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P14210

- HGF_HUMAN

UniProt

P14210 - HGF_HUMAN

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Protein

Hepatocyte growth factor

Gene

HGF

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

Functioni

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.2 Publications

GO - Molecular functioni

  1. catalytic activity Source: InterPro
  2. chemoattractant activity Source: BHF-UCL
  3. growth factor activity Source: UniProtKB
  4. identical protein binding Source: IntAct

GO - Biological processi

  1. activation of MAPK activity Source: Ensembl
  2. blood coagulation Source: Reactome
  3. cell chemotaxis Source: BHF-UCL
  4. cellular response to hepatocyte growth factor stimulus Source: BHF-UCL
  5. epithelial to mesenchymal transition Source: HGNC
  6. hepatocyte growth factor receptor signaling pathway Source: BHF-UCL
  7. hyaluronan metabolic process Source: Ensembl
  8. liver development Source: Ensembl
  9. mitotic nuclear division Source: UniProtKB
  10. myoblast proliferation Source: Ensembl
  11. negative regulation of apoptotic process Source: Ensembl
  12. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
  13. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  14. negative regulation of hydrogen peroxide-mediated programmed cell death Source: BHF-UCL
  15. negative regulation of release of cytochrome c from mitochondria Source: BHF-UCL
  16. organ regeneration Source: Ensembl
  17. platelet activation Source: Reactome
  18. platelet degranulation Source: Reactome
  19. positive chemotaxis Source: GOC
  20. positive regulation of cell migration Source: BHF-UCL
  21. positive regulation of DNA biosynthetic process Source: UniProtKB
  22. positive regulation of osteoblast differentiation Source: BHF-UCL
  23. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  24. positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  25. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  26. regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Growth factor, Serine protease homolog

Enzyme and pathway databases

ReactomeiREACT_115529. Interleukin-7 signaling.
SignaLinkiP14210.

Protein family/group databases

MEROPSiS01.976.

Names & Taxonomyi

Protein namesi
Recommended name:
Hepatocyte growth factor
Alternative name(s):
Hepatopoietin-A
Scatter factor
Short name:
SF
Cleaved into the following 2 chains:
Gene namesi
Name:HGF
Synonyms:HPTA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:4893. HGF.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: Ensembl
  3. membrane Source: UniProtKB
  4. platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi494 – 4941R → Q: Loss of activity due to absence of proteolytic cleavage. 1 Publication

Keywords - Diseasei

Deafness, Non-syndromic deafness

Organism-specific databases

MIMi608265. phenotype.
Orphaneti90636. Autosomal recessive non-syndromic sensorineural deafness type DFNB.
PharmGKBiPA29269.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 31311 PublicationAdd
BLAST
Chaini32 – 494463Hepatocyte growth factor alpha chainPRO_0000028091Add
BLAST
Chaini495 – 728234Hepatocyte growth factor beta chainPRO_0000028092Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Pyrrolidone carboxylic acid1 Publication
Disulfide bondi70 ↔ 96
Disulfide bondi74 ↔ 84
Disulfide bondi128 ↔ 206
Disulfide bondi149 ↔ 189
Disulfide bondi177 ↔ 201
Disulfide bondi211 ↔ 288By similarity
Disulfide bondi232 ↔ 271By similarity
Disulfide bondi260 ↔ 283By similarity
Glycosylationi294 – 2941N-linked (GlcNAc...) (complex)CAR_000021
Disulfide bondi305 ↔ 383By similarity
Disulfide bondi326 ↔ 365By similarity
Disulfide bondi354 ↔ 377By similarity
Disulfide bondi391 ↔ 469By similarity
Glycosylationi402 – 4021N-linked (GlcNAc...) (complex)CAR_000022
Disulfide bondi412 ↔ 452By similarity
Disulfide bondi440 ↔ 464By similarity
Glycosylationi476 – 4761O-linked (GalNAc...)1 PublicationCAR_000023
Disulfide bondi487 ↔ 604Interchain (between alpha and beta chains)PROSITE-ProRule annotation
Disulfide bondi519 ↔ 535By similarity
Glycosylationi566 – 5661N-linked (GlcNAc...) (complex)CAR_000024
Disulfide bondi612 ↔ 679By similarity
Disulfide bondi642 ↔ 658By similarity
Glycosylationi653 – 6531N-linked (GlcNAc...) (complex)CAR_000025
Disulfide bondi669 ↔ 697By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP14210.
PaxDbiP14210.
PRIDEiP14210.

PTM databases

PhosphoSiteiP14210.
UniCarbKBiP14210.

Miscellaneous databases

PMAP-CutDBP14210.

Expressioni

Gene expression databases

BgeeiP14210.
ExpressionAtlasiP14210. baseline and differential.
GenevestigatoriP14210.

Organism-specific databases

HPAiCAB010333.
HPA040360.
HPA044088.

Interactioni

Subunit structurei

Dimer of an alpha chain and a beta chain linked by a disulfide bond. Interacts with SRPX2; the interaction increases HGF mitogenic activity.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
METP085814EBI-1039104,EBI-1039152
MetP160562EBI-1039104,EBI-1798780From a different organism.

Protein-protein interaction databases

BioGridi109330. 7 interactions.
DIPiDIP-37535N.
IntActiP14210. 5 interactions.
MINTiMINT-219560.

Structurei

Secondary structure

1
728
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi39 – 413
Beta strandi42 – 5211
Beta strandi55 – 573
Beta strandi60 – 634
Helixi67 – 7610
Turni77 – 793
Beta strandi80 – 823
Beta strandi86 – 905
Turni91 – 944
Beta strandi95 – 1006
Beta strandi105 – 1073
Beta strandi108 – 12114
Helixi122 – 1243
Beta strandi128 – 1325
Beta strandi148 – 1503
Beta strandi156 – 1583
Helixi164 – 1674
Turni168 – 1714
Beta strandi187 – 1937
Beta strandi198 – 2003
Helixi206 – 2094
Beta strandi211 – 2133
Beta strandi239 – 2413
Turni247 – 2493
Turni251 – 2544
Beta strandi270 – 2745
Beta strandi279 – 2824
Beta strandi508 – 52518
Beta strandi528 – 5325
Helixi533 – 5353
Beta strandi537 – 5393
Helixi541 – 5433
Beta strandi544 – 5496
Beta strandi551 – 5544
Turni557 – 5615
Beta strandi563 – 57210
Beta strandi579 – 5868
Beta strandi591 – 5933
Beta strandi611 – 6188
Beta strandi630 – 6378
Helixi639 – 6413
Turni646 – 6483
Beta strandi656 – 6605
Beta strandi662 – 6643
Turni670 – 6745
Beta strandi676 – 6805
Beta strandi682 – 69110
Beta strandi695 – 6984
Beta strandi704 – 7085
Helixi709 – 7124
Helixi713 – 7208

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4O3TX-ray2.99A495-728[»]
4O3UX-ray3.04A495-728[»]
ProteinModelPortaliP14210.
SMRiP14210. Positions 34-724.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14210.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 12387PANPROSITE-ProRule annotationAdd
BLAST
Domaini128 – 20679Kringle 1PROSITE-ProRule annotationAdd
BLAST
Domaini211 – 28878Kringle 2PROSITE-ProRule annotationAdd
BLAST
Domaini305 – 38379Kringle 3PROSITE-ProRule annotationAdd
BLAST
Domaini391 – 46979Kringle 4PROSITE-ProRule annotationAdd
BLAST
Domaini495 – 721227Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Plasminogen subfamily.PROSITE-ProRule annotation
Contains 4 kringle domains.PROSITE-ProRule annotation
Contains 1 PAN domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Kringle, Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000119133.
HOVERGENiHBG004381.
InParanoidiP14210.
KOiK05460.
OMAiGSESPWC.
OrthoDBiEOG75B84T.
PhylomeDBiP14210.
TreeFamiTF329901.

Family and domain databases

Gene3Di2.40.20.10. 4 hits.
InterProiIPR027284. 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]
PfamiPF00051. Kringle. 4 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF500183. Hepatocyte_GF. 1 hit.
PIRSF001152. HGF_MST1. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00130. KR. 4 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 4 hits.
PROSITEiPS00021. KRINGLE_1. 4 hits.
PS50070. KRINGLE_2. 4 hits.
PS50948. PAN. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P14210-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MWVTKLLPAL LLQHVLLHLL LLPIAIPYAE GQRKRRNTIH EFKKSAKTTL
60 70 80 90 100
IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP
110 120 130 140 150
FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ
160 170 180 190 200
PWSSMIPHEH SFLPSSYRGK DLQENYCRNP RGEEGGPWCF TSNPEVRYEV
210 220 230 240 250
CDIPQCSEVE CMTCNGESYR GLMDHTESGK ICQRWDHQTP HRHKFLPERY
260 270 280 290 300
PDKGFDDNYC RNPDGQPRPW CYTLDPHTRW EYCAIKTCAD NTMNDTDVPL
310 320 330 340 350
ETTECIQGQG EGYRGTVNTI WNGIPCQRWD SQYPHEHDMT PENFKCKDLR
360 370 380 390 400
ENYCRNPDGS ESPWCFTTDP NIRVGYCSQI PNCDMSHGQD CYRGNGKNYM
410 420 430 440 450
GNLSQTRSGL TCSMWDKNME DLHRHIFWEP DASKLNENYC RNPDDDAHGP
460 470 480 490 500
WCYTGNPLIP WDYCPISRCE GDTTPTIVNL DHPVISCAKT KQLRVVNGIP
510 520 530 540 550
TRTNIGWMVS LRYRNKHICG GSLIKESWVL TARQCFPSRD LKDYEAWLGI
560 570 580 590 600
HDVHGRGDEK CKQVLNVSQL VYGPEGSDLV LMKLARPAVL DDFVSTIDLP
610 620 630 640 650
NYGCTIPEKT SCSVYGWGYT GLINYDGLLR VAHLYIMGNE KCSQHHRGKV
660 670 680 690 700
TLNESEICAG AEKIGSGPCE GDYGGPLVCE QHKMRMVLGV IVPGRGCAIP
710 720
NRPGIFVRVA YYAKWIHKII LTYKVPQS
Length:728
Mass (Da):83,134
Last modified:August 1, 1991 - v2
Checksum:i2D997938295ADD2F
GO
Isoform 2 (identifier: P14210-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     289-290: AD → ET
     291-728: Missing.

Show »
Length:290
Mass (Da):33,766
Checksum:iC8A18A6F0D63200A
GO
Isoform 3 (identifier: P14210-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     161-165: Missing.

Show »
Length:723
Mass (Da):82,602
Checksum:i627B1EF99FAD931B
GO
Isoform 4 (identifier: P14210-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:296
Mass (Da):34,547
Checksum:iA45E456B87AE03BE
GO
Isoform 5 (identifier: P14210-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:285
Mass (Da):33,234
Checksum:i0A93B073EA86EA61
GO
Isoform 6 (identifier: P14210-6) [UniParc]FASTAAdd to Basket

Also known as: HGF/NK1

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

Show »
Length:210
Mass (Da):24,116
Checksum:i94A6EE9C50DE5A86
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 332QR → HK in CAA34387. (PubMed:2531289)Curated
Sequence conflicti78 – 781K → N in CAA34387. (PubMed:2531289)Curated
Sequence conflicti180 – 1801P → T AA sequence (PubMed:1824873)Curated
Sequence conflicti293 – 2931M → V in CAA34387. (PubMed:2531289)Curated
Sequence conflicti300 – 3001L → M in CAA34387. (PubMed:2531289)Curated
Sequence conflicti317 – 3171V → A in CAA34387. (PubMed:2531289)Curated
Sequence conflicti336 – 3361E → K in CAA34387. (PubMed:2531289)Curated
Sequence conflicti387 – 3871H → N in CAA34387. (PubMed:2531289)Curated
Sequence conflicti416 – 4161D → N in CAA34387. (PubMed:2531289)Curated
Sequence conflicti505 – 5051I → V in CAA34387. (PubMed:2531289)Curated
Sequence conflicti509 – 5091V → I in CAA34387. (PubMed:2531289)Curated
Sequence conflicti558 – 5581D → E in CAA34387. (PubMed:2531289)Curated
Sequence conflicti561 – 5611C → R in CAA34387. (PubMed:2531289)Curated
Sequence conflicti592 – 5921D → N AA sequence (PubMed:1824873)Curated
Sequence conflicti595 – 5951S → N in CAA34387. (PubMed:2531289)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti153 – 1531S → I.
Corresponds to variant rs17566 [ dbSNP | Ensembl ].
VAR_014570
Natural varianti304 – 3041E → K.1 Publication
Corresponds to variant rs5745687 [ dbSNP | Ensembl ].
VAR_019199
Natural varianti330 – 3301D → Y.1 Publication
Corresponds to variant rs5745688 [ dbSNP | Ensembl ].
VAR_019200

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei161 – 1655Missing in isoform 3 and isoform 5. 2 PublicationsVSP_009617
Alternative sequencei209 – 2102VE → GK in isoform 6. 2 PublicationsVSP_009618
Alternative sequencei211 – 728518Missing in isoform 6. 2 PublicationsVSP_009619Add
BLAST
Alternative sequencei287 – 29610TCADNTMNDT → NMRDITWALN in isoform 4. 1 PublicationVSP_009620
Alternative sequencei289 – 2902AD → ET in isoform 2 and isoform 5. 3 PublicationsVSP_009622
Alternative sequencei291 – 728438Missing in isoform 2 and isoform 5. 3 PublicationsVSP_009623Add
BLAST
Alternative sequencei297 – 728432Missing in isoform 4. 1 PublicationVSP_009621Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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
, M75967, M75966, M75968, M75969 Genomic DNA. Translation: AAG53459.1.
M75983
, M75972, M75973, M75974, M75975, M75976, M75977, M75978, M75979, M75980, M75981, M75982 Genomic DNA. Translation: AAG53460.1.
CCDSiCCDS47626.1. [P14210-3]
CCDS47627.1. [P14210-2]
CCDS47628.1. [P14210-5]
CCDS47629.1. [P14210-6]
CCDS5597.1. [P14210-1]
PIRiJH0579.
RefSeqiNP_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]
UniGeneiHs.396530.

Genome annotation databases

EnsembliENST00000222390; ENSP00000222390; ENSG00000019991. [P14210-1]
ENST00000423064; ENSP00000413829; ENSG00000019991. [P14210-6]
ENST00000444829; ENSP00000389854; ENSG00000019991. [P14210-2]
ENST00000453411; ENSP00000408270; ENSG00000019991. [P14210-5]
ENST00000457544; ENSP00000391238; ENSG00000019991. [P14210-3]
GeneIDi3082.
KEGGihsa:3082.
UCSCiuc003uhl.3. human. [P14210-1]
uc003uhm.3. human. [P14210-3]
uc003uhn.1. human. [P14210-2]
uc003uho.1. human. [P14210-5]
uc003uhp.3. human. [P14210-6]

Polymorphism databases

DMDMi123116.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Hepatocyte growth factor entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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
, M75967 , M75966 , M75968 , M75969 Genomic DNA. Translation: AAG53459.1 .
M75983
, M75972 , M75973 , M75974 , M75975 , M75976 , M75977 , M75978 , M75979 , M75980 , M75981 , M75982 Genomic DNA. Translation: AAG53460.1 .
CCDSi CCDS47626.1. [P14210-3 ]
CCDS47627.1. [P14210-2 ]
CCDS47628.1. [P14210-5 ]
CCDS47629.1. [P14210-6 ]
CCDS5597.1. [P14210-1 ]
PIRi JH0579.
RefSeqi NP_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 ]
UniGenei Hs.396530.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BHT X-ray 2.00 A/B 35-210 [» ]
1GMN X-ray 2.30 A/B 28-210 [» ]
1GMO X-ray 3.00 A/B/C/D/E/F/G/H 28-210 [» ]
1GP9 X-ray 2.50 A/B/C/D 40-210 [» ]
1NK1 X-ray 2.50 A/B 28-210 [» ]
1SHY X-ray 3.22 A 495-728 [» ]
1SI5 X-ray 2.53 H 495-728 [» ]
2HGF NMR - A 31-127 [» ]
2QJ2 X-ray 1.81 A/B 28-209 [» ]
3HMS X-ray 1.70 A 28-126 [» ]
3HMT X-ray 2.00 A/B 28-126 [» ]
3HN4 X-ray 2.60 A 28-289 [» ]
3MKP X-ray 2.81 A/B/C/D 28-210 [» ]
3SP8 X-ray 1.86 A/B 28-288 [» ]
4K3J X-ray 2.80 A 495-721 [» ]
4O3T X-ray 2.99 A 495-728 [» ]
4O3U X-ray 3.04 A 495-728 [» ]
ProteinModelPortali P14210.
SMRi P14210. Positions 34-724.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109330. 7 interactions.
DIPi DIP-37535N.
IntActi P14210. 5 interactions.
MINTi MINT-219560.

Chemistry

ChEMBLi CHEMBL5479.

Protein family/group databases

MEROPSi S01.976.

PTM databases

PhosphoSitei P14210.
UniCarbKBi P14210.

Polymorphism databases

DMDMi 123116.

Proteomic databases

MaxQBi P14210.
PaxDbi P14210.
PRIDEi P14210.

Protocols and materials databases

DNASUi 3082.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000222390 ; ENSP00000222390 ; ENSG00000019991 . [P14210-1 ]
ENST00000423064 ; ENSP00000413829 ; ENSG00000019991 . [P14210-6 ]
ENST00000444829 ; ENSP00000389854 ; ENSG00000019991 . [P14210-2 ]
ENST00000453411 ; ENSP00000408270 ; ENSG00000019991 . [P14210-5 ]
ENST00000457544 ; ENSP00000391238 ; ENSG00000019991 . [P14210-3 ]
GeneIDi 3082.
KEGGi hsa:3082.
UCSCi uc003uhl.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

CTDi 3082.
GeneCardsi GC07M081328.
GeneReviewsi HGF.
HGNCi HGNC:4893. HGF.
HPAi CAB010333.
HPA040360.
HPA044088.
MIMi 142409. gene.
608265. phenotype.
neXtProti NX_P14210.
Orphaneti 90636. Autosomal recessive non-syndromic sensorineural deafness type DFNB.
PharmGKBi PA29269.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00760000119133.
HOVERGENi HBG004381.
InParanoidi P14210.
KOi K05460.
OMAi GSESPWC.
OrthoDBi EOG75B84T.
PhylomeDBi P14210.
TreeFami TF329901.

Enzyme and pathway databases

Reactomei REACT_115529. Interleukin-7 signaling.
SignaLinki P14210.

Miscellaneous databases

ChiTaRSi HGF. human.
EvolutionaryTracei P14210.
GeneWikii Hepatocyte_growth_factor.
GenomeRNAii 3082.
NextBioi 12211.
PMAP-CutDB P14210.
PROi P14210.
SOURCEi Search...

Gene expression databases

Bgeei P14210.
ExpressionAtlasi P14210. baseline and differential.
Genevestigatori P14210.

Family and domain databases

Gene3Di 2.40.20.10. 4 hits.
InterProi IPR027284. 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 ]
Pfami PF00051. Kringle. 4 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PIRSFi PIRSF500183. Hepatocyte_GF. 1 hit.
PIRSF001152. HGF_MST1. 1 hit.
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00130. KR. 4 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 4 hits.
PROSITEi PS00021. KRINGLE_1. 4 hits.
PS50070. KRINGLE_2. 4 hits.
PS50948. PAN. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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.
    , 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.
    , 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 28-289, DISULFIDE BONDS, FUNCTION.

Entry informationi

Entry nameiHGF_HUMAN
AccessioniPrimary (citable) accession number: P14210
Secondary accession number(s): A1L3U6
, Q02935, Q13494, Q14519, Q3KRB2, Q8TCE2, Q9BYL9, Q9BYM0, Q9UDU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: August 1, 1991
Last modified: October 29, 2014
This is version 186 of the entry and version 2 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3