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UniProtKB/Swiss-Prot entry P31371


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FGF9_HUMAN
Primary accession number P31371
Secondary accession number Q3SY32
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on October 1, 1994 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 102)
Name and origin of the protein
Protein name Glia-activating factor [Precursor]
Synonyms GAF
Fibroblast growth factor 9
FGF-9
HBGF-9
Gene name
Name: FGF9
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Foreskin;
PubMed=8321227 [NCBI, ExPASy, EBI, Israel, Japan]
Miyamoto M., Naruo K., Seko C., Matsumoto S., Kondo T., Kurokawa T.;
"Molecular cloning of a novel cytokine cDNA encoding the ninth member of the fibroblast growth factor family, which has a unique secretion property.";
Mol. Cell. Biol. 13:4251-4259(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-94.
NIEHS SNPs program;
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02379; PubMed=15057823 [NCBI, ExPASy, EBI, Israel, Japan]
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 4-26 AND 34-54.
TISSUE=Glial tumor;
PubMed=8428960 [NCBI, ExPASy, EBI, Israel, Japan]
Naruo K., Seko C., Kuroshima K., Matsutani E., Sasada R., Kondo T., Kurokawa T.;
"Novel secretory heparin-binding factors from human glioma cells (glia-activating factors) involved in glial cell growth. Purification and biological properties.";
J. Biol. Chem. 268:2857-2864(1993).
[6]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
DOI=10.1107/S0907444900020813; PubMed=11223514 [NCBI, ExPASy, EBI, Israel, Japan]
Hecht H.J., Adar R., Hofmann B., Bogin O., Weich H., Yayon A.;
"Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces.";
Acta Crystallogr. D 57:378-384(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D14838; BAA03572.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY682094; AAT74624.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139378; CAC17692.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069692; AAH69692.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC103978; AAI03979.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC103979; AAI03980.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00011172; -.
PIR A48137; A48137.
RefSeq NP_002001.1; -.
UniGene Hs.111
3D structure databases
PDB
1G82; X-ray; 2.60 A; A/B/C/D=49-208.[ExPASy / RCSB / EBI]
1IHK; X-ray; 2.20 A; A=35-208.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1G82; -.
1IHK; -.
ModBase P31371.
Protein-protein interaction databases
DIP DIP:6036N; -.
Enzyme and pathway databases
Pathway_Interaction_DB fgf_pathway; FGF signaling pathway.
Reactome REACT_9470; Signaling by FGFR.
Organism-specific databases
GeneCards GC13P021144; -.
H-InvDB HIX0037350; -.
HGNC HGNC:3687; FGF9.
GenAtlas FGF9.
HPA CAB004392; -.
MIM 600921; gene. [NCBI / EBI]
PharmGKB PA28126; -.
Gene expression databases
ArrayExpress P31371; -.
Bgee P31371; -.
CleanEx HS_FGF9; -.
GermOnline ENSG00000102678; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (inferred from direct assay from MGI).
GO:0008083; Molecular function: growth factor activity (traceable author statement from ProtInc).
GO:0008201; Molecular function: heparin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008283; Biological process: cell proliferation (inferred from electronic annotation from UniProtKB-KW).
GO:0007267; Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0008543; Biological process: fibroblast growth factor receptor signaling pathway (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR002209; GF_heparin_bd.
IPR002348; IL1_HBGF.
Graphical view of domain structure.
PANTHER PTHR11486; IL1_HBGF; 1.
Pfam PF00167; FGF; 1.
Pfam graphical view of domain structure.
PRINTS PR00263; HBGFFGF.
PR00262; IL1HBGF.
ProDom PD000831; IL1_HBGF; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00442; FGF; 1.
SMART graphical view of domain structure.
PROSITE PS00247; HBGF_FGF; 1.
Proteomic databases
PRIDE P31371; -.
Genome annotation databases
Ensembl ENSG00000102678; Homo sapiens. [Contig view]
GeneID 2254; -.
KEGG hsa:2254; -.
Phylogenomic databases
HOGENOM P31371; -.
HOVERGEN P31371; -.
OMA P31371; RFTHFLP.
Other
NextBio 9131; -.
SOURCE FGF9; Homo sapiens.
ProtoNet P31371.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Developmental protein; Differentiation; Direct protein sequencing; Glycoprotein; Growth factor; Heparin-binding; Mitogen; Polymorphism; Secreted.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
PROPEP   1     3  3      PRO_0000008973
CHAIN   4   208  205     Glia-activating factor. PRO_0000008974
CARBOHYD   79    79        N-linked (GlcNAc...). 
VARIANT   94    94  1     I -> V (in dbSNP:rs12427696 [NCBI]). VAR_020944 
CONFLICT   24    26        VLP -> SLL (in Ref. 5; AA sequence). 
CONFLICT   34    34        S -> A (in Ref. 5; AA sequence). 
HELIX   53    60  8      
STRAND   63    68  6      
STRAND   73    76  4      
STRAND   82    87  6      
HELIX   91    93  3      
STRAND   95   101  7      
STRAND   104   109  6      
TURN   110   112  3      
STRAND   115   118  4      
STRAND   124   129  6      
HELIX   132   134  3      
STRAND   136   142  7      
STRAND   145   154  10      
TURN   156   158  3      
STRAND   161   163  3      
HELIX   175   177  3      
HELIX   183   185  3      
STRAND   187   190  4      
HELIX   194   196  3      
HELIX   200   203  4      
Sequence information
Length: 208 AA [This is the length of the unprocessed precursor] Molecular weight: 23441 Da [This is the MW of the unprocessed precursor] CRC64: F32A0E7106EF59C9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAPLGEVGNY FGVQDAVPFG NVPVLPVDSP VLLSDHLGQS EAGGLPRGPA VTDLDHLKGI 

        70         80         90        100        110        120 
LRRRQLYCRT GFHLEIFPNG TIQGTRKDHS RFGILEFISI AVGLVSIRGV DSGLYLGMNE 

       130        140        150        160        170        180 
KGELYGSEKL TQECVFREQF EENWYNTYSS NLYKHVDTGR RYYVALNKDG TPREGTRTKR 

       190        200 
HQKFTHFLPR PVDPDKVPEL YKDILSQS 

P31371 in FASTA format

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