CPLM-022233

Genbank Nucleotide ID

Poly(A) RNA polymerase, mitochondrial

Protein Synonyms/Alias

PAP; PAP-associated domain-containing protein 1; Polynucleotide adenylyltransferase; Terminal uridylyltransferase 1; TUTase 1; mtPAP

Homo sapiens (Human)

Position	Peptide	Type	References
90	PEKISENKFLKYLSQ	acetylation	[1]
283	SERIATQKILSVLGE	ubiquitination	[2, 3]
403	LPTLDSLKTLADAED	ubiquitination	[4]
411	TLADAEDKCVIEGNN	ubiquitination	[2, 3]
429	VRDLSRIKPSQNTET	ubiquitination	[3]
468	RQGREQNKPDSSPLY	ubiquitination	[5]
488	ETSLNISKNVSQSQL	ubiquitination	[4, 5]
497	VSQSQLQKFVDLARE	ubiquitination	[3]
555	KFAIETVKNLLESLK	ubiquitination	[2, 3, 5, 6]

[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] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[3] 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]
[4] 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]
[5] 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]
[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

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.

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.

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.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

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.

IPR002058; PAP_assoc.