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Protein

Fibroblast growth factor-binding protein 1

Gene

FGFBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a carrier protein that release fibroblast-binding factors (FGFs) from the extracellular matrix (EM) storage and thus enhance the mitogenic activity of FGFs. Enhances FGF2 signaling during tissue repair, angiogenesis and in tumor growth.4 Publications

GO - Molecular functioni

  1. heparin binding Source: ProtInc

GO - Biological processi

  1. cell-cell signaling Source: ProtInc
  2. negative regulation of cell proliferation Source: ProtInc
  3. positive regulation of cell proliferation Source: Ensembl
  4. positive regulation of fibroblast growth factor receptor signaling pathway Source: Ensembl
  5. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Growth factor binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor-binding protein 1
Short name:
FGF-BP
Short name:
FGF-BP1
Short name:
FGF-binding protein 1
Short name:
FGFBP-1
Alternative name(s):
17 kDa heparin-binding growth factor-binding protein
Short name:
17 kDa HBGF-binding protein
Short name:
HBp17
Gene namesi
Name:FGFBP1
Synonyms:FGFBP, HBP17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:19695. FGFBP1.

Subcellular locationi

Secretedextracellular space. Cell membrane; Peripheral membrane protein
Note: Extracellular and plasma membrane-associated. Colocalizes with HSPG2 in the pericellular environment of squamous cell carcinomas.

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. extracellular space Source: ProtInc
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi214 – 2141C → A: Strongly reduces interaction with FGF2. 1 Publication

Organism-specific databases

PharmGKBiPA134880558.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 234211Fibroblast growth factor-binding protein 1PRO_0000245512Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi68 ↔ 85By similarity
Disulfide bondi94 ↔ 127By similarity
Disulfide bondi103 ↔ 139By similarity
Glycosylationi169 – 1691O-linked (GalNAc...)By similarity
Disulfide bondi197 ↔ 234By similarity
Disulfide bondi214 ↔ 222By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ14512.
PaxDbiQ14512.
PRIDEiQ14512.

PTM databases

PhosphoSiteiQ14512.

Expressioni

Tissue specificityi

Expressed in the suprabasal region of the epidermis, in hair follicles, the basement membrane at the dermo-epidermal junction (occasionally extending into the basement membrane of dermal blood vessels), wounded skin and several invasive squamous cell carcinomas (at protein level). Expressed in normal and wounded skin and various squamous cell carcinomas.3 Publications

Inductioni

Up-regulated in epithelial cells after skin injury. Keratinocyte mitogens.1 Publication

Gene expression databases

BgeeiQ14512.
CleanExiHS_FGFBP1.
GenevestigatoriQ14512.

Organism-specific databases

HPAiHPA004332.

Interactioni

Subunit structurei

Found in a complex with FGFBP1, FGF1 and FGF2. Interacts with FGF1, FGF2, FGF7, FGF10, FGF22 and HSPG2.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FGF2P090383EBI-953742,EBI-977447

Protein-protein interaction databases

BioGridi115304. 5 interactions.
IntActiQ14512. 2 interactions.
MINTiMINT-2867884.
STRINGi9606.ENSP00000259988.

Structurei

3D structure databases

ProteinModelPortaliQ14512.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni193 – 23442Sufficient for interaction with FGF2 and FGF2-induced effectsAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG42715.
GeneTreeiENSGT00730000111278.
HOGENOMiHOG000013097.
HOVERGENiHBG053095.
InParanoidiQ14512.
OMAiLKVECTR.
OrthoDBiEOG7S4X70.
PhylomeDBiQ14512.
TreeFamiTF335877.

Family and domain databases

InterProiIPR010510. FGF1-bd.
[Graphical view]
PANTHERiPTHR15258. PTHR15258. 1 hit.
PfamiPF06473. FGF-BP1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q14512-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKICSLTLLS FLLLAAQVLL VEGKKKVKNG LHSKVVSEQK DTLGNTQIKQ
60 70 80 90 100
KSRPGNKGKF VTKDQANCRW AATEQEEGIS LKVECTQLDH EFSCVFAGNP
110 120 130 140 150
TSCLKLKDER VYWKQVARNL RSQKDICRYS KTAVKTRVCR KDFPESSLKL
160 170 180 190 200
VSSTLFGNTK PRKEKTEMSP REHIKGKETT PSSLAVTQTM ATKAPECVED
210 220 230
PDMANQRKTA LEFCGETWSS LCTFFLSIVQ DTSC
Length:234
Mass (Da):26,264
Last modified:November 1, 1996 - v1
Checksum:iAAF4209F29F2D058
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60047 mRNA. Translation: AAA58636.1.
AF149412 Genomic DNA. Translation: AAD39216.1.
AK291307 mRNA. Translation: BAF83996.1.
CH471069 Genomic DNA. Translation: EAW92748.1.
BC003628 mRNA. Translation: AAH03628.1.
BC008910 mRNA. Translation: AAH08910.1.
CCDSiCCDS3418.1.
PIRiA41178.
RefSeqiNP_005121.1. NM_005130.4.
UniGeneiHs.1690.

Genome annotation databases

EnsembliENST00000382333; ENSP00000371770; ENSG00000137440.
GeneIDi9982.
KEGGihsa:9982.
UCSCiuc003gom.3. human.

Polymorphism databases

DMDMi74739840.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60047 mRNA. Translation: AAA58636.1.
AF149412 Genomic DNA. Translation: AAD39216.1.
AK291307 mRNA. Translation: BAF83996.1.
CH471069 Genomic DNA. Translation: EAW92748.1.
BC003628 mRNA. Translation: AAH03628.1.
BC008910 mRNA. Translation: AAH08910.1.
CCDSiCCDS3418.1.
PIRiA41178.
RefSeqiNP_005121.1. NM_005130.4.
UniGeneiHs.1690.

3D structure databases

ProteinModelPortaliQ14512.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115304. 5 interactions.
IntActiQ14512. 2 interactions.
MINTiMINT-2867884.
STRINGi9606.ENSP00000259988.

PTM databases

PhosphoSiteiQ14512.

Polymorphism databases

DMDMi74739840.

Proteomic databases

MaxQBiQ14512.
PaxDbiQ14512.
PRIDEiQ14512.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000382333; ENSP00000371770; ENSG00000137440.
GeneIDi9982.
KEGGihsa:9982.
UCSCiuc003gom.3. human.

Organism-specific databases

CTDi9982.
GeneCardsiGC04M015937.
HGNCiHGNC:19695. FGFBP1.
HPAiHPA004332.
MIMi607737. gene.
neXtProtiNX_Q14512.
PharmGKBiPA134880558.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42715.
GeneTreeiENSGT00730000111278.
HOGENOMiHOG000013097.
HOVERGENiHBG053095.
InParanoidiQ14512.
OMAiLKVECTR.
OrthoDBiEOG7S4X70.
PhylomeDBiQ14512.
TreeFamiTF335877.

Miscellaneous databases

GeneWikiiFGFBP1.
GenomeRNAii9982.
NextBioi37692.
PROiQ14512.
SOURCEiSearch...

Gene expression databases

BgeeiQ14512.
CleanExiHS_FGFBP1.
GenevestigatoriQ14512.

Family and domain databases

InterProiIPR010510. FGF1-bd.
[Graphical view]
PANTHERiPTHR15258. PTHR15258. 1 hit.
PfamiPF06473. FGF-BP1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors."
    Wu D.Q., Kan M.K., Sato G.H., Okamoto T., Sato J.D.
    J. Biol. Chem. 266:16778-16785(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEIN SEQUENCE OF 34-67; 92-118 AND 146-158, IDENTIFICATION IN A COMPLEX WITH FGF1 AND FGF2, INTERACTION WITH FGF1, TISSUE SPECIFICITY.
    Tissue: Epidermal carcinoma.
  2. "Gene sequence for the human FGF-binding protein HBp17."
    Shi S., Sato J.D.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Tongue.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary and Pancreas.
  6. "A secreted FGF-binding protein can serve as the angiogenic switch in human cancer."
    Czubayko F., Liaudet-Coopman E.D., Aigner A., Tuveson A.T., Berchem G.J., Wellstein A.
    Nat. Med. 3:1137-1140(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Fibroblast growth factor-binding protein is a novel partner for perlecan protein core."
    Mongiat M., Otto J., Oldershaw R., Ferrer F., Sato J.D., Iozzo R.V.
    J. Biol. Chem. 276:10263-10271(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSPG2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Enhancement of fibroblast growth factor (FGF) activity by an FGF-binding protein."
    Tassi E., Al-Attar A., Aigner A., Swift M.R., McDonnell K., Karavanov A., Wellstein A.
    J. Biol. Chem. 276:40247-40253(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FGF2.
  9. "The fibroblast growth factor binding protein is a novel interaction partner of FGF-7, FGF-10 and FGF-22 and regulates FGF activity: implications for epithelial repair."
    Beer H.-D., Bittner M., Niklaus G., Munding C., Max N., Goppelt A., Werner S.
    Oncogene 24:5269-5277(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FGF7; FGF10 AND FGF22, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  10. "Identification of the fibroblast growth factor (FGF)-interacting domain in a secreted FGF-binding protein by phage display."
    Xie B., Tassi E., Swift M.R., McDonnell K., Bowden E.T., Wang S., Ueda Y., Tomita Y., Riegel A.T., Wellstein A.
    J. Biol. Chem. 281:1137-1144(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGF2, MUTAGENESIS OF CYS-214.

Entry informationi

Entry nameiFGFP1_HUMAN
AccessioniPrimary (citable) accession number: Q14512
Secondary accession number(s): A8K5J2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Expression is significantly up-regulated in carcinogen-induced skin tumors, various squamous cell carcinomas, some colon cancer cell lines and tumors.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.