CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023854
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase RNF115 
Protein Synonyms/Alias
 RING finger protein 115; Rabring 7; Zinc finger protein 364 
Gene Name
 RNF115 
Gene Synonyms/Alias
 ZNF364 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
26RFFCHFCKGEVSPKLubiquitination[1, 2, 3, 4, 5]
32CKGEVSPKLPEYICPubiquitination[3, 4]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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
Functional Description
 Acts as an E2-dependent E3 ubiquitin-protein ligase. May be involved in endocytic trafficking. 
Sequence Annotation
 ZN_FING 228 269 RING-type.
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Ligase; Metal-binding; Polymorphism; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 304 AA 
Protein Sequence
MAEASAAGAD SGAAVAAHRF FCHFCKGEVS PKLPEYICPR CESGFIEEVT DDSSFLGGGG 60
SRIDNTTTTH FAELWGHLDH TMFFQDFRPF LSSSPLDQDN RANERGHQTH TDFWGARPPR 120
LPLGRRYRSR GSSRPDRSPA IEGILQHIFA GFFANSAIPG SPHPFSWSGM LHSNPGDYAW 180
GQTGLDAIVT QLLGQLENTG PPPADKEKIT SLPTVTVTQE QVDMGLECPV CKEDYTVEEE 240
VRQLPCNHFF HSSCIVPWLE LHDTCPVCRK SLNGEDSTRQ SQSTEASASN RFSNDSQLHD 300
RWTF 304 
Gene Ontology
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0051865; P:protein autoubiquitination; IDA:UniProtKB. 
Interpro
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF13639; zf-RING_2 
SMART
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS