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P14210

- HGF_HUMAN

UniProt

P14210 - HGF_HUMAN

Protein

Hepatocyte growth factor

Gene

HGF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 185 (01 Oct 2014)
      Sequence version 2 (01 Aug 1991)
      Previous versions | rss
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    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
    5. 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

    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

    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. 2 Publications

    Keywords - Diseasei

    Deafness, Non-syndromic deafness

    Organism-specific databases

    MIMi608265. phenotype.
    Orphaneti90636. Autosomal recessive nonsyndromic 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

    ArrayExpressiP14210.
    BgeeiP14210.
    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. 6 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 34-471, 495-721.
    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.
    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

    MWVTKLLPAL LLQHVLLHLL LLPIAIPYAE GQRKRRNTIH EFKKSAKTTL    50
    IKIDPALKIK TKKVNTADQC ANRCTRNKGL PFTCKAFVFD KARKQCLWFP 100
    FNSMSSGVKK EFGHEFDLYE NKDYIRNCII GKGRSYKGTV SITKSGIKCQ 150
    PWSSMIPHEH SFLPSSYRGK DLQENYCRNP RGEEGGPWCF TSNPEVRYEV 200
    CDIPQCSEVE CMTCNGESYR GLMDHTESGK ICQRWDHQTP HRHKFLPERY 250
    PDKGFDDNYC RNPDGQPRPW CYTLDPHTRW EYCAIKTCAD NTMNDTDVPL 300
    ETTECIQGQG EGYRGTVNTI WNGIPCQRWD SQYPHEHDMT PENFKCKDLR 350
    ENYCRNPDGS ESPWCFTTDP NIRVGYCSQI PNCDMSHGQD CYRGNGKNYM 400
    GNLSQTRSGL TCSMWDKNME DLHRHIFWEP DASKLNENYC RNPDDDAHGP 450
    WCYTGNPLIP WDYCPISRCE GDTTPTIVNL DHPVISCAKT KQLRVVNGIP 500
    TRTNIGWMVS LRYRNKHICG GSLIKESWVL TARQCFPSRD LKDYEAWLGI 550
    HDVHGRGDEK CKQVLNVSQL VYGPEGSDLV LMKLARPAVL DDFVSTIDLP 600
    NYGCTIPEKT SCSVYGWGYT GLINYDGLLR VAHLYIMGNE KCSQHHRGKV 650
    TLNESEICAG AEKIGSGPCE GDYGGPLVCE QHKMRMVLGV IVPGRGCAIP 700
    NRPGIFVRVA YYAKWIHKII LTYKVPQS 728
    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 34-471, 495-721.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109330. 6 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 nonsyndromic sensorineural deafness type DFNB.
    PharmGKBi PA29269.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    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

    ArrayExpressi P14210.
    Bgeei P14210.
    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

    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 1, 2014
    This is version 185 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