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P14616

- INSRR_HUMAN

UniProt

P14616 - INSRR_HUMAN

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Protein

Insulin receptor-related protein

Gene

INSRR

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

Functioni

Receptor with tyrosine-protein kinase activity. Functions as a pH sensing receptor which is activated by increased extracellular pH. Activates an intracellular signaling pathway that involves IRS1 and AKT1/PKB.1 Publication

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1013 – 10131ATPPROSITE-ProRule annotation
Active sitei1115 – 11151Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi985 – 9939ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. cellular response to alkaline pH Source: UniProtKB
  3. male sex determination Source: Ensembl
  4. peptidyl-tyrosine phosphorylation Source: GOC
  5. protein autophosphorylation Source: UniProtKB
  6. transmembrane receptor protein tyrosine kinase signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin receptor-related protein (EC:2.7.10.1)
Short name:
IRR
Alternative name(s):
IR-related receptor
Cleaved into the following 2 chains:
Gene namesi
Name:INSRR
Synonyms:IRR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6093. INSRR.

Subcellular locationi

GO - Cellular componenti

  1. integral component of plasma membrane Source: UniProtKB
  2. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1145 – 11462YY → FF: Abolishes autophosphorylation. 1 Publication

Organism-specific databases

PharmGKBiPA29899.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 12971271Insulin receptor-related proteinPRO_0000016701Add
BLAST
Chaini27 – 742716Insulin receptor-related protein alpha chainCuratedPRO_0000016702Add
BLAST
Chaini747 – 1297551Insulin receptor-related protein beta chainCuratedPRO_0000016703Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi47 – 471N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi214 ↔ 222By similarity
Disulfide bondi216 ↔ 228By similarity
Disulfide bondi229 ↔ 237By similarity
Disulfide bondi233 ↔ 246By similarity
Disulfide bondi249 ↔ 258By similarity
Disulfide bondi262 ↔ 274By similarity
Disulfide bondi280 ↔ 300By similarity
Disulfide bondi304 ↔ 317By similarity
Glycosylationi311 – 3111N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi320 ↔ 324By similarity
Glycosylationi411 – 4111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi492 – 4921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi528 – 5281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi616 – 6161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi634 – 6341N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi657 ↔ 864Interchain (between alpha and beta chains)Sequence Analysis
Glycosylationi756 – 7561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi885 – 8851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi898 – 8981N-linked (GlcNAc...)Sequence Analysis
Modified residuei1145 – 11451Phosphotyrosine; by autocatalysisCurated
Modified residuei1146 – 11461Phosphotyrosine; by autocatalysisCurated

Post-translational modificationi

Autophosphorylated on tyrosine residues between pH 7.9 and pH 10.5.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP14616.
PaxDbiP14616.
PRIDEiP14616.

PTM databases

PhosphoSiteiP14616.

Expressioni

Gene expression databases

BgeeiP14616.
CleanExiHS_INSRR.
ExpressionAtlasiP14616. baseline.
GenevestigatoriP14616.

Organism-specific databases

HPAiHPA025285.

Interactioni

Subunit structurei

Probable tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains contribute to the formation of the ligand-binding domain, while the beta chains carry the kinase domain.

Protein-protein interaction databases

BioGridi109856. 3 interactions.
IntActiP14616. 1 interaction.
STRINGi9606.ENSP00000357178.

Structurei

3D structure databases

ProteinModelPortaliP14616.
SMRiP14616. Positions 971-1262.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini747 – 921175ExtracellularSequence AnalysisAdd
BLAST
Topological domaini944 – 1297354CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei922 – 94322HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini483 – 603121Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini607 – 707101Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini818 – 91396Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini979 – 1254276Protein kinasePROSITE-ProRule annotationAdd
BLAST

Domaini

The extracellular domain is required for sensing alterations in external pH.

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation
Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000038045.
HOVERGENiHBG006134.
InParanoidiP14616.
KOiK05086.
OMAiFARTMPH.
OrthoDBiEOG73RB9N.
PhylomeDBiP14616.
TreeFamiTF351636.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProiIPR000494. EGF_rcpt_L.
IPR003961. Fibronectin_type3.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR028792. INSRR.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016246. Tyr_kinase_insulin-like_rcpt.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PANTHERiPTHR24416:SF107. PTHR24416:SF107. 1 hit.
PfamiPF00041. fn3. 1 hit.
PF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFiPIRSF000620. Insulin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 4 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS50853. FN3. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14616 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVPSLWPWG ACLPVIFLSL GFGLDTVEVC PSLDIRSEVA ELRQLENCSV
60 70 80 90 100
VEGHLQILLM FTATGEDFRG LSFPRLTQVT DYLLLFRVYG LESLRDLFPN
110 120 130 140 150
LAVIRGTRLF LGYALVIFEM PHLRDVALPA LGAVLRGAVR VEKNQELCHL
160 170 180 190 200
STIDWGLLQP APGANHIVGN KLGEECADVC PGVLGAAGEP CAKTTFSGHT
210 220 230 240 250
DYRCWTSSHC QRVCPCPHGM ACTARGECCH TECLGGCSQP EDPRACVACR
260 270 280 290 300
HLYFQGACLW ACPPGTYQYE SWRCVTAERC ASLHSVPGRA STFGIHQGSC
310 320 330 340 350
LAQCPSGFTR NSSSIFCHKC EGLCPKECKV GTKTIDSIQA AQDLVGCTHV
360 370 380 390 400
EGSLILNLRQ GYNLEPQLQH SLGLVETITG FLKIKHSFAL VSLGFFKNLK
410 420 430 440 450
LIRGDAMVDG NYTLYVLDNQ NLQQLGSWVA AGLTIPVGKI YFAFNPRLCL
460 470 480 490 500
EHIYRLEEVT GTRGRQNKAE INPRTNGDRA ACQTRTLRFV SNVTEADRIL
510 520 530 540 550
LRWERYEPLE ARDLLSFIVY YKESPFQNAT EHVGPDACGT QSWNLLDVEL
560 570 580 590 600
PLSRTQEPGV TLASLKPWTQ YAVFVRAITL TTEEDSPHQG AQSPIVYLRT
610 620 630 640 650
LPAAPTVPQD VISTSNSSSH LLVRWKPPTQ RNGNLTYYLV LWQRLAEDGD
660 670 680 690 700
LYLNDYCHRG LRLPTSNNDP RFDGEDGDPE AEMESDCCPC QHPPPGQVLP
710 720 730 740 750
PLEAQEASFQ KKFENFLHNA ITIPISPWKV TSINKSPQRD SGRHRRAAGP
760 770 780 790 800
LRLGGNSSDF EIQEDKVPRE RAVLSGLRHF TEYRIDIHAC NHAAHTVGCS
810 820 830 840 850
AATFVFARTM PHREADGIPG KVAWEASSKN SVLLRWLEPP DPNGLILKYE
860 870 880 890 900
IKYRRLGEEA TVLCVSRLRY AKFGGVHLAL LPPGNYSARV RATSLAGNGS
910 920 930 940 950
WTDSVAFYIL GPEEEDAGGL HVLLTATPVG LTLLIVLAAL GFFYGKKRNR
960 970 980 990 1000
TLYASVNPEY FSASDMYVPD EWEVPREQIS IIRELGQGSF GMVYEGLARG
1010 1020 1030 1040 1050
LEAGEESTPV ALKTVNELAS PRECIEFLKE ASVMKAFKCH HVVRLLGVVS
1060 1070 1080 1090 1100
QGQPTLVIME LMTRGDLKSH LRSLRPEAEN NPGLPQPALG EMIQMAGEIA
1110 1120 1130 1140 1150
DGMAYLAANK FVHRDLAARN CMVSQDFTVK IGDFGMTRDV YETDYYRKGG
1160 1170 1180 1190 1200
KGLLPVRWMA PESLKDGIFT THSDVWSFGV VLWEIVTLAE QPYQGLSNEQ
1210 1220 1230 1240 1250
VLKFVMDGGV LEELEGCPLQ LQELMSRCWQ PNPRLRPSFT HILDSIQEEL
1260 1270 1280 1290
RPSFRLLSFY YSPECRGARG SLPTTDAEPD SSPTPRDCSP QNGGPGH
Length:1,297
Mass (Da):143,720
Last modified:January 11, 2001 - v2
Checksum:iBB22C7FF61E3065D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti127 – 1271A → E.1 Publication
Corresponds to variant rs55757706 [ dbSNP | Ensembl ].
VAR_041434
Natural varianti161 – 1611A → V.1 Publication
Corresponds to variant rs55971900 [ dbSNP | Ensembl ].
VAR_041435
Natural varianti244 – 2441R → H.1 Publication
Corresponds to variant rs55951840 [ dbSNP | Ensembl ].
VAR_041436
Natural varianti246 – 2461C → R.1 Publication
Corresponds to variant rs56377825 [ dbSNP | Ensembl ].
VAR_041437
Natural varianti278 – 2781E → Q in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041438
Natural varianti554 – 5541R → C.1 Publication
Corresponds to variant rs56068937 [ dbSNP | Ensembl ].
VAR_041439
Natural varianti928 – 9281P → L.1 Publication
Corresponds to variant rs56252149 [ dbSNP | Ensembl ].
VAR_041440
Natural varianti1065 – 10651G → E in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_041441

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF064078 mRNA. Translation: AAC17167.1.
AL158169 Genomic DNA. Translation: CAH70009.1.
CH471121 Genomic DNA. Translation: EAW52903.1.
J05046 mRNA. Translation: AAC31759.1.
CCDSiCCDS1160.1.
PIRiB36502.
RefSeqiNP_055030.1. NM_014215.2.
UniGeneiHs.248138.

Genome annotation databases

EnsembliENST00000368195; ENSP00000357178; ENSG00000027644.
GeneIDi3645.
KEGGihsa:3645.
UCSCiuc010pht.2. human.

Polymorphism databases

DMDMi12644000.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF064078 mRNA. Translation: AAC17167.1 .
AL158169 Genomic DNA. Translation: CAH70009.1 .
CH471121 Genomic DNA. Translation: EAW52903.1 .
J05046 mRNA. Translation: AAC31759.1 .
CCDSi CCDS1160.1.
PIRi B36502.
RefSeqi NP_055030.1. NM_014215.2.
UniGenei Hs.248138.

3D structure databases

ProteinModelPortali P14616.
SMRi P14616. Positions 971-1262.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109856. 3 interactions.
IntActi P14616. 1 interaction.
STRINGi 9606.ENSP00000357178.

Chemistry

BindingDBi P14616.
ChEMBLi CHEMBL5483.
GuidetoPHARMACOLOGYi 1802.

PTM databases

PhosphoSitei P14616.

Polymorphism databases

DMDMi 12644000.

Proteomic databases

MaxQBi P14616.
PaxDbi P14616.
PRIDEi P14616.

Protocols and materials databases

DNASUi 3645.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368195 ; ENSP00000357178 ; ENSG00000027644 .
GeneIDi 3645.
KEGGi hsa:3645.
UCSCi uc010pht.2. human.

Organism-specific databases

CTDi 3645.
GeneCardsi GC01M156809.
H-InvDB HIX0028530.
HGNCi HGNC:6093. INSRR.
HPAi HPA025285.
MIMi 147671. gene.
neXtProti NX_P14616.
PharmGKBi PA29899.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118818.
HOGENOMi HOG000038045.
HOVERGENi HBG006134.
InParanoidi P14616.
KOi K05086.
OMAi FARTMPH.
OrthoDBi EOG73RB9N.
PhylomeDBi P14616.
TreeFami TF351636.

Miscellaneous databases

GeneWikii INSRR.
GenomeRNAii 3645.
NextBioi 14267.
PROi P14616.
SOURCEi Search...

Gene expression databases

Bgeei P14616.
CleanExi HS_INSRR.
ExpressionAtlasi P14616. baseline.
Genevestigatori P14616.

Family and domain databases

Gene3Di 2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProi IPR000494. EGF_rcpt_L.
IPR003961. Fibronectin_type3.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR028792. INSRR.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016246. Tyr_kinase_insulin-like_rcpt.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view ]
PANTHERi PTHR24416:SF107. PTHR24416:SF107. 1 hit.
Pfami PF00041. fn3. 1 hit.
PF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view ]
PIRSFi PIRSF000620. Insulin_receptor. 1 hit.
PRINTSi PR00109. TYRKINASE.
SMARTi SM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 4 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEi PS50853. FN3. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of the complete cDNA encoding the human insulin receptor related receptor."
    Haenze J., Berthold A., Klammt J., Gallaher B., Siebler T., Kratzsch J., Elmlinger M., Kiess W.
    Horm. Metab. Res. 31:77-79(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Primary structure of a putative receptor for a ligand of the insulin family."
    Shier P., Watt V.M.
    J. Biol. Chem. 264:14605-14608(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-1297.
  5. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-127; VAL-161; HIS-244; ARG-246; GLN-278; CYS-554; LEU-928 AND GLU-1065.
  6. Cited for: FUNCTION, MUTAGENESIS OF 1145-TYR-TYR-1146, AUTOPHOSPHORYLATION.

Entry informationi

Entry nameiINSRR_HUMAN
AccessioniPrimary (citable) accession number: P14616
Secondary accession number(s): O60724, Q5VZS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 11, 2001
Last modified: October 29, 2014
This is version 152 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3