproduction and glucose homeostasis. May act as negative regulators of the IGF1 signaling pathway by suppressing the function of IRS1 and IRS2. Ref.4 Ref.6 Ref.7 Ref.10 Ref.14

Subunit structure

Interacts with SOCS6 in response to stimulatiom with either insulin or IGF1 By similarity. Interacts with CRK and CRKL. Interaction with CRK is stronger than with CRKL. Interacts with CRK via the phosphorylated YXXM motifs. Interacts with GRB2 and PIK3R1. Interacts with PLC-gamma, SHC1, PTK6, PPP4C and NISCH. Ref.4 Ref.5 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13

Subcellular location

Cell membrane; Peripheral membrane protein; Cytoplasmic side Ref.4.

Tissue specificity

Expressed in myoblasts. Expressed in liver and hepatocellular carcinoma. Ref.10 Ref.14

Induction

Down-regulated by PPP4C in a phosphatase activity-dependent manner. Ref.12

Post-translational modification

Phosphorylated on tyrosine residues in response to both insulin and IGF1 signaling. Phosphorylated on Tyr-921 in response to FGF2 signaling. Phosphorylation of Tyr-921 is required for GRB2, phospholipase C-gamma and phosphatidylinositol 3-kinase interaction. Ref.1 Ref.4 Ref.11

Sequence similarities

Contains 1 IRS-type PTB domain.

Contains 1 PH domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainRepeat
   Molecular functionTransducer
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processpositive regulation of signal transduction

Traceable author statement Ref.1. Source: GOC

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentplasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionSH3/SH2 adaptor activity

Traceable author statement Ref.1. Source: ProtInc

signal transducer activity

Traceable author statement Ref.1Ref.4. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CRKP461088EBI-356594,EBI-886
EGFRP005332EBI-356594,EBI-297353

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12571257Insulin receptor substrate 4
PRO_0000314678

Regions

Domain78 – 199122PH
Domain231 – 335105IRS-type PTB
Region678 – 800123CRK-binding
Region895 – 8973GRB2-binding
Motif487 – 4904YXXM motif 1
Motif700 – 7034YXXM motif 2
Motif717 – 7204YXXM motif 3
Motif743 – 7464YXXM motif 4
Motif779 – 7824YXXM motif 5
Motif828 – 8314YXXM motif 6
Motif921 – 9244YXXM motif 7
Compositional bias18 – 2811Poly-Ala
Compositional bias124 – 13714Ala-rich
Compositional bias218 – 2269Poly-Ala
Compositional bias628 – 63912Pro-rich
Compositional bias1094 – 1212119Ala-rich

Amino acid modifications

Modified residue9211Phosphotyrosine Ref.11

Natural variations

Natural variant201A → V in a colorectal cancer sample; somatic mutation. Ref.16
VAR_038042
Natural variant341L → F.
Corresponds to variant rs1801162 [ dbSNP | Ensembl ].
VAR_051078
Natural variant2151G → E in a colorectal cancer sample; somatic mutation. Ref.16
VAR_038043
Natural variant5081N → K.
Corresponds to variant rs34287560 [ dbSNP | Ensembl ].
VAR_051079
Natural variant5571G → R in a colorectal cancer sample; somatic mutation. Ref.16
VAR_038044
Natural variant8791H → D.
Corresponds to variant rs1801164 [ dbSNP | Ensembl ].
VAR_051080
Natural variant12301D → Y.
Corresponds to variant rs28546943 [ dbSNP | Ensembl ].
VAR_061669

Experimental info

Mutagenesis7001Y → F: No effect. Reduces interaction with CRK by 50%; when associated with F-717. Abolishes interaction with CRK; when associated with F-717; F-743 and F-779. Ref.8
Mutagenesis7171Y → F: No effect. Reduces interaction with CRK by 50%; when associated with F-700. Abolishes interaction with CRK; when associated with F-700; F-743 and F-779. Ref.8
Mutagenesis7431Y → F: No effect. Reduces interaction with CRK by 50%; when associated with F-779. Abolishes interaction with CRK; when associated with F-700; F-717 and F-779. Ref.8
Mutagenesis7791Y → F: No effect. Reduces interaction with CRK by 50%; when associated with F-743. Abolishes interaction with CRK; when associated with F-700; F-717 and F-743. Ref.8

Sequences

Sequence LengthMass (Da)Tools
O14654 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 4D512D65A7A80374

FASTA1,257133,768
        10         20         30         40         50         60 
MASCSFTRDQ ATRRLRGAAA AAAAALAAVV TTPLLSSGTP TALIGTGSSC PGAMWLSTAT 

        70         80         90        100        110        120 
GSRSDSESEE EDLPVGEEVC KRGYLRKQKH GHRRYFVLKL ETADAPARLE YYENARKFRH 

       130        140        150        160        170        180 
SVRAAAAAAA AAASGAAIPP LIPPRRVITL YQCFSVSQRA DARYRHLIAL FTQDEYFAMV 

       190        200        210        220        230        240 
AENESEQESW YLLLSRLILE SKRRRCGTLG AQPDGEPAAL AAAAAAEPPF YKDVWQVIVK 

       250        260        270        280        290        300 
PRGLGHRKEL SGVFRLCLTD EEVVFVRLNT EVASVVVQLL SIRRCGHSEQ YFFLEVGRST 

       310        320        330        340        350        360 
VIGPGELWMQ VDDCVVAQNM HELFLEKMRA LCADEYRARC RSYSISIGAH LLTLLSARRH 

       370        380        390        400        410        420 
LGLVPLEPGG WLRRSRFEQF CHLRAIGDGE DEMLFTRRFV TPSEPVAHSR RGRLHLPRGR 

       430        440        450        460        470        480 
RSRRAVSVPA SFFRRLAPSP ARPRHPAEAP NNGARLSSEV SGSGSGNFGE EGNPQGKEDQ 

       490        500        510        520        530        540 
EGSGGDYMPM NNWGSGNGRG SGGGQGSNGQ GSSSHSSGGN QCSGEGQGSR GGQGSNGQGS 

       550        560        570        580        590        600 
GGNQCSRDGQ GTAGGHGSGG GQRPGGGHGS GGGQGPGDGH GSGGGKNSGG GKGSGSGKGS 

       610        620        630        640        650        660 
DGDGERGKSL KKRSYFGKLT QSKQQQMPPP PPPPPPPPPA GGTGGKGKSG GRFRLYFCVD 

       670        680        690        700        710        720 
RGATKECKEA KEVKDAEIPE GAARGPHRAR AFDEDEDDPY VPMRPGVATP LVSSSDYMPM 

       730        740        750        760        770        780 
APQNVSASKK RHSRSPFEDS RGYMMMFPRV SPPPAPSPPK APDTNKEDDS KDNDSESDYM 

       790        800        810        820        830        840 
FMAPGAGAIP KNPRNPQGGS SSKSWSSYFS LPNPFRSSPL GQNDNSEYVP MLPGKFLGRG 

       850        860        870        880        890        900 
LDKEVSYNWD PKDAASKPSG EGSFSKPGDG GSPSKPSDHE PPKNKAKRPN RLSFITKGYK 

       910        920        930        940        950        960 
IKPKPQKPTH EQREADSSSD YVNMDFTKRE SNTPAPSTQG LPDSWGIIAE PRQSAFSNYV 

       970        980        990       1000       1010       1020 
NVEFGVPFPN PANDLSDLLR AIPRANPLSL DSARWPLPPL PLSATGSNAI EEEGDYIEVI 

      1030       1040       1050       1060       1070       1080 
FNSAMTPAMA LADSAIRYDA ETGRIYVVDP FSECCMDISL SPSRCSEPPP VARLLQEEEQ 

      1090       1100       1110       1120       1130       1140 
ERRRPQSRSQ SFFAAARAAV SAFPTDSLER DLSPSSAPAV ASAAEPTLAL SQVVAAASAL 

      1150       1160       1170       1180       1190       1200 
AAAPGIGAAA AAAGFDSASA RWFQPVANAA DAEAVRGAQD VAGGSNPGAH NPSANLARGD 

      1210       1220       1230       1240       1250 
NQAGGAAAAA AAPEPPPRSR RVPRPPERED SDNDDDTHVR MDFARRDNQF DSPKRGR 

« Hide

References

« Hide 'large scale' references
[1]"A novel 160-kDa phosphotyrosine protein in insulin-treated embryonic kidney cells is a new member of the insulin receptor substrate family."
Lavan B.E., Fantin V.R., Chang E.T., Lane W.S., Keller S.R., Lienhard G.E.
J. Biol. Chem. 272:21403-21407(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 100-117; 233-240; 613-618; 836-843 AND 844-852, PHOSPHORYLATION.
Tissue: Kidney.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Characterization of insulin receptor substrate 4 in human embryonic kidney 293 cells."
Fantin V.R., Sparling J.D., Slot J.W., Keller S.R., Lienhard G.E., Lavan B.E.
J. Biol. Chem. 273:10726-10732(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GRB2 AND PIK3R1, PHOSPHORYLATION.
[5]"Interplay of the proto-oncogene proteins CrkL and CrkII in insulin-like growth factor-I receptor-mediated signal transduction."
Koval A.P., Karas M., Zick Y., LeRoith D.
J. Biol. Chem. 273:14780-14787(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRK AND CRKL.
[6]"Insulin receptor substrate-4 enhances insulin-like growth factor-I-induced cell proliferation."
Qu B.-H., Karas M., Koval A., LeRoith D.
J. Biol. Chem. 274:31179-31184(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"IRS-4 mediates protein kinase B signaling during insulin stimulation without promoting antiapoptosis."
Uchida T., Myers M.G. Jr., White M.F.
Mol. Cell. Biol. 20:126-138(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GRB2 AND PIK3R1.
[8]"The insulin-like growth factor I receptor-induced interaction of insulin receptor substrate-4 and Crk-II."
Karas M., Koval A.P., Zick Y., LeRoith D.
Endocrinology 142:1835-1840(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRK, MUTAGENESIS OF TYR-700; TYR-717; TYR-743 AND TYR-779.
[9]"Insulin receptor substrate 4 associates with the protein IRAS."
Sano H., Liu S.C.H., Lane W.S., Piletz J.E., Lienhard G.E.
J. Biol. Chem. 277:19439-19447(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NISCH.
[10]"Insulin receptor substrate-4 is expressed in muscle tissue without acting as a substrate for the insulin receptor."
Schreyer S., Ledwig D., Rakatzi I., Kloeting I., Eckel J.
Endocrinology 144:1211-1218(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[11]"Tyrosine phosphoproteomics of fibroblast growth factor signaling: a role for insulin receptor substrate-4."
Hinsby A.M., Olsen J.V., Mann M.
J. Biol. Chem. 279:46438-46447(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-921, INTERACTION WITH SHC1; GRB2; PHOSPHOLIPASE C-GAMMA AND PHOSPHATIDYLINOSITOL 3-KINASE, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"Protein phosphatase 4 interacts with and down-regulates insulin receptor substrate 4 following tumor necrosis factor-alpha stimulation."
Mihindukulasuriya K.A., Zhou G., Qin J., Tan T.-H.
J. Biol. Chem. 279:46588-46594(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP4C, INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[13]"Interaction between Brk kinase and insulin receptor substrate-4."
Qiu H., Zappacosta F., Su W., Annan R.S., Miller W.T.
Oncogene 24:5656-5664(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTK6, IDENTIFICATION BY MASS SPECTROMETRY.
[14]"Role of insulin receptor substrate-4 in IGF-I-stimulated HEPG2 proliferation."
Cuevas E.P., Escribano O., Chiloeches A., Ramirez Rubio S., Roman I.D., Fernandez-Moreno M.D., Guijarro L.G.
J. Hepatol. 46:1089-1098(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[15]"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].
[16]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-20; GLU-215 AND ARG-557.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF007567 mRNA. Translation: AAC51738.1.
AL035425 Genomic DNA. Translation: CAB90290.1.
CH471120 Genomic DNA. Translation: EAX02682.1.
RefSeqNP_003595.1. NM_003604.2.
UniGeneHs.460872.

3D structure databases

ProteinModelPortalO14654.
SMRO14654. Positions 78-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114048. 57 interactions.
IntActO14654. 32 interactions.
MINTMINT-1151881.
STRING9606.ENSP00000361202.

PTM databases

PhosphoSiteO14654.

Proteomic databases

PaxDbO14654.
PRIDEO14654.

Protocols and materials databases

DNASU8471.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372129; ENSP00000361202; ENSG00000133124.
GeneID8471.
KEGGhsa:8471.
UCSCuc004eoc.2. human.

Organism-specific databases

CTD8471.
GeneCardsGC0XM107975.
HGNCHGNC:6128. IRS4.
HPAHPA017372.
MIM300904. gene.
neXtProtNX_O14654.
PharmGKBPA29923.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG81285.
HOGENOMHOG000113104.
HOVERGENHBG107140.
InParanoidO14654.
KOK17446.
OMARCGHSEQ.
OrthoDBEOG7XM2X6.
PhylomeDBO14654.
TreeFamTF325994.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkO14654.

Gene expression databases

BgeeO14654.
CleanExHS_IRS4.
GenevestigatorO14654.

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.
[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

GeneWikiIRS4.
GenomeRNAi8471.
NextBio31702.
PROO14654.
SOURCESearch...

Entry information

Entry nameIRS4_HUMAN
AccessionPrimary (citable) accession number: O14654
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 115 of the entry and version 1 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

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 X

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