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Protein

Tyrosine-protein kinase receptor

Gene

Kit

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.UniRule annotationSAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei793 – 7931Proton acceptorUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, ReceptorUniRule annotationSAAS annotationImported, Transferase, Tyrosine-protein kinaseUniRule annotationSAAS annotation

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-1257604. PIP3 activates AKT signaling.
R-RNO-1433557. Signaling by SCF-KIT.
R-RNO-1433559. Regulation of KIT signaling.
R-RNO-5673001. RAF/MAP kinase cascade.
R-RNO-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase receptorUniRule annotation (EC:2.7.10.1UniRule annotation)
Gene namesi
Name:KitImported
Synonyms:KITImported
ORF Names:rCG_56893Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi620568. Kit.

Subcellular locationi

  • Membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei523 – 55028HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • acrosomal vesicle Source: RGD
  • cell-cell junction Source: Ensembl
  • cytoplasm Source: RGD
  • cytoplasmic side of plasma membrane Source: RGD
  • external side of plasma membrane Source: RGD
  • extracellular space Source: Ensembl
  • integral component of membrane Source: UniProtKB-KW
  • mast cell granule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 978953Tyrosine-protein kinase receptorSequence analysisPRO_5007211210Add
BLAST

Keywords - PTMi

Disulfide bondSAAS annotation, PhosphoproteinUniRule annotation

PTM databases

iPTMnetiQ63116.

Expressioni

Gene expression databases

ExpressionAtlasiQ63116. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003050.

Structurei

3D structure databases

SMRiQ63116. Positions 33-509, 549-936.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 9761Ig-like (immunoglobulin-like)InterPro annotationAdd
BLAST
Domaini212 – 31099Ig-like (immunoglobulin-like)InterPro annotationAdd
BLAST
Domaini591 – 938348Protein kinaseInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family.SAAS annotation
Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.UniRule annotation
Contains protein kinase domain.SAAS annotation

Keywords - Domaini

Immunoglobulin domainUniRule annotationSAAS annotation, RepeatSAAS annotation, SignalSequence analysis, Transmembrane, Transmembrane helixSequence analysisSAAS annotation

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000112008.
HOVERGENiHBG004335.
KOiK05091.
OMAiYFCPGTE.
OrthoDBiEOG7S7SCZ.
PhylomeDBiQ63116.
TreeFamiTF325768.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR027263. SCGF_receptor.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
IPR001824. Tyr_kinase_rcpt_3_CS.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF500951. SCGF_recepter. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTiSM00409. IG. 4 hits.
SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q63116-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGARGAWDL LCVLLVLLRG QTGTSQPSAS PGEPSPPSIQ PAQSELIVEA
60 70 80 90 100
GDTIRLTCTD PAFVKWTFEI LDVRIENKQS EWIREKAEAT HTGKYTCVSG
110 120 130 140 150
SGLRSSIYVF VRDPAVLFLV GLPLFGKEDN DALVRCPLTD PQVSNYSLIE
160 170 180 190 200
CDGKSLPTDL KFVPNPKAGI TIKNVKRAYH RLCIRCAAQR EGKWMRSDKF
210 220 230 240 250
TLKVRAAIKA IPVVSVPETS HLLKEGDTFT VICTIKDVST SVDSMWIKLN
260 270 280 290 300
PQPQSKAQVK RNSWHQGDFN YERQETLTIS SARVNDSGVF MCYANNTFGS
310 320 330 340 350
ANVTTTLKVV EKGFINIFPV KNTTVFVTDG ENVDLVVEFE AYPKPEHQQW
360 370 380 390 400
IYMNRTPTNR GEDYVKSDNQ SNIRYVNELR LTRLKGTEGG TYTFLVSNSD
410 420 430 440 450
VSASVTFDVY VNTKPEILTY DRLMNGRLQC VAAGFPEPTI DWYFCTGAEQ
460 470 480 490 500
RCTVPVPPVD VQIQNASVSP FGKLVVQSSI DSSVFRHNGT VECKASNAVG
510 520 530 540 550
KSSAFFNFAF KGNSKEQIQP HTLFTPLLIG FVVTAGLMGI IVMVLAYKYL
560 570 580 590 600
QKPMYEVQWK VVEEINGNNY VYIDPTQLPY DHKWEFPRNR LSFGKTLGAG
610 620 630 640 650
AFGKVVEATA YGLIKSDAAM TVAVKMLKPS AHLTEREALM SELKVLSYLG
660 670 680 690 700
NHMNIVNLLG ACTVGGPTLV ITEYCCYGDL LNFLRRKRDS FIFSKQEEQA
710 720 730 740 750
DAALYKNLLH SKESSCDSSN EYMDMKPGVS YVVPTKTDKR RSARIDSYIE
760 770 780 790 800
RDVTPAIMED DELALDLEDL LSFSYQVAKG MAFLASKNCI HRDLAARNIL
810 820 830 840 850
LTHGRITKIC DFGLARDIRN DSNYVVKGNA RLPVKWMAPE SIFNCVYTFE
860 870 880 890 900
SDVWSYGIFL WELFSLGSSP YPGMPVDSKF YKMIKEGFRM LSPEHAPAAM
910 920 930 940 950
YEVMKTCWDA DPLKRPTFKQ VVQLIEKQIS DSSKHIYSNL ANCNPNPENP
960 970
VVVDHSVRVN SVGSSTSSTQ PLLVHEDA
Length:978
Mass (Da):109,342
Last modified:November 1, 1996 - v1
Checksum:i0958C33F19889051
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07014877 Genomic DNA. No translation available.
AABR07014878 Genomic DNA. No translation available.
AABR07014879 Genomic DNA. No translation available.
EU247827 mRNA. Translation: ABX45067.1.
EU247828 mRNA. Translation: ABX45068.1.
D12524 mRNA. Translation: BAA02094.1.
CH473981 Genomic DNA. Translation: EDL89921.1.
PIRiA49814.
RefSeqiNP_071600.1. NM_022264.1.
UniGeneiRn.54004.

Genome annotation databases

EnsembliENSRNOT00000003050; ENSRNOP00000003050; ENSRNOG00000002227.
GeneIDi64030.
KEGGirno:64030.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07014877 Genomic DNA. No translation available.
AABR07014878 Genomic DNA. No translation available.
AABR07014879 Genomic DNA. No translation available.
EU247827 mRNA. Translation: ABX45067.1.
EU247828 mRNA. Translation: ABX45068.1.
D12524 mRNA. Translation: BAA02094.1.
CH473981 Genomic DNA. Translation: EDL89921.1.
PIRiA49814.
RefSeqiNP_071600.1. NM_022264.1.
UniGeneiRn.54004.

3D structure databases

SMRiQ63116. Positions 33-509, 549-936.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003050.

PTM databases

iPTMnetiQ63116.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000003050; ENSRNOP00000003050; ENSRNOG00000002227.
GeneIDi64030.
KEGGirno:64030.

Organism-specific databases

CTDi3815.
RGDi620568. Kit.

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000112008.
HOVERGENiHBG004335.
KOiK05091.
OMAiYFCPGTE.
OrthoDBiEOG7S7SCZ.
PhylomeDBiQ63116.
TreeFamiTF325768.

Enzyme and pathway databases

ReactomeiR-RNO-1257604. PIP3 activates AKT signaling.
R-RNO-1433557. Signaling by SCF-KIT.
R-RNO-1433559. Regulation of KIT signaling.
R-RNO-5673001. RAF/MAP kinase cascade.
R-RNO-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.

Gene expression databases

ExpressionAtlasiQ63116. baseline and differential.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR027263. SCGF_receptor.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
IPR001824. Tyr_kinase_rcpt_3_CS.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF500951. SCGF_recepter. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTiSM00409. IG. 4 hits.
SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50835. IG_LIKE. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of Ws mutant allele of rats: a 12-base deletion in tyrosine kinase domain of c-kit gene."
    Tsujimura T., Hirota S., Nomura S., Niwa Y., Yamazaki M., Tono T., Morii E., Kim H., Kondo K., Nishimune Y., Kitamura Y.
    Blood 78:1942-1946(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Sprague-DawleyImported.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  5. "Characterization of Renag1 Candidates."
    Lachel C.M., Fisher K.W., Shull J.D.
    Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ACIImported and BNImported.
    Tissue: LungImported.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiQ63116_RAT
AccessioniPrimary (citable) accession number: Q63116
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.