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P09958

- FURIN_HUMAN

UniProt

P09958 - FURIN_HUMAN

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Protein

Furin

Gene
FURIN, FUR, PACE, PCSK3
Organism
Homo sapiens (Human)
Status
Reviewed - 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.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 vWF from their respective precursors.

Cofactori

Calcium.

Enzyme regulationi

Could be inhibited by the not secondly cleaved propeptide.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei75 – 762Cleavage, second; by autolysis
Sitei107 – 1082Cleavage, first; by autolysis
Metal bindingi115 – 1151Calcium 1 By similarity
Active sitei153 – 1531Charge relay system By similarity
Metal bindingi162 – 1621Calcium 1 By similarity
Active sitei194 – 1941Charge relay system By similarity
Metal bindingi208 – 2081Calcium 1 By similarity
Metal bindingi258 – 2581Calcium 2 By similarity
Metal bindingi301 – 3011Calcium 2 By similarity
Metal bindingi331 – 3311Calcium 2 By similarity
Active sitei368 – 3681Charge relay system By similarity

GO - Molecular functioni

  1. endopeptidase activity Source: BHF-UCL
  2. metal ion binding Source: UniProtKB-KW
  3. nerve growth factor binding Source: BHF-UCL
  4. peptidase activity Source: UniProtKB
  5. peptide binding Source: BHF-UCL
  6. protease binding Source: BHF-UCL
  7. serine-type endopeptidase activity Source: BHF-UCL
  8. serine-type endopeptidase inhibitor activity Source: BHF-UCL

GO - Biological processi

  1. cell proliferation Source: BHF-UCL
  2. cellular protein metabolic process Source: Reactome
  3. collagen catabolic process Source: Reactome
  4. extracellular matrix disassembly Source: Reactome
  5. extracellular matrix organization Source: Reactome
  6. negative regulation of endopeptidase activity Source: GOC
  7. negative regulation of low-density lipoprotein particle receptor catabolic process Source: HGNC
  8. negative regulation of transforming growth factor beta1 production Source: BHF-UCL
  9. nerve growth factor processing Source: Reactome
  10. nerve growth factor production Source: BHF-UCL
  11. neurotrophin TRK receptor signaling pathway Source: Reactome
  12. Notch signaling pathway Source: Reactome
  13. peptide biosynthetic process Source: BHF-UCL
  14. peptide hormone processing Source: BHF-UCL
  15. peptidyl-glutamic acid carboxylation Source: Reactome
  16. positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
  17. post-translational protein modification Source: Reactome
  18. protein processing Source: UniProtKB
  19. proteolysis Source: Reactome
  20. regulation of endopeptidase activity Source: BHF-UCL
  21. regulation of protein catabolic process Source: BHF-UCL
  22. regulation of signal transduction Source: Ensembl
  23. secretion by cell Source: BHF-UCL
  24. signal peptide processing Source: HGNC
  25. transforming growth factor beta receptor signaling pathway Source: Reactome
  26. viral life cycle Source: BHF-UCL
  27. viral process Source: Reactome
  28. viral protein processing Source: Reactome
  29. virion assembly Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_11062. NGF processing.
REACT_111057. Signaling by NODAL.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_118798. Pre-NOTCH Processing in Golgi.
REACT_120850. TGF-beta receptor signaling activates SMADs.
REACT_150366. Elastic fibre formation.
REACT_150401. Collagen degradation.
REACT_163660. Synthesis and processing of ENV and VPU.
REACT_16888. Signaling by PDGF.
REACT_733. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
SignaLinkiP09958.

Protein family/group databases

MEROPSiS08.071.

Names & Taxonomyi

Protein namesi
Recommended name:
Furin (EC:3.4.21.75)
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
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:8568. FURIN.

Subcellular locationi

Golgi apparatustrans-Golgi network membrane; Single-pass type I membrane protein. Cell membrane; Single-pass type I membrane protein
Note: Shuttles between the trans-Golgi network and the cell surface. Propeptide cleavage is a prerequisite for exit of furin molecules out of the endoplasmic reticulum (ER). A second cleavage within the propeptide occurs in the trans Golgi network (TGN), followed by the release of the propeptide and the activation of furin.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei716 – 73823Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. cell surface Source: BHF-UCL
  2. extracellular vesicular exosome Source: UniProt
  3. Golgi lumen Source: Reactome
  4. Golgi membrane Source: Reactome
  5. integral component of membrane Source: UniProtKB-KW
  6. membrane raft Source: BHF-UCL
  7. plasma membrane Source: Reactome
  8. trans-Golgi network Source: BHF-UCL
  9. trans-Golgi network transport vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32894.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424 Reviewed predictionAdd
BLAST
Propeptidei25 – 10783Inhibition peptidePRO_0000027028Add
BLAST
Chaini108 – 794687FurinPRO_0000027029Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi211 ↔ 360 By similarity
Disulfide bondi303 ↔ 333 By similarity
Glycosylationi387 – 3871N-linked (GlcNAc...) Reviewed prediction
Glycosylationi440 – 4401N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi450 ↔ 474 By similarity
Glycosylationi553 – 5531N-linked (GlcNAc...) Reviewed prediction
Modified residuei773 – 7731Phosphoserine; by CK21 Publication
Modified residuei775 – 7751Phosphoserine; by CK21 Publication

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.
Phosphorylation is required for TGN localization of the endoprotease. In vivo, exists as di-, mono- and non-phosphorylated forms.1 Publication

Keywords - PTMi

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

Proteomic databases

MaxQBiP09958.
PaxDbiP09958.
PeptideAtlasiP09958.
PRIDEiP09958.

2D gel databases

OGPiP09958.

PTM databases

PhosphoSiteiP09958.

Miscellaneous databases

PMAP-CutDBP09958.

Expressioni

Tissue specificityi

Seems to be expressed ubiquitously.

Gene expression databases

ArrayExpressiP09958.
BgeeiP09958.
CleanExiHS_FURIN.
GenevestigatoriP09958.

Organism-specific databases

HPAiCAB009499.

Interactioni

Subunit structurei

Interacts with FLNA By similarity. Binds to PACS1 which mediates TGN localization and connection to clathrin adapters.1 Publication

Protein-protein interaction databases

BioGridi111082. 8 interactions.
DIPiDIP-29904N.
IntActiP09958. 7 interactions.
MINTiMINT-1209355.
STRINGi9606.ENSP00000268171.

Structurei

Secondary structure

1
794
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi118 – 1203
Turni122 – 1243
Helixi134 – 1396
Beta strandi148 – 1547
Turni161 – 1666
Helixi169 – 1713
Turni175 – 1784
Helixi191 – 1933
Helixi194 – 20310
Beta strandi206 – 2116
Turni215 – 2184
Beta strandi219 – 2257
Beta strandi227 – 2293
Helixi233 – 2408
Turni244 – 2463
Beta strandi249 – 2524
Beta strandi259 – 2613
Helixi268 – 28013
Helixi282 – 2843
Beta strandi288 – 2925
Helixi297 – 2993
Helixi303 – 3053
Turni307 – 3093
Beta strandi314 – 3207
Beta strandi338 – 3414
Beta strandi351 – 3555
Turni356 – 3583
Beta strandi359 – 3646
Helixi367 – 38418
Helixi390 – 40011
Beta strandi419 – 4213
Turni422 – 4243
Helixi431 – 44010
Beta strandi448 – 4536
Beta strandi464 – 4718
Beta strandi482 – 49615
Helixi498 – 5003
Beta strandi501 – 5066
Beta strandi512 – 5165
Beta strandi528 – 5358
Turni537 – 5404
Beta strandi545 – 5539
Beta strandi555 – 5573
Beta strandi561 – 57313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OMCX-ray2.30A/B/C/D/E/F108-574[»]
4OMDX-ray2.70A/B/C/D/E/F108-574[»]
ProteinModelPortaliP09958.
SMRiP09958. Positions 30-99, 109-578, 585-648.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni759 – 7624Cell surface signal

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi498 – 5003Cell attachment site Reviewed prediction
Motifi773 – 7797Trans Golgi network signal

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi556 – 705150Cys-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 homo B/P domain.

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG4935.
HOGENOMiHOG000192536.
HOVERGENiHBG008705.
InParanoidiP09958.
KOiK01349.
OMAiTWAVRIP.
OrthoDBiEOG7BW0JD.
PhylomeDBiP09958.
TreeFamiTF314277.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR006212. Furin_repeat.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
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.
IPR009020. Prot_inh_propept.
IPR002884. PrprotnconvertsP.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SMARTiSM00261. FU. 2 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09958-1 [UniParc]FASTAAdd to Basket

« Hide

MELRPWLLWV VAATGTLVLL AADAQGQKVF TNTWAVRIPG GPAVANSVAR    50
KHGFLNLGQI FGDYYHFWHR GVTKRSLSPH RPRHSRLQRE PQVQWLEQQV 100
AKRRTKRDVY QEPTDPKFPQ QWYLSGVTQR DLNVKAAWAQ GYTGHGIVVS 150
ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG 200
EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY 250
SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH 300
DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ 350
IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT 400
SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC 450
IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD 500
LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE 550
IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE 600
EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHASCAT 650
CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA 700
GQRLRAGLLP SHLPEVVAGL SCAFIVLVFV TVFLVLQLRS GFSFRGVKVY 750
TMDRGLISYK GLPPEAWQEE CPSDSEEDEG RGERTAFIKD QSAL 794
Length:794
Mass (Da):86,678
Last modified:April 1, 1990 - v2
Checksum:i10C44DD5892EF85D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431A → V.
Corresponds to variant rs16944971 [ dbSNP | Ensembl ].
VAR_051821
Natural varianti547 – 5471W → R in cell line LoVo; does not undergo autocatalytic activation and is not transported to the Golgi apparatus. 1 Publication
VAR_055343

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi5045.
KEGGihsa:5045.
UCSCiuc002bpu.1. human.

Polymorphism databases

DMDMi120611.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X17094 mRNA. Translation: CAA34948.1 .
BC012181 mRNA. Translation: AAH12181.1 .
X15723 Genomic DNA. Translation: CAA33745.1 .
X04329 Genomic DNA. Translation: CAA27860.1 .
CCDSi CCDS10364.1.
PIRi A39552. KXHUF.
RefSeqi NP_001276752.1. NM_001289823.1.
NP_001276753.1. NM_001289824.1.
NP_002560.1. NM_002569.3.
UniGenei Hs.513153.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4OMC X-ray 2.30 A/B/C/D/E/F 108-574 [» ]
4OMD X-ray 2.70 A/B/C/D/E/F 108-574 [» ]
ProteinModelPortali P09958.
SMRi P09958. Positions 30-99, 109-578, 585-648.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111082. 8 interactions.
DIPi DIP-29904N.
IntActi P09958. 7 interactions.
MINTi MINT-1209355.
STRINGi 9606.ENSP00000268171.

Chemistry

BindingDBi P09958.
ChEMBLi CHEMBL2611.
GuidetoPHARMACOLOGYi 2366.

Protein family/group databases

MEROPSi S08.071.

PTM databases

PhosphoSitei P09958.

Polymorphism databases

DMDMi 120611.

2D gel databases

OGPi P09958.

Proteomic databases

MaxQBi P09958.
PaxDbi P09958.
PeptideAtlasi P09958.
PRIDEi P09958.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000268171 ; ENSP00000268171 ; ENSG00000140564 .
GeneIDi 5045.
KEGGi hsa:5045.
UCSCi uc002bpu.1. human.

Organism-specific databases

CTDi 5045.
GeneCardsi GC15P091411.
HGNCi HGNC:8568. FURIN.
HPAi CAB009499.
MIMi 136950. gene.
neXtProti NX_P09958.
PharmGKBi PA32894.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4935.
HOGENOMi HOG000192536.
HOVERGENi HBG008705.
InParanoidi P09958.
KOi K01349.
OMAi TWAVRIP.
OrthoDBi EOG7BW0JD.
PhylomeDBi P09958.
TreeFami TF314277.

Enzyme and pathway databases

Reactomei REACT_11062. NGF processing.
REACT_111057. Signaling by NODAL.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_118798. Pre-NOTCH Processing in Golgi.
REACT_120850. TGF-beta receptor signaling activates SMADs.
REACT_150366. Elastic fibre formation.
REACT_150401. Collagen degradation.
REACT_163660. Synthesis and processing of ENV and VPU.
REACT_16888. Signaling by PDGF.
REACT_733. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
SignaLinki P09958.

Miscellaneous databases

ChiTaRSi FURIN. human.
GeneWikii Furin.
GenomeRNAii 5045.
NextBioi 19422.
PMAP-CutDB P09958.
PROi P09958.
SOURCEi Search...

Gene expression databases

ArrayExpressi P09958.
Bgeei P09958.
CleanExi HS_FURIN.
Genevestigatori P09958.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
3.40.50.200. 1 hit.
InterProi IPR006212. Furin_repeat.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
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.
IPR009020. Prot_inh_propept.
IPR002884. PrprotnconvertsP.
[Graphical view ]
PANTHERi PTHR10795. PTHR10795. 1 hit.
Pfami PF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view ]
PRINTSi PR00723. SUBTILISIN.
SMARTi SM00261. FU. 2 hits.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEi PS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structural homology between the human fur gene product and the subtilisin-like protease encoded by yeast KEX2."
    van den Ouweland A.M.W., van Duijnhoven H.L.P., Keizer G.D., Dorssers L.C.J., van de Ven W.J.M.
    Nucleic Acids Res. 18:664-664(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Blood.
  2. "Expression of a human proprotein processing enzyme: correct cleavage of the von Willebrand factor precursor at a paired basic amino acid site."
    Wise R.J., Barr P.J., Wong P.A., Kiefer M.C., Brake A.J., Kaufman R.J.
    Proc. Natl. Acad. Sci. U.S.A. 87:9378-9382(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "cDNA and gene structure for a human subtilisin-like protease with cleavage specificity for paired basic amino acid residues."
    Barr P.J., Mason O.B., Landsberg K.E., Wong P.A., Kiefer M.C., Brake A.J.
    DNA Cell Biol. 10:319-328(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
    Tissue: Lung.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-280.
  6. "Evolutionary conserved close linkage of the c-fes/fps proto-oncogene and genetic sequences encoding a receptor-like protein."
    Roebroek A.J.M., Schalken J.A., Leunissen J.A.M., Onnekink C., Bloemers H.P.J., van de Ven W.J.M.
    EMBO J. 5:2197-2202(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 296-794.
  7. "A mutation of furin causes the lack of precursor-processing activity in human colon carcinoma LoVo cells."
    Takahashi S., Kasai K., Hatsuzawa K., Kitamura N., Misumi Y., Ikehara Y., Murakami K., Nakayama K.
    Biochem. Biophys. Res. Commun. 195:1019-1026(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 402-428, FUNCTION.
    Tissue: Colon carcinoma.
  8. "A second mutant allele of furin in the processing-incompetent cell line, LoVo. Evidence for involvement of the homo B domain in autocatalytic activation."
    Takahashi S., Nakagawa T., Kasai K., Banno T., Duguay S.J., Van de Ven W.J.M., Murakami K., Nakayama K.
    J. Biol. Chem. 270:26565-26569(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 527-553, VARIANT ARG-547.
    Tissue: Colon carcinoma.
  9. "Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage."
    Leduc R., Molloy S.S., Thorne B.A., Thomas G.
    J. Biol. Chem. 267:14304-14308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  10. "Homology modelling of the catalytic domain of human furin. A model for the eukaryotic subtilisin-like proprotein convertases."
    Siezen R.J., Creemers J.W.M., van de Ven W.J.M.
    Eur. J. Biochem. 222:255-266(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF CATALYTIC DOMAIN.
  11. "Intracellular trafficking of furin is modulated by the phosphorylation state of a casein kinase II site in its cytoplasmic tail."
    Jones B.G., Thomas L., Molloy S.S., Thulin C.D., Fry M.D., Walsh K.A., Thomas G.
    EMBO J. 14:5869-5883(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-773 AND SER-775.
  12. "PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic."
    Crump C.M., Xiang Y., Thomas L., Gu F., Austin C., Tooze S.A., Thomas G.
    EMBO J. 20:2191-2201(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PACS1.

Entry informationi

Entry nameiFURIN_HUMAN
AccessioniPrimary (citable) accession number: P09958
Secondary accession number(s): Q14336, Q6LBS3, Q9UCZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 1, 1990
Last modified: September 3, 2014
This is version 178 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, 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

External Data

Dasty 3

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