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Protein

Fibroblast growth factor receptor

Gene

Fgfr1

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 sitei530 – 5301Proton 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-109704. PI3K Cascade.
R-RNO-1257604. PIP3 activates AKT signaling.
R-RNO-190370. FGFR1b ligand binding and activation.
R-RNO-190373. FGFR1c ligand binding and activation.
R-RNO-190374. FGFR1c and Klotho ligand binding and activation.
R-RNO-445144. Signal transduction by L1.
R-RNO-5654219. Phospholipase C-mediated cascade: FGFR1.
R-RNO-5654687. Downstream signaling of activated FGFR1.
R-RNO-5654688. SHC-mediated cascade:FGFR1.
R-RNO-5654689. PI-3K cascade:FGFR1.
R-RNO-5654693. FRS-mediated FGFR1 signaling.
R-RNO-5654726. Negative regulation of FGFR1 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:
Fibroblast growth factor receptorUniRule annotation (EC:2.7.10.1UniRule annotation)
Gene namesi
Name:Fgfr1Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi620713. Fgfr1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei286 – 30621HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 729708Fibroblast growth factor receptorSequence analysisPRO_5007707234Add
BLAST

Keywords - PTMi

Disulfide bondSAAS annotation

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000036885.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 15589Ig-like (immunoglobulin-like)InterPro annotationAdd
BLAST
Domaini164 – 266103Ig-like (immunoglobulin-like)InterPro annotationAdd
BLAST
Domaini385 – 674290Protein kinaseInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.UniRule annotation
Contains protein kinase domain.SAAS annotation

Keywords - Domaini

Immunoglobulin domainSAAS annotation, RepeatSAAS annotation, SignalSequence analysis, Transmembrane, Transmembrane helixSequence analysisSAAS annotation

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000263410.
HOVERGENiHBG000345.
OrthoDBiEOG7NGQ9N.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR028174. FGF_rcpt_1.
IPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
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.
[Graphical view]
PANTHERiPTHR24416:SF131. PTHR24416:SF131. 1 hit.
PfamiPF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000628. FGFR. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50835. IG_LIKE. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q63827-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWGWRGLLFW AVLVTATLCT ARPAPTLPEQ DALPSSEDDD DDDDSSSEEK
60 70 80 90 100
ETDNTKPNPV APYWTSPEKM EKKLHAVPAA KTVKFKCPSS GTPSPTLRWL
110 120 130 140 150
KNGKEFKPDH RIGGYKVRYA TWSIIMDSVV PSDKGNYTCI VENEYGSINH
160 170 180 190 200
TYQLDVVERS PHRPILQAGL PANKTVALGS NVEFMCKVYS DPQPHIQWLK
210 220 230 240 250
HIEVNGSKIG PDNLPYVQIL KTAGVNTTDK EMEVLHLRNV SFEDAGEYTC
260 270 280 290 300
LAGNSIGLSH HSAWLTVLEA LEERPAVMTS PLYLEIIIYC TGAFLISCMV
310 320 330 340 350
GSVIIYKMKS GTKKSDFHSQ MAVHKLAKSI PLRRQVSADS SASMNSGVLL
360 370 380 390 400
VRPSRLSSSG TPMLAGVSEY ELPEDPRWEL PRDRLVLGKP LGEGCFGQVV
410 420 430 440 450
LAEAIGLDKD KPNRVTKVAV KMLKSDATEK DLSDLISEME MMKMIGKHKN
460 470 480 490 500
IINLLGACTQ DGPLYVIVEY ASKGNLREYL QARRPPGLEY CYNPSHNPEE
510 520 530 540 550
QLSSKDLVSC AYQVARGMEY LASKKCIHRD LAARNVLVTE DNVMKIADFG
560 570 580 590 600
LARDIHHIDY YKKTTNGRLP VKWMAPEALF DRIYTHQSDV WSFGVLLWEI
610 620 630 640 650
FTLGGSPYPG VPVEELFKLL KEGHRMDKPS NCTNELYMMM RDCWHAVPSQ
660 670 680 690 700
RPTFKQLVED LDRIVALTSN QEYLDLSMPL DQYSPSFPDT RSSTCSSGED
710 720
SVFSHEPLPE EPCLPRHPTQ LANGGLKRR
Length:729
Mass (Da):81,627
Last modified:November 1, 1996 - v1
Checksum:iC19DFDAFFD5BA0BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07026305 Genomic DNA. No translation available.
AABR07026306 Genomic DNA. No translation available.
S54008 mRNA. Translation: AAB54274.1.
PIRiA56795.
RefSeqiXP_006253389.1. XM_006253327.1.
UniGeneiRn.207203.
Rn.9797.

Genome annotation databases

EnsembliENSRNOT00000050980; ENSRNOP00000043459; ENSRNOG00000016050.
GeneIDi79114.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07026305 Genomic DNA. No translation available.
AABR07026306 Genomic DNA. No translation available.
S54008 mRNA. Translation: AAB54274.1.
PIRiA56795.
RefSeqiXP_006253389.1. XM_006253327.1.
UniGeneiRn.207203.
Rn.9797.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000036885.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000050980; ENSRNOP00000043459; ENSRNOG00000016050.
GeneIDi79114.

Organism-specific databases

CTDi2260.
RGDi620713. Fgfr1.

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000263410.
HOVERGENiHBG000345.
OrthoDBiEOG7NGQ9N.

Enzyme and pathway databases

ReactomeiR-RNO-109704. PI3K Cascade.
R-RNO-1257604. PIP3 activates AKT signaling.
R-RNO-190370. FGFR1b ligand binding and activation.
R-RNO-190373. FGFR1c ligand binding and activation.
R-RNO-190374. FGFR1c and Klotho ligand binding and activation.
R-RNO-445144. Signal transduction by L1.
R-RNO-5654219. Phospholipase C-mediated cascade: FGFR1.
R-RNO-5654687. Downstream signaling of activated FGFR1.
R-RNO-5654688. SHC-mediated cascade:FGFR1.
R-RNO-5654689. PI-3K cascade:FGFR1.
R-RNO-5654693. FRS-mediated FGFR1 signaling.
R-RNO-5654726. Negative regulation of FGFR1 signaling.
R-RNO-5673001. RAF/MAP kinase cascade.
R-RNO-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR028174. FGF_rcpt_1.
IPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
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.
[Graphical view]
PANTHERiPTHR24416:SF131. PTHR24416:SF131. 1 hit.
PfamiPF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000628. FGFR. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50835. IG_LIKE. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of rat fibroblast growth factor receptor 1 as three splicing variants during kidney development."
    Kim E.G., Kwon H.M., Burrow C.R., Ballermann B.J.
    Am. J. Physiol. 264:F66-F73(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  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. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.
  4. "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].

Entry informationi

Entry nameiQ63827_RAT
AccessioniPrimary (citable) accession number: Q63827
Secondary accession number(s): F1LPM6
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.