CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017598
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase RNF149 
Protein Synonyms/Alias
 DNA polymerase-transactivated protein 2; RING finger protein 149 
Gene Name
 RNF149 
Gene Synonyms/Alias
 DNAPTP2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
245SHRKETKKVIGQLLLubiquitination[1, 2, 3, 4]
260HTVKHGEKGIDVDAEubiquitination[3, 5]
279CIENFKVKDIIRILPubiquitination[3]
288IIRILPCKHIFHRICubiquitination[2, 3]
310HRTCPMCKLDVIKALubiquitination[3]
315MCKLDVIKALGYWGEubiquitination[6]
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] 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]
 [3] 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]
 [4] 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]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] 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
Functional Description
 E3 ubiquitin-protein ligase. Ubiquitinates BRAF, inducing its proteasomal degradation. 
Sequence Annotation
 DOMAIN 67 175 PA.
 ZN_FING 269 310 RING-type; atypical.
 CARBOHYD 52 52 N-linked (GlcNAc...) (Potential).
 CARBOHYD 145 145 N-linked (GlcNAc...) (Potential).  
Keyword
 Complete proteome; Glycoprotein; Ligase; Membrane; Metal-binding; Polymorphism; Reference proteome; Signal; Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 400 AA 
Protein Sequence
MAWRRREASV GARGVLALAL LALALCVPGA RGRALEWFSA VVNIEYVDPQ TNLTVWSVSE 60
SGRFGDSSPK EGAHGLVGVP WAPGGDLEGC APDTRFFVPE PGGRGAAPWV ALVARGGCTF 120
KDKVLVAARR NASAVVLYNE ERYGNITLPM SHAGTGNIVV IMISYPKGRE ILELVQKGIP 180
VTMTIGVGTR HVQEFISGQS VVFVAIAFIT MMIISLAWLI FYYIQRFLYT GSQIGSQSHR 240
KETKKVIGQL LLHTVKHGEK GIDVDAENCA VCIENFKVKD IIRILPCKHI FHRICIDPWL 300
LDHRTCPMCK LDVIKALGYW GEPGDVQEMP APESPPGRDP AANLSLALPD DDGSDDSSPP 360
SASPAESEPQ CDPSFKGDAG ENTALLEAGR SDSRHGGPIS 400 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. 
Interpro
 IPR003137; Protease-assoc_domain.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF02225; PA
 PF13639; zf-RING_2 
SMART
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS