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Reviewed, UniProtKB/Swiss-Prot P14210 (HGF_HUMAN)

Last modified November 3, 2009. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Hepatocyte growth factor
Alternative name(s):
    Scatter factor
      Short name=SF
    Hepatopoeitin-A
Cleaved into the following 2 chains:
    1- Recommended name:
            Hepatocyte growth factor alpha chain
    2- Recommended name:
            Hepatocyte growth factor beta chain
Gene names
Name: HGF
Synonyms: HPTA
OrganismHomo sapiens (Human) [Complete 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

HGF is a potent mitogen for mature parenchymal hepatocyte cells, seems to be an hepatotrophic factor, and acts as growth factor for a broad spectrum of tissues and cell types. It has no detectable protease activity.

Subunit structure

Dimer of an alpha chain and a beta chain linked by a disulfide bond.

Sequence similarities

Belongs to the peptidase S1 family. Plasminogen subfamily.

Contains 4 kringle domains.

Contains 1 PAN domain.

Contains 1 peptidase S1 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

METP085812EBI-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)

The sequence of this isoform differs from the canonical sequence as follows:
     287-296: TCADNTMNDT → NMRDITWALN
     297-728: Missing.
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
Disulfide bond74 ↔ 84
Disulfide bond128 ↔ 206
Disulfide bond149 ↔ 189
Disulfide bond177 ↔ 201
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: dbSNP rs17566.
VAR_014570
Natural variant3041E → K: dbSNP rs5745687. Ref.11
VAR_019199
Natural variant3301D → Y: dbSNP rs5745688. Ref.11
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.

Checksum: C8A18A6F0D63200A
Show »

FASTA29033,766
Isoform 3.

Checksum: 627B1EF99FAD931B
Show »

FASTA72382,602
Isoform 4.

Checksum: A45E456B87AE03BE
Show »

FASTA29634,547
Isoform 5.

Checksum: 0A93B073EA86EA61
Show »

FASTA28533,234
Isoform 6 (HGF/NK1).

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: 2528952] [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: 2531289] [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: 2145836] [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: 1831432] [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: 1826653] [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: 1824873] [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: 1831266] [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: 1720571] [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: 1280830] [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: 8662798] [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: 12853948] [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: 12690205] [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: 15489334] [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: 1832556] [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: 1826837] [Abstract]
Cited for: SIGNAL SEQUENCE CLEAVAGE SITE.
[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: 1482348] [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: 1321034] [Abstract]
Cited for: MUTAGENESIS.
[19]"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: 9493272] [Abstract]
Cited for: STRUCTURE BY NMR OF 31-127.
[20]"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: 9817840] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 35-210.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
Wikipedia

Hepatocyte growth factor entry

Cross-references

Sequence databases

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.
IPIIPI00025767.
IPI00400878.
IPI00400879.
IPI00400880.
IPI00400881.
IPI00941852.
PIRJH0579.
RefSeqNP_000592.3.
NP_001010931.1.
NP_001010932.1.
NP_001010933.1.
NP_001010934.1.
UniGeneHs.396530

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BHTX-ray2.00A/B35-210[»]
1GMNX-ray2.30A/B30-210[»]
1GMOX-ray3.00A/B/C/D/E/F/G/H30-210[»]
1GP9X-ray2.50A/B/C/D40-210[»]
1NK1X-ray2.50A/B30-210[»]
1SHYX-ray3.22A495-728[»]
1SI5X-ray2.53H495-728[»]
2HGFNMR-A31-127[»]
2QJ2X-ray1.81A/B28-209[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP14210. 2 interactions.
STRINGP14210.

Protein family/group databases

MEROPSS01.976.

PTM databases

GlycoSuiteDBP14210.

Proteomic databases

PRIDEP14210.

Genome annotation databases

EnsemblENST00000222390; ENSP00000222390; ENSG00000019991; Homo sapiens. [Genome view]
ENST00000354224; ENSP00000346164; ENSG00000019991; Homo sapiens. [Genome view]
ENST00000394769; ENSP00000378250; ENSG00000019991; Homo sapiens. [Genome view]
ENST00000412881; ENSP00000396307; ENSG00000019991; Homo sapiens. [Genome view]
ENST00000421558; ENSP00000388592; ENSG00000019991; Homo sapiens. [Genome view]
ENST00000423064; ENSP00000413829; ENSG00000019991; Homo sapiens. [Genome view]
ENST00000444829; ENSP00000389854; ENSG00000019991; Homo sapiens. [Genome view]
ENST00000453018; ENSP00000395468; ENSG00000019991; Homo sapiens. [Genome view]
ENST00000453411; ENSP00000408270; ENSG00000019991; Homo sapiens. [Genome view]
ENST00000457544; ENSP00000391238; ENSG00000019991; Homo sapiens. [Genome view]
GeneID3082.
KEGGhsa:3082.
UCSCuc003uhl.1. human.
uc003uhm.1. human.
uc003uhn.1. human.
uc003uho.1. human.

Organism-specific databases

CTD3082.
GeneCardsGC07M081166.
H-InvDBHIX0033620.
HGNCHGNC:4893. HGF.
HPACAB010333.
MIM142409. gene.
PharmGKBPA29269.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP14210.
OMALTYKVPQ.

Enzyme and pathway databases

Pathway_Interaction_DBarf6cyclingpathway. Arf6 signaling events.
faspathway. FAS signaling pathway (CD95).
fgf_pathway. FGF signaling pathway.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
syndecan_1_pathway. Syndecan-1-mediated signaling events.
ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP14210.
BgeeP14210.
GenevestigatorP14210.
GermOnlineENSG00000019991. Homo sapiens.

Family and domain databases

InterProIPR000001. Kringle.
IPR018056. Kringle_CS.
IPR018059. Kringle_sub.
IPR003014. PAN-1_domain.
IPR003609. Pan_app.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
Gene3DG3DSA:2.40.20.10. Kringle. 4 hits.
PfamPF00051. Kringle. 4 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
PR00018. KRINGLE.
ProDomPD000395. Kringle. 4 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00130. KR. 4 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS00021. KRINGLE_1. 4 hits.
PS50070. KRINGLE_2. 4 hits.
PS50948. PAN. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
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Other Resources

NextBio12211.
PMAP-CutDBP14210.
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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: November 3, 2009
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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