CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019075
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase RNF25 
Protein Synonyms/Alias
 RING finger protein 25 
Gene Name
 RNF25 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
120MLYELIEKGKEILTDubiquitination[1, 2, 3, 4, 5, 6]
318ATQHICEKIPGTRSNubiquitination[4]
334QRLGETQKAMLDPPKubiquitination[2, 3, 4, 6, 7, 8]
341KAMLDPPKPSRGPWRubiquitination[2, 4, 6, 7, 8]
356QPERRHPKGGECHAPubiquitination[4, 8]
364GGECHAPKGTRDTQEubiquitination[4, 8]
386LKEPMDLKPEPHSQGubiquitination[3]
456ESLGLESKDGS****ubiquitination[3, 8]
Reference
 [1] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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
Functional Description
 E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NKD2 (By similarity). Stimulates transcription mediated by NF-kappa-B. 
Sequence Annotation
 DOMAIN 18 128 RWD.
 ZN_FING 135 202 RING-type.
 MOD_RES 450 450 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Ligase; Metal-binding; Phosphoprotein; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 459 AA 
Protein Sequence
MAASASAAAG EEDWVLPSEV EVLESIYLDE LQVIKGNGRT SPWEIYITLH PATAEDQDSQ 60
YVCFTLVLQV PAEYPHEVPQ ISIRNPRGLS DEQIHTILQV LGHVAKAGLG TAMLYELIEK 120
GKEILTDNNI PHGQCVICLY GFQEKEAFTK TPCYHYFHCH CLARYIQHME QELKAQGQEQ 180
EQERQHATTK QKAVGVQCPV CREPLVYDLA SLKAAPEPQQ PMELYQPSAE SLRQQEERKR 240
LYQRQQERGG IIDLEAERNR YFISLQQPPA PAEPESAVDV SKGSQPPSTL AAELSTSPAV 300
QSTLPPPLPV ATQHICEKIP GTRSNQQRLG ETQKAMLDPP KPSRGPWRQP ERRHPKGGEC 360
HAPKGTRDTQ ELPPPEGPLK EPMDLKPEPH SQGVEGPPQE KGPGSWQGPP PRRTRDCVRW 420
ERSKGRTPGS SYPRLPRGQG AYRPGTRRES LGLESKDGS 459 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB. 
Interpro
 IPR006575; RWD-domain.
 IPR016135; UBQ-conjugating_enzyme/RWD.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF05773; RWD
 PF13639; zf-RING_2 
SMART
 SM00184; RING
 SM00591; RWD 
PROSITE
 PS50908; RWD
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS