CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019205
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase RNF125 
Protein Synonyms/Alias
 RING finger protein 125; T-cell RING activation protein 1; TRAC-1 
Gene Name
 RNF125 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
66SCIATSLKNNKWTCPubiquitination[1]
69ATSLKNNKWTCPYCRubiquitination[2, 3]
91VPATDVAKRMKSEYKubiquitination[2, 3, 4]
98KRMKSEYKNCAECDTubiquitination[2]
125TCQKYIDKYGPLQELubiquitination[2, 4]
Reference
 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [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] 
Functional Description
 E3 ubiquitin-protein ligase that acts as a positive regulator of T-cell activation. E3 ligase proteins mediate ubiquitination and subsequent proteasomal degradation of target proteins. 
Sequence Annotation
 ZN_FING 37 76 RING-type.
 LIPID 2 2 N-myristoyl glycine (Probable).  
Keyword
 Adaptive immunity; Complete proteome; Immunity; Ligase; Lipoprotein; Metal-binding; Myristate; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 232 AA 
Protein Sequence
MGSVLSTDSG KSAPASATAR ALERRRDPEL PVTSFDCAVC LEVLHQPVRT RCGHVFCRSC 60
IATSLKNNKW TCPYCRAYLP SEGVPATDVA KRMKSEYKNC AECDTLVCLS EMRAHIRTCQ 120
KYIDKYGPLQ ELEETAARCV CPFCQRELYE DSLLDHCITH HRSERRPVFC PLCRLIPDEN 180
PSSFSGSLIR HLQVSHTLFY DDFIDFNIIE EALIRRVLDR SLLEYVNHSN TT 232 
Gene Ontology
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome. 
Interpro
 IPR015880; Znf_C2H2-like.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
  
SMART
 SM00184; RING
 SM00355; ZnF_C2H2 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS