CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014076
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RNA-binding E3 ubiquitin-protein ligase MEX3C 
Protein Synonyms/Alias
 RING finger and KH domain-containing protein 2; RING finger protein 194 
Gene Name
 MEX3C 
Gene Synonyms/Alias
 RKHD2; RNF194; BM-013 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
309MIRASRNKNGPALGGubiquitination[1, 2]
367IVTPSRDKEPVFEVTubiquitination[1, 2, 3]
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] 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]
 [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] 
Functional Description
 E3 ubiquitin ligase responsible for the post- transcriptional regulation of common HLA-A allotypes. Binds to the 3' UTR of HLA-A2 mRNA, and regulates its levels by promoting mRNA decay. RNA binding is sufficient to prevent translation, but ubiquitin ligase activity is required for mRNA degradation. 
Sequence Annotation
 DOMAIN 232 293 KH 1.
 DOMAIN 326 387 KH 2.
 ZN_FING 608 648 RING-type.  
Keyword
 Complete proteome; Cytoplasm; Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; RNA-binding; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 659 AA 
Protein Sequence
MPSGSSAALA LAAAPAPLPQ PPPPPPPPPP PLPPPSGGPE LEGDGLLLRE RLAALGLDDP 60
SPAEPGAPAL RAPAAAAQGQ ARRAAELSPE ERAPPGRPGA PEAAELELEE DEEEGEEAEL 120
DGDLLEEEEL EEAEEEDRSS LLLLSPPAAT ASQTQQIPGG SLGSVLLPAA RFDAREAAAA 180
AAAAGVLYGG DDAQGMMAAM LSHAYGPGGC GAAAAALNGE QAALLRRKSV NTTECVPVPS 240
SEHVAEIVGR QGCKIKALRA KTNTYIKTPV RGEEPIFVVT GRKEDVAMAK REILSAAEHF 300
SMIRASRNKN GPALGGLSCS PNLPGQTTVQ VRVPYRVVGL VVGPKGATIK RIQQQTHTYI 360
VTPSRDKEPV FEVTGMPENV DRAREEIEMH IAMRTGNYIE LNEENDFHYN GTDVSFEGGT 420
LGSAWLSSNP VPPSRARMIS NYRNDSSSSL GSGSTDSYFG SNRLADFSPT SPFSTGNFWF 480
GDTLPSVGSE DLAVDSPAFD SLPTSAQTIW TPFEPVNPLS GFGSDPSGNM KTQRRGSQPS 540
TPRLSPTFPE SIEHPLARRV RSDPPSTGNH VGLPIYIPAF SNGTNSYSSS NGGSTSSSPP 600
ESRRKHDCVI CFENEVIAAL VPCGHNLFCM ECANKICEKR TPSCPVCQTA VTQAIQIHS 659 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR004087; KH_dom.
 IPR004088; KH_dom_type_1.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00013; KH_1 
SMART
 SM00322; KH
 SM00184; RING 
PROSITE
 PS50084; KH_TYPE_1
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS