CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010980
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribonuclease P protein component, mitochondrial 
Protein Synonyms/Alias
 RNase P 
Gene Name
 RPM2 
Gene Synonyms/Alias
 YML091C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
1084SPSIENDKSMKEKLRubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 Ribonuclease P generates mature tRNA molecules by cleaving their 5'-ends. 
Sequence Annotation
  
Keyword
 Complete proteome; Direct protein sequencing; Endonuclease; Hydrolase; Mitochondrion; Nuclease; Reference proteome; Transit peptide; tRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1202 AA 
Protein Sequence
MAFKSFIYSK GYHRSAAQKK TATSFFDSSY QYLRQNQGLV NSDPVLHASH LHPHPVVVAN 60
VNYNNVDDIL HPHDLDSSIN NTNNPLTHEE LLYNQNVSLR SLKQQQSTNY VNNNNNNQHR 120
YYSTGPTLPT NQYDPLNFSN RNFQDLSLKT SQPSVQQPQN EYSLLKDENA PVWKEDTEPC 180
LNKSTYLQTH IDEINRCYEQ KNYNKINSLY QSLKRNDIVP PLEIFTKVLD SLCKRPLDNN 240
DLDNKMYELL TCYQDMINNR LKPPDEIYNI VLLSLFKGSI LAYQFENPNG SDFYKIAIEL 300
FNTTTNDPKQ KSVVKFRNFS KDVLDYNLLA MNIYPGHITL SKAQQVIKSS PAFIKDSFYF 360
IACFSYAKLT NDKFAIKELY EDFRLSLSSG SPDQGLFDDQ FEIYSVILSS FIETGEVELA 420
TNLLDDLVSK IQSSNGLASN ISLLLSSFLI SMSKVDPSKA YEIWFKFHNL NWIPEFSYEF 480
YLVFMANSFQ DWNLTKKIYD YIFPMERNLS PLKKQKLSDY LLHPIGVDSI TTSLLDYSLQ 540
LKDNEVIMKI LEESIVKNFS FDIGIYPFVF NYLREIQCGE DYLMRFIESH AEFIKKSNSI 600
NKFQFLNMIV DNFQSQSLLN KISHAKFFKN FVEDFNLENC ELVSYNGLIS CINNFIKIPK 660
TIKDFPYILE IHAILVTKLF DFDTYPILQN GNNEVLLKFR DQIEHQFKML AQNFCRLNLD 720
PNLLAGVVSQ AMKMVNLDDT ANGQDLLNFF NHPGDWDKSY PLSLGSFIRN SPRGGIREFT 780
KLSKEGYCFD YDTYKELIIK RAINKQIIDK CLEVCPDSIE LKNIVNLMIS KIPGRNLTQL 840
IINNPKFSKV FVPNLRNDSM LKLIENCESL SNFIRICDFP EKFKSIAIQA ENKNAIELIY 900
ERLFDGGKYA DILRYNNIVP VLNLELLLKS CIRSGEFKKY ESLSKKFNDK ISESSKIDIQ 960
LEYLINKNDL KGAFTLFEKT PRELRTPHKT MDLYTFALFL DSFNRNITYY ESPENTLQFA 1020
NILSSQTSFI NLLSTYNLIA HSDHLMNFNV GGMAAKVKKE ILNQMLNNLY DSIRLLSPSI 1080
ENDKSMKEKL REKVKNYCRF KAYLKSPELD MDELKTLVSV ESFLNPFTPS MLFNNLIETI 1140
YINEHASSLV LQNGLIYSLQ QKGLNKILSY LEESFITSGN DANIEKVREF RSLLRKSKPL 1200
QA 1202 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IDA:SGD.
 GO:0030678; C:mitochondrial ribonuclease P complex; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0004526; F:ribonuclease P activity; IEA:EC.
 GO:0002181; P:cytoplasmic translation; IMP:SGD.
 GO:0007005; P:mitochondrion organization; IMP:SGD.
 GO:0006397; P:mRNA processing; IGI:SGD.
 GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:SGD.
 GO:0001682; P:tRNA 5'-leader removal; IDA:SGD. 
Interpro
 IPR013888; RNase_P_Rpm2_mt. 
Pfam
 PF08579; RPM2 
SMART
  
PROSITE
  
PRINTS