CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021457
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase RNF167 
Protein Synonyms/Alias
 RING finger protein 167; RING105 
Gene Name
 RNF167 
Gene Synonyms/Alias
 LP2254 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
97FDCNFDLKVLNAQKAubiquitination[1, 2, 3]
156RALFVYEKGARVLLVubiquitination[2, 4, 5, 6]
210LQRNRLTKEQLKQIPubiquitination[1, 2, 3]
214RLTKEQLKQIPTHDYubiquitination[1, 3, 4]
223IPTHDYQKGDQYDVCubiquitination[2, 6]
266PWLTQTRKTCPICKQubiquitination[6]
272RKTCPICKQPVHRGPubiquitination[1, 2, 3, 5, 6, 7]
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] 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]
 [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] 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] 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] 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
Functional Description
 May act as an E3 ubiquitin-protein ligase, or as part of the E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2E1, and then transfers it to substrates, such as SLC22A18. May play a role in growth regulation involved in G1/S transition. 
Sequence Annotation
 DOMAIN 49 152 PA.
 ZN_FING 230 272 RING-type; atypical.
 CARBOHYD 79 79 N-linked (GlcNAc...) (Potential).  
Keyword
 Complete proteome; Glycoprotein; Ligase; Membrane; Metal-binding; Polymorphism; Reference proteome; Signal; Transmembrane; Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 350 AA 
Protein Sequence
MHPAAFPLPV VVAAVLWGAA PTRGLIRATS DHNASMDFAD LPALFGATLS QEGLQGFLVE 60
AHPDNACSPI APPPPAPVNG SVFIALLRRF DCNFDLKVLN AQKAGYGAAV VHNVNSNELL 120
NMVWNSEEIQ QQIWIPSVFI GERSSEYLRA LFVYEKGARV LLVPDNTFPL GYYLIPFTGI 180
VGLLVLAMGA VMIARCIQHR KRLQRNRLTK EQLKQIPTHD YQKGDQYDVC AICLDEYEDG 240
DKLRVLPCAH AYHSRCVDPW LTQTRKTCPI CKQPVHRGPG DEDQEEETQG QEEGDEGEPR 300
DHPASERTPL LGSSPTLPTS FGSLAPAPLV FPGPSTDPPL SPPSSPVILV 350 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0045786; P:negative regulation of cell cycle; IMP:UniProtKB.
 GO:0000209; P:protein polyubiquitination; IDA:UniProtKB. 
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