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P26927

- HGFL_HUMAN

UniProt

P26927 - HGFL_HUMAN

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Protein

Hepatocyte growth factor-like protein

Gene

MST1

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

Functioni

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. embryo implantation Source: Ensembl
  2. spermatogenesis Source: Ensembl
  3. sperm motility Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Serine protease homolog

Enzyme and pathway databases

SignaLinkiP26927.

Protein family/group databases

MEROPSiS01.975.

Names & Taxonomyi

Protein namesi
Recommended name:
Hepatocyte growth factor-like protein
Alternative name(s):
Macrophage stimulatory protein
Macrophage-stimulating protein
Short name:
MSP
Cleaved into the following 2 chains:
Gene namesi
Name:MST1
Synonyms:D3F15S2, DNF15S2, HGFL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:7380. MST1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

MST1 variant Cys-686 may be associated with inflammatory bowel disease (IBD), a chronic, relapsing inflammation of the gastrointestinal tract with a complex etiology. It is unsure whether Cys-689 itself or a variation in linkage disequilibrium with Cys-689 is responsible for the association with IBD.2 Publications

Organism-specific databases

Orphaneti171. Primary sclerosing cholangitis.
PharmGKBiPA31185.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 711693Hepatocyte growth factor-like proteinPRO_0000028085Add
BLAST
Chaini19 – 483465Hepatocyte growth factor-like protein alpha chainCuratedPRO_0000028086Add
BLAST
Chaini484 – 711228Hepatocyte growth factor-like protein beta chainCuratedPRO_0000028087Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 78By similarity
Disulfide bondi60 ↔ 66By similarity
Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi110 ↔ 186By similarity
Disulfide bondi131 ↔ 169By similarity
Disulfide bondi157 ↔ 181By similarity
Disulfide bondi191 ↔ 268By similarity
Disulfide bondi194 ↔ 324By similarity
Disulfide bondi212 ↔ 251By similarity
Disulfide bondi240 ↔ 263By similarity
Disulfide bondi283 ↔ 361By similarity
Glycosylationi296 – 2961N-linked (GlcNAc...)1 Publication
Disulfide bondi304 ↔ 343By similarity
Disulfide bondi332 ↔ 355By similarity
Disulfide bondi370 ↔ 448By similarity
Disulfide bondi391 ↔ 431By similarity
Disulfide bondi419 ↔ 443By similarity
Disulfide bondi468 ↔ 588Interchain (between alpha and beta chains)
Disulfide bondi507 ↔ 523By similarity
Disulfide bondi602 ↔ 667By similarity
Glycosylationi615 – 6151N-linked (GlcNAc...)1 Publication
Disulfide bondi632 ↔ 646By similarity
Disulfide bondi657 ↔ 685By similarity

Post-translational modificationi

Cleaved after Arg-483, probably by HPN/Hepsin, to yield the active form consisting of two disulfide-linked chains.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP26927.
PaxDbiP26927.
PRIDEiP26927.

PTM databases

PhosphoSiteiP26927.

Miscellaneous databases

PMAP-CutDBP26927.

Expressioni

Gene expression databases

BgeeiP26927.
CleanExiHS_MST1.
ExpressionAtlasiP26927. baseline.
GenevestigatoriP26927.

Organism-specific databases

HPAiHPA024036.

Interactioni

Subunit structurei

Dimer of an alpha chain and a beta chain linked by a disulfide bond. Interacts (via beta chain) with MST1R (via SEMA domain).3 Publications

Protein-protein interaction databases

BioGridi110591. 4 interactions.
DIPiDIP-6028N.
IntActiP26927. 3 interactions.
MINTiMINT-4787531.
STRINGi9606.ENSP00000308226.

Structurei

Secondary structure

1
711
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi495 – 4995
Beta strandi505 – 5139
Beta strandi516 – 5205
Helixi521 – 5233
Beta strandi535 – 5395
Beta strandi541 – 5444
Beta strandi553 – 56210
Beta strandi569 – 5768
Beta strandi581 – 5844
Beta strandi601 – 6088
Beta strandi620 – 6278
Helixi629 – 6357
Turni636 – 6383
Beta strandi644 – 6474
Beta strandi664 – 6696
Beta strandi672 – 6798
Beta strandi683 – 6864
Beta strandi692 – 6965
Helixi697 – 6993
Helixi701 – 7077

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ASUX-ray1.85A465-483[»]
B484-711[»]
4QT8X-ray3.00C/D465-711[»]
ProteinModelPortaliP26927.
SMRiP26927. Positions 22-709.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26927.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 10585PANPROSITE-ProRule annotationAdd
BLAST
Domaini110 – 18677Kringle 1PROSITE-ProRule annotationAdd
BLAST
Domaini191 – 26878Kringle 2PROSITE-ProRule annotationAdd
BLAST
Domaini283 – 36179Kringle 3PROSITE-ProRule annotationAdd
BLAST
Domaini370 – 44879Kringle 4PROSITE-ProRule annotationAdd
BLAST
Domaini484 – 709226Peptidase 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.
HOGENOMiHOG000112892.
HOVERGENiHBG004381.
InParanoidiP26927.
PhylomeDBiP26927.

Family and domain databases

Gene3Di2.40.20.10. 4 hits.
InterProiIPR024174. 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]
PIRSFiPIRSF001152. 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]

Sequencei

Sequence statusi: Complete.

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

P26927-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGWLPLLLLL TQCLGVPGQR SPLNDFQVLR GTELQHLLHA VVPGPWQEDV
60 70 80 90 100
ADAEECAGRC GPLMDCRAFH YNVSSHGCQL LPWTQHSPHT RLRRSGRCDL
110 120 130 140 150
FQKKDYVRTC IMNNGVGYRG TMATTVGGLP CQAWSHKFPN DHKYTPTLRN
160 170 180 190 200
GLEENFCRNP DGDPGGPWCY TTDPAVRFQS CGIKSCREAA CVWCNGEEYR
210 220 230 240 250
GAVDRTESGR ECQRWDLQHP HQHPFEPGKF LDQGLDDNYC RNPDGSERPW
260 270 280 290 300
CYTTDPQIER EFCDLPRCGS EAQPRQEATT VSCFRGKGEG YRGTANTTTA
310 320 330 340 350
GVPCQRWDAQ IPHQHRFTPE KYACKDLREN FCRNPDGSEA PWCFTLRPGM
360 370 380 390 400
RAAFCYQIRR CTDDVRPQDC YHGAGEQYRG TVSKTRKGVQ CQRWSAETPH
410 420 430 440 450
KPQFTFTSEP HAQLEENFCR NPDGDSHGPW CYTMDPRTPF DYCALRRCAD
460 470 480 490 500
DQPPSILDPP DQVQFEKCGK RVDRLDQRRS KLRVVGGHPG NSPWTVSLRN
510 520 530 540 550
RQGQHFCGGS LVKEQWILTA RQCFSSCHMP LTGYEVWLGT LFQNPQHGEP
560 570 580 590 600
SLQRVPVAKM VCGPSGSQLV LLKLERSVTL NQRVALICLP PEWYVVPPGT
610 620 630 640 650
KCEIAGWGET KGTGNDTVLN VALLNVISNQ ECNIKHRGRV RESEMCTEGL
660 670 680 690 700
LAPVGACEGD YGGPLACFTH NCWVLEGIII PNRVCARSRW PAVFTRVSVF
710
VDWIHKVMRL G
Length:711
Mass (Da):80,320
Last modified:May 15, 2007 - v2
Checksum:i2E4B3C7D4AA9B566
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti292 – 2921R → G AA sequence (PubMed:1827141)Curated
Sequence conflicti304 – 3041C → E AA sequence (PubMed:1827141)Curated
Sequence conflicti306 – 3061R → E AA sequence (PubMed:1827141)Curated
Sequence conflicti550 – 5501Missing AA sequence (PubMed:1827141)Curated
Sequence conflicti593 – 5931W → E AA sequence (PubMed:1827141)Curated
Sequence conflicti623 – 6231L → F in AAA59872. (PubMed:8393443)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131C → Y.1 Publication
VAR_006631
Natural varianti212 – 2121C → F.
VAR_006632
Natural varianti551 – 5511S → G.
Corresponds to variant rs6791037 [ dbSNP | Ensembl ].
VAR_059787
Natural varianti676 – 6761E → K.
Corresponds to variant rs7798 [ dbSNP | Ensembl ].
VAR_014569
Natural varianti689 – 6891R → C Common polymorphism; may be associated with inflammatory bowel disease; results in reduced binding affinity to MST1R. 2 Publications
Corresponds to variant rs3197999 [ dbSNP | Ensembl ].
VAR_070224

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M74178 mRNA. Translation: AAA50165.1.
U37055 Genomic DNA. Translation: AAC50471.1.
L11924 mRNA. Translation: AAA59872.1.
AC099668 Genomic DNA. No translation available.
BC048330 mRNA. Translation: AAH48330.1.
PIRiA40331. A47136.
RefSeqiNP_066278.3. NM_020998.3.
UniGeneiHs.349110.
Hs.512587.

Genome annotation databases

EnsembliENST00000383728; ENSP00000373234; ENSG00000173531.
GeneIDi4485.
KEGGihsa:4485.

Polymorphism databases

DMDMi147744563.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M74178 mRNA. Translation: AAA50165.1 .
U37055 Genomic DNA. Translation: AAC50471.1 .
L11924 mRNA. Translation: AAA59872.1 .
AC099668 Genomic DNA. No translation available.
BC048330 mRNA. Translation: AAH48330.1 .
PIRi A40331. A47136.
RefSeqi NP_066278.3. NM_020998.3.
UniGenei Hs.349110.
Hs.512587.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ASU X-ray 1.85 A 465-483 [» ]
B 484-711 [» ]
4QT8 X-ray 3.00 C/D 465-711 [» ]
ProteinModelPortali P26927.
SMRi P26927. Positions 22-709.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110591. 4 interactions.
DIPi DIP-6028N.
IntActi P26927. 3 interactions.
MINTi MINT-4787531.
STRINGi 9606.ENSP00000308226.

Chemistry

ChEMBLi CHEMBL6042.

Protein family/group databases

MEROPSi S01.975.

PTM databases

PhosphoSitei P26927.

Polymorphism databases

DMDMi 147744563.

Proteomic databases

MaxQBi P26927.
PaxDbi P26927.
PRIDEi P26927.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000383728 ; ENSP00000373234 ; ENSG00000173531 .
GeneIDi 4485.
KEGGi hsa:4485.

Organism-specific databases

CTDi 4485.
GeneCardsi GC03M049730.
H-InvDB HIX0024339.
HGNCi HGNC:7380. MST1.
HPAi HPA024036.
MIMi 142408. gene.
neXtProti NX_P26927.
Orphaneti 171. Primary sclerosing cholangitis.
PharmGKBi PA31185.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000112892.
HOVERGENi HBG004381.
InParanoidi P26927.
PhylomeDBi P26927.

Enzyme and pathway databases

SignaLinki P26927.

Miscellaneous databases

EvolutionaryTracei P26927.
GeneWikii MST1.
GenomeRNAii 4485.
NextBioi 17351.
PMAP-CutDB P26927.
PROi P26927.
SOURCEi Search...

Gene expression databases

Bgeei P26927.
CleanExi HS_MST1.
ExpressionAtlasi P26927. baseline.
Genevestigatori P26927.

Family and domain databases

Gene3Di 2.40.20.10. 4 hits.
InterProi 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 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. "Characterization of the DNF15S2 locus on human chromosome 3: identification of a gene coding for four kringle domains with homology to hepatocyte growth factor."
    Han S., Stuart L.A., Friezner Degen S.J.
    Biochemistry 30:9768-9780(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TYR-13.
    Tissue: Liver.
  2. "Cloning, sequencing, and expression of human macrophage stimulating protein (MSP, MST1) confirms MSP as a member of the family of kringle proteins and locates the MSP gene on chromosome 3."
    Yoshimura T., Yuhki N., Wang M.H., Skeel A., Leonard E.J.
    J. Biol. Chem. 268:15461-15468(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
  5. "Macrophage stimulating protein: purification, partial amino acid sequence, and cellular activity."
    Skeel A., Yoshimura T., Showalter S.D., Tanaka S., Appella E., Leonard E.J.
    J. Exp. Med. 173:1227-1234(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 230-247; 288-310; 326-341; 484-501; 530-552; 574-596 AND 602-611, SUBUNIT.
    Tissue: Plasma.
  6. "Macrophage stimulating protein (MSP) binds to its receptor via the MSP beta chain."
    Wang M.H., Julian F.M., Breathnach R., Godowski P.J., Takehara T., Yoshikawa W., Hagiya M., Leonard E.J.
    J. Biol. Chem. 272:16999-17004(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MST1R.
  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-296.
    Tissue: Plasma.
  8. Cited for: POSSIBLE INVOLVEMENT IN INFLAMMATORY BOWEL DISEASE, VARIANT CYS-689.
  9. "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-615.
    Tissue: Liver.
  10. "Genome-wide association identifies multiple ulcerative colitis susceptibility loci."
    McGovern D.P., Gardet A., Torkvist L., Goyette P., Essers J., Taylor K.D., Neale B.M., Ong R.T., Lagace C., Li C., Green T., Stevens C.R., Beauchamp C., Fleshner P.R., Carlson M., D'Amato M., Halfvarson J., Hibberd M.L.
    , Lordal M., Padyukov L., Andriulli A., Colombo E., Latiano A., Palmieri O., Bernard E.J., Deslandres C., Hommes D.W., de Jong D.J., Stokkers P.C., Weersma R.K., Sharma Y., Silverberg M.S., Cho J.H., Wu J., Roeder K., Brant S.R., Schumm L.P., Duerr R.H., Dubinsky M.C., Glazer N.L., Haritunians T., Ippoliti A., Melmed G.Y., Siscovick D.S., Vasiliauskas E.A., Targan S.R., Annese V., Wijmenga C., Pettersson S., Rotter J.I., Xavier R.J., Daly M.J., Rioux J.D., Seielstad M.
    Nat. Genet. 42:332-337(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN INFLAMMATORY BOWEL DISEASE, VARIANT CYS-689.
  11. Cited for: PROTEOLYTIC CLEAVAGE.
  12. "Protein characterization of a candidate mechanism SNP for Crohn's disease: the macrophage stimulating protein R689C substitution."
    Gorlatova N., Chao K., Pal L.R., Araj R.H., Galkin A., Turko I., Moult J., Herzberg O.
    PLoS ONE 6:E27269-E27269(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MST1R, CHARACTERIZATION OF VARIANT CYS-689.
  13. "Crystal structure of the beta-chain of human hepatocyte growth factor-like/macrophage stimulating protein."
    Carafoli F., Chirgadze D.Y., Blundell T.L., Gherardi E.
    FEBS J. 272:5799-5807(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 465-711, INTERCHAIN DISULFIDE BOND.

Entry informationi

Entry nameiHGFL_HUMAN
AccessioniPrimary (citable) accession number: P26927
Secondary accession number(s): A6NLA3
, A8MSX3, Q13350, Q14870, Q6GTN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: May 15, 2007
Last modified: October 29, 2014
This is version 152 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

Caution

Although related to peptidase S1 family, the active site residues characteristic of serine proteases appear to be absent from this protein, which may therefore lack protease activity.Curated

Keywords - Technical termi

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

Documents

  1. Human chromosome 3
    Human chromosome 3: 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