UniProt Accession

 FURIN_HUMAN; P09958; Q14336; Q6LBS3; Q9UCZ5 

Genbank Protein ID

 X17094; BC012181; X15723; X04329 

Genbank Nucleotide ID

 CAA34948.1; AAH12181.1; CAA33745.1; CAA27860.1 

Protein Name

 Furin 

Protein Synonyms/Alias

 Dibasic-processing enzyme; Paired basic amino acid residue-cleaving enzyme; PACE 

Gene Name

 FURIN 

Gene Synonyms/Alias

 FUR; PACE; PCSK3 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
748	GFSFRGVKVYTMDRG	ubiquitination	[1, 2]
789	GERTAFIKDQSAL**	acetylation	[3]
789	GERTAFIKDQSAL**	ubiquitination	[4, 5]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 

Functional Description

 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. 

Sequence Annotation

 REGION 759 762 Cell surface signal.
 MOTIF 498 500 Cell attachment site (Potential).
 MOTIF 773 779 Trans Golgi network signal.
 ACT_SITE 153 153 Charge relay system (By similarity).
 ACT_SITE 194 194 Charge relay system (By similarity).
 ACT_SITE 368 368 Charge relay system (By similarity).
 METAL 115 115 Calcium 1 (By similarity).
 METAL 162 162 Calcium 1 (By similarity).
 METAL 208 208 Calcium 1 (By similarity).
 METAL 258 258 Calcium 2 (By similarity).
 METAL 301 301 Calcium 2 (By similarity).
 METAL 331 331 Calcium 2 (By similarity).
 MOD_RES 773 773 Phosphoserine; by CK2.
 MOD_RES 775 775 Phosphoserine; by CK2.
 CARBOHYD 387 387 N-linked (GlcNAc...) (Potential).
 CARBOHYD 440 440 N-linked (GlcNAc...) (Potential).
 CARBOHYD 553 553 N-linked (GlcNAc...) (Potential).
 DISULFID 211 360 By similarity.
 DISULFID 303 333 By similarity.
 DISULFID 450 474 By similarity.  

Keyword

 Autocatalytic cleavage; Calcium; Cell membrane; Cleavage on pair of basic residues; Complete proteome; Disulfide bond; Glycoprotein; Golgi apparatus; Hydrolase; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Protease; Reference proteome; Serine protease; Signal; Transmembrane; Transmembrane helix; Zymogen. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 794 AA 

Protein Sequence

Gene Ontology

 GO:0009986; C:cell surface; IDA:BHF-UCL.
 GO:0005796; C:Golgi lumen; TAS:Reactome.
 GO:0000139; C:Golgi membrane; TAS:Reactome.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0045121; C:membrane raft; IDA:BHF-UCL.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0005802; C:trans-Golgi network; IDA:BHF-UCL.
 GO:0030140; C:trans-Golgi network transport vesicle; IDA:MGI.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0048406; F:nerve growth factor binding; IDA:BHF-UCL.
 GO:0042277; F:peptide binding; IDA:BHF-UCL.
 GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
 GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:BHF-UCL.
 GO:0008283; P:cell proliferation; IMP:BHF-UCL.
 GO:0030574; P:collagen catabolic process; TAS:Reactome.
 GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
 GO:0032804; P:negative regulation of low-density lipoprotein particle receptor catabolic process; IDA:HGNC.
 GO:0032911; P:negative regulation of transforming growth factor beta1 production; IMP:BHF-UCL.
 GO:0032455; P:nerve growth factor processing; TAS:Reactome.
 GO:0032902; P:nerve growth factor production; IDA:BHF-UCL.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0007219; P:Notch signaling pathway; TAS:Reactome.
 GO:0043043; P:peptide biosynthetic process; IDA:BHF-UCL.
 GO:0017187; P:peptidyl-glutamic acid carboxylation; TAS:Reactome.
 GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IC:BHF-UCL.
 GO:0043687; P:post-translational protein modification; TAS:Reactome.
 GO:0006508; P:proteolysis; TAS:Reactome.
 GO:0009966; P:regulation of signal transduction; IEA:Compara.
 GO:0032940; P:secretion by cell; IDA:BHF-UCL.
 GO:0006465; P:signal peptide processing; IDA:HGNC.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
 GO:0019067; P:viral assembly, maturation, egress, and release; IEP:BHF-UCL. 

Interpro

 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. 

Pfam

 PF01483; P_proprotein
 PF00082; Peptidase_S8 

SMART

 SM00261; FU 

PROSITE

 PS00136; SUBTILASE_ASP
 PS00137; SUBTILASE_HIS
 PS00138; SUBTILASE_SER 

PRINTS

 PR00723; SUBTILISIN.