CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014014
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase RNF187 
Protein Synonyms/Alias
 RING domain AP1 coactivator 1; RACO-1; RING finger protein 187 
Gene Name
 RNF187 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
130WRKALRGKENKGSVEubiquitination[1]
133ALRGKENKGSVEIMRubiquitination[1]
161ESAAAVWKGHVMDRRubiquitination[1, 2, 3, 4]
177KALTDYKKLRAFFVEubiquitination[1, 4]
195HFLQEAEKEEGLPEDubiquitination[2]
223QAVSELEKKHRNLGLubiquitination[2, 3, 4]
224AVSELEKKHRNLGLSubiquitination[1, 3, 4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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] 
Functional Description
 E3 ubiquitin-protein ligase that acts as a coactivator of JUN-mediated gene activation in response to growth factor signaling via the MAP3K1 pathway, independently from MAPK8. 
Sequence Annotation
 ZN_FING 12 53 RING-type.
 CROSSLNK 195 195 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 223 223 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 224 224 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Complete proteome; Cytoplasm; Isopeptide bond; Ligase; Metal-binding; Nucleus; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 235 AA 
Protein Sequence
MALPAGPAEA ACALCQRAPR EPVRADCGHR FCRACVVRFW AEEDGPFPCP ECADDCWQRA 60
VEPGRPPLSR RLLALEEAAA APARDGPASE AALQLLCRAD AGPLCAACRM AAGPEPPEWE 120
PRWRKALRGK ENKGSVEIMR KDLNDARDLH GQAESAAAVW KGHVMDRRKK ALTDYKKLRA 180
FFVEEEEHFL QEAEKEEGLP EDELADPTER FRSLLQAVSE LEKKHRNLGL SMLLQ 235 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IMP:UniProtKB.
 GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
 GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
 GO:0070936; P:protein K48-linked ubiquitination; IMP:UniProtKB. 
Interpro
 IPR018957; Znf_C3HC4_RING-type.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00097; zf-C3HC4 
SMART
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS