Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Furin

Gene

FURIN

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

Functioni

Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif.9 Publications
(Microbial infection) Probably cleaves and activates anthrax and diphtheria toxins. Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin.1 Publication

Catalytic activityi

Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors.9 Publications

Cofactori

Ca2+3 PublicationsNote: Binds 3 calcium ions per subunit.3 Publications

Enzyme regulationi

Inhibited by the not secondly cleaved propeptide (PubMed:9130696, PubMed:11799113). Inhibited by m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine (m-guanidinomethyl-Phac-RVR-Amb) and 4-guanidinomethyl-phenylacteyl-Arg-Tle-Arg-4-amidinobenzylamide (MI-1148) (PubMed:24666235, PubMed:25974265).4 Publications

pH dependencei

Optimum pH is 6.0.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi115Calcium 1Combined sources2 Publications1
Active sitei153Charge relay systemPROSITE-ProRule annotation1
Binding sitei154SubstrateCombined sources2 Publications1
Metal bindingi162Calcium 1Combined sources2 Publications1
Metal bindingi174Calcium 2Combined sources2 Publications1
Metal bindingi179Calcium 2Combined sources2 Publications1
Metal bindingi181Calcium 2; via carbonyl oxygenCombined sources2 Publications1
Active sitei194Charge relay systemPROSITE-ProRule annotation1
Metal bindingi205Calcium 1; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi208Calcium 1Combined sources2 Publications1
Metal bindingi210Calcium 1; via carbonyl oxygenCombined sources2 Publications1
Metal bindingi212Calcium 1; via carbonyl oxygenCombined sources2 Publications1
Binding sitei236SubstrateCombined sources2 Publications1
Metal bindingi258Calcium 3Combined sources2 Publications1
Binding sitei264SubstrateCombined sources2 Publications1
Metal bindingi301Calcium 3Combined sources2 Publications1
Binding sitei306SubstrateCombined sources2 Publications1
Binding sitei308SubstrateCombined sources2 Publications1
Metal bindingi331Calcium 3Combined sources2 Publications1
Active sitei368Charge relay systemPROSITE-ProRule annotation1
Binding sitei368SubstrateCombined sources2 Publications1

GO - Molecular functioni

  • endopeptidase activity Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • nerve growth factor binding Source: BHF-UCL
  • peptidase activity Source: UniProtKB
  • peptide binding Source: BHF-UCL
  • protease binding Source: BHF-UCL
  • serine-type endopeptidase activity Source: BHF-UCL
  • serine-type endopeptidase inhibitor activity Source: BHF-UCL

GO - Biological processi

  • cell proliferation Source: BHF-UCL
  • cellular protein metabolic process Source: Reactome
  • collagen catabolic process Source: Reactome
  • cornification Source: Reactome
  • dibasic protein processing Source: UniProtKB
  • extracellular matrix disassembly Source: Reactome
  • extracellular matrix organization Source: Reactome
  • lipoprotein metabolic process Source: Reactome
  • negative regulation of low-density lipoprotein particle receptor catabolic process Source: HGNC
  • negative regulation of transforming growth factor beta1 production Source: BHF-UCL
  • nerve growth factor processing Source: Reactome
  • nerve growth factor production Source: BHF-UCL
  • peptide biosynthetic process Source: BHF-UCL
  • peptide hormone processing Source: BHF-UCL
  • positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
  • protein processing Source: UniProtKB
  • regulation of endopeptidase activity Source: BHF-UCL
  • regulation of low-density lipoprotein particle receptor biosynthetic process Source: Ensembl
  • regulation of protein catabolic process Source: BHF-UCL
  • regulation of signal transduction Source: Ensembl
  • secretion by cell Source: BHF-UCL
  • signal peptide processing Source: HGNC
  • transforming growth factor beta receptor signaling pathway Source: Reactome
  • viral life cycle Source: BHF-UCL
  • viral protein processing Source: Reactome
  • zymogen activation Source: UniProtKB
  • zymogen inhibition Source: UniProtKB

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-1181150. Signaling by NODAL.
R-HSA-1442490. Collagen degradation.
R-HSA-1566948. Elastic fibre formation.
R-HSA-1592389. Activation of Matrix Metalloproteinases.
R-HSA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
R-HSA-167060. NGF processing.
R-HSA-171286. Synthesis and processing of ENV and VPU.
R-HSA-174800. Chylomicron-mediated lipid transport.
R-HSA-186797. Signaling by PDGF.
R-HSA-1912420. Pre-NOTCH Processing in Golgi.
R-HSA-2173789. TGF-beta receptor signaling activates SMADs.
R-HSA-5210891. Uptake and function of anthrax toxins.
R-HSA-6809371. Formation of the cornified envelope.
R-HSA-977225. Amyloid fiber formation.
SignaLinkiP09958.
SIGNORiP09958.

Protein family/group databases

MEROPSiS08.071.

Names & Taxonomyi

Protein namesi
Recommended name:
Furin (EC:3.4.21.758 Publications)
Alternative name(s):
Dibasic-processing enzyme
Paired basic amino acid residue-cleaving enzyme
Short name:
PACE
Gene namesi
Name:FURIN
Synonyms:FUR, PACE, PCSK3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:8568. FURIN.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini108 – 715LumenalCuratedAdd BLAST608
Transmembranei716 – 738HelicalSequence analysisAdd BLAST23
Topological domaini739 – 794CytoplasmicCuratedAdd BLAST56

GO - Cellular componenti

  • cell surface Source: BHF-UCL
  • endoplasmic reticulum Source: BHF-UCL
  • endosome membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • Golgi lumen Source: Reactome
  • Golgi membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • membrane raft Source: BHF-UCL
  • plasma membrane Source: Reactome
  • trans-Golgi network Source: BHF-UCL
  • trans-Golgi network transport vesicle Source: MGI

Keywords - Cellular componenti

Cell membrane, Endosome, Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi72V → R: Loss of catalytic activity and propeptide second cleavage and removal. Abnormal accumulation in the early secretory pathway. 1 Publication1
Mutagenesisi75R → A: Loss of catalytic activity and, propeptide second cleavage and removal. Normal trafficking to the Golgi. 1 Publication1
Mutagenesisi153D → N: Loss of catalytic activity and propeptide first cleavage. Abnormal accumulation in the early secretory pathway. 2 Publications1
Mutagenesisi773 – 775SDS → DDD: Phosphomimetic mutant. Localization in early endosome is increased. 1 Publication3
Mutagenesisi773S → A: Slight reduction in phosphorylation. Loss of phosphorylation and abnormal accumulation in the early secretory pathway; when associated with A-775. 1 Publication1
Mutagenesisi775S → A: Slight reduction in phosphorylation. Loss of phosphorylation and abnormal accumulation in the early secretory pathway; when associated with A-773. 1 Publication1

Organism-specific databases

DisGeNETi5045.
OpenTargetsiENSG00000140564.
PharmGKBiPA32894.

Chemistry databases

ChEMBLiCHEMBL2611.
DrugBankiDB03600. Decanoic Acid.
DB04951. Pirfenidone.
GuidetoPHARMACOLOGYi2366.

Polymorphism and mutation databases

BioMutaiFURIN.
DMDMi120611.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
PropeptideiPRO_000002702827 – 107Inhibition peptide1 PublicationAdd BLAST81
ChainiPRO_0000027029108 – 794FurinAdd BLAST687

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi211 ↔ 3602 Publications
Disulfide bondi303 ↔ 3332 Publications
Glycosylationi387N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi440N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi450 ↔ 4742 Publications
Glycosylationi553N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei773Phosphoserine; by CK21 Publication1
Modified residuei775Phosphoserine; by CK21 Publication1

Post-translational modificationi

The inhibition peptide, which plays the role of an intramolecular chaperone, is autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound to furin as a potent autoinhibitor. Following transport to the trans Golgi, a second cleavage within the inhibition propeptide results in propeptide dissociation and furin activation.2 Publications
Phosphorylation is required for TGN localization of the endoprotease. In vivo, exists as di-, mono- and non-phosphorylated forms.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei75 – 76Cleavage, second; by autolysis1 Publication2
Sitei107 – 108Cleavage, first; by autolysis2 Publications2

Keywords - PTMi

Autocatalytic cleavage, Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

EPDiP09958.
MaxQBiP09958.
PaxDbiP09958.
PeptideAtlasiP09958.
PRIDEiP09958.

2D gel databases

OGPiP09958.

PTM databases

iPTMnetiP09958.
PhosphoSitePlusiP09958.

Miscellaneous databases

PMAP-CutDBiP09958.

Expressioni

Tissue specificityi

Seems to be expressed ubiquitously.1 Publication

Gene expression databases

BgeeiENSG00000140564.
CleanExiHS_FURIN.
ExpressionAtlasiP09958. baseline and differential.
GenevisibleiP09958. HS.

Organism-specific databases

HPAiCAB009499.

Interactioni

Subunit structurei

Interacts with FLNA (By similarity). Binds to PACS1 which mediates TGN localization and connection to clathrin adapters (PubMed:11331585).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MSTNO147932EBI-1056807,EBI-8542977

GO - Molecular functioni

  • nerve growth factor binding Source: BHF-UCL
  • protease binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi111082. 15 interactors.
DIPiDIP-29904N.
IntActiP09958. 11 interactors.
MINTiMINT-1209355.
STRINGi9606.ENSP00000268171.

Chemistry databases

BindingDBiP09958.

Structurei

Secondary structure

1794
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi118 – 120Combined sources3
Turni122 – 124Combined sources3
Beta strandi127 – 129Combined sources3
Helixi134 – 139Combined sources6
Beta strandi148 – 154Combined sources7
Turni161 – 166Combined sources6
Helixi169 – 171Combined sources3
Turni175 – 178Combined sources4
Helixi191 – 193Combined sources3
Helixi194 – 203Combined sources10
Beta strandi206 – 211Combined sources6
Turni215 – 218Combined sources4
Beta strandi219 – 225Combined sources7
Beta strandi227 – 229Combined sources3
Helixi233 – 240Combined sources8
Turni244 – 246Combined sources3
Beta strandi249 – 252Combined sources4
Beta strandi259 – 261Combined sources3
Helixi268 – 280Combined sources13
Helixi282 – 284Combined sources3
Beta strandi288 – 292Combined sources5
Helixi297 – 299Combined sources3
Helixi303 – 305Combined sources3
Turni307 – 310Combined sources4
Beta strandi314 – 320Combined sources7
Beta strandi338 – 341Combined sources4
Beta strandi351 – 355Combined sources5
Turni356 – 358Combined sources3
Beta strandi359 – 364Combined sources6
Helixi367 – 384Combined sources18
Helixi390 – 400Combined sources11
Beta strandi419 – 421Combined sources3
Turni422 – 424Combined sources3
Helixi431 – 438Combined sources8
Beta strandi448 – 453Combined sources6
Beta strandi464 – 471Combined sources8
Beta strandi482 – 496Combined sources15
Helixi498 – 500Combined sources3
Beta strandi501 – 506Combined sources6
Beta strandi512 – 516Combined sources5
Beta strandi528 – 535Combined sources8
Turni537 – 540Combined sources4
Beta strandi545 – 553Combined sources9
Beta strandi555 – 557Combined sources3
Beta strandi561 – 574Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4OMCX-ray2.30A/B/C/D/E/F108-574[»]
4OMDX-ray2.70A/B/C/D/E/F108-574[»]
4RYDX-ray2.15A/B/C/D/E/F108-574[»]
4Z2AX-ray1.89A110-574[»]
5JMOX-ray2.00A/B108-574[»]
5JXGX-ray1.80A108-574[»]
5JXHX-ray2.00A108-574[»]
5JXIX-ray2.00A108-574[»]
5JXJX-ray2.00A108-574[»]
ProteinModelPortaliP09958.
SMRiP09958.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini144 – 427Peptidase S8Sequence analysisAdd BLAST284
Domaini444 – 576P/Homo BPROSITE-ProRule annotationAdd BLAST133
Repeati577 – 620FU 1Sequence analysisAdd BLAST44
Repeati638 – 681FU 2Sequence analysisAdd BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni191 – 192Substrate bindingCombined sources2 Publications2
Regioni253 – 258Substrate bindingCombined sources2 Publications6
Regioni292 – 295Substrate bindingCombined sources2 Publications4
Regioni759 – 762Cell surface signal1 Publication4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi498 – 500Cell attachment siteSequence analysis3
Motifi773 – 779Trans Golgi network signal1 Publication7

Domaini

Contains a cytoplasmic domain responsible for its TGN localization and recycling from the cell surface.1 Publication

Sequence similaritiesi

Belongs to the peptidase S8 family. Furin subfamily.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3525. Eukaryota.
COG1404. LUCA.
COG4935. LUCA.
GeneTreeiENSGT00750000117358.
HOGENOMiHOG000192536.
HOVERGENiHBG008705.
InParanoidiP09958.
KOiK01349.
OMAiIIRASVC.
OrthoDBiEOG091G05HI.
PhylomeDBiP09958.
TreeFamiTF314277.

Family and domain databases

CDDicd04059. Peptidases_S8_Protein_converta. 1 hit.
Gene3Di2.60.120.260. 1 hit.
3.40.50.200. 1 hit.
InterProiView protein in InterPro
IPR006212. Furin_repeat.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_.
IPR034182. Kexin/furin.
IPR009020. Peptidase/Inhibitor_I9.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR002884. PrprotnconvertsP.
IPR032815. S8_pro-domain.
PfamiView protein in Pfam
PF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
PF16470. S8_pro-domain. 1 hit.
PRINTSiPR00723. SUBTILISIN.
SMARTiView protein in SMART
SM00261. FU. 2 hits.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiView protein in PROSITE
PS51829. P_HOMO_B. 1 hit.
PS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P09958-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELRPWLLWV VAATGTLVLL AADAQGQKVF TNTWAVRIPG GPAVANSVAR
60 70 80 90 100
KHGFLNLGQI FGDYYHFWHR GVTKRSLSPH RPRHSRLQRE PQVQWLEQQV
110 120 130 140 150
AKRRTKRDVY QEPTDPKFPQ QWYLSGVTQR DLNVKAAWAQ GYTGHGIVVS
160 170 180 190 200
ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG
210 220 230 240 250
EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY
260 270 280 290 300
SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH
310 320 330 340 350
DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ
360 370 380 390 400
IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT
410 420 430 440 450
SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC
460 470 480 490 500
IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD
510 520 530 540 550
LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE
560 570 580 590 600
IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE
610 620 630 640 650
EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHASCAT
660 670 680 690 700
CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA
710 720 730 740 750
GQRLRAGLLP SHLPEVVAGL SCAFIVLVFV TVFLVLQLRS GFSFRGVKVY
760 770 780 790
TMDRGLISYK GLPPEAWQEE CPSDSEEDEG RGERTAFIKD QSAL
Length:794
Mass (Da):86,678
Last modified:April 1, 1990 - v2
Checksum:i10C44DD5892EF85D
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05182143A → V. Corresponds to variant dbSNP:rs16944971Ensembl.1
Natural variantiVAR_055343547W → R in cell line LoVo; does not undergo autocatalytic activation and is not transported to the Golgi apparatus. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17094 mRNA. Translation: CAA34948.1.
BC012181 mRNA. Translation: AAH12181.1.
X15723 Genomic DNA. Translation: CAA33745.1.
X04329 Genomic DNA. Translation: CAA27860.1.
CCDSiCCDS10364.1.
PIRiA39552. KXHUF.
RefSeqiNP_001276752.1. NM_001289823.1.
NP_001276753.1. NM_001289824.1.
NP_002560.1. NM_002569.3.
UniGeneiHs.513153.

Genome annotation databases

EnsembliENST00000268171; ENSP00000268171; ENSG00000140564.
ENST00000610579; ENSP00000484952; ENSG00000140564.
ENST00000618099; ENSP00000483552; ENSG00000140564.
GeneIDi5045.
KEGGihsa:5045.
UCSCiuc002bpu.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17094 mRNA. Translation: CAA34948.1.
BC012181 mRNA. Translation: AAH12181.1.
X15723 Genomic DNA. Translation: CAA33745.1.
X04329 Genomic DNA. Translation: CAA27860.1.
CCDSiCCDS10364.1.
PIRiA39552. KXHUF.
RefSeqiNP_001276752.1. NM_001289823.1.
NP_001276753.1. NM_001289824.1.
NP_002560.1. NM_002569.3.
UniGeneiHs.513153.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4OMCX-ray2.30A/B/C/D/E/F108-574[»]
4OMDX-ray2.70A/B/C/D/E/F108-574[»]
4RYDX-ray2.15A/B/C/D/E/F108-574[»]
4Z2AX-ray1.89A110-574[»]
5JMOX-ray2.00A/B108-574[»]
5JXGX-ray1.80A108-574[»]
5JXHX-ray2.00A108-574[»]
5JXIX-ray2.00A108-574[»]
5JXJX-ray2.00A108-574[»]
ProteinModelPortaliP09958.
SMRiP09958.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111082. 15 interactors.
DIPiDIP-29904N.
IntActiP09958. 11 interactors.
MINTiMINT-1209355.
STRINGi9606.ENSP00000268171.

Chemistry databases

BindingDBiP09958.
ChEMBLiCHEMBL2611.
DrugBankiDB03600. Decanoic Acid.
DB04951. Pirfenidone.
GuidetoPHARMACOLOGYi2366.

Protein family/group databases

MEROPSiS08.071.

PTM databases

iPTMnetiP09958.
PhosphoSitePlusiP09958.

Polymorphism and mutation databases

BioMutaiFURIN.
DMDMi120611.

2D gel databases

OGPiP09958.

Proteomic databases

EPDiP09958.
MaxQBiP09958.
PaxDbiP09958.
PeptideAtlasiP09958.
PRIDEiP09958.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000268171; ENSP00000268171; ENSG00000140564.
ENST00000610579; ENSP00000484952; ENSG00000140564.
ENST00000618099; ENSP00000483552; ENSG00000140564.
GeneIDi5045.
KEGGihsa:5045.
UCSCiuc002bpu.2. human.

Organism-specific databases

CTDi5045.
DisGeNETi5045.
GeneCardsiFURIN.
HGNCiHGNC:8568. FURIN.
HPAiCAB009499.
MIMi136950. gene.
neXtProtiNX_P09958.
OpenTargetsiENSG00000140564.
PharmGKBiPA32894.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3525. Eukaryota.
COG1404. LUCA.
COG4935. LUCA.
GeneTreeiENSGT00750000117358.
HOGENOMiHOG000192536.
HOVERGENiHBG008705.
InParanoidiP09958.
KOiK01349.
OMAiIIRASVC.
OrthoDBiEOG091G05HI.
PhylomeDBiP09958.
TreeFamiTF314277.

Enzyme and pathway databases

ReactomeiR-HSA-1181150. Signaling by NODAL.
R-HSA-1442490. Collagen degradation.
R-HSA-1566948. Elastic fibre formation.
R-HSA-1592389. Activation of Matrix Metalloproteinases.
R-HSA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
R-HSA-167060. NGF processing.
R-HSA-171286. Synthesis and processing of ENV and VPU.
R-HSA-174800. Chylomicron-mediated lipid transport.
R-HSA-186797. Signaling by PDGF.
R-HSA-1912420. Pre-NOTCH Processing in Golgi.
R-HSA-2173789. TGF-beta receptor signaling activates SMADs.
R-HSA-5210891. Uptake and function of anthrax toxins.
R-HSA-6809371. Formation of the cornified envelope.
R-HSA-977225. Amyloid fiber formation.
SignaLinkiP09958.
SIGNORiP09958.

Miscellaneous databases

ChiTaRSiFURIN. human.
GeneWikiiFurin.
GenomeRNAii5045.
PMAP-CutDBiP09958.
PROiPR:P09958.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000140564.
CleanExiHS_FURIN.
ExpressionAtlasiP09958. baseline and differential.
GenevisibleiP09958. HS.

Family and domain databases

CDDicd04059. Peptidases_S8_Protein_converta. 1 hit.
Gene3Di2.60.120.260. 1 hit.
3.40.50.200. 1 hit.
InterProiView protein in InterPro
IPR006212. Furin_repeat.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_.
IPR034182. Kexin/furin.
IPR009020. Peptidase/Inhibitor_I9.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR002884. PrprotnconvertsP.
IPR032815. S8_pro-domain.
PfamiView protein in Pfam
PF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
PF16470. S8_pro-domain. 1 hit.
PRINTSiPR00723. SUBTILISIN.
SMARTiView protein in SMART
SM00261. FU. 2 hits.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiView protein in PROSITE
PS51829. P_HOMO_B. 1 hit.
PS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFURIN_HUMAN
AccessioniPrimary (citable) accession number: P09958
Secondary accession number(s): Q14336, Q6LBS3, Q9UCZ5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 1, 1990
Last modified: May 10, 2017
This is version 208 of the entry and version 2 of the sequence. See 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, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.