ID A0A0A0MR25_HUMAN Unreviewed; 821 AA. AC A0A0A0MR25; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 02-OCT-2024, entry version 70. DE RecName: Full=Fibroblast growth factor receptor {ECO:0000256|PIRNR:PIRNR000628}; DE EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR000628}; GN Name=FGFR2 {ECO:0000313|Ensembl:ENSP00000309878}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000309878, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000309878, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I., RA Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., RA Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., RA Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., RA Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., RA Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., RA Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., RA Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., RA Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., RA Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., RA Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., RA Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., RA Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., RA Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., RA Fechtel K., Bentley D., Durbin R., Hubbard T., Doucette-Stamm L., Beck S., RA Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [2] {ECO:0007829|PubMed:19369195} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [3] {ECO:0000313|Ensembl:ENSP00000309878} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2014) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; CC Evidence={ECO:0000256|ARBA:ARBA00001171, CC ECO:0000256|PIRNR:PIRNR000628}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. CC Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}. Membrane CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. Fibroblast growth factor receptor subfamily. CC {ECO:0000256|PIRNR:PIRNR000628}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC009988; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455288; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; A0A0A0MR25; -. DR SMR; A0A0A0MR25; -. DR MassIVE; A0A0A0MR25; -. DR PeptideAtlas; A0A0A0MR25; -. DR Antibodypedia; 4393; 1543 antibodies from 48 providers. DR Ensembl; ENST00000351936; ENSP00000309878; ENSG00000066468. DR UCSC; uc057wld.1; human. DR HGNC; HGNC:3689; FGFR2. DR OpenTargets; ENSG00000066468; -. DR VEuPathDB; HostDB:ENSG00000066468; -. DR ChiTaRS; FGFR2; human. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; ENSG00000066468; Expressed in C1 segment of cervical spinal cord and 202 other cell types or tissues. DR ExpressionAtlas; A0A0A0MR25; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0005007; F:fibroblast growth factor receptor activity; IEA:InterPro. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:InterPro. DR CDD; cd04973; IgI_1_FGFR; 1. DR CDD; cd05857; IgI_2_FGFR; 1. DR CDD; cd05858; IgI_3_FGFR2; 1. DR CDD; cd05101; PTKc_FGFR2; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 3. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR016248; FGF_rcpt_fam. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR050122; RTK. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR PANTHER; PTHR24416:SF130; FIBROBLAST GROWTH FACTOR RECEPTOR 2; 1. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR Pfam; PF07679; I-set; 1. DR Pfam; PF13927; Ig_3; 2. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR PIRSF; PIRSF000628; FGFR; 1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00409; IG; 3. DR SMART; SM00408; IGc2; 3. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF48726; Immunoglobulin; 3. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50835; IG_LIKE; 3. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000628}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR000628-3}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR000628- KW 4}; Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000628}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000628}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRNR:PIRNR000628}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0A0MR25, KW ECO:0007829|ProteomicsDB:A0A0A0MR25}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000628}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000628}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137, KW ECO:0000256|PIRNR:PIRNR000628}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..821 FT /note="Fibroblast growth factor receptor" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5001974407" FT TRANSMEM 380..400 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 39..125 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 154..247 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 256..360 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 481..770 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 131..151 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 626 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000628-1" FT BINDING 487..493 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2" FT BINDING 517 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2, FT ECO:0000256|PROSITE-ProRule:PRU10141" FT BINDING 565..567 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2" FT BINDING 571 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2" FT BINDING 630 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2" FT BINDING 644 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2" FT CARBOHYD 83 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR000628-4" FT CARBOHYD 123 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR000628-4" FT CARBOHYD 228 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR000628-4" FT CARBOHYD 241 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR000628-4" FT CARBOHYD 265 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR000628-4" FT CARBOHYD 297 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR000628-4" FT CARBOHYD 320 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR000628-4" FT CARBOHYD 333 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000256|PIRSR:PIRSR000628-4" FT DISULFID 62..107 FT /evidence="ECO:0000256|PIRSR:PIRSR000628-3" FT DISULFID 179..231 FT /evidence="ECO:0000256|PIRSR:PIRSR000628-3" FT DISULFID 278..344 FT /evidence="ECO:0000256|PIRSR:PIRSR000628-3" SQ SEQUENCE 821 AA; 92071 MW; 58F3A4B9D44F2828 CRC64; MVSWGRFICL VVVTMATLSL ARPSFSLVED TTLEPEEPPT KYQISQPEVY VAAPGESLEV RCLLKDAAVI SWTKDGVHLG PNNRTVLIGE YLQIKGATPR DSGLYACTAS RTVDSETWYF MVNVTDAISS GDDEDDTDGA EDFVSENSNN KRAPYWTNTE KMEKRLHAVP AANTVKFRCP AGGNPMPTMR WLKNGKEFKQ EHRIGGYKVR NQHWSLIMES VVPSDKGNYT CVVENEYGSI NHTYHLDVVE RSPHRPILQA GLPANASTVV GGDVEFVCKV YSDAQPHIQW IKHVEKNGSK YGPDGLPYLK VLKVFAAGVN TTDKEIEVLY IRNVTFEDAG EYTCLAGNSI GISFHSAWLT VLPAPGREKE ITASPDYLEI AIYCIGVFLI ACMVVTVILC RMKNTTKKPD FSSQPAVHKL TKRIPLRRQV SAESSSSMNS NTPLVRITTR LSSTADTPML AGVSEYELPE DPKWEFPRDK LTLGKPLGEG CFGQVVMAEA VGIDKDKPKE AVTVAVKMLK DDATEKDLSD LVSEMEMMKM IGKHKNIINL LGACTQDGPL YVIVEYASKG NLREYLRARR PPGMEYSYDI NRVPEEQMTF KDLVSCTYQL ARGMEYLASQ KCIHRDLAAR NVLVTENNVM KIADFGLARD INNIDYYKKT TNGRLPVKWM APEALFDRVY THQSDVWSFG VLMWEIFTLG GSPYPGIPVE ELFKLLKEGH RMDKPANCTN ELYMMMRDCW HAVPSQRPTF KQLVEDLDRI LTLTTNEEYL DLSQPLEQYS PSYPDTRSSC SSGDDSVFSP DPMPYEPCLP QYPHINGSVK T //