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Q04756

- HGFA_HUMAN

UniProt

Q04756 - HGFA_HUMAN

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Protein

Hepatocyte growth factor activator

Gene

HGFAC

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ04756.
CleanExiHS_HGFAC.
ExpressionAtlasiQ04756. baseline and differential.
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.
GeneTreeiENSGT00760000119133.
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

        10         20         30         40         50
MGRWAWVPSP WPPPGLGPFL LLLLLLLLLP RGFQPQPGGN RTESPEPNAT
60 70 80 90 100
ATPAIPTILV TSVTSETPAT SAPEAEGPQS GGLPPPPRAV PSSSSPQAQA
110 120 130 140 150
LTEDGRPCRF PFRYGGRMLH ACTSEGSAHR KWCATTHNYD RDRAWGYCVE
160 170 180 190 200
ATPPPGGPAA LDPCASGPCL NGGSCSNTQD PQSYHCSCPR AFTGKDCGTE
210 220 230 240 250
KCFDETRYEY LEGGDRWARV RQGHVEQCEC FGGRTWCEGT RHTACLSSPC
260 270 280 290 300
LNGGTCHLIV ATGTTVCACP PGFAGRLCNI EPDERCFLGN GTGYRGVAST
310 320 330 340 350
SASGLSCLAW NSDLLYQELH VDSVGAAALL GLGPHAYCRN PDNDERPWCY
360 370 380 390 400
VVKDSALSWE YCRLEACESL TRVQLSPDLL ATLPEPASPG RQACGRRHKK
410 420 430 440 450
RTFLRPRIIG GSSSLPGSHP WLAAIYIGDS FCAGSLVHTC WVVSAAHCFS
460 470 480 490 500
HSPPRDSVSV VLGQHFFNRT TDVTQTFGIE KYIPYTLYSV FNPSDHDLVL
510 520 530 540 550
IRLKKKGDRC ATRSQFVQPI CLPEPGSTFP AGHKCQIAGW GHLDENVSGY
560 570 580 590 600
SSSLREALVP LVADHKCSSP EVYGADISPN MLCAGYFDCK SDACQGDSGG
610 620 630 640 650
PLACEKNGVA YLYGIISWGD GCGRLHKPGV YTRVANYVDW INDRIRPPRR

LVAPS
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_001284368.1. NM_001297439.1.
NP_001519.1. NM_001528.3.
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_001284368.1. NM_001297439.1.
NP_001519.1. NM_001528.3.
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.
GeneTreei ENSGT00760000119133.
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

Bgeei Q04756.
CleanExi HS_HGFAC.
ExpressionAtlasi Q04756. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 145 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