CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000076
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 RNA 3'-terminal phosphate cyclase 
Protein Synonyms/Alias
 RNA cyclase; RNA-3'-phosphate cyclase; RNA terminal phosphate cyclase domain-containing protein 1; RTC domain-containing protein 1 
Gene Name
 RTCA 
Gene Synonyms/Alias
 RPC; RPC1; RTC1; RTCD1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
154DYTVMVFKPIVEKFGubiquitination[1]
169FIFNCDIKTRGYYPKubiquitination[1]
176KTRGYYPKGGGEVIVubiquitination[1, 2]
189IVRMSPVKQLNPINLubiquitination[1]
204TERGCVTKIYGRAFVubiquitination[1]
221VLPFKVAKDMAAAAVubiquitination[1]
285KRGVNADKVGIEAAEubiquitination[1]
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] 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
 Catalyzes the conversion of 3'-phosphate to a 2',3'- cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA- N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'- phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing. 
Sequence Annotation
 NP_BIND 294 298 ATP (By similarity).
 ACT_SITE 320 320 Tele-AMP-histidine intermediate (By
 BINDING 104 104 ATP (By similarity).  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Direct protein sequencing; Ligase; Nucleotide-binding; Nucleus; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 366 AA 
Protein Sequence
MAGPRVEVDG SIMEGGGQIL RVSTALSCLL GLPLRVQKIR AGRSTPGLSS GGWKSKIKVL 60
TRPQHLSGLE MIRDLCDGQL EGAEIGSTEI TFTPEKIKGG IHTADTKTAG SVCLLMQVSM 120
PCVLFAASPS ELHLKGGTNA EMAPQIDYTV MVFKPIVEKF GFIFNCDIKT RGYYPKGGGE 180
VIVRMSPVKQ LNPINLTERG CVTKIYGRAF VAGVLPFKVA KDMAAAAVRC IRKEIRDLYV 240
NIQPVQEPKD QAFGNGNGII IIAETSTGCL FAGSSLGKRG VNADKVGIEA AEMLLANLRH 300
GGTVDEYLQD QLIVFMALAN GVSRIKTGPV TLHTQTAIHF AEQIAKAKFI VKKSEDEEDA 360
AKDTYIIECQ GIGMTNPNL 379 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:ProtInc.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0003963; F:RNA-3'-phosphate cyclase activity; TAS:ProtInc.
 GO:0006396; P:RNA processing; IEA:InterPro. 
Interpro
 IPR013791; RNA3'-term_phos_cycl_insert.
 IPR023797; RNA3'_phos_cyclase_dom.
 IPR000228; RNA3'_term_phos_cyc.
 IPR017770; RNA3'_term_phos_cyc_type_1.
 IPR020719; RNA3'_term_phos_cycl-like_CS.
 IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b. 
Pfam
 PF01137; RTC
 PF05189; RTC_insert 
SMART
  
PROSITE
 PS01287; RTC 
PRINTS