PAPD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PAPD1_HUMAN
• UniProt AC: Q9NVV4
• Protein Name: Poly(A) RNA polymerase, mitochondrial
• Gene Name: MTPAP
• Organism: Homo sapiens (Human).
• Sequence Length: 582
• Subcellular Localization: Cytoplasm . Mitochondrion .
• Protein 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..
• Protein Sequence: MAVPGVGLLTRLNLCARRRTRVQRPIVRLLSCPGTVAKDLRRDEQPSGSVETGFEDKIPKRRFSEMQNERREQAQRTVLIHCPEKISENKFLKYLSQFGPINNHFFYESFGLYAVVEFCQKESIGSLQNGTHTPSTAMETAIPFRSRFFNLKLKNQTSERSRVRSSNQLPRSNKQLFELLCYAESIDDQLNTLLKEFQLTEENTKLRYLTCSLIEDMAAAYFPDCIVRPFGSSVNTFGKLGCDLDMFLDLDETRNLSAHKISGNFLMEFQVKNVPSERIATQKILSVLGECLDHFGPGCVGVQKILNARCPLVRFSHQASGFQCDLTTNNRIALTSSELLYIYGALDSRVRALVFSVRCWARAHSLTSSIPGAWITNFSLTMMVIFFLQRRSPPILPTLDSLKTLADAEDKCVIEGNNCTFVRDLSRIKPSQNTETLELLLKEFFEYFGNFAFDKNSINIRQGREQNKPDSSPLYIQNPFETSLNISKNVSQSQLQKFVDLARESAWILQQEDTDRPSISSNRPWGLVSLLLPSAPNRKSFTKKKSNKFAIETVKNLLESLKGNRTENFTKTSGKRTISTQT

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	VPGVGLLTRLNLCAR CCCCHHHHHHHHHHH	37.85	23532336
31	Phosphorylation	RPIVRLLSCPGTVAK CCHHHHHCCCCCHHH	23.90	-
47	Phosphorylation	LRRDEQPSGSVETGF HHCCCCCCCCCCCCC	43.31	26471730
49	Phosphorylation	RDEQPSGSVETGFED CCCCCCCCCCCCCCC	22.55	26471730
64	Phosphorylation	KIPKRRFSEMQNERR CCCHHHHHHHHHHHH	30.28	29449344
85	Acetylation	VLIHCPEKISENKFL EEEECCHHCCCCHHH	36.35	25953088
85	Ubiquitination	VLIHCPEKISENKFL EEEECCHHCCCCHHH	36.35	29967540
85	Malonylation	VLIHCPEKISENKFL EEEECCHHCCCCHHH	36.35	26320211
90	Ubiquitination	PEKISENKFLKYLSQ CHHCCCCHHHHHHHH	48.28	19608861
90	Succinylation	PEKISENKFLKYLSQ CHHCCCCHHHHHHHH	48.28	27452117
90	Malonylation	PEKISENKFLKYLSQ CHHCCCCHHHHHHHH	48.28	26320211
90	Acetylation	PEKISENKFLKYLSQ CHHCCCCHHHHHHHH	48.28	19608861
152	Ubiquitination	RSRFFNLKLKNQTSE HHHHCCEEECCCCCC	59.53	29967540
154	Ubiquitination	RFFNLKLKNQTSERS HHCCEEECCCCCCHH	45.48	27667366
165	Phosphorylation	SERSRVRSSNQLPRS CCHHHHHCCCCCCCC	30.68	21406692
166	Phosphorylation	ERSRVRSSNQLPRSN CHHHHHCCCCCCCCH	20.31	19691289
172	Phosphorylation	SSNQLPRSNKQLFEL CCCCCCCCHHHHHHH	46.57	21406692
205	Acetylation	QLTEENTKLRYLTCS CCCCCCHHHHHHHHH	42.42	26051181
205	Ubiquitination	QLTEENTKLRYLTCS CCCCCCHHHHHHHHH	42.42	29967540
253	Phosphorylation	MFLDLDETRNLSAHK EEECHHHCCCCEECC	25.23	29759185
262	Phosphorylation	NLSAHKISGNFLMEF CCEECCCCCCEEEEE	32.27	-
282 (in isoform 2)	Ubiquitination	-	23.05	-
283	Ubiquitination	SERIATQKILSVLGE HHHHHHHHHHHHHHH	41.06	21963094
284 (in isoform 2)	Ubiquitination	-	2.20	-
304	Acetylation	PGCVGVQKILNARCP CCCHHHHHHHHCCCC	46.91	26051181
335 (in isoform 2)	Ubiquitination	-	22.61	-
403	Ubiquitination	LPTLDSLKTLADAED CCCHHHHHHHCCCCC	45.50	21906983
403 (in isoform 1)	Ubiquitination	-	45.50	21906983
411	Ubiquitination	TLADAEDKCVIEGNN HHCCCCCCEEEECCC	23.16	21963094
411	Acetylation	TLADAEDKCVIEGNN HHCCCCCCEEEECCC	23.16	25953088
413 (in isoform 2)	Ubiquitination	-	5.71	-
429	Ubiquitination	VRDLSRIKPSQNTET EEEHHHCCCCCCHHH	37.19	29967540
468	Ubiquitination	RQGREQNKPDSSPLY CCCCCCCCCCCCCCE	50.31	23503661
488 (in isoform 1)	Ubiquitination	-	58.53	21906983
488	Ubiquitination	ETSLNISKNVSQSQL HHCCCCCCCCCHHHH	58.53	29967540
491	Phosphorylation	LNISKNVSQSQLQKF CCCCCCCCHHHHHHH	33.24	26471730
493	Phosphorylation	ISKNVSQSQLQKFVD CCCCCCHHHHHHHHH	25.92	25159151
497	Acetylation	VSQSQLQKFVDLARE CCHHHHHHHHHHHHH	56.82	26051181
497	Ubiquitination	VSQSQLQKFVDLARE CCHHHHHHHHHHHHH	56.82	-
533 (in isoform 2)	Ubiquitination	-	28.54	21906983
540	Phosphorylation	PSAPNRKSFTKKKSN CCCCCCCCCCCHHCC	34.61	26074081
541 (in isoform 2)	Ubiquitination	-	15.11	-
548	Ubiquitination	FTKKKSNKFAIETVK CCCHHCCHHHHHHHH	43.17	29967540
553	Phosphorylation	SNKFAIETVKNLLES CCHHHHHHHHHHHHH	30.57	-
555	Ubiquitination	KFAIETVKNLLESLK HHHHHHHHHHHHHCC	49.66	21963094
559 (in isoform 2)	Ubiquitination	-	58.13	-
560	Phosphorylation	TVKNLLESLKGNRTE HHHHHHHHCCCCCCC	35.04	23186163
562	Ubiquitination	KNLLESLKGNRTENF HHHHHHCCCCCCCCC	64.52	29967540
562	Methylation	KNLLESLKGNRTENF HHHHHHCCCCCCCCC	64.52	115974603
575	Ubiquitination	NFTKTSGKRTISTQT CCEECCCCCEEECCC	46.25	24816145
598 (in isoform 2)	Ubiquitination	-		-
618 (in isoform 2)	Ubiquitination	-		21906983
627 (in isoform 2)	Ubiquitination	-		-
685 (in isoform 2)	Ubiquitination	-		-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PAPD1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PAPD1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PAPD1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of PAPD1_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 613672: Spastic ataxia 4, autosomal recessive (SPAX4)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-90, AND MASS SPECTROMETRY.
PubMed: 19608861