CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007593
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Leucine-rich PPR motif-containing protein, mitochondrial 
Protein Synonyms/Alias
 130 kDa leucine-rich protein; LRP 130; GP130 
Gene Name
 LRPPRC 
Gene Synonyms/Alias
 LRP130 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
66YAIAAKEKDIQEESTubiquitination[1]
155RIWDTLQKLGAVYDVacetylation[2]
155RIWDTLQKLGAVYDVubiquitination[3]
178VYLQNEYKFSPTDFLubiquitination[1]
187SPTDFLAKMEEANIQacetylation[2]
187SPTDFLAKMEEANIQubiquitination[1]
292HVKQTLEKVEKSELHacetylation[2]
453LVGRRKEKNVQGIIEubiquitination[3]
613QYFHQLEKMNVKIPEacetylation[2, 4, 5, 6]
613QYFHQLEKMNVKIPEubiquitination[3]
617QLEKMNVKIPENIYRubiquitination[3]
649AHLLVESKNLDFQKTacetylation[6]
649AHLLVESKNLDFQKTubiquitination[3]
655SKNLDFQKTVQLTSSubiquitination[1]
726NLCCRHDKVEDALNLacetylation[2, 4, 5]
750SAVLDTGKYVGLVRVacetylation[2, 5]
763RVLAKHGKLQDAINIacetylation[5]
864RIHDVLCKLVEKGETacetylation[2]
868VLCKLVEKGETDLIQacetylation[5]
941NQVETLEKLVELTQKacetylation[5]
980RADAVWNKIQEENVIacetylation[5]
980RADAVWNKIQEENVIubiquitination[3]
1098AFAETHIKGFTLNDAubiquitination[3]
1332MKSYVSEKDVTSAKAacetylation[6]
1350HLTAKNTKLDDLFLKubiquitination[3]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] 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]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] 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
 May play a role in RNA metabolism in both nuclei and mitochondria. In the nucleus binds to HNRPA1-associated poly(A) mRNAs and is part of nmRNP complexes at late stages of mRNA maturation which are possibly associated with nuclear mRNA export. May bind mature mRNA in the nucleus outer membrane. In mitochondria binds to poly(A) mRNA. Plays a role in translation or stability of mitochondrially encoded cytochrome c oxidase (COX) subunits. May be involved in transcription regulation. Cooperates with PPARGC1A to regulate certain mitochondrially encoded genes and gluconeogenic genes and may regulate docking of PPARGC1A to transcription factors. Seems to be involved in the transcription regulation of the multidrug-related genes MDR1 and MVP. Part of a nuclear factor that binds to the invMED1 element of MDR1 and MVP gene promoters. Binds single-stranded DNA (By similarity). 
Sequence Annotation
 REPEAT 126 160 PPR 1.
 REPEAT 161 195 PPR 2.
 REPEAT 196 230 PPR 3.
 REPEAT 231 265 PPR 4.
 REPEAT 266 300 PPR 5.
 REPEAT 301 335 PPR 6.
 REPEAT 403 437 PPR 7.
 REPEAT 438 472 PPR 8.
 REPEAT 678 709 PPR 9.
 REPEAT 710 746 PPR 10.
 REPEAT 747 784 PPR 11.
 REPEAT 785 820 PPR 12.
 REPEAT 821 856 PPR 13.
 REPEAT 954 988 PPR 14.
 REPEAT 1031 1065 PPR 15.
 REPEAT 1066 1102 PPR 16.
 REPEAT 1103 1137 PPR 17.
 REPEAT 1138 1175 PPR 18.
 REPEAT 1176 1210 PPR 19.
 REPEAT 1317 1351 PPR 20.
 REGION 1121 1394 RNA-binding.
 MOD_RES 155 155 N6-acetyllysine.
 MOD_RES 187 187 N6-acetyllysine.
 MOD_RES 292 292 N6-acetyllysine.
 MOD_RES 613 613 N6-acetyllysine.
 MOD_RES 726 726 N6-acetyllysine.
 MOD_RES 750 750 N6-acetyllysine.  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; Disease mutation; DNA-binding; Leigh syndrome; Membrane; Mitochondrion; mRNA transport; Nucleus; Polymorphism; Reference proteome; Repeat; RNA-binding; Transcription; Transcription regulation; Transit peptide; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1394 AA 
Protein Sequence
MAALLRSARW LLRAGAAPRL PLSLRLLPGG PGRLHAASYL PAARAGPVAG GLLSPARLYA 60
IAAKEKDIQE ESTFSSRKIS NQFDWALMRL DLSVRRTGRI PKKLLQKVFN DTCRSGGLGG 120
SHALLLLRSC GSLLPELKLE ERTEFAHRIW DTLQKLGAVY DVSHYNALLK VYLQNEYKFS 180
PTDFLAKMEE ANIQPNRVTY QRLIASYCNV GDIEGASKIL GFMKTKDLPV TEAVFSALVT 240
GHARAGDMEN AENILTVMRD AGIEPGPDTY LALLNAYAEK GDIDHVKQTL EKVEKSELHL 300
MDRDLLQIIF SFSKAGYPQY VSEILEKVTC ERRYIPDAMN LILLLVTEKL EDVALQILLA 360
CPVSKEDGPS VFGSFFLQHC VTMNTPVEKL TDYCKKLKEV QMHSFPLQFT LHCALLANKT 420
DLAKALMKAV KEEGFPIRPH YFWPLLVGRR KEKNVQGIIE ILKGMQELGV HPDQETYTDY 480
VIPCFDSVNS ARAILQENGC LSDSDMFSQA GLRSEAANGN LDFVLSFLKS NTLPISLQSI 540
RSSLLLGFRR SMNINLWSEI TELLYKDGRY CQEPRGPTEA VGYFLYNLID SMSDSEVQAK 600
EEHLRQYFHQ LEKMNVKIPE NIYRGIRNLL ESYHVPELIK DAHLLVESKN LDFQKTVQLT 660
SSELESTLET LKAENQPIRD VLKQLILVLC SEENMQKALE LKAKYESDMV TGGYAALINL 720
CCRHDKVEDA LNLKEEFDRL DSSAVLDTGK YVGLVRVLAK HGKLQDAINI LKEMKEKDVL 780
IKDTTALSFF HMLNGAALRG EIETVKQLHE AIVTLGLAEP STNISFPLVT VHLEKGDLST 840
ALEVAIDCYE KYKVLPRIHD VLCKLVEKGE TDLIQKAMDF VSQEQGEMVM LYDLFFAFLQ 900
TGNYKEAKKI IETPGIRARS ARLQWFCDRC VANNQVETLE KLVELTQKLF ECDRDQMYYN 960
LLKLYKINGD WQRADAVWNK IQEENVIPRE KTLRLLAEIL REGNQEVPFD VPELWYEDEK 1020
HSLNSSSAST TEPDFQKDIL IACRLNQKKG AYDIFLNAKE QNIVFNAETY SNLIKLLMSE 1080
DYFTQAMEVK AFAETHIKGF TLNDAANSRL IITQVRRDYL KEAVTTLKTV LDQQQTPSRL 1140
AVTRVIQALA MKGDVENIEV VQKMLNGLED SIGLSKMVFI NNIALAQIKN NNIDAAIENI 1200
ENMLTSENKV IEPQYFGLAY LFRKVIEEQL EPAVEKISIM AERLANQFAI YKPVTDFFLQ 1260
LVDAGKVDDA RALLQRCGAI AEQTPILLLF LLRNSRKQGK ASTVKSVLEL IPELNEKEEA 1320
YNSLMKSYVS EKDVTSAKAL YEHLTAKNTK LDDLFLKRYA SLLKYAGEPV PFIEPPESFE 1380
FYAQQLRKLR ENSS 1394 
Gene Ontology
 GO:0000794; C:condensed nuclear chromosome; IDA:HGNC.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
 GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
 GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC.
 GO:0048487; F:beta-tubulin binding; IDA:HGNC.
 GO:0008017; F:microtubule binding; TAS:HGNC.
 GO:0003723; F:RNA binding; NAS:UniProtKB.
 GO:0003697; F:single-stranded DNA binding; IEA:Compara.
 GO:0047497; P:mitochondrion transport along microtubule; TAS:HGNC.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR002885; Pentatricopeptide_repeat.
 IPR011990; TPR-like_helical. 
Pfam
 PF01535; PPR 
SMART
  
PROSITE
 PS51375; PPR 
PRINTS