ID   D2CGD1_HUMAN            Unreviewed;       732 AA.
AC   D2CGD1;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   13-FEB-2019, entry version 81.
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:ENSP00000484154};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:ABO25744.1};
RN   [1] {ECO:0000313|Ensembl:ENSP00000484154, 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.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   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.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   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.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R., Hubbard T.,
RA   Doucette-Stamm L., Beck S., 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:0000313|EMBL:ABO25744.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Feng Y.-H., Cheng H.;
RT   "Identification of a fibroblast growth factor receptor subtype-2
RT   variant.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000213|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   [4] {ECO:0000213|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [5] {ECO:0000313|Ensembl:ENSP00000484154}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2014) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-
CC         tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136,
CC         Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC         EC=2.7.10.1; Evidence={ECO:0000256|PIRNR:PIRNR000628,
CC         ECO:0000256|SAAS:SAAS01124082};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Fibroblast growth factor receptor subfamily.
CC       {ECO:0000256|PIRNR:PIRNR000628}.
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DR   EMBL; AC009988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF455288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; EF057068; ABO25744.1; -; mRNA.
DR   RefSeq; NP_075418.1; NM_023029.2.
DR   UniGene; Hs.533683; -.
DR   Ensembl; ENST00000613048; ENSP00000484154; ENSG00000066468.
DR   GeneID; 2263; -.
DR   UCSC; uc057wkv.1; human.
DR   CTD; 2263; -.
DR   EuPathDB; HostDB:ENSG00000066468.20; -.
DR   HGNC; HGNC:3689; FGFR2.
DR   OpenTargets; ENSG00000066468; -.
DR   eggNOG; KOG0200; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   GeneTree; ENSGT00940000155447; -.
DR   OrthoDB; 220433at2759; -.
DR   ChiTaRS; FGFR2; human.
DR   GenomeRNAi; 2263; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000066468; Expressed in 222 organ(s), highest expression level in C1 segment of cervical spinal cord.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005007; F:fibroblast growth factor-activated receptor activity; IEA:InterPro.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 2.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PIRSF; PIRSF000628; FGFR; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
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|PIRNR:PIRNR000628,
KW   ECO:0000256|SAAS:SAAS00708816};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00916669};
KW   Immunoglobulin domain {ECO:0000256|SAAS:SAAS00941986};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000628, ECO:0000256|SAAS:SAAS00582553};
KW   Membrane {ECO:0000256|SAAS:SAAS00602683, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000628,
KW   ECO:0000256|SAAS:SAAS00708816};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:D2CGD1};
KW   Receptor {ECO:0000256|PIRNR:PIRNR000628,
KW   ECO:0000256|SAAS:SAAS00600436, ECO:0000313|EMBL:ABO25744.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Repeat {ECO:0000256|SAAS:SAAS00457685};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000628,
KW   ECO:0000256|SAAS:SAAS00582553};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00602683,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00602683,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000628,
KW   ECO:0000256|SAAS:SAAS00582553}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    732       Fibroblast growth factor receptor.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5014087146.
FT   TRANSMEM    289    309       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       65    158       Ig-like. {ECO:0000259|PROSITE:PS50835}.
FT   DOMAIN      167    269       Ig-like. {ECO:0000259|PROSITE:PS50835}.
FT   DOMAIN      392    681       Protein kinase.
FT                                {ECO:0000259|PROSITE:PS50011}.
FT   ACT_SITE    537    537       Proton acceptor.
FT                                {ECO:0000256|PIRSR:PIRSR000628-1}.
SQ   SEQUENCE   732 AA;  82225 MW;  DC1D018D4F7C4803 CRC64;
     MVSWGRFICL VVVTMATLSL ARPSFSLVED TTLEPEDAIS SGDDEDDTDG AEDFVSENSN
     NKRAPYWTNT EKMEKRLHAV PAANTVKFRC PAGGNPMPTM RWLKNGKEFK QEHRIGGYKV
     RNQHWSLIME SVVPSDKGNY TCVVENEYGS INHTYHLDVV ERSPHRPILQ AGLPANASTV
     VGGDVEFVCK VYSDAQPHIQ WIKHVEKNGS KYGPDGLPYL KVLKAAGVNT TDKEIEVLYI
     RNVTFEDAGE YTCLAGNSIG ISFHSAWLTV LPAPGREKEI TASPDYLEIA IYCIGVFLIA
     CMVVTVILCR MKNTTKKPDF SSQPAVHKLT KRIPLRRQVT VSAESSSSMN SNTPLVRITT
     RLSSTADTPM LAGVSEYELP EDPKWEFPRD KLTLGKPLGE GCFGQVVMAE AVGIDKDKPK
     EAVTVAVKML KDDATEKDLS DLVSEMEMMK MIGKHKNIIN LLGACTQDGP LYVIVEYASK
     GNLREYLRAR RPPGMEYSYD INRVPEEQMT FKDLVSCTYQ LARGMEYLAS QKCIHRDLAA
     RNVLVTENNV MKIADFGLAR DINNIDYYKK TTNGRLPVKW MAPEALFDRV YTHQSDVWSF
     GVLMWEIFTL GGSPYPGIPV EELFKLLKEG HRMDKPANCT NELYMMMRDC WHAVPSQRPT
     FKQLVEDLDR ILTLTTNEEY LDLSQPLEQY SPSYPDTRSS CSSGDDSVFS PDPMPYEPCL
     PQYPHINGSV KT
//