USC-OGP 2-DE database Two-dimensional polyacrylamide gel electrophoresis database

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Searching in 'USC-OGP 2-DE database' for entry matching: P09958 USC-OGP 2-DE database:  P09958 P09958 General information about the entry View entry in simple text format Entry name FURIN_HUMAN Primary accession number P09958 integrated into USC-OGP 2-DE database on  January 17, 2017 (release 1) 2D Annotations were last modified on January 17, 2017 (version 1) General Annotations were last modified on  April 5, 2017 (version 2) Name and origin of the protein Description RecName: Full=Furin; EC=3.4.21.75; AltName: Full=Dibasic-processing enzyme; AltName: Full=Paired basic amino acid residue-cleaving enzyme; Short=PACE; Flags: Precursor;. Gene name Name=FURIN Synonyms=FUR, PACE, PCSK3 Annotated species Homo sapiens (Human) [TaxID: 9606] Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. References [1]   2D GEL CHARACTERIZATION Author 1., Author 2. Submitted (Mar-2011) to Current 2D PAGE maps for identified proteins How to interpret a protein PLATELET_4-7 {PLATELET 4-7} Homo sapiens (Human)   map experimental info   PLATELET_4-7 MAP LOCATIONS: SPOT OGP-0363: pI=6.21; Mw=51338 Cross-references UniProtKB/Swiss-Prot P09958; FURIN_HUMAN. 2D PAGE maps for identified proteins How to interpret a protein map You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw. Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly. Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed. External data extracted from UniProtKB/Swiss-Prot Extracted from UniProtKB/Swiss-Prot, release: 0.0 Entry name FURIN_HUMAN Primary accession number P09958 Secondary accession number(s) Q14336 Q6LBS3 Q9UCZ5 Sequence was last modified on  April 1, 1990 (version 2) Annotations were last modified on  March 15, 2017 (version 206) Name and origin of the protein Description RecName: Full=Furin; EC=3.4.21.75; AltName: Full=Dibasic-processing enzyme; AltName: Full=Paired basic amino acid residue-cleaving enzyme; Short=PACE; Flags: Precursor; Gene name Name=FURIN Synonyms=FUR, PACE, PCSK3 Encoded on Name=FURIN; Synonyms=FUR, PACE, PCSK3 Keywords 3D-structure; 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. Copyright Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL X17094; CAA34948.1; -; mRNA EMBL BC012181; AAH12181.1; -; mRNA EMBL X15723; CAA33745.1; -; Genomic_DNA EMBL X04329; CAA27860.1; -; Genomic_DNA CCDS CCDS10364.1; -; . PIR A39552; KXHUF; . RefSeq NP_001276752.1; NM_001289823.1; . RefSeq NP_001276753.1; NM_001289824.1; . RefSeq NP_002560.1; NM_002569.3; . UniGene Hs.513153; -; . PDB 4OMC; X-ray; 2.30 A; A/B/C/D/E/F=108-574 PDB 4OMD; X-ray; 2.70 A; A/B/C/D/E/F=108-574 PDB 4RYD; X-ray; 2.15 A; A/B/C/D/E/F=108-574 PDB 4Z2A; X-ray; 1.89 A; A=110-574 PDB 5JMO; X-ray; 2.00 A; A/B=108-574 PDB 5JXG; X-ray; 1.80 A; A=108-574 PDB 5JXH; X-ray; 2.00 A; A=108-574 PDB 5JXI; X-ray; 2.00 A; A=108-574 PDB 5JXJ; X-ray; 2.00 A; A=108-574 PDBsum 4OMC; -; . PDBsum 4OMD; -; . PDBsum 4RYD; -; . PDBsum 4Z2A; -; . PDBsum 5JMO; -; . PDBsum 5JXG; -; . PDBsum 5JXH; -; . PDBsum 5JXI; -; . PDBsum 5JXJ; -; . ProteinModelPortal P09958; -; . SMR P09958; -; . BioGrid 111082; 15; . DIP DIP-29904N; -; . IntAct P09958; 11; . MINT MINT-1209355; -; . STRING 9606.ENSP00000268171; -; . BindingDB P09958; -; . ChEMBL CHEMBL2611; -; . DrugBank DB03600; Decanoic Acid; . DrugBank DB04951; Pirfenidone; . GuidetoPHARMACOLOGY 2366; -; . MEROPS S08.071; -; . iPTMnet P09958; -; . PhosphoSitePlus P09958; -; . BioMuta FURIN; -; . DMDM 120611; -; . OGP P09958; -; . EPD P09958; -; . MaxQB P09958; -; . PaxDb P09958; -; . PeptideAtlas P09958; -; . PRIDE P09958; -; . Ensembl ENST00000268171; ENSP00000268171; ENSG00000140564; . Ensembl ENST00000610579; ENSP00000484952; ENSG00000140564; . Ensembl ENST00000618099; ENSP00000483552; ENSG00000140564; . GeneID 5045; -; . KEGG hsa:5045; -; . UCSC uc002bpu.2; human; . CTD 5045; -; . DisGeNET 5045; -; . GeneCards FURIN; -; . HGNC HGNC:8568; FURIN; . HPA CAB009499; -; . MIM 136950; gene; . neXtProt NX_P09958; -; . OpenTargets ENSG00000140564; -; . PharmGKB PA32894; -; . eggNOG KOG3525; Eukaryota; . eggNOG COG1404; LUCA; . eggNOG COG4935; LUCA; . GeneTree ENSGT00750000117358; -; . HOGENOM HOG000192536; -; . HOVERGEN HBG008705; -; . InParanoid P09958; -; . KO K01349; -; . OMA IIRASVC; -; . OrthoDB EOG091G05HI; -; . PhylomeDB P09958; -; . TreeFam TF314277; -; . Reactome R-HSA-1181150; Signaling by NODAL; . Reactome R-HSA-1442490; Collagen degradation; . Reactome R-HSA-1566948; Elastic fibre formation; . Reactome R-HSA-1592389; Activation of Matrix Metalloproteinases; . Reactome R-HSA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins; . Reactome R-HSA-167060; NGF processing; . Reactome R-HSA-171286; Synthesis and processing of ENV and VPU; . Reactome R-HSA-174800; Chylomicron-mediated lipid transport; . Reactome R-HSA-186797; Signaling by PDGF; . Reactome R-HSA-1912420; Pre-NOTCH Processing in Golgi; . Reactome R-HSA-2173789; TGF-beta receptor signaling activates SMADs; . Reactome R-HSA-5210891; Uptake and function of anthrax toxins; . Reactome R-HSA-6809371; Formation of the cornified envelope; . Reactome R-HSA-977225; Amyloid fiber formation; . SignaLink P09958; -; . SIGNOR P09958; -; . ChiTaRS FURIN; human; . GeneWiki Furin; -; . GenomeRNAi 5045; -; . PMAP-CutDB P09958; -; . PRO PR:P09958; -; . Proteomes UP000005640; Chromosome 15; . Bgee ENSG00000140564; -; . CleanEx HS_FURIN; -; . ExpressionAtlas P09958; baseline and differential; . Genevisible P09958; HS; . GO GO:0009986; C:cell surface; IDA:BHF-UCL; . GO GO:0005783; C:endoplasmic reticulum; IGI:BHF-UCL; . GO GO:0070062; C:extracellular exosome; IDA:UniProtKB; . GO GO:0005576; C:extracellular region; TAS:Reactome; . GO GO:0005796; C:Golgi lumen; TAS:Reactome; . GO GO:0000139; C:Golgi membrane; TAS:Reactome; . GO GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW; . GO GO:0016020; C:membrane; IDA:UniProtKB; . GO GO:0045121; C:membrane raft; IDA:BHF-UCL; . GO GO:0005886; C:plasma membrane; TAS:Reactome; . GO GO:0005802; C:trans-Golgi network; IDA:BHF-UCL; . GO GO:0030140; C:trans-Golgi network transport vesicle; IDA:MGI; . GO GO:0004175; F:endopeptidase activity; IDA:BHF-UCL; . GO GO:0046872; F:metal ion binding; IEA:UniProtKB-KW; . GO GO:0048406; F:nerve growth factor binding; IDA:BHF-UCL; . GO GO:0008233; F:peptidase activity; IDA:UniProtKB; . GO GO:0042277; F:peptide binding; IDA:BHF-UCL; . GO GO:0002020; F:protease binding; IPI:BHF-UCL; . GO GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL; . GO GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:BHF-UCL; . GO GO:0008283; P:cell proliferation; IMP:BHF-UCL; . GO GO:0044267; P:cellular protein metabolic process; TAS:Reactome; . GO GO:0030574; P:collagen catabolic process; TAS:Reactome; . GO GO:0070268; P:cornification; TAS:Reactome; . GO GO:0022617; P:extracellular matrix disassembly; TAS:Reactome; . GO GO:0030198; P:extracellular matrix organization; TAS:Reactome; . GO GO:0042157; P:lipoprotein metabolic process; TAS:Reactome; . GO GO:0032804; P:negative regulation of low-density lipoprotein particle receptor catabolic process; IDA:HGNC; . GO GO:0032911; P:negative regulation of transforming growth factor beta1 production; IMP:BHF-UCL; . GO GO:0032455; P:nerve growth factor processing; TAS:Reactome; . GO GO:0032902; P:nerve growth factor production; IDA:BHF-UCL; . GO GO:0043043; P:peptide biosynthetic process; IDA:BHF-UCL; . GO GO:0016486; P:peptide hormone processing; IDA:BHF-UCL; . GO GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IC:BHF-UCL; . GO GO:0016485; P:protein processing; IDA:UniProtKB; . GO GO:0052548; P:regulation of endopeptidase activity; IDA:BHF-UCL; . GO GO:0045714; P:regulation of low-density lipoprotein particle receptor biosynthetic process; IEA:Ensembl; . GO GO:0042176; P:regulation of protein catabolic process; IMP:BHF-UCL; . GO GO:0009966; P:regulation of signal transduction; IEA:Ensembl; . GO GO:0032940; P:secretion by cell; IDA:BHF-UCL; . GO GO:0006465; P:signal peptide processing; IDA:HGNC; . GO GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome; . GO GO:0019058; P:viral life cycle; IEP:BHF-UCL; . GO GO:0019082; P:viral protein processing; TAS:Reactome; . CDD cd04059; Peptidases_S8_Protein_converta; 1; . Gene3D 2.60.120.260; -; 1; . Gene3D 3.30.70.850; -; 1; . Gene3D 3.40.50.200; -; 1; . InterPro IPR006212; Furin_repeat; . InterPro IPR008979; Galactose-bd-like; . InterPro IPR009030; Growth_fac_rcpt_; . InterPro IPR034182; Kexin/furin; . InterPro IPR000209; Peptidase_S8/S53_dom; . InterPro IPR023827; Peptidase_S8_Asp-AS; . InterPro IPR022398; Peptidase_S8_His-AS; . InterPro IPR023828; Peptidase_S8_Ser-AS; . InterPro IPR015500; Peptidase_S8_subtilisin-rel; . InterPro IPR009020; Propept_inh; . InterPro IPR002884; PrprotnconvertsP; . InterPro IPR032815; S8_pro-domain; . Pfam PF01483; P_proprotein; 1; . Pfam PF00082; Peptidase_S8; 1; . Pfam PF16470; S8_pro-domain; 1; . PRINTS PR00723; SUBTILISIN; . SMART SM00261; FU; 2; . SUPFAM SSF49785; SSF49785; 1; . SUPFAM SSF52743; SSF52743; 1; . SUPFAM SSF54897; SSF54897; 1; . SUPFAM SSF57184; SSF57184; 1; . PROSITE PS51829; P_HOMO_B; 1; . PROSITE PS00136; SUBTILASE_ASP; 1; . PROSITE PS00137; SUBTILASE_HIS; 1; . PROSITE PS00138; SUBTILASE_SER; 1; .

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