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Protein

Fibroblast growth factor-binding protein 3

Gene

FGFBP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Heparin-binding protein which binds to FGF2, prevents binding of FGF2 to heparin and probably inhibits immobilization of FGF2 on extracellular matrix glycosaminoglycans, allowing its release and subsequent activation of FGFR signaling which leads to increased vascular permeability.1 Publication

GO - Molecular functioni

  • fibroblast growth factor binding Source: MGI
  • heparin binding Source: MGI

GO - Biological processi

  • positive regulation of fibroblast growth factor receptor signaling pathway Source: MGI
  • positive regulation of vascular permeability Source: MGI
Complete GO annotation...

Keywords - Ligandi

Growth factor binding, Heparin-binding

Enzyme and pathway databases

ReactomeiR-HSA-190377. FGFR2b ligand binding and activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor-binding protein 3
Short name:
FGF-BP3
Short name:
FGF-binding protein 3
Short name:
FGFBP-3
Gene namesi
Name:FGFBP3
Synonyms:C10orf13
ORF Names:PSEC0101
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:23428. FGFBP3.

Subcellular locationi

GO - Cellular componenti

  • extracellular matrix Source: UniProtKB
  • extracellular region Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162388444.

Polymorphism and mutation databases

BioMutaiFGFBP3.
DMDMi74751362.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 258232Fibroblast growth factor-binding protein 3PRO_0000244264Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi59 ↔ 80By similarity
Disulfide bondi90 ↔ 124By similarity
Disulfide bondi241 ↔ 249By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiQ8TAT2.
PaxDbiQ8TAT2.
PeptideAtlasiQ8TAT2.
PRIDEiQ8TAT2.

PTM databases

iPTMnetiQ8TAT2.

Expressioni

Gene expression databases

BgeeiQ8TAT2.
CleanExiHS_FGFBP3.
GenevisibleiQ8TAT2. HS.

Organism-specific databases

HPAiHPA053943.

Interactioni

Subunit structurei

Interacts with FGF2.1 Publication

GO - Molecular functioni

  • fibroblast growth factor binding Source: MGI

Structurei

3D structure databases

ProteinModelPortaliQ8TAT2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J22M. Eukaryota.
ENOG4112ARC. LUCA.
GeneTreeiENSGT00680000100139.
HOGENOMiHOG000059653.
HOVERGENiHBG066419.
InParanoidiQ8TAT2.
OMAiKRRPCHD.
OrthoDBiEOG73BVDT.
PhylomeDBiQ8TAT2.
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.

Q8TAT2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPPKLRASL SPSLLLLLSG CLLAAARREK GAASNVAEPV PGPTGGSSGR
60 70 80 90 100
FLSPEQHACS WQLLLPAPEA AAGSELALRC QSPDGARHQC AYRGHPERCA
110 120 130 140 150
AYAARRAHFW KQVLGGLRKK RRPCHDPAPL QARLCAGKKG HGAELRLVPR
160 170 180 190 200
ASPPARPTVA GFAGESKPRA RNRGRTRERA SGPAAGTPPP QSAPPKENPS
210 220 230 240 250
ERKTNEGKRK AALVPNEERP MGTGPDPDGL DGNAELTETY CAEKWHSLCN

FFVNFWNG
Length:258
Mass (Da):27,590
Last modified:June 1, 2002 - v1
Checksum:iC6290744F0AB9DEF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071A → T.
Corresponds to variant rs10881994 [ dbSNP | Ensembl ].
VAR_059288
Natural varianti206 – 2061E → V.1 Publication
Corresponds to variant rs1107947 [ dbSNP | Ensembl ].
VAR_026888

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ503576 mRNA. Translation: ABF56582.1.
AK075410 mRNA. Translation: BAC11602.1.
AK315427 mRNA. Translation: BAG37815.1.
AL359198 Genomic DNA. No translation available.
CH471066 Genomic DNA. Translation: EAW50104.1.
BC025966 mRNA. Translation: AAH25966.1.
CCDSiCCDS7418.1.
RefSeqiNP_689642.3. NM_152429.4.
UniGeneiHs.466120.

Genome annotation databases

EnsembliENST00000311575; ENSP00000339067; ENSG00000174721.
GeneIDi143282.
KEGGihsa:143282.
UCSCiuc001khq.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ503576 mRNA. Translation: ABF56582.1.
AK075410 mRNA. Translation: BAC11602.1.
AK315427 mRNA. Translation: BAG37815.1.
AL359198 Genomic DNA. No translation available.
CH471066 Genomic DNA. Translation: EAW50104.1.
BC025966 mRNA. Translation: AAH25966.1.
CCDSiCCDS7418.1.
RefSeqiNP_689642.3. NM_152429.4.
UniGeneiHs.466120.

3D structure databases

ProteinModelPortaliQ8TAT2.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiQ8TAT2.

Polymorphism and mutation databases

BioMutaiFGFBP3.
DMDMi74751362.

Proteomic databases

EPDiQ8TAT2.
PaxDbiQ8TAT2.
PeptideAtlasiQ8TAT2.
PRIDEiQ8TAT2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311575; ENSP00000339067; ENSG00000174721.
GeneIDi143282.
KEGGihsa:143282.
UCSCiuc001khq.5. human.

Organism-specific databases

CTDi143282.
GeneCardsiFGFBP3.
HGNCiHGNC:23428. FGFBP3.
HPAiHPA053943.
neXtProtiNX_Q8TAT2.
PharmGKBiPA162388444.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J22M. Eukaryota.
ENOG4112ARC. LUCA.
GeneTreeiENSGT00680000100139.
HOGENOMiHOG000059653.
HOVERGENiHBG066419.
InParanoidiQ8TAT2.
OMAiKRRPCHD.
OrthoDBiEOG73BVDT.
PhylomeDBiQ8TAT2.
TreeFamiTF335877.

Enzyme and pathway databases

ReactomeiR-HSA-190377. FGFR2b ligand binding and activation.

Miscellaneous databases

GenomeRNAii143282.
PROiQ8TAT2.

Gene expression databases

BgeeiQ8TAT2.
CleanExiHS_FGFBP3.
GenevisibleiQ8TAT2. HS.

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. "Identification and characterization of a novel member of the fibroblast growth factor-binding protein family, FGF-BP3."
    Swift M.R., Tassi E., Wellstein A.
    Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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: Brain.
  3. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-206.
    Tissue: Teratocarcinoma.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Brain.
  7. Cited for: FUNCTION, INTERACTION WITH FGF2, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiFGFP3_HUMAN
AccessioniPrimary (citable) accession number: Q8TAT2
Secondary accession number(s): B2RD68, Q8NBN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 1, 2002
Last modified: July 6, 2016
This is version 102 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

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.