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O14654

- IRS4_HUMAN

UniProt

O14654 - IRS4_HUMAN

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Protein

Insulin receptor substrate 4

Gene

IRS4

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

Functioni

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 IRS2.5 Publications

GO - Molecular functioni

  1. SH3/SH2 adaptor activity Source: ProtInc
  2. signal transducer activity Source: ProtInc

GO - Biological processi

  1. positive regulation of signal transduction Source: GOC
  2. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Enzyme and pathway databases

ReactomeiREACT_150203. IRS-related events triggered by IGF1R.
SignaLinkiO14654.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:IRS4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:6128. IRS4.

Subcellular locationi

Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

GO - Cellular componenti

  1. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi700 – 7001Y → 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. 1 Publication
Mutagenesisi717 – 7171Y → 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. 1 Publication
Mutagenesisi743 – 7431Y → 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. 1 Publication
Mutagenesisi779 – 7791Y → 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. 1 Publication

Organism-specific databases

PharmGKBiPA29923.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12571257Insulin receptor substrate 4PRO_0000314678Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei921 – 9211Phosphotyrosine1 Publication

Post-translational modificationi

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.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO14654.
PaxDbiO14654.
PRIDEiO14654.

PTM databases

PhosphoSiteiO14654.

Expressioni

Tissue specificityi

Expressed in myoblasts. Expressed in liver and hepatocellular carcinoma.2 Publications

Inductioni

Down-regulated by PPP4C in a phosphatase activity-dependent manner.1 Publication

Gene expression databases

BgeeiO14654.
CleanExiHS_IRS4.
GenevestigatoriO14654.

Organism-specific databases

HPAiHPA017372.

Interactioni

Subunit structurei

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.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CRKP461088EBI-356594,EBI-886
EGFRP005332EBI-356594,EBI-297353
PTGES3Q151852EBI-356594,EBI-1049387

Protein-protein interaction databases

BioGridi114048. 89 interactions.
IntActiO14654. 81 interactions.
MINTiMINT-1151881.
STRINGi9606.ENSP00000361202.

Structurei

3D structure databases

ProteinModelPortaliO14654.
SMRiO14654. Positions 78-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini78 – 199122PHPROSITE-ProRule annotationAdd
BLAST
Domaini231 – 335105IRS-type PTBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni678 – 800123CRK-bindingAdd
BLAST
Regioni895 – 8973GRB2-binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi487 – 4904YXXM motif 1
Motifi700 – 7034YXXM motif 2
Motifi717 – 7204YXXM motif 3
Motifi743 – 7464YXXM motif 4
Motifi779 – 7824YXXM motif 5
Motifi828 – 8314YXXM motif 6
Motifi921 – 9244YXXM motif 7

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi18 – 2811Poly-AlaAdd
BLAST
Compositional biasi124 – 13714Ala-richAdd
BLAST
Compositional biasi218 – 2269Poly-Ala
Compositional biasi628 – 63912Pro-richAdd
BLAST
Compositional biasi1094 – 1212119Ala-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG81285.
GeneTreeiENSGT00530000063420.
HOGENOMiHOG000113104.
HOVERGENiHBG107140.
InParanoidiO14654.
KOiK17446.
OMAiRCGHSEQ.
OrthoDBiEOG7XM2X6.
PhylomeDBiO14654.
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.
[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.

O14654 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASCSFTRDQ ATRRLRGAAA AAAAALAAVV TTPLLSSGTP TALIGTGSSC
60 70 80 90 100
PGAMWLSTAT GSRSDSESEE EDLPVGEEVC KRGYLRKQKH GHRRYFVLKL
110 120 130 140 150
ETADAPARLE YYENARKFRH SVRAAAAAAA AAASGAAIPP LIPPRRVITL
160 170 180 190 200
YQCFSVSQRA DARYRHLIAL FTQDEYFAMV AENESEQESW YLLLSRLILE
210 220 230 240 250
SKRRRCGTLG AQPDGEPAAL AAAAAAEPPF YKDVWQVIVK PRGLGHRKEL
260 270 280 290 300
SGVFRLCLTD EEVVFVRLNT EVASVVVQLL SIRRCGHSEQ YFFLEVGRST
310 320 330 340 350
VIGPGELWMQ VDDCVVAQNM HELFLEKMRA LCADEYRARC RSYSISIGAH
360 370 380 390 400
LLTLLSARRH LGLVPLEPGG WLRRSRFEQF CHLRAIGDGE DEMLFTRRFV
410 420 430 440 450
TPSEPVAHSR RGRLHLPRGR RSRRAVSVPA SFFRRLAPSP ARPRHPAEAP
460 470 480 490 500
NNGARLSSEV SGSGSGNFGE EGNPQGKEDQ EGSGGDYMPM NNWGSGNGRG
510 520 530 540 550
SGGGQGSNGQ GSSSHSSGGN QCSGEGQGSR GGQGSNGQGS GGNQCSRDGQ
560 570 580 590 600
GTAGGHGSGG GQRPGGGHGS GGGQGPGDGH GSGGGKNSGG GKGSGSGKGS
610 620 630 640 650
DGDGERGKSL KKRSYFGKLT QSKQQQMPPP PPPPPPPPPA GGTGGKGKSG
660 670 680 690 700
GRFRLYFCVD RGATKECKEA KEVKDAEIPE GAARGPHRAR AFDEDEDDPY
710 720 730 740 750
VPMRPGVATP LVSSSDYMPM APQNVSASKK RHSRSPFEDS RGYMMMFPRV
760 770 780 790 800
SPPPAPSPPK APDTNKEDDS KDNDSESDYM FMAPGAGAIP KNPRNPQGGS
810 820 830 840 850
SSKSWSSYFS LPNPFRSSPL GQNDNSEYVP MLPGKFLGRG LDKEVSYNWD
860 870 880 890 900
PKDAASKPSG EGSFSKPGDG GSPSKPSDHE PPKNKAKRPN RLSFITKGYK
910 920 930 940 950
IKPKPQKPTH EQREADSSSD YVNMDFTKRE SNTPAPSTQG LPDSWGIIAE
960 970 980 990 1000
PRQSAFSNYV NVEFGVPFPN PANDLSDLLR AIPRANPLSL DSARWPLPPL
1010 1020 1030 1040 1050
PLSATGSNAI EEEGDYIEVI FNSAMTPAMA LADSAIRYDA ETGRIYVVDP
1060 1070 1080 1090 1100
FSECCMDISL SPSRCSEPPP VARLLQEEEQ ERRRPQSRSQ SFFAAARAAV
1110 1120 1130 1140 1150
SAFPTDSLER DLSPSSAPAV ASAAEPTLAL SQVVAAASAL AAAPGIGAAA
1160 1170 1180 1190 1200
AAAGFDSASA RWFQPVANAA DAEAVRGAQD VAGGSNPGAH NPSANLARGD
1210 1220 1230 1240 1250
NQAGGAAAAA AAPEPPPRSR RVPRPPERED SDNDDDTHVR MDFARRDNQF

DSPKRGR
Length:1,257
Mass (Da):133,768
Last modified:January 1, 1998 - v1
Checksum:i4D512D65A7A80374
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201A → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_038042
Natural varianti34 – 341L → F.
Corresponds to variant rs1801162 [ dbSNP | Ensembl ].
VAR_051078
Natural varianti215 – 2151G → E in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_038043
Natural varianti508 – 5081N → K.
Corresponds to variant rs34287560 [ dbSNP | Ensembl ].
VAR_051079
Natural varianti557 – 5571G → R in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_038044
Natural varianti879 – 8791H → D.
Corresponds to variant rs1801164 [ dbSNP | Ensembl ].
VAR_051080
Natural varianti1230 – 12301D → Y.
Corresponds to variant rs28546943 [ dbSNP | Ensembl ].
VAR_061669

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF007567 mRNA. Translation: AAC51738.1.
AL035425 Genomic DNA. Translation: CAB90290.1.
CH471120 Genomic DNA. Translation: EAX02682.1.
CCDSiCCDS14544.1.
RefSeqiNP_003595.1. NM_003604.2.
UniGeneiHs.460872.

Genome annotation databases

EnsembliENST00000372129; ENSP00000361202; ENSG00000133124.
GeneIDi8471.
KEGGihsa:8471.
UCSCiuc004eoc.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF007567 mRNA. Translation: AAC51738.1 .
AL035425 Genomic DNA. Translation: CAB90290.1 .
CH471120 Genomic DNA. Translation: EAX02682.1 .
CCDSi CCDS14544.1.
RefSeqi NP_003595.1. NM_003604.2.
UniGenei Hs.460872.

3D structure databases

ProteinModelPortali O14654.
SMRi O14654. Positions 78-339.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114048. 89 interactions.
IntActi O14654. 81 interactions.
MINTi MINT-1151881.
STRINGi 9606.ENSP00000361202.

PTM databases

PhosphoSitei O14654.

Proteomic databases

MaxQBi O14654.
PaxDbi O14654.
PRIDEi O14654.

Protocols and materials databases

DNASUi 8471.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000372129 ; ENSP00000361202 ; ENSG00000133124 .
GeneIDi 8471.
KEGGi hsa:8471.
UCSCi uc004eoc.2. human.

Organism-specific databases

CTDi 8471.
GeneCardsi GC0XM107975.
HGNCi HGNC:6128. IRS4.
HPAi HPA017372.
MIMi 300904. gene.
neXtProti NX_O14654.
PharmGKBi PA29923.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG81285.
GeneTreei ENSGT00530000063420.
HOGENOMi HOG000113104.
HOVERGENi HBG107140.
InParanoidi O14654.
KOi K17446.
OMAi RCGHSEQ.
OrthoDBi EOG7XM2X6.
PhylomeDBi O14654.
TreeFami TF325994.

Enzyme and pathway databases

Reactomei REACT_150203. IRS-related events triggered by IGF1R.
SignaLinki O14654.

Miscellaneous databases

GeneWikii IRS4.
GenomeRNAii 8471.
NextBioi 31702.
PROi O14654.
SOURCEi Search...

Gene expression databases

Bgeei O14654.
CleanExi HS_IRS4.
Genevestigatori O14654.

Family and domain databases

Gene3Di 2.30.29.30. 2 hits.
InterProi IPR002404. Insln_rcpt_S1.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
[Graphical view ]
Pfami PF02174. IRS. 1 hit.
[Graphical view ]
PRINTSi PR00628. INSULINRSI.
SMARTi SM00233. PH. 1 hit.
SM00310. PTBI. 1 hit.
[Graphical view ]
PROSITEi PS51064. IRS_PTB. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-20; GLU-215 AND ARG-557.

Entry informationi

Entry nameiIRS4_HUMAN
AccessioniPrimary (citable) accession number: O14654
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 121 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. SIMILARITY comments
    Index of protein domains and families

External Data

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