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P14210 (HGF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 183. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hepatocyte growth factor
Alternative name(s):
Hepatopoietin-A
Scatter factor
Short name=SF
Gene names
Name:HGF
Synonyms:HPTA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length728 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types. Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization. Ref.23 Ref.24

Subunit structure

Dimer of an alpha chain and a beta chain linked by a disulfide bond. Interacts with SRPX2; the interaction increases HGF mitogenic activity. Ref.20 Ref.23

Involvement in disease

Deafness, autosomal recessive, 39 (DFNB39) [MIM:608265]: A form of profound prelingual sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19

Sequence similarities

Belongs to the peptidase S1 family. Plasminogen subfamily.

Contains 4 kringle domains.

Contains 1 PAN domain.

Contains 1 peptidase S1 domain.

Caution

Has lost two of the three essential catalytic residues and so probably has no enzymatic activity.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDeafness
Non-syndromic deafness
   DomainKringle
Repeat
Signal
   Molecular functionGrowth factor
Serine protease homolog
   PTMDisulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

cell chemotaxis

Inferred from direct assay PubMed 21245381. Source: BHF-UCL

cellular response to hepatocyte growth factor stimulus

Inferred from direct assay PubMed 21245381. Source: BHF-UCL

epithelial to mesenchymal transition

Traceable author statement PubMed 14679171. Source: HGNC

hepatocyte growth factor receptor signaling pathway

Inferred from direct assay PubMed 21245381. Source: BHF-UCL

hyaluronan metabolic process

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

mitotic nuclear division

Non-traceable author statement Ref.2. Source: UniProtKB

myoblast proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 20655899. Source: BHF-UCL

negative regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from electronic annotation. Source: Ensembl

negative regulation of hydrogen peroxide-mediated programmed cell death

Inferred from direct assay PubMed 20655899. Source: BHF-UCL

negative regulation of release of cytochrome c from mitochondria

Inferred from direct assay PubMed 20655899. Source: BHF-UCL

organ regeneration

Inferred from electronic annotation. Source: Ensembl

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive chemotaxis

Inferred from direct assay PubMed 21245381. Source: GOC

positive regulation of DNA biosynthetic process

Inferred from direct assay Ref.2. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay PubMed 21245381. Source: BHF-UCL

positive regulation of osteoblast differentiation

Non-traceable author statement PubMed 22521434. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 21245381. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from direct assay PubMed 20655899. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Non-traceable author statement PubMed 22521434. Source: BHF-UCL

regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling

Inferred from direct assay PubMed 14517989. Source: MGI

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: Ensembl

platelet alpha granule lumen

Traceable author statement. Source: Reactome

   Molecular_functioncatalytic activity

Inferred from electronic annotation. Source: InterPro

chemoattractant activity

Inferred from direct assay PubMed 21245381. Source: BHF-UCL

growth factor activity

Non-traceable author statement Ref.2. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 22897854. Source: IntAct

protein binding

Inferred from physical interaction PubMed 22897854. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

METP085814EBI-1039104,EBI-1039152
MetP160562EBI-1039104,EBI-1798780From a different organism.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P14210-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P14210-2)

The sequence of this isoform differs from the canonical sequence as follows:
     289-290: AD → ET
     291-728: Missing.
Isoform 3 (identifier: P14210-3)

The sequence of this isoform differs from the canonical sequence as follows:
     161-165: Missing.
Isoform 4 (identifier: P14210-4)

Also known as: HGF/NK2;

The sequence of this isoform differs from the canonical sequence as follows:
     287-296: TCADNTMNDT → NMRDITWALN
     297-728: Missing.
Note: Acts as a competitive antagonist in MET-signaling.
Isoform 5 (identifier: P14210-5)

The sequence of this isoform differs from the canonical sequence as follows:
     161-165: Missing.
     289-290: AD → ET
     291-728: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: P14210-6)

Also known as: HGF/NK1;

The sequence of this isoform differs from the canonical sequence as follows:
     209-210: VE → GK
     211-728: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131
Chain32 – 494463Hepatocyte growth factor alpha chain
PRO_0000028091
Chain495 – 728234Hepatocyte growth factor beta chain
PRO_0000028092

Regions

Domain37 – 12387PAN
Domain128 – 20679Kringle 1
Domain211 – 28878Kringle 2
Domain305 – 38379Kringle 3
Domain391 – 46979Kringle 4
Domain495 – 721227Peptidase S1

Amino acid modifications

Modified residue321Pyrrolidone carboxylic acid
Glycosylation2941N-linked (GlcNAc...) (complex)
CAR_000021
Glycosylation4021N-linked (GlcNAc...) (complex)
CAR_000022
Glycosylation4761O-linked (GalNAc...) Ref.17
CAR_000023
Glycosylation5661N-linked (GlcNAc...) (complex)
CAR_000024
Glycosylation6531N-linked (GlcNAc...) (complex)
CAR_000025
Disulfide bond70 ↔ 96 Ref.23 Ref.24
Disulfide bond74 ↔ 84 Ref.23 Ref.24
Disulfide bond128 ↔ 206 Ref.23 Ref.24
Disulfide bond149 ↔ 189 Ref.23 Ref.24
Disulfide bond177 ↔ 201 Ref.23 Ref.24
Disulfide bond211 ↔ 288 By similarity
Disulfide bond232 ↔ 271 By similarity
Disulfide bond260 ↔ 283 By similarity
Disulfide bond305 ↔ 383 By similarity
Disulfide bond326 ↔ 365 By similarity
Disulfide bond354 ↔ 377 By similarity
Disulfide bond391 ↔ 469 By similarity
Disulfide bond412 ↔ 452 By similarity
Disulfide bond440 ↔ 464 By similarity
Disulfide bond487 ↔ 604Interchain (between alpha and beta chains) By similarity
Disulfide bond519 ↔ 535 By similarity
Disulfide bond612 ↔ 679 By similarity
Disulfide bond642 ↔ 658 By similarity
Disulfide bond669 ↔ 697 By similarity

Natural variations

Alternative sequence161 – 1655Missing in isoform 3 and isoform 5.
VSP_009617
Alternative sequence209 – 2102VE → GK in isoform 6.
VSP_009618
Alternative sequence211 – 728518Missing in isoform 6.
VSP_009619
Alternative sequence287 – 29610TCADNTMNDT → NMRDITWALN in isoform 4.
VSP_009620
Alternative sequence289 – 2902AD → ET in isoform 2 and isoform 5.
VSP_009622
Alternative sequence291 – 728438Missing in isoform 2 and isoform 5.
VSP_009623
Alternative sequence297 – 728432Missing in isoform 4.
VSP_009621
Natural variant1531S → I.
Corresponds to variant rs17566 [ dbSNP | Ensembl ].
VAR_014570
Natural variant3041E → K. Ref.11
Corresponds to variant rs5745687 [ dbSNP | Ensembl ].
VAR_019199
Natural variant3301D → Y. Ref.11
Corresponds to variant rs5745688 [ dbSNP | Ensembl ].
VAR_019200

Experimental info

Mutagenesis4941R → Q: Loss of activity due to absence of proteolytic cleavage. Ref.9
Sequence conflict32 – 332QR → HK in CAA34387. Ref.2
Sequence conflict781K → N in CAA34387. Ref.2
Sequence conflict1801P → T AA sequence Ref.6
Sequence conflict2931M → V in CAA34387. Ref.2
Sequence conflict3001L → M in CAA34387. Ref.2
Sequence conflict3171V → A in CAA34387. Ref.2
Sequence conflict3361E → K in CAA34387. Ref.2
Sequence conflict3871H → N in CAA34387. Ref.2
Sequence conflict4161D → N in CAA34387. Ref.2
Sequence conflict5051I → V in CAA34387. Ref.2
Sequence conflict5091V → I in CAA34387. Ref.2
Sequence conflict5581D → E in CAA34387. Ref.2
Sequence conflict5611C → R in CAA34387. Ref.2
Sequence conflict5921D → N AA sequence Ref.6
Sequence conflict5951S → N in CAA34387. Ref.2

Secondary structure

........................................................................................... 728
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 1, 1991. Version 2.
Checksum: 2D997938295ADD2F

FASTA72883,134
        10         20         30         40         50         60 
MWVTKLLPAL LLQHVLLHLL LLPIAIPYAE GQRKRRNTIH EFKKSAKTTL IKIDPALKIK 

        70         80         90        100        110        120 
TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP FNSMSSGVKK EFGHEFDLYE 

       130        140        150        160        170        180 
NKDYIRNCII GKGRSYKGTV SITKSGIKCQ PWSSMIPHEH SFLPSSYRGK DLQENYCRNP 

       190        200        210        220        230        240 
RGEEGGPWCF TSNPEVRYEV CDIPQCSEVE CMTCNGESYR GLMDHTESGK ICQRWDHQTP 

       250        260        270        280        290        300 
HRHKFLPERY PDKGFDDNYC RNPDGQPRPW CYTLDPHTRW EYCAIKTCAD NTMNDTDVPL 

       310        320        330        340        350        360 
ETTECIQGQG EGYRGTVNTI WNGIPCQRWD SQYPHEHDMT PENFKCKDLR ENYCRNPDGS 

       370        380        390        400        410        420 
ESPWCFTTDP NIRVGYCSQI PNCDMSHGQD CYRGNGKNYM GNLSQTRSGL TCSMWDKNME 

       430        440        450        460        470        480 
DLHRHIFWEP DASKLNENYC RNPDDDAHGP WCYTGNPLIP WDYCPISRCE GDTTPTIVNL 

       490        500        510        520        530        540 
DHPVISCAKT KQLRVVNGIP TRTNIGWMVS LRYRNKHICG GSLIKESWVL TARQCFPSRD 

       550        560        570        580        590        600 
LKDYEAWLGI HDVHGRGDEK CKQVLNVSQL VYGPEGSDLV LMKLARPAVL DDFVSTIDLP 

       610        620        630        640        650        660 
NYGCTIPEKT SCSVYGWGYT GLINYDGLLR VAHLYIMGNE KCSQHHRGKV TLNESEICAG 

       670        680        690        700        710        720 
AEKIGSGPCE GDYGGPLVCE QHKMRMVLGV IVPGRGCAIP NRPGIFVRVA YYAKWIHKII 


LTYKVPQS 

« Hide

Isoform 2 [UniParc].

Checksum: C8A18A6F0D63200A
Show »

FASTA29033,766
Isoform 3 [UniParc].

Checksum: 627B1EF99FAD931B
Show »

FASTA72382,602
Isoform 4 (HGF/NK2) [UniParc].

Checksum: A45E456B87AE03BE
Show »

FASTA29634,547
Isoform 5 [UniParc].

Checksum: 0A93B073EA86EA61
Show »

FASTA28533,234
Isoform 6 (HGF/NK1) [UniParc].

Checksum: 94A6EE9C50DE5A86
Show »

FASTA21024,116

References

« Hide 'large scale' references
[1]"Molecular cloning and sequence analysis of cDNA for human hepatocyte growth factor."
Miyazawa K., Tsubouchi H., Naka D., Takahashi K., Okigaki M., Arakaki N., Nakayama H., Hirono S., Sakiyama O., Takahashi K., Gohda E., Daikuhara Y., Kitamura N.
Biochem. Biophys. Res. Commun. 163:967-973(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]"Molecular cloning and expression of human hepatocyte growth factor."
Nakamura T., Nishizawa T., Hagiya M., Seki T., Shimonishi M., Sugimura A., Tashiro K., Shimizu S.
Nature 342:440-443(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 55-73 AND 495-520.
Tissue: Liver.
[3]"Isolation and expression of cDNA for different forms of hepatocyte growth factor from human leukocyte."
Seki T., Ihara I., Sugimura A., Shimonishi M., Nishizawa T., Asami O., Hagiya M., Nakamura T., Shimizu S.
Biochem. Biophys. Res. Commun. 172:321-327(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Leukocyte.
[4]"Organization of the human hepatocyte growth factor-encoding gene."
Seki T., Hagiya M., Shimonishi M., Nakamura T., Shimizu S.
Gene 102:213-219(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[5]"An alternatively processed mRNA generated from human hepatocyte growth factor gene."
Miyazawa K., Kitamura A., Naka D., Kitamura N.
Eur. J. Biochem. 197:15-22(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Placenta.
[6]"A broad-spectrum human lung fibroblast-derived mitogen is a variant of hepatocyte growth factor."
Rubin J.S., Chan A.M.-L., Bottaro D.P., Burgess W.H., Taylor W.G., Cech A.C., Hirschfield D.W., Wong J., Miki T., Finch P.W., Aaronson S.A.
Proc. Natl. Acad. Sci. U.S.A. 88:415-419(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PROTEIN SEQUENCE OF 583-592.
Tissue: Lung fibroblast.
[7]"Evidence for the identity of human scatter factor and human hepatocyte growth factor."
Weidner K.M., Arakaki N., Hartmann G., Vandekerckhove J., Weingart S., Rieder H., Fonatsch C., Tsubouchi H., Hishida T., Daikuhara Y., Birchmeier W.
Proc. Natl. Acad. Sci. U.S.A. 88:7001-7005(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Embryonic fibroblast.
[8]"Identification of a competitive HGF antagonist encoded by an alternative transcript."
Chan A.M.-L., Rubin J.S., Bottaro D.P., Hirschfield D.W., Chedid M., Aaronson S.A.
Science 254:1382-1385(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[9]"A functional domain in the heavy chain of scatter factor/hepatocyte growth factor binds the c-Met receptor and induces cell dissociation but not mitogenesis."
Hartmann G., Naldini L., Weidner K.M., Sachs M., Vigna E., Comoglio P.M., Birchmeier W.
Proc. Natl. Acad. Sci. U.S.A. 89:11574-11578(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), MUTAGENESIS OF ARG-494.
[10]"Hepatocyte growth factor (HGF)/NK1 is a naturally occurring HGF/scatter factor variant with partial agonist/antagonist activity."
Cioce V., Csaky K.G., Chan A.M.-L., Bottaro D.P., Taylor W.G., Jensen R., Aaronson S.A., Rubin J.S.
J. Biol. Chem. 271:13110-13115(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
[11]NIEHS SNPs program
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-304 AND TYR-330.
[12]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]"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] (ISOFORMS 1; 5 AND 6).
Tissue: Brain.
[15]"Structural organization and the transcription initiation site of the human hepatocyte growth factor gene."
Miyazawa K., Kitamura A., Kitamura N.
Biochemistry 30:9170-9176(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-208 AND 249-695 (ISOFORM 1).
[16]"Identification of the N-terminal residue of the heavy chain of both native and recombinant human hepatocyte growth factor."
Yoshiyama Y., Arakaki N., Naka D., Takahashi K., Hirono S., Kondo J., Nakayama H., Gohda E., Kitamura N., Tsubouchi H., Ishii T., Hishida T., Daikuhara Y.
Biochem. Biophys. Res. Commun. 175:660-667(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SIGNAL SEQUENCE CLEAVAGE SITE, PYROGLUTAMATE FORMATION AT GLN-32.
[17]"Hepatocyte growth factor is linked by O-glycosylated oligosaccharide on the alpha chain."
Shimizu N., Hara H., Sogabe T., Sakai H., Ihara I., Inoue H., Nakamura T., Shimizu S.
Biochem. Biophys. Res. Commun. 189:1329-1335(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-476.
[18]"Structure-function analysis of hepatocyte growth factor: identification of variants that lack mitogenic activity yet retain high affinity receptor binding."
Lokker N.A., Mark M.R., Luis E.A., Bennett G.L., Robbins K.A., Baker J.B., Godowski P.J.
EMBO J. 11:2503-2510(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[19]"Noncoding mutations of HGF are associated with nonsyndromic hearing loss, DFNB39."
Schultz J.M., Khan S.N., Ahmed Z.M., Riazuddin S., Waryah A.M., Chhatre D., Starost M.F., Ploplis B., Buckley S., Velasquez D., Kabra M., Lee K., Hassan M.J., Ali G., Ansar M., Ghosh M., Wilcox E.R., Ahmad W. expand/collapse author list , Merlino G., Leal S.M., Riazuddin S., Friedman T.B., Morell R.J.
Am. J. Hum. Genet. 85:25-39(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN DFNB39.
[20]"SRPX2 is a novel chondroitin sulfate proteoglycan that is overexpressed in gastrointestinal cancer."
Tanaka K., Arao T., Tamura D., Aomatsu K., Furuta K., Matsumoto K., Kaneda H., Kudo K., Fujita Y., Kimura H., Yanagihara K., Yamada Y., Okamoto I., Nakagawa K., Nishio K.
PLoS ONE 7:E27922-E27922(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRPX2.
[21]"The solution structure of the N-terminal domain of hepatocyte growth factor reveals a potential heparin-binding site."
Zhou H., Mazzulla M.J., Kaufman J.D., Stahl S.J., Wingfield P.T., Rubin J.S., Bottaro D.P., Byrd R.A.
Structure 6:109-116(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 31-127.
[22]"Crystal structure of the NK1 fragment of human hepatocyte growth factor at 2.0-A resolution."
Ultsch M., Lokker N.A., Godowski P.J., de Vos A.M.
Structure 6:1383-1393(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 35-210.
[23]"Crystal structure of the HGF beta-chain in complex with the Sema domain of the Met receptor."
Stamos J., Lazarus R.A., Yao X., Kirchhofer D., Wiesmann C.
EMBO J. 23:2325-2335(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.22 ANGSTROMS) OF 495-728 IN COMPLEX WITH MET, FUNCTION, SUBUNIT, DISULFIDE BONDS.
[24]"Structural basis for agonism and antagonism of hepatocyte growth factor."
Tolbert W.D., Daugherty-Holtrop J., Gherardi E., Vande Woude G., Xu H.E.
Proc. Natl. Acad. Sci. U.S.A. 107:13264-13269(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 28-289, DISULFIDE BONDS, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M29145 mRNA. Translation: AAA52650.1.
X16323 mRNA. Translation: CAA34387.1.
M60718 mRNA. Translation: AAA52648.1.
D90334 Genomic DNA. Translation: BAA14348.1.
X57574 mRNA. Translation: CAA40802.1.
M55379 mRNA. No translation available.
M73239 mRNA. Translation: AAA64239.1.
M73240 mRNA. Translation: AAA64297.1.
M77227 mRNA. Translation: AAA35980.1.
L02931 mRNA. Translation: AAA52649.1.
U46010 mRNA. Translation: AAC50539.1.
AY246560 Genomic DNA. Translation: AAO61091.1.
AC004960 Genomic DNA. Translation: AAC71655.1.
CH236949 Genomic DNA. Translation: EAL24189.1.
BC022308 mRNA. Translation: AAH22308.1.
BC063485 mRNA. Translation: AAH63485.1.
BC105797 mRNA. Translation: AAI05798.1.
BC130284 mRNA. Translation: AAI30285.1.
BC130286 mRNA. Translation: AAI30287.1.
M75971 expand/collapse EMBL AC list , M75967, M75966, M75968, M75969 Genomic DNA. Translation: AAG53459.1.
M75983 expand/collapse EMBL AC list , M75972, M75973, M75974, M75975, M75976, M75977, M75978, M75979, M75980, M75981, M75982 Genomic DNA. Translation: AAG53460.1.
CCDSCCDS47626.1. [P14210-3]
CCDS47627.1. [P14210-2]
CCDS47628.1. [P14210-5]
CCDS47629.1. [P14210-6]
CCDS5597.1. [P14210-1]
PIRJH0579.
RefSeqNP_000592.3. NM_000601.4. [P14210-1]
NP_001010931.1. NM_001010931.1. [P14210-2]
NP_001010932.1. NM_001010932.1. [P14210-3]
NP_001010933.1. NM_001010933.1. [P14210-5]
NP_001010934.1. NM_001010934.1. [P14210-6]
XP_006716019.1. XM_006715956.1. [P14210-1]
UniGeneHs.396530.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BHTX-ray2.00A/B35-210[»]
1GMNX-ray2.30A/B28-210[»]
1GMOX-ray3.00A/B/C/D/E/F/G/H28-210[»]
1GP9X-ray2.50A/B/C/D40-210[»]
1NK1X-ray2.50A/B28-210[»]
1SHYX-ray3.22A495-728[»]
1SI5X-ray2.53H495-728[»]
2HGFNMR-A31-127[»]
2QJ2X-ray1.81A/B28-209[»]
3HMSX-ray1.70A28-126[»]
3HMTX-ray2.00A/B28-126[»]
3HN4X-ray2.60A28-289[»]
3MKPX-ray2.81A/B/C/D28-210[»]
3SP8X-ray1.86A/B28-288[»]
4K3JX-ray2.80A495-721[»]
ProteinModelPortalP14210.
SMRP14210. Positions 34-471, 495-721.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109330. 6 interactions.
DIPDIP-37535N.
IntActP14210. 4 interactions.
MINTMINT-219560.

Chemistry

ChEMBLCHEMBL5479.

Protein family/group databases

MEROPSS01.976.

PTM databases

PhosphoSiteP14210.
UniCarbKBP14210.

Polymorphism databases

DMDM123116.

Proteomic databases

MaxQBP14210.
PaxDbP14210.
PRIDEP14210.

Protocols and materials databases

DNASU3082.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000222390; ENSP00000222390; ENSG00000019991. [P14210-1]
ENST00000423064; ENSP00000413829; ENSG00000019991. [P14210-6]
ENST00000444829; ENSP00000389854; ENSG00000019991. [P14210-2]
ENST00000453411; ENSP00000408270; ENSG00000019991. [P14210-5]
ENST00000457544; ENSP00000391238; ENSG00000019991. [P14210-3]
GeneID3082.
KEGGhsa:3082.
UCSCuc003uhl.3. human. [P14210-1]
uc003uhm.3. human. [P14210-3]
uc003uhn.1. human. [P14210-2]
uc003uho.1. human. [P14210-5]
uc003uhp.3. human. [P14210-6]

Organism-specific databases

CTD3082.
GeneCardsGC07M081328.
GeneReviewsHGF.
HGNCHGNC:4893. HGF.
HPACAB010333.
HPA040360.
HPA044088.
MIM142409. gene.
608265. phenotype.
neXtProtNX_P14210.
Orphanet90636. Autosomal recessive nonsyndromic sensorineural deafness type DFNB.
PharmGKBPA29269.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOVERGENHBG004381.
InParanoidP14210.
KOK05460.
OMAGSESPWC.
OrthoDBEOG75B84T.
PhylomeDBP14210.
TreeFamTF329901.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP14210.

Gene expression databases

ArrayExpressP14210.
BgeeP14210.
GenevestigatorP14210.

Family and domain databases

Gene3D2.40.20.10. 4 hits.
InterProIPR027284. Hepatocyte_GF.
IPR024174. HGF_MST1.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR003014. PAN-1_domain.
IPR003609. Pan_app.
IPR001254. Peptidase_S1.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00051. Kringle. 4 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF500183. Hepatocyte_GF. 1 hit.
PIRSF001152. HGF_MST1. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00130. KR. 4 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 4 hits.
PROSITEPS00021. KRINGLE_1. 4 hits.
PS50070. KRINGLE_2. 4 hits.
PS50948. PAN. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHGF. human.
EvolutionaryTraceP14210.
GeneWikiHepatocyte_growth_factor.
GenomeRNAi3082.
NextBio12211.
PMAP-CutDBP14210.
PROP14210.
SOURCESearch...

Entry information

Entry nameHGF_HUMAN
AccessionPrimary (citable) accession number: P14210
Secondary accession number(s): A1L3U6 expand/collapse secondary AC list , Q02935, Q13494, Q14519, Q3KRB2, Q8TCE2, Q9BYL9, Q9BYM0, Q9UDU6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: August 1, 1991
Last modified: July 9, 2014
This is version 183 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM