FGFP1_HUMAN
ID FGFP1_HUMAN Reviewed; 234 AA.
AC Q14512; A8K5J2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Fibroblast growth factor-binding protein 1;
DE Short=FGF-BP;
DE Short=FGF-BP1;
DE Short=FGF-binding protein 1;
DE Short=FGFBP-1;
DE AltName: Full=17 kDa heparin-binding growth factor-binding protein;
DE Short=17 kDa HBGF-binding protein;
DE Short=HBp17;
DE Flags: Precursor;
GN Name=FGFBP1; Synonyms=FGFBP, HBP17;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEIN SEQUENCE OF 34-67; 92-118 AND
RP 146-158, IDENTIFICATION IN A COMPLEX WITH FGF1 AND FGF2, INTERACTION WITH
RP FGF1, AND TISSUE SPECIFICITY.
RC TISSUE=Epidermal carcinoma;
RX PubMed=1885605; DOI=10.1016/s0021-9258(18)55368-0;
RA Wu D.Q., Kan M.K., Sato G.H., Okamoto T., Sato J.D.;
RT "Characterization and molecular cloning of a putative binding protein for
RT heparin-binding growth factors.";
RL J. Biol. Chem. 266:16778-16785(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shi S., Sato J.D.;
RT "Gene sequence for the human FGF-binding protein HBp17.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION.
RX PubMed=9334727; DOI=10.1038/nm1097-1137;
RA Czubayko F., Liaudet-Coopman E.D., Aigner A., Tuveson A.T., Berchem G.J.,
RA Wellstein A.;
RT "A secreted FGF-binding protein can serve as the angiogenic switch in human
RT cancer.";
RL Nat. Med. 3:1137-1140(1997).
RN [7]
RP INTERACTION WITH HSPG2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11148217; DOI=10.1074/jbc.m011493200;
RA Mongiat M., Otto J., Oldershaw R., Ferrer F., Sato J.D., Iozzo R.V.;
RT "Fibroblast growth factor-binding protein is a novel partner for perlecan
RT protein core.";
RL J. Biol. Chem. 276:10263-10271(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH FGF2.
RX PubMed=11509569; DOI=10.1074/jbc.m104933200;
RA Tassi E., Al-Attar A., Aigner A., Swift M.R., McDonnell K., Karavanov A.,
RA Wellstein A.;
RT "Enhancement of fibroblast growth factor (FGF) activity by an FGF-binding
RT protein.";
RL J. Biol. Chem. 276:40247-40253(2001).
RN [9]
RP FUNCTION, INTERACTION WITH FGF7; FGF10 AND FGF22, INDUCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15806171; DOI=10.1038/sj.onc.1208560;
RA Beer H.-D., Bittner M., Niklaus G., Munding C., Max N., Goppelt A.,
RA Werner S.;
RT "The fibroblast growth factor binding protein is a novel interaction
RT partner of FGF-7, FGF-10 and FGF-22 and regulates FGF activity:
RT implications for epithelial repair.";
RL Oncogene 24:5269-5277(2005).
RN [10]
RP INTERACTION WITH FGF2, AND MUTAGENESIS OF CYS-214.
RX PubMed=16257968; DOI=10.1074/jbc.m510754200;
RA Xie B., Tassi E., Swift M.R., McDonnell K., Bowden E.T., Wang S., Ueda Y.,
RA Tomita Y., Riegel A.T., Wellstein A.;
RT "Identification of the fibroblast growth factor (FGF)-interacting domain in
RT a secreted FGF-binding protein by phage display.";
RL J. Biol. Chem. 281:1137-1144(2006).
CC -!- FUNCTION: Acts as a carrier protein that release fibroblast-binding
CC factors (FGFs) from the extracellular matrix (EM) storage and thus
CC enhance the mitogenic activity of FGFs. Enhances FGF2 signaling during
CC tissue repair, angiogenesis and in tumor growth.
CC {ECO:0000269|PubMed:11509569, ECO:0000269|PubMed:15806171,
CC ECO:0000269|PubMed:1885605, ECO:0000269|PubMed:9334727}.
CC -!- SUBUNIT: Found in a complex with FGFBP1, FGF1 and FGF2. Interacts with
CC FGF1, FGF2, FGF7, FGF10, FGF22 and HSPG2. {ECO:0000269|PubMed:11148217,
CC ECO:0000269|PubMed:11509569, ECO:0000269|PubMed:15806171,
CC ECO:0000269|PubMed:16257968, ECO:0000269|PubMed:1885605}.
CC -!- INTERACTION:
CC Q14512; Q12797-6: ASPH; NbExp=3; IntAct=EBI-953742, EBI-12092171;
CC Q14512; P09038: FGF2; NbExp=3; IntAct=EBI-953742, EBI-977447;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:11148217, ECO:0000269|PubMed:15806171}. Cell
CC membrane {ECO:0000269|PubMed:11148217, ECO:0000269|PubMed:15806171};
CC Peripheral membrane protein {ECO:0000269|PubMed:11148217,
CC ECO:0000269|PubMed:15806171}. Note=Extracellular and plasma membrane-
CC associated. Colocalizes with HSPG2 in the pericellular environment of
CC squamous cell carcinomas. {ECO:0000269|PubMed:11148217}.
CC -!- TISSUE SPECIFICITY: Expressed in the suprabasal region of the
CC epidermis, in hair follicles, the basement membrane at the dermo-
CC epidermal junction (occasionally extending into the basement membrane
CC of dermal blood vessels), wounded skin and several invasive squamous
CC cell carcinomas (at protein level). Expressed in normal and wounded
CC skin and various squamous cell carcinomas.
CC {ECO:0000269|PubMed:11148217, ECO:0000269|PubMed:15806171,
CC ECO:0000269|PubMed:1885605}.
CC -!- INDUCTION: Up-regulated in epithelial cells after skin injury.
CC Keratinocyte mitogens. {ECO:0000269|PubMed:15806171}.
CC -!- MISCELLANEOUS: Expression is significantly up-regulated in carcinogen-
CC induced skin tumors, various squamous cell carcinomas, some colon
CC cancer cell lines and tumors.
CC -!- SIMILARITY: Belongs to the fibroblast growth factor-binding protein
CC family. {ECO:0000305}.
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DR EMBL; M60047; AAA58636.1; -; mRNA.
DR EMBL; AF149412; AAD39216.1; -; Genomic_DNA.
DR EMBL; AK291307; BAF83996.1; -; mRNA.
DR EMBL; CH471069; EAW92748.1; -; Genomic_DNA.
DR EMBL; BC003628; AAH03628.1; -; mRNA.
DR EMBL; BC008910; AAH08910.1; -; mRNA.
DR CCDS; CCDS3418.1; -.
DR PIR; A41178; A41178.
DR RefSeq; NP_005121.1; NM_005130.4.
DR AlphaFoldDB; Q14512; -.
DR SMR; Q14512; -.
DR BioGRID; 115304; 272.
DR IntAct; Q14512; 4.
DR STRING; 9606.ENSP00000371770; -.
DR GlyGen; Q14512; 1 site.
DR iPTMnet; Q14512; -.
DR PhosphoSitePlus; Q14512; -.
DR BioMuta; FGFBP1; -.
DR DMDM; 74739840; -.
DR EPD; Q14512; -.
DR MassIVE; Q14512; -.
DR MaxQB; Q14512; -.
DR PaxDb; Q14512; -.
DR PeptideAtlas; Q14512; -.
DR PRIDE; Q14512; -.
DR ProteomicsDB; 60017; -.
DR Antibodypedia; 977; 255 antibodies from 26 providers.
DR DNASU; 9982; -.
DR Ensembl; ENST00000382333.2; ENSP00000371770.1; ENSG00000137440.5.
DR GeneID; 9982; -.
DR KEGG; hsa:9982; -.
DR MANE-Select; ENST00000382333.2; ENSP00000371770.1; NM_005130.5; NP_005121.1.
DR UCSC; uc003gom.4; human.
DR CTD; 9982; -.
DR DisGeNET; 9982; -.
DR GeneCards; FGFBP1; -.
DR HGNC; HGNC:19695; FGFBP1.
DR HPA; ENSG00000137440; Tissue enhanced (esophagus, vagina).
DR MIM; 607737; gene.
DR neXtProt; NX_Q14512; -.
DR OpenTargets; ENSG00000137440; -.
DR PharmGKB; PA134880558; -.
DR VEuPathDB; HostDB:ENSG00000137440; -.
DR eggNOG; ENOG502RZQ6; Eukaryota.
DR GeneTree; ENSGT00940000154372; -.
DR HOGENOM; CLU_102227_0_0_1; -.
DR InParanoid; Q14512; -.
DR OMA; LKVECTR; -.
DR OrthoDB; 1046740at2759; -.
DR PhylomeDB; Q14512; -.
DR TreeFam; TF335877; -.
DR PathwayCommons; Q14512; -.
DR Reactome; R-HSA-190377; FGFR2b ligand binding and activation.
DR SignaLink; Q14512; -.
DR BioGRID-ORCS; 9982; 16 hits in 1071 CRISPR screens.
DR ChiTaRS; FGFBP1; human.
DR GeneWiki; FGFBP1; -.
DR GenomeRNAi; 9982; -.
DR Pharos; Q14512; Tbio.
DR PRO; PR:Q14512; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q14512; protein.
DR Bgee; ENSG00000137440; Expressed in pharyngeal mucosa and 121 other tissues.
DR Genevisible; Q14512; HS.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017134; F:fibroblast growth factor binding; IEA:Ensembl.
DR GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; TAS:ProtInc.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0051450; P:myoblast proliferation; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IDA:BHF-UCL.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IDA:BHF-UCL.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:2000288; P:positive regulation of myoblast proliferation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR InterPro; IPR010510; FGF1-bd.
DR PANTHER; PTHR15258; PTHR15258; 1.
DR Pfam; PF06473; FGF-BP1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Growth factor binding; Membrane; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..234
FT /note="Fibroblast growth factor-binding protein 1"
FT /id="PRO_0000245512"
FT REGION 160..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..234
FT /note="Sufficient for interaction with FGF2 and FGF2-
FT induced effects"
FT COMPBIAS 160..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 169
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT DISULFID 68..85
FT /evidence="ECO:0000250"
FT DISULFID 94..127
FT /evidence="ECO:0000250"
FT DISULFID 103..139
FT /evidence="ECO:0000250"
FT DISULFID 197..234
FT /evidence="ECO:0000250"
FT DISULFID 214..222
FT /evidence="ECO:0000250"
FT MUTAGEN 214
FT /note="C->A: Strongly reduces interaction with FGF2."
FT /evidence="ECO:0000269|PubMed:16257968"
SQ SEQUENCE 234 AA; 26264 MW; AAF4209F29F2D058 CRC64;
MKICSLTLLS FLLLAAQVLL VEGKKKVKNG LHSKVVSEQK DTLGNTQIKQ KSRPGNKGKF
VTKDQANCRW AATEQEEGIS LKVECTQLDH EFSCVFAGNP TSCLKLKDER VYWKQVARNL
RSQKDICRYS KTAVKTRVCR KDFPESSLKL VSSTLFGNTK PRKEKTEMSP REHIKGKETT
PSSLAVTQTM ATKAPECVED PDMANQRKTA LEFCGETWSS LCTFFLSIVQ DTSC
