dbPTM

PNPT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PNPT1_HUMAN
UniProt AC	Q8TCS8
Protein Name	Polyribonucleotide nucleotidyltransferase 1, mitochondrial
Gene Name	PNPT1
Organism	Homo sapiens (Human).
Sequence Length	783
Subcellular Localization	Cytoplasm. Mitochondrion. Mitochondrion intermembrane space Peripheral membrane protein.
Protein Description	RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Plays also a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA..
Protein Sequence	MAACRYCCSCLRLRPLSDGPFLLPRRDRALTQLQVRALWSSAGSRAVAVDLGNRKLEISSGKLARFADGSAVVQSGDTAVMVTAVSKTKPSPSQFMPLVVDYRQKAAAAGRIPTNYLRREIGTSDKEILTSRIIDRSIRPLFPAGYFYDTQVLCNLLAVDGVNEPDVLAINGASVALSLSDIPWNGPVGAVRIGIIDGEYVVNPTRKEMSSSTLNLVVAGAPKSQIVMLEASAENILQQDFCHAIKVGVKYTQQIIQGIQQLVKETGVTKRTPQKLFTPSPEIVKYTHKLAMERLYAVFTDYEHDKVSRDEAVNKIRLDTEEQLKEKFPEADPYEIIESFNVVAKEVFRSIVLNEYKRCDGRDLTSLRNVSCEVDMFKTLHGSALFQRGQTQVLCTVTFDSLESGIKSDQVITAINGIKDKNFMLHYEFPPYATNEIGKVTGLNRRELGHGALAEKALYPVIPRDFPFTIRVTSEVLESNGSSSMASACGGSLALMDSGVPISSAVAGVAIGLVTKTDPEKGEIEDYRLLTDILGIEDYNGDMDFKIAGTNKGITALQADIKLPGIPIKIVMEAIQQASVAKKEILQIMNKTISKPRASRKENGPVVETVQVPLSKRAKFVGPGGYNLKKLQAETGVTISQVDEETFSVFAPTPSAMHEARDFITEICKDDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAVLLHNTQLDQRKIKHPTALGLEVGQEIQVKYFGRDPADGRMRLSRKVLQSPATTVVRTLNDRSSIVMGEPISQSSSNSQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MAACRYCCSCLRL --CCHHHHCHHHCEE	9.55	23401153
9	Phosphorylation	AACRYCCSCLRLRPL CHHHHCHHHCEEEEC	16.78	23401153
59	Phosphorylation	GNRKLEISSGKLARF CCCEEEECCCCCEEE	24.54	20860994
60	Phosphorylation	NRKLEISSGKLARFA CCEEEECCCCCEEEC	45.68	30387612
62	Acetylation	KLEISSGKLARFADG EEEECCCCCEEECCC	40.70	25953088
62	Ubiquitination	KLEISSGKLARFADG EEEECCCCCEEECCC	40.70	24816145
70	Phosphorylation	LARFADGSAVVQSGD CEEECCCCEEEECCC	20.59	25247763
75	Phosphorylation	DGSAVVQSGDTAVMV CCCEEEECCCEEEEE	27.33	22210691
86	Phosphorylation	AVMVTAVSKTKPSPS EEEEEEEECCCCCHH	31.95	25247763
88	Phosphorylation	MVTAVSKTKPSPSQF EEEEEECCCCCHHHC	40.45	20068231
89	Malonylation	VTAVSKTKPSPSQFM EEEEECCCCCHHHCC	47.43	32601280
91	Phosphorylation	AVSKTKPSPSQFMPL EEECCCCCHHHCCCE	38.45	20068231
93	Phosphorylation	SKTKPSPSQFMPLVV ECCCCCHHHCCCEEE	40.15	22210691
102	Phosphorylation	FMPLVVDYRQKAAAA CCCEEEEHHHHHHHC	11.88	20068231
114	Phosphorylation	AAAGRIPTNYLRREI HHCCCCCHHHHHHHH	33.84	24719451
123	Phosphorylation	YLRREIGTSDKEILT HHHHHHCCCCHHHHH	39.14	17924679
124	Phosphorylation	LRREIGTSDKEILTS HHHHHCCCCHHHHHH	41.28	17924679
126	2-Hydroxyisobutyrylation	REIGTSDKEILTSRI HHHCCCCHHHHHHHH	46.55	-
126	Acetylation	REIGTSDKEILTSRI HHHCCCCHHHHHHHH	46.55	10736103
130	Phosphorylation	TSDKEILTSRIIDRS CCCHHHHHHHHHCCC	22.94	24719451
184	Ubiquitination	LSLSDIPWNGPVGAV EECCCCCCCCCCCEE	23.81	23503661
190	Ubiquitination	PWNGPVGAVRIGIID CCCCCCCEEEEEEEC	6.40	23503661
200	Phosphorylation	IGIIDGEYVVNPTRK EEEECCEEEECCCCH	18.41	-
246	Acetylation	QDFCHAIKVGVKYTQ HHHHHHHHHCHHHHH	33.45	25038526
250	Acetylation	HAIKVGVKYTQQIIQ HHHHHCHHHHHHHHH	36.33	23954790
250	Ubiquitination	HAIKVGVKYTQQIIQ HHHHHCHHHHHHHHH	36.33	30230243
264	Acetylation	QGIQQLVKETGVTKR HHHHHHHHHHCCCCC	59.14	19608861
264	Succinylation	QGIQQLVKETGVTKR HHHHHHHHHHCCCCC	59.14	23954790
264	Ubiquitination	QGIQQLVKETGVTKR HHHHHHHHHHCCCCC	59.14	23503661
270	Ubiquitination	VKETGVTKRTPQKLF HHHHCCCCCCCCCCC	52.44	23503661
272	Phosphorylation	ETGVTKRTPQKLFTP HHCCCCCCCCCCCCC	31.46	20068230
275	Acetylation	VTKRTPQKLFTPSPE CCCCCCCCCCCCCHH	46.93	88781
275	Ubiquitination	VTKRTPQKLFTPSPE CCCCCCCCCCCCCHH	46.93	29967540
277	Ubiquitination	KRTPQKLFTPSPEIV CCCCCCCCCCCHHHH	14.05	24816145
278	Phosphorylation	RTPQKLFTPSPEIVK CCCCCCCCCCHHHHH	33.04	-
280	Phosphorylation	PQKLFTPSPEIVKYT CCCCCCCCHHHHHHH	31.91	-
285	2-Hydroxyisobutyrylation	TPSPEIVKYTHKLAM CCCHHHHHHHHHHHH	50.52	-
285	Acetylation	TPSPEIVKYTHKLAM CCCHHHHHHHHHHHH	50.52	19608861
285	Malonylation	TPSPEIVKYTHKLAM CCCHHHHHHHHHHHH	50.52	26320211
285	Succinylation	TPSPEIVKYTHKLAM CCCHHHHHHHHHHHH	50.52	27452117
285	Ubiquitination	TPSPEIVKYTHKLAM CCCHHHHHHHHHHHH	50.52	19608861
289	Acetylation	EIVKYTHKLAMERLY HHHHHHHHHHHHHHH	30.09	19608861
289	Succinylation	EIVKYTHKLAMERLY HHHHHHHHHHHHHHH	30.09	27452117
296	Phosphorylation	KLAMERLYAVFTDYE HHHHHHHHHHHCCCC	13.62	-
300	Phosphorylation	ERLYAVFTDYEHDKV HHHHHHHCCCCCCCC	30.95	-
302	Phosphorylation	LYAVFTDYEHDKVSR HHHHHCCCCCCCCCH	16.47	-
306	2-Hydroxyisobutyrylation	FTDYEHDKVSRDEAV HCCCCCCCCCHHHHH	43.98	-
306	Acetylation	FTDYEHDKVSRDEAV HCCCCCCCCCHHHHH	43.98	23954790
306	Malonylation	FTDYEHDKVSRDEAV HCCCCCCCCCHHHHH	43.98	26320211
306	Ubiquitination	FTDYEHDKVSRDEAV HCCCCCCCCCHHHHH	43.98	29967540
315	2-Hydroxyisobutyrylation	SRDEAVNKIRLDTEE CHHHHHHHHCCCCHH	23.70	-
315	Ubiquitination	SRDEAVNKIRLDTEE CHHHHHHHHCCCCHH	23.70	-
327	Acetylation	TEEQLKEKFPEADPY CHHHHHHHCCCCCHH	65.71	25038526
327	Ubiquitination	TEEQLKEKFPEADPY CHHHHHHHCCCCCHH	65.71	29967540
334	Phosphorylation	KFPEADPYEIIESFN HCCCCCHHHHHHHHH	21.95	-
339	Phosphorylation	DPYEIIESFNVVAKE CHHHHHHHHHHHHHH	16.23	-
339	Ubiquitination	DPYEIIESFNVVAKE CHHHHHHHHHHHHHH	16.23	23503661
341	Ubiquitination	YEIIESFNVVAKEVF HHHHHHHHHHHHHHH	36.31	23503661
350	Phosphorylation	VAKEVFRSIVLNEYK HHHHHHHHHHHHCCC	12.94	20068231
356	Phosphorylation	RSIVLNEYKRCDGRD HHHHHHCCCCCCCCC	11.58	28152594
357	2-Hydroxyisobutyrylation	SIVLNEYKRCDGRDL HHHHHCCCCCCCCCC	40.13	-
357	Acetylation	SIVLNEYKRCDGRDL HHHHHCCCCCCCCCC	40.13	25953088
357	Succinylation	SIVLNEYKRCDGRDL HHHHHCCCCCCCCCC	40.13	23954790
357	Ubiquitination	SIVLNEYKRCDGRDL HHHHHCCCCCCCCCC	40.13	24816145
371	Phosphorylation	LTSLRNVSCEVDMFK CHHHCCCEEEEECHH	14.22	28509920
376	Ubiquitination	NVSCEVDMFKTLHGS CCEEEEECHHHHHHH	4.48	23503661
378	2-Hydroxyisobutyrylation	SCEVDMFKTLHGSAL EEEEECHHHHHHHHH	43.47	-
378	Acetylation	SCEVDMFKTLHGSAL EEEEECHHHHHHHHH	43.47	25038526
378	Ubiquitination	SCEVDMFKTLHGSAL EEEEECHHHHHHHHH	43.47	-
419	Ubiquitination	ITAINGIKDKNFMLH EEEECCCCCCCEEEE	65.14	23503661
421	Ubiquitination	AINGIKDKNFMLHYE EECCCCCCCEEEEEE	47.27	23503661
439	Acetylation	YATNEIGKVTGLNRR CCCCCHHCCCCCCHH	42.14	23954790
456	2-Hydroxyisobutyrylation	GHGALAEKALYPVIP CCCHHHHHHHCCCCC	37.78	-
456	Ubiquitination	GHGALAEKALYPVIP CCCHHHHHHHCCCCC	37.78	23503661
459	Phosphorylation	ALAEKALYPVIPRDF HHHHHHHCCCCCCCC	10.58	-
469	Phosphorylation	IPRDFPFTIRVTSEV CCCCCCEEEEEEHHH	14.22	24719451
473	Phosphorylation	FPFTIRVTSEVLESN CCEEEEEEHHHHHCC	14.88	-
474	Phosphorylation	PFTIRVTSEVLESNG CEEEEEEHHHHHCCC	23.89	-
511	Ubiquitination	SAVAGVAIGLVTKTD HHHHHHHEEEEECCC	3.99	21890473
521	Acetylation	VTKTDPEKGEIEDYR EECCCCCCCCCCCHH	68.20	23954790
521	Malonylation	VTKTDPEKGEIEDYR EECCCCCCCCCCCHH	68.20	26320211
521	Ubiquitination	VTKTDPEKGEIEDYR EECCCCCCCCCCCHH	68.20	24816145
552	2-Hydroxyisobutyrylation	FKIAGTNKGITALQA EEEEECCCCEEEEEC	52.07	-
552	Malonylation	FKIAGTNKGITALQA EEEEECCCCEEEEEC	52.07	26320211
552	Succinylation	FKIAGTNKGITALQA EEEEECCCCEEEEEC	52.07	-
552	Succinylation	FKIAGTNKGITALQA EEEEECCCCEEEEEC	52.07	27452117
562	Succinylation	TALQADIKLPGIPIK EEEECCCCCCCCCHH	49.53	23954790
569	Methylation	KLPGIPIKIVMEAIQ CCCCCCHHHHHHHHH	24.72	23644510
582	2-Hydroxyisobutyrylation	IQQASVAKKEILQIM HHHHHHHHHHHHHHH	49.10	-
582	Succinylation	IQQASVAKKEILQIM HHHHHHHHHHHHHHH	49.10	23954790
582	Ubiquitination	IQQASVAKKEILQIM HHHHHHHHHHHHHHH	49.10	-
583	Malonylation	QQASVAKKEILQIMN HHHHHHHHHHHHHHH	40.00	26320211
583	Succinylation	QQASVAKKEILQIMN HHHHHHHHHHHHHHH	40.00	23954790
591	Acetylation	EILQIMNKTISKPRA HHHHHHHHHCCCCCH	29.83	19608861
591	Ubiquitination	EILQIMNKTISKPRA HHHHHHHHHCCCCCH	29.83	19608861
592	Phosphorylation	ILQIMNKTISKPRAS HHHHHHHHCCCCCHH	26.02	-
601	Ubiquitination	SKPRASRKENGPVVE CCCCHHCCCCCCEEE	53.70	24816145
616	Acetylation	TVQVPLSKRAKFVGP EEEEECHHCCCEECC	65.15	25953088
619	Acetylation	VPLSKRAKFVGPGGY EECHHCCCEECCCCC	44.61	25953088
626	Phosphorylation	KFVGPGGYNLKKLQA CEECCCCCCHHHCCC	24.20	-
629	2-Hydroxyisobutyrylation	GPGGYNLKKLQAETG CCCCCCHHHCCCCCC	48.04	-
629	Acetylation	GPGGYNLKKLQAETG CCCCCCHHHCCCCCC	48.04	25953088
629	Succinylation	GPGGYNLKKLQAETG CCCCCCHHHCCCCCC	48.04	23954790
629	Ubiquitination	GPGGYNLKKLQAETG CCCCCCHHHCCCCCC	48.04	29967540
630	Ubiquitination	PGGYNLKKLQAETGV CCCCCHHHCCCCCCC	49.34	-
665	Phosphorylation	HEARDFITEICKDDQ HHHHHHHHHHCCCCH	21.20	-
670	Ubiquitination	FITEICKDDQEQQLE HHHHHCCCCHHHHHE	59.42	24816145
683	Phosphorylation	LEFGAVYTATITEIR HECCCEEEEEEEEEC	15.66	-
687	Phosphorylation	AVYTATITEIRDTGV CEEEEEEEEECCCCE	22.47	-
692	Phosphorylation	TITEIRDTGVMVKLY EEEEECCCCEEEEEC	23.10	20068231
721	Phosphorylation	QRKIKHPTALGLEVG HHCCCCCCHHCCCCC	33.94	-
750	Ubiquitination	GRMRLSRKVLQSPAT CCHHHCHHHHHCCCE	43.87	24816145
754	Phosphorylation	LSRKVLQSPATTVVR HCHHHHHCCCEEEEE	16.61	25159151
758	Phosphorylation	VLQSPATTVVRTLND HHHCCCEEEEEECCC	21.07	17525332
767	Phosphorylation	VRTLNDRSSIVMGEP EEECCCCCCEEECCC	27.55	23663014
771	Sulfoxidation	NDRSSIVMGEPISQS CCCCCEEECCCCCCC	4.85	21406390
776	Phosphorylation	IVMGEPISQSSSNSQ EEECCCCCCCCCCCC	34.42	23663014
778	Phosphorylation	MGEPISQSSSNSQ-- ECCCCCCCCCCCC--	29.01	23663014
779	Phosphorylation	GEPISQSSSNSQ--- CCCCCCCCCCCC---	26.38	23663014
780	Phosphorylation	EPISQSSSNSQ---- CCCCCCCCCCC----	45.83	23663014
782	Phosphorylation	ISQSSSNSQ------ CCCCCCCCC------	38.93	17525332

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
776	S	Phosphorylation	Kinase	PRKDC	P78527	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PNPT1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PNPT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAGP1_HUMAN	RANGAP1	physical	22939629
PTBP1_HUMAN	PTBP1	physical	22939629
CLCB_HUMAN	CLTB	physical	26344197
IF4A1_HUMAN	EIF4A1	physical	26344197
MPPA_HUMAN	PMPCA	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614932	Combined oxidative phosphorylation deficiency 13 (COXPD13)
614934	Deafness, autosomal recessive, 70 (DFNB70)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PNPT1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-264; LYS-285; LYS-289 ANDLYS-591, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-758; SER-776 ANDSER-782, AND MASS SPECTROMETRY.	17525332 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-123 AND SER-124, ANDMASS SPECTROMETRY.	17924679 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-356, AND MASSSPECTROMETRY.	19413330 [Abstract]