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Q04756

- HGFA_HUMAN

UniProt

Q04756 - HGFA_HUMAN

Protein

Hepatocyte growth factor activator

Gene

HGFAC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Activates hepatocyte growth factor (HGF) by converting it from a single chain to a heterodimeric form.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei447 – 4471Charge relay system1 Publication
    Active sitei497 – 4971Charge relay system1 Publication
    Active sitei598 – 5981Charge relay system1 Publication

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: ProtInc
    2. serine-type peptidase activity Source: ProtInc

    GO - Biological processi

    1. proteolysis Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS01.228.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hepatocyte growth factor activator (EC:3.4.21.-)
    Short name:
    HGF activator
    Short name:
    HGFA
    Cleaved into the following 2 chains:
    Gene namesi
    Name:HGFAC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:4894. HGFAC.

    Subcellular locationi

    Secreted
    Note: Secreted as an inactive single-chain precursor and is then activated to a heterodimeric form.

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB
    2. extracellular space Source: InterPro
    3. rough endoplasmic reticulum Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29270.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 35351 PublicationAdd
    BLAST
    Propeptidei36 – 372337Removed in mature formPRO_0000027911Add
    BLAST
    Chaini373 – 40735Hepatocyte growth factor activator short chainPRO_0000027912Add
    BLAST
    Chaini408 – 655248Hepatocyte growth factor activator long chainPRO_0000027913Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi108 ↔ 133By similarity
    Disulfide bondi122 ↔ 148By similarity
    Disulfide bondi164 ↔ 175By similarity
    Disulfide bondi169 ↔ 186By similarity
    Disulfide bondi188 ↔ 197By similarity
    Disulfide bondi202 ↔ 230By similarity
    Disulfide bondi228 ↔ 237By similarity
    Disulfide bondi245 ↔ 256By similarity
    Disulfide bondi250 ↔ 267By similarity
    Disulfide bondi269 ↔ 278By similarity
    Disulfide bondi286 ↔ 367By similarity
    Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi307 ↔ 349By similarity
    Disulfide bondi338 ↔ 362By similarity
    Disulfide bondi394 ↔ 521Interchain (between short and long chains)
    Disulfide bondi432 ↔ 448
    Disulfide bondi440 ↔ 510
    Glycosylationi468 – 4681N-linked (GlcNAc...)3 Publications
    Glycosylationi492 – 4921N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi535 ↔ 604
    Glycosylationi546 – 5461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi567 ↔ 583
    Disulfide bondi594 ↔ 622

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiQ04756.
    PaxDbiQ04756.
    PeptideAtlasiQ04756.
    PRIDEiQ04756.

    PTM databases

    PhosphoSiteiQ04756.

    Miscellaneous databases

    PMAP-CutDBQ04756.

    Expressioni

    Tissue specificityi

    Liver.

    Gene expression databases

    ArrayExpressiQ04756.
    BgeeiQ04756.
    CleanExiHS_HGFAC.
    GenevestigatoriQ04756.

    Organism-specific databases

    HPAiHPA058279.
    HPA059076.

    Interactioni

    Subunit structurei

    Heterodimer of a short chain and a long chain linked by a disulfide bond.2 Publications

    Protein-protein interaction databases

    DIPiDIP-6022N.
    IntActiQ04756. 1 interaction.
    STRINGi9606.ENSP00000372224.

    Structurei

    Secondary structure

    1
    655
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi422 – 4276
    Beta strandi430 – 4389
    Beta strandi441 – 4444
    Helixi446 – 4494
    Helixi455 – 4573
    Beta strandi458 – 4636
    Beta strandi475 – 4773
    Beta strandi479 – 4846
    Beta strandi490 – 4923
    Turni493 – 4964
    Beta strandi499 – 5035
    Beta strandi506 – 5083
    Beta strandi509 – 5113
    Beta strandi514 – 5163
    Beta strandi534 – 5407
    Beta strandi543 – 5464
    Beta strandi555 – 5617
    Helixi564 – 5674
    Turni570 – 5734
    Helixi574 – 5763
    Beta strandi581 – 5855
    Beta strandi587 – 5893
    Turni595 – 5995
    Beta strandi601 – 6066
    Beta strandi609 – 61810
    Turni621 – 6233
    Beta strandi625 – 6273
    Beta strandi629 – 6335
    Helixi634 – 6374
    Helixi638 – 6458

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YBWX-ray2.70A/B373-655[»]
    1YC0X-ray2.60A373-655[»]
    2R0KX-ray3.51A373-655[»]
    2R0LX-ray2.20A408-655[»]
    B373-407[»]
    2WUBX-ray2.90A/C408-655[»]
    B/D373-407[»]
    2WUCX-ray2.70A408-654[»]
    B373-407[»]
    3K2UX-ray2.35A408-655[»]
    B373-407[»]
    ProteinModelPortaliQ04756.
    SMRiQ04756. Positions 92-646.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04756.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini103 – 15048Fibronectin type-IIPROSITE-ProRule annotationAdd
    BLAST
    Domaini160 – 19839EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini200 – 24041Fibronectin type-IPROSITE-ProRule annotationAdd
    BLAST
    Domaini241 – 27939EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini286 – 36782KringlePROSITE-ProRule annotationAdd
    BLAST
    Domaini408 – 646239Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 2 EGF-like domains.PROSITE-ProRule annotation
    Contains 1 fibronectin type-I domain.PROSITE-ProRule annotation
    Contains 1 fibronectin type-II domain.PROSITE-ProRule annotation
    Contains 1 kringle domain.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Kringle, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    HOGENOMiHOG000237314.
    HOVERGENiHBG004345.
    InParanoidiQ04756.
    KOiK09631.
    OrthoDBiEOG75B84T.
    PhylomeDBiQ04756.
    TreeFamiTF329901.

    Family and domain databases

    Gene3Di2.10.10.10. 1 hit.
    2.40.20.10. 1 hit.
    InterProiIPR014394. Coagulation_fac_XIIa/HGFA.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR000083. Fibronectin_type1.
    IPR000562. FN_type2_col-bd.
    IPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00008. EGF. 2 hits.
    PF00039. fn1. 1 hit.
    PF00040. fn2. 1 hit.
    PF00051. Kringle. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001146. Factor_XII_HGFA. 1 hit.
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00181. EGF. 2 hits.
    SM00058. FN1. 1 hit.
    SM00059. FN2. 1 hit.
    SM00130. KR. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 2 hits.
    PROSITEiPS00022. EGF_1. 2 hits.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 2 hits.
    PS01253. FN1_1. 1 hit.
    PS51091. FN1_2. 1 hit.
    PS00023. FN2_1. 1 hit.
    PS51092. FN2_2. 1 hit.
    PS00021. KRINGLE_1. 1 hit.
    PS50070. KRINGLE_2. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q04756-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGRWAWVPSP WPPPGLGPFL LLLLLLLLLP RGFQPQPGGN RTESPEPNAT    50
    ATPAIPTILV TSVTSETPAT SAPEAEGPQS GGLPPPPRAV PSSSSPQAQA 100
    LTEDGRPCRF PFRYGGRMLH ACTSEGSAHR KWCATTHNYD RDRAWGYCVE 150
    ATPPPGGPAA LDPCASGPCL NGGSCSNTQD PQSYHCSCPR AFTGKDCGTE 200
    KCFDETRYEY LEGGDRWARV RQGHVEQCEC FGGRTWCEGT RHTACLSSPC 250
    LNGGTCHLIV ATGTTVCACP PGFAGRLCNI EPDERCFLGN GTGYRGVAST 300
    SASGLSCLAW NSDLLYQELH VDSVGAAALL GLGPHAYCRN PDNDERPWCY 350
    VVKDSALSWE YCRLEACESL TRVQLSPDLL ATLPEPASPG RQACGRRHKK 400
    RTFLRPRIIG GSSSLPGSHP WLAAIYIGDS FCAGSLVHTC WVVSAAHCFS 450
    HSPPRDSVSV VLGQHFFNRT TDVTQTFGIE KYIPYTLYSV FNPSDHDLVL 500
    IRLKKKGDRC ATRSQFVQPI CLPEPGSTFP AGHKCQIAGW GHLDENVSGY 550
    SSSLREALVP LVADHKCSSP EVYGADISPN MLCAGYFDCK SDACQGDSGG 600
    PLACEKNGVA YLYGIISWGD GCGRLHKPGV YTRVANYVDW INDRIRPPRR 650
    LVAPS 655
    Length:655
    Mass (Da):70,682
    Last modified:June 1, 1994 - v1
    Checksum:i2CF72F1E1B862ED7
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti218 – 2181A → S.
    Corresponds to variant rs3748034 [ dbSNP | Ensembl ].
    VAR_051851
    Natural varianti225 – 2251V → M.
    Corresponds to variant rs16844370 [ dbSNP | Ensembl ].
    VAR_033651
    Natural varianti231 – 2311F → L.1 Publication
    Corresponds to variant rs1987546 [ dbSNP | Ensembl ].
    VAR_033652
    Natural varianti509 – 5091R → H.
    Corresponds to variant rs16844401 [ dbSNP | Ensembl ].
    VAR_024294
    Natural varianti644 – 6441R → Q.
    Corresponds to variant rs2498323 [ dbSNP | Ensembl ].
    VAR_024295

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14012 mRNA. Translation: BAA03113.1.
    BC112190 mRNA. Translation: AAI12191.1.
    D50030 Genomic DNA. Translation: BAA74450.1.
    AL590235 Genomic DNA. Translation: CAM21456.1.
    CH471131 Genomic DNA. Translation: EAW82464.1.
    BC112192 mRNA. Translation: AAI12193.1.
    CCDSiCCDS3369.1.
    PIRiA46688.
    RefSeqiNP_001519.1. NM_001528.2.
    UniGeneiHs.104.

    Genome annotation databases

    EnsembliENST00000382774; ENSP00000372224; ENSG00000109758.
    GeneIDi3083.
    KEGGihsa:3083.
    UCSCiuc003ghc.3. human.

    Polymorphism databases

    DMDMi547643.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14012 mRNA. Translation: BAA03113.1 .
    BC112190 mRNA. Translation: AAI12191.1 .
    D50030 Genomic DNA. Translation: BAA74450.1 .
    AL590235 Genomic DNA. Translation: CAM21456.1 .
    CH471131 Genomic DNA. Translation: EAW82464.1 .
    BC112192 mRNA. Translation: AAI12193.1 .
    CCDSi CCDS3369.1.
    PIRi A46688.
    RefSeqi NP_001519.1. NM_001528.2.
    UniGenei Hs.104.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YBW X-ray 2.70 A/B 373-655 [» ]
    1YC0 X-ray 2.60 A 373-655 [» ]
    2R0K X-ray 3.51 A 373-655 [» ]
    2R0L X-ray 2.20 A 408-655 [» ]
    B 373-407 [» ]
    2WUB X-ray 2.90 A/C 408-655 [» ]
    B/D 373-407 [» ]
    2WUC X-ray 2.70 A 408-654 [» ]
    B 373-407 [» ]
    3K2U X-ray 2.35 A 408-655 [» ]
    B 373-407 [» ]
    ProteinModelPortali Q04756.
    SMRi Q04756. Positions 92-646.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-6022N.
    IntActi Q04756. 1 interaction.
    STRINGi 9606.ENSP00000372224.

    Protein family/group databases

    MEROPSi S01.228.

    PTM databases

    PhosphoSitei Q04756.

    Polymorphism databases

    DMDMi 547643.

    Proteomic databases

    MaxQBi Q04756.
    PaxDbi Q04756.
    PeptideAtlasi Q04756.
    PRIDEi Q04756.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000382774 ; ENSP00000372224 ; ENSG00000109758 .
    GeneIDi 3083.
    KEGGi hsa:3083.
    UCSCi uc003ghc.3. human.

    Organism-specific databases

    CTDi 3083.
    GeneCardsi GC04P003443.
    HGNCi HGNC:4894. HGFAC.
    HPAi HPA058279.
    HPA059076.
    MIMi 604552. gene.
    neXtProti NX_Q04756.
    PharmGKBi PA29270.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000237314.
    HOVERGENi HBG004345.
    InParanoidi Q04756.
    KOi K09631.
    OrthoDBi EOG75B84T.
    PhylomeDBi Q04756.
    TreeFami TF329901.

    Miscellaneous databases

    EvolutionaryTracei Q04756.
    GeneWikii HGFAC.
    GenomeRNAii 3083.
    NextBioi 12223.
    PMAP-CutDB Q04756.
    PROi Q04756.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q04756.
    Bgeei Q04756.
    CleanExi HS_HGFAC.
    Genevestigatori Q04756.

    Family and domain databases

    Gene3Di 2.10.10.10. 1 hit.
    2.40.20.10. 1 hit.
    InterProi IPR014394. Coagulation_fac_XIIa/HGFA.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR000083. Fibronectin_type1.
    IPR000562. FN_type2_col-bd.
    IPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00008. EGF. 2 hits.
    PF00039. fn1. 1 hit.
    PF00040. fn2. 1 hit.
    PF00051. Kringle. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001146. Factor_XII_HGFA. 1 hit.
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00181. EGF. 2 hits.
    SM00058. FN1. 1 hit.
    SM00059. FN2. 1 hit.
    SM00130. KR. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 2 hits.
    PROSITEi PS00022. EGF_1. 2 hits.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 2 hits.
    PS01253. FN1_1. 1 hit.
    PS51091. FN1_2. 1 hit.
    PS00023. FN2_1. 1 hit.
    PS51092. FN2_2. 1 hit.
    PS00021. KRINGLE_1. 1 hit.
    PS50070. KRINGLE_2. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and sequence analysis of the cDNA for a human serine protease responsible for activation of hepatocyte growth factor. Structural similarity of the protease precursor to blood coagulation factor XII."
      Miyazawa K., Shimomura T., Kitamura A., Kondo J., Morimoto Y., Kitamura N.
      J. Biol. Chem. 268:10024-10028(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver and Serum.
    2. "Structural organization and chromosomal localization of the human hepatocyte growth factor activator gene -- phylogenetic and functional relationship with blood coagulation factor XII, urokinase, and tissue-type plasminogen activator."
      Miyazawa K., Wang Y., Minoshima S., Shimizu N., Kitamura N.
      Eur. J. Biochem. 258:355-361(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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], VARIANT LEU-231.
      Tissue: Liver.
    6. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 36-50.
    7. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-468.
      Tissue: Plasma.
    8. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-468.
      Tissue: Liver.
    9. "Conformational lability in serine protease active sites: structures of hepatocyte growth factor activator (HGFA) alone and with the inhibitory domain from HGFA inhibitor-1B."
      Shia S., Stamos J., Kirchhofer D., Fan B., Wu J., Corpuz R.T., Santell L., Lazarus R.A., Eigenbrot C.
      J. Mol. Biol. 346:1335-1349(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 373-655 ALONE AND IN COMPLEX WITH INHIBITOR HAI1B, ACTIVE SITE, DISULFIDE BONDS.
    10. "Structural insight into distinct mechanisms of protease inhibition by antibodies."
      Wu Y., Eigenbrot C., Liang W.C., Stawicki S., Shia S., Fan B., Ganesan R., Lipari M.T., Kirchhofer D.
      Proc. Natl. Acad. Sci. U.S.A. 104:19784-19789(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 373-655 IN COMPLEX WITH ANTIBODY, GLYCOSYLATION AT ASN-468, DISULFIDE BONDS.

    Entry informationi

    Entry nameiHGFA_HUMAN
    AccessioniPrimary (citable) accession number: Q04756
    Secondary accession number(s): Q14726, Q2M1W7, Q53X47
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 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

    Caution

    It is uncertain whether Met-1 is the initiator.Curated

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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