CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019735
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribonucleases P/MRP protein subunit POP1 
Protein Synonyms/Alias
 hPOP1 
Gene Name
 POP1 
Gene Synonyms/Alias
 KIAA0061 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
40KHHSGGEKPFQAQKQacetylation[1]
46EKPFQAQKQEPHPGTacetylation[1]
566CKSVTENKISDQDLNubiquitination[2]
605LLIQQPGKVTGEDRLubiquitination[2]
734VASSPNGKESDLRRSubiquitination[2]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [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] 
Functional Description
 Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP. 
Sequence Annotation
 MOD_RES 367 367 Phosphoserine.
 MOD_RES 584 584 Phosphoserine.
 MOD_RES 729 729 Phosphoserine.
 MOD_RES 730 730 Phosphoserine.  
Keyword
 Complete proteome; Disease mutation; Dwarfism; Hydrolase; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; tRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1024 AA 
Protein Sequence
MSNAKERKHA KKMRNQPTNV TLSSGFVADR GVKHHSGGEK PFQAQKQEPH PGTSRQRQTR 60
VNPHSLPDPE VNEQSSSKGM FRKKGGWKAG PEGTSQEIPK YITASTFAQA RAAEISAMLK 120
AVTQKSSNSL VFQTLPRHMR RRAMSHNVKR LPRRLQEIAQ KEAEKAVHQK KEHSKNKCHK 180
ARRCHMNRTL EFNRRQKKNI WLETHIWHAK RFHMVKKWGY CLGERPTVKS HRACYRAMTN 240
RCLLQDLSYY CCLELKGKEE EILKALSGMC NIDTGLTFAA VHCLSGKRQG SLVLYRVNKY 300
PREMLGPVTF IWKSQRTPGD PSESRQLWIW LHPTLKQDIL EEIKAACQCV EPIKSAVCIA 360
DPLPTPSQEK SQTELPDEKI GKKRKRKDDG ENAKPIKKII GDGTRDPCLP YSWISPTTGI 420
IISDLTMEMN RFRLIGPLSH SILTEAIKAA SVHTVGEDTE ETPHRWWIET CKKPDSVSLH 480
CRQEAIFELL GGITSPAEIP AGTILGLTVG DPRINLPQKK SKALPNPEKC QDNEKVRQLL 540
LEGVPVECTH SFIWNQDICK SVTENKISDQ DLNRMRSELL VPGSQLILGP HESKIPILLI 600
QQPGKVTGED RLGWGSGWDV LLPKGWGMAF WIPFIYRGVR VGGLKESAVH SQYKRSPNVP 660
GDFPDCPAGM LFAEEQAKNL LEKYKRRPPA KRPNYVKLGT LAPFCCPWEQ LTQDWESRVQ 720
AYEEPSVASS PNGKESDLRR SEVPCAPMPK KTHQPSDEVG TSIEHPREAE EVMDAGCQES 780
AGPERITDQE ASENHVAATG SHLCVLRSRK LLKQLSAWCG PSSEDSRGGR RAPGRGQQGL 840
TREACLSILG HFPRALVWVS LSLLSKGSPE PHTMICVPAK EDFLQLHEDW HYCGPQESKH 900
SDPFRSKILK QKEKKKREKR QKPGRASSDG PAGEEPVAGQ EALTLGLWSG PLPRVTLHCS 960
RTLLGFVTQG DFSMAVGCGE ALGFVSLTGL LDMLSSQPAA QRGLVLLRPP ASLQYRFARI 1020
AIEV 1024 
Gene Ontology
 GO:0005655; C:nucleolar ribonuclease P complex; IDA:UniProtKB.
 GO:0000172; C:ribonuclease MRP complex; IDA:UniProtKB.
 GO:0000171; F:ribonuclease MRP activity; IDA:UniProtKB.
 GO:0004526; F:ribonuclease P activity; IDA:UniProtKB.
 GO:0001682; P:tRNA 5'-leader removal; IEA:InterPro.
 GO:0016078; P:tRNA catabolic process; IDA:UniProtKB. 
Interpro
 IPR012590; POPLD.
 IPR009723; RNase_P/MRP_POP1. 
Pfam
 PF06978; POP1
 PF08170; POPLD 
SMART
  
PROSITE
  
PRINTS