CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022234
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Poly(A) RNA polymerase, mitochondrial 
Protein Synonyms/Alias
 PAP; PAP-associated domain-containing protein 1; Polynucleotide adenylyltransferase; Terminal uridylyltransferase 1; TUTase 1; mtPAP 
Gene Name
 MTPAP 
Gene Synonyms/Alias
 PAPD1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
282RSRFFNLKLKNQTSEubiquitination[1]
284RFFNLKLKNQTSERSubiquitination[1]
335QLTEENTKLRYLTCSubiquitination[1]
413SERIATQKILSVLGEubiquitination[1]
541TLADAEDKCVIEGNNubiquitination[1]
559VRDLSRIKPSQNTETubiquitination[1]
598RQGREQNKPDSSPLYubiquitination[2]
618ETSLNISKNVSQSQLubiquitination[2]
627VSQSQLQKFVDLAREubiquitination[1]
685KFAIETVKNLLESLKubiquitination[1, 2]
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] 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
Functional Description
 Polymerase that creates the 3' poly(A) tail of mitochondrial transcripts. Can use all four nucleotides, but has higher activity with ATP and UTP (in vitro). Plays a role in replication-dependent histone mRNA degradation. May be involved in the terminal uridylation of mature histone mRNAs before their degradation is initiated. Might be responsible for the creation of some UAA stop codons which are not encoded in mtDNA. 
Sequence Annotation
 DOMAIN 437 483 PAP-associated.
 NP_BIND 107 109 ATP (Potential).
 NP_BIND 241 242 ATP (Potential).
 METAL 243 243 Magnesium or manganese; catalytic (By
 METAL 245 245 Magnesium or manganese; catalytic (By
 MOD_RES 90 90 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Disease mutation; Magnesium; Manganese; Metal-binding; Mitochondrion; mRNA processing; Neurodegeneration; Nucleotide-binding; Nucleotidyltransferase; Polymorphism; Reference proteome; RNA-binding; Transcription; Transferase; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 582 AA 
Protein Sequence
MAWAKKVGGR AGQGRSLSRC DPIILDPEWL YGPPEGEGGP EGVGGETRAS IHPPLRTGRH 60
HQKVNHNIRG PEGSAKDAAP GGGGHHQAGP GQRGDEDGAL QHLCGGGGGV GVSVGRGTGT 120
SVAAEHPSLQ VKLLELQELV LRLAGDHNEG HGKFLAAAQN PADDPAPGAP APQELGAADK 180
QGGFEDKIPK RRFSEMQNER REQAQRTVLI HCPEKISENK FLKYLSQFGP INNHFFYESF 240
GLYAVVEFCQ KESIGSLQNG THTPSTAMET AIPFRSRFFN LKLKNQTSER SRVRSSNQLP 300
RSNKQLFELL CYAESIDDQL NTLLKEFQLT EENTKLRYLT CSLIEDMAAA YFPDCIVRPF 360
GSSVNTFGKL GCDLDMFLDL DETRNLSAHK ISGNFLMEFQ VKNVPSERIA TQKILSVLGE 420
CLDHFGPGCV GVQKILNARC PLVRFSHQAS GFQCDLTTNN RIALTSSELL YIYGALDSRV 480
RALVFSVRCW ARAHSLTSSI PGAWITNFSL TMMVIFFLQR RSPPILPTLD SLKTLADAED 540
KCVIEGNNCT FVRDLSRIKP SQNTETLELL LKEFFEYFGN FAFDKNSINI RQGREQNKPD 600
SSPLYIQNPF ETSLNISKNV SQSQLQKFVD LARESAWILQ QEDTDRPSIS SNRPWGLVSL 660
LLPSAPNRKS FTKKKSNKFA IETVKNLLES LKGNRTENFT KTSGKRTIST QT 712 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0030145; F:manganese ion binding; IDA:UniProtKB.
 GO:0004652; F:polynucleotide adenylyltransferase activity; IDA:UniProtKB.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0002134; F:UTP binding; IDA:UniProtKB.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0071044; P:histone mRNA catabolic process; IMP:UniProtKB.
 GO:0006378; P:mRNA polyadenylation; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR002058; PAP_assoc. 
Pfam
 PF03828; PAP_assoc 
SMART
  
PROSITE
  
PRINTS