CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015942
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 BRCA1-associated protein 
Protein Synonyms/Alias
 BRAP2; Impedes mitogenic signal propagation; IMP; RING finger protein 52; Renal carcinoma antigen NY-REN-63 
Gene Name
 BRAP 
Gene Synonyms/Alias
 RNF52 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
85KSNPDELKTTVEERKubiquitination[1]
381VHRLVASKTDGKIVQubiquitination[1, 2, 3, 4, 5, 6, 7]
385VASKTDGKIVQYECEubiquitination[1, 2, 3, 4, 5, 6, 7]
400GDTCQEEKIDALQLEubiquitination[4, 7]
426QRIYWENKIVRIEKDubiquitination[1]
442AEEINNMKTKFKETIubiquitination[1]
444EINNMKTKFKETIEKubiquitination[1]
446NNMKTKFKETIEKCDubiquitination[1]
507NQVLLQNKLKEEERVubiquitination[1]
580ASSGGSGKLPSRKGRubiquitination[3]
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] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [3] 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]
 [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] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [6] 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]
 [7] 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
 Negatively regulates MAP kinase activation by limiting the formation of Raf/MEK complexes probably by inactivation of the KSR1 scaffold protein. Also acts as a Ras responsive E3 ubiquitin ligase that, on activation of Ras, is modified by auto- polyubiquitination resulting in the release of inhibition of Raf/MEK complex formation. May also act as a cytoplasmic retention protein with a role in regulating nuclear transport. 
Sequence Annotation
 ZN_FING 264 304 RING-type.
 ZN_FING 315 376 UBP-type.
 MOD_RES 52 52 Phosphoserine.
 MOD_RES 117 117 Phosphoserine (By similarity).
 MOD_RES 119 119 Phosphoserine.  
Keyword
 Coiled coil; Complete proteome; Cytoplasm; Ligase; Metal-binding; Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 592 AA 
Protein Sequence
MSVSLVVIRL ELAEHSPVPA GFGFSAAAGE MSDEEIKKTT LASAVACLEG KSPGEKVAII 60
HQHLGRREMT DVIIETMKSN PDELKTTVEE RKSSEASPTA QRSKDHSKEC INAAPDSPSK 120
QLPDQISFFS GNPSVEIVHG IMHLYKTNKM TSLKEDVRRS AMLCILTVPA AMTSHDLMKF 180
VAPFNEVIEQ MKIIRDSTPN QYMVLIKFRA QADADSFYMT CNGRQFNSIE DDVCQLVYVE 240
RAEVLKSEDG ASLPVMDLTE LPKCTVCLER MDESVNGILT TLCNHSFHSQ CLQRWDDTTC 300
PVCRYCQTPE PVEENKCFEC GVQENLWICL ICGHIGCGRY VSRHAYKHFE ETQHTYAMQL 360
TNHRVWDYAG DNYVHRLVAS KTDGKIVQYE CEGDTCQEEK IDALQLEYSY LLTSQLESQR 420
IYWENKIVRI EKDTAEEINN MKTKFKETIE KCDNLEHKLN DLLKEKQSVE RKCTQLNTKV 480
AKLTNELKEE QEMNKCLRAN QVLLQNKLKE EERVLKETCD QKDLQITEIQ EQLRDVMFYL 540
ETQQKINHLP AETRQEIQEG QINIAMASAS SPASSGGSGK LPSRKGRSKR GK 592 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0000151; C:ubiquitin ligase complex; IDA:MGI.
 GO:0008139; F:nuclear localization sequence binding; IDA:MGI.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0000165; P:MAPK cascade; IDA:MGI.
 GO:0009968; P:negative regulation of signal transduction; IDA:UniProtKB.
 GO:0007265; P:Ras protein signal transduction; IDA:MGI. 
Interpro
 IPR011422; BRAP2.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR001607; Znf_UBP. 
Pfam
 PF07576; BRAP2
 PF13639; zf-RING_2
 PF02148; zf-UBP 
SMART
 SM00184; RING
 SM00290; ZnF_UBP 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2
 PS50271; ZF_UBP 
PRINTS