CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022463
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bifunctional apoptosis regulator 
Protein Synonyms/Alias
 RING finger protein 47 
Gene Name
 BFAR 
Gene Synonyms/Alias
 BAR; RNF47 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
76ECPECREKWEGFPKVubiquitination[1]
82EKWEGFPKVSILLRDubiquitination[2, 3]
93LLRDAIEKLFPDAIRubiquitination[1]
121QSLAAFQKYGNDQIPubiquitination[1, 4, 5, 6]
177EHDLLVHKAVAKWTAubiquitination[4]
225LTEEEFSKTPYTIENubiquitination[1, 2, 3, 4, 6]
247LMELERVKALGVKPPubiquitination[2, 3]
252RVKALGVKPPQNLWEubiquitination[1, 2, 3, 6]
261PQNLWEYKAVNPGRSubiquitination[1, 2, 3, 4]
322VTKLLDLKEPTWKQWubiquitination[2, 3, 4]
327DLKEPTWKQWREFLVubiquitination[2, 3]
387IWSRSELKTVPQRMWubiquitination[4, 6]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] 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]
 [3] 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]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional Description
 Apoptosis regulator. Has anti-apoptotic activity, both for apoptosis triggered via death-receptors and via mitochondrial factors. 
Sequence Annotation
 DOMAIN 182 249 SAM.
 ZN_FING 34 74 RING-type.
 CARBOHYD 232 232 N-linked (GlcNAc...) (Potential).  
Keyword
 Apoptosis; Complete proteome; Endoplasmic reticulum; Glycoprotein; Membrane; Metal-binding; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 450 AA 
Protein Sequence
MEEPQKSYVN TMDLERDEPL KSTGPQISVS EFSCHCCYDI LVNPTTLNCG HSFCRHCLAL 60
WWASSKKTEC PECREKWEGF PKVSILLRDA IEKLFPDAIR LRFEDIQQNN DIVQSLAAFQ 120
KYGNDQIPLA PNTGRANQQM GGGFFSGVLT ALTGVAVVLL VYHWSSRESE HDLLVHKAVA 180
KWTAEEVVLW LEQLGPWASL YRERFLSERV NGRLLLTLTE EEFSKTPYTI ENSSHRRAIL 240
MELERVKALG VKPPQNLWEY KAVNPGRSLF LLYALKSSPR LSLLYLYLFD YTDTFLPFIH 300
TICPLQEDSS GEDIVTKLLD LKEPTWKQWR EFLVKYSFLP YQLIAEFAWD WLEVHYWTSR 360
FLIINAMLLS VLELFSFWRI WSRSELKTVP QRMWSHFWKV STQGLFVAMF WPLIPQFVCN 420
CLFYWALYFN PIINIDLVVK ELRRLETQVL 450 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0005198; F:structural molecule activity; TAS:ProtInc.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0043066; P:negative regulation of apoptotic process; IDA:MGI. 
Interpro
 IPR001660; SAM.
 IPR013761; SAM/pointed.
 IPR021129; SAM_type1.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00536; SAM_1 
SMART
 SM00184; RING
 SM00454; SAM 
PROSITE
 PS50105; SAM_DOMAIN
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS