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P09958

- FURIN_HUMAN

UniProt

P09958 - FURIN_HUMAN

Protein

Furin

Gene

FURIN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 179 (01 Oct 2014)
      Sequence version 2 (01 Apr 1990)
      Previous versions | rss
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    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 1By similarity
    Active sitei153 – 1531Charge relay systemBy similarity
    Metal bindingi162 – 1621Calcium 1By similarity
    Active sitei194 – 1941Charge relay systemBy similarity
    Metal bindingi208 – 2081Calcium 1By similarity
    Metal bindingi258 – 2581Calcium 2By similarity
    Metal bindingi301 – 3011Calcium 2By similarity
    Metal bindingi331 – 3311Calcium 2By similarity
    Active sitei368 – 3681Charge relay systemBy 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

    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.

    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 Source: UniProtKB
    7. membrane raft Source: BHF-UCL
    8. plasma membrane Source: Reactome
    9. trans-Golgi network Source: BHF-UCL
    10. trans-Golgi network transport vesicle Source: MGI

    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 – 2424Sequence AnalysisAdd
    BLAST
    Propeptidei25 – 10783Inhibition peptidePRO_0000027028Add
    BLAST
    Chaini108 – 794687FurinPRO_0000027029Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi211 ↔ 360By similarity
    Disulfide bondi303 ↔ 333By similarity
    Glycosylationi387 – 3871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi450 ↔ 474By similarity
    Glycosylationi553 – 5531N-linked (GlcNAc...)Sequence Analysis
    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.1 Publication
    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.By similarity1 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei716 – 73823HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini148 – 435288Peptidase S8Add
    BLAST

    Region

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

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi498 – 5003Cell attachment siteSequence Analysis
    Motifi773 – 7797Trans Golgi network signal

    Domaini

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

    Sequence similaritiesi

    Belongs to the peptidase S8 family. Furin subfamily.Curated
    Contains 1 peptidase S8 domain.Curated

    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

    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: October 1, 2014
    This is version 179 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