dbPTM

PAPOA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PAPOA_HUMAN
UniProt AC	P51003
Protein Name	Poly(A) polymerase alpha
Gene Name	PAPOLA
Organism	Homo sapiens (Human).
Sequence Length	745
Subcellular Localization	Cytoplasm. Nucleus. The 90 kDa form is nuclear while the 100 kDa and the 106 kDa forms are both nuclear and cytoplasmic.
Protein Description	Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus..
Protein Sequence	MPFPVTTQGSQQTQPPQKHYGITSPISLAAPKETDCVLTQKLIETLKPFGVFEEEEELQRRILILGKLNNLVKEWIREISESKNLPQSVIENVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVDRSDFFTSFYDKLKLQEEVKDLRAVEEAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNIDNFRLTLRAIKLWAKRHNIYSNILGFLGGVSWAMLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVWDPRVNPSDRYHLMPIITPAYPQQNSTYNVSVSTRMVMVEEFKQGLAITDEILLSKAEWSKLFEAPNFFQKYKHYIVLLASAPTEKQRLEWVGLVESKIRILVGSLEKNEFITLAHVNPQSFPAPKENPDKEEFRTMWVIGLVFKKTENSENLSVDLTYDIQSFTDTVYRQAINSKMFEVDMKIAAMHVKRKQLHQLLPNHVLQKKKKHSTEGVKLTALNDSSLDLSMDSDNSMSVPSPTSATKTSPLNSSGSSQGRNSPAPAVTAASVTNIQATEVSVPQVNSSESSGGTSSESIPQTATQPAISPPPKPTVSRVVSSTRLVNPPPRSSGNAATSGNAATKIPTPIVGVKRTSSPHKEESPKKTKTEEDETSEDANCLALSGHDKTEAKEQLDTETSTTQSETIQTAASLLASQKTSSTDLSDIPALPANPIPVIKNSIKLRLNR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MPFPVTTQGSQQT --CCCCCCCCCCCCC	17.40	26074081
7	O-linked_Glycosylation	-MPFPVTTQGSQQTQ -CCCCCCCCCCCCCC	31.03	28510447
7	Phosphorylation	-MPFPVTTQGSQQTQ -CCCCCCCCCCCCCC	31.03	26074081
10	Phosphorylation	FPVTTQGSQQTQPPQ CCCCCCCCCCCCCCC	14.86	26074081
13	Phosphorylation	TTQGSQQTQPPQKHY CCCCCCCCCCCCCCC	35.09	26074081
20	Phosphorylation	TQPPQKHYGITSPIS CCCCCCCCCCCCCCC	19.77	23927012
23	Phosphorylation	PQKHYGITSPISLAA CCCCCCCCCCCCCCC	24.88	29255136
24	Phosphorylation	QKHYGITSPISLAAP CCCCCCCCCCCCCCC	20.51	29255136
27	Phosphorylation	YGITSPISLAAPKET CCCCCCCCCCCCCCC	18.49	23927012
32	Acetylation	PISLAAPKETDCVLT CCCCCCCCCCCCCHH	69.40	26051181
32	Ubiquitination	PISLAAPKETDCVLT CCCCCCCCCCCCCHH	69.40	-
41	Ubiquitination	TDCVLTQKLIETLKP CCCCHHHHHHHHHCC	46.31	-
47	Ubiquitination	QKLIETLKPFGVFEE HHHHHHHCCCCCCCC	45.80	-
67	Ubiquitination	RRILILGKLNNLVKE HHHHHHHHHHHHHHH	44.59	-
83	Ubiquitination	IREISESKNLPQSVI HHHHHHCCCCCHHHH	59.46	-
88	Phosphorylation	ESKNLPQSVIENVGG HCCCCCHHHHHHCCC	24.11	20068231
99	Phosphorylation	NVGGKIFTFGSYRLG HCCCEEEEECCEECC	30.47	20068231
102	Phosphorylation	GKIFTFGSYRLGVHT CEEEEECCEECCCCC	11.68	20068231
103	Phosphorylation	KIFTFGSYRLGVHTK EEEEECCEECCCCCC	15.38	20068231
109	Phosphorylation	SYRLGVHTKGADIDA CEECCCCCCCCCCCE	28.85	27422710
110	Ubiquitination	YRLGVHTKGADIDAL EECCCCCCCCCCCEE	36.90	-
118	Glutathionylation	GADIDALCVAPRHVD CCCCCEEEECCCCCC	2.35	22555962
136	Ubiquitination	FFTSFYDKLKLQEEV HHHHHHHHHHHHHHH	35.82	21890473
136 (in isoform 2)	Ubiquitination	-	35.82	21890473
138	Ubiquitination	TSFYDKLKLQEEVKD HHHHHHHHHHHHHHH	54.59	-
144	Acetylation	LKLQEEVKDLRAVEE HHHHHHHHHHHHHHH	55.09	25953088
144	Ubiquitination	LKLQEEVKDLRAVEE HHHHHHHHHHHHHHH	55.09	-
144 (in isoform 2)	Ubiquitination	-	55.09	21890473
152 (in isoform 1)	Ubiquitination	-	9.38	21890473
160 (in isoform 1)	Ubiquitination	-	2.19	21890473
188	Phosphorylation	DLDLRDDSLLKNLDI CCCCCCCHHHHCCCH	39.63	24719451
191	Ubiquitination	LRDDSLLKNLDIRCI CCCCHHHHCCCHHHH	61.84	-
191 (in isoform 2)	Ubiquitination	-	61.84	21890473
207 (in isoform 1)	Ubiquitination	-	14.46	21890473
307	Phosphorylation	WDPRVNPSDRYHLMP CCCCCCHHHCCCCCE	29.53	24275569
310	Phosphorylation	RVNPSDRYHLMPIIT CCCHHHCCCCCEEEC	12.33	-
317	Phosphorylation	YHLMPIITPAYPQQN CCCCEEECCCCCCCC	11.55	23403867
355	Ubiquitination	TDEILLSKAEWSKLF CHHHHCCHHHHHHHH	50.74	-
360	Ubiquitination	LSKAEWSKLFEAPNF CCHHHHHHHHHCCCH	59.26	21890473
370	Ubiquitination	EAPNFFQKYKHYIVL HCCCHHHHCCEEEEE	51.62	-
372	Ubiquitination	PNFFQKYKHYIVLLA CCHHHHCCEEEEEEE	36.65	-
376 (in isoform 1)	Ubiquitination	-	2.56	21890473
380	Phosphorylation	HYIVLLASAPTEKQR EEEEEEEECCCHHHH	34.45	-
444	Sumoylation	WVIGLVFKKTENSEN HHHEEEEECCCCCCC	51.83	-
444	Sumoylation	WVIGLVFKKTENSEN HHHEEEEECCCCCCC	51.83	-
445	Sumoylation	VIGLVFKKTENSENL HHEEEEECCCCCCCE	50.00	-
445	Sumoylation	VIGLVFKKTENSENL HHEEEEECCCCCCCE	50.00	-
474	Phosphorylation	VYRQAINSKMFEVDM HHHHHHHCCHHHHHH	21.27	28851738
482	Acetylation	KMFEVDMKIAAMHVK CHHHHHHHHHHHHHC	25.40	15611779
486	Sulfoxidation	VDMKIAAMHVKRKQL HHHHHHHHHHCHHHH	2.49	30846556
489	Acetylation	KIAAMHVKRKQLHQL HHHHHHHCHHHHHHH	38.92	25953088
509	Phosphorylation	LQKKKKHSTEGVKLT HHCCCCCCCCCCEEE	36.71	30576142
510	Phosphorylation	QKKKKHSTEGVKLTA HCCCCCCCCCCEEEE	36.16	20068231
516	Phosphorylation	STEGVKLTALNDSSL CCCCCEEEECCCCCC	24.31	20873877
521	Phosphorylation	KLTALNDSSLDLSMD EEEECCCCCCCCCCC	31.56	20873877
522	Phosphorylation	LTALNDSSLDLSMDS EEECCCCCCCCCCCC	28.85	25137130
526	Phosphorylation	NDSSLDLSMDSDNSM CCCCCCCCCCCCCCC	21.88	30278072
529	Phosphorylation	SLDLSMDSDNSMSVP CCCCCCCCCCCCCCC	30.01	30278072
532	Phosphorylation	LSMDSDNSMSVPSPT CCCCCCCCCCCCCCC	19.88	20873877
534	Phosphorylation	MDSDNSMSVPSPTSA CCCCCCCCCCCCCCC	30.60	30278072
537	Phosphorylation	DNSMSVPSPTSATKT CCCCCCCCCCCCCCC	38.36	30278072
539	Phosphorylation	SMSVPSPTSATKTSP CCCCCCCCCCCCCCC	35.02	30278072
540	Phosphorylation	MSVPSPTSATKTSPL CCCCCCCCCCCCCCC	37.01	30278072
542	Phosphorylation	VPSPTSATKTSPLNS CCCCCCCCCCCCCCC	34.32	30278072
544	Phosphorylation	SPTSATKTSPLNSSG CCCCCCCCCCCCCCC	31.08	30278072
545	Phosphorylation	PTSATKTSPLNSSGS CCCCCCCCCCCCCCC	29.01	21955146
549	Phosphorylation	TKTSPLNSSGSSQGR CCCCCCCCCCCCCCC	43.70	28450419
550	Phosphorylation	KTSPLNSSGSSQGRN CCCCCCCCCCCCCCC	41.44	28450419
552	Phosphorylation	SPLNSSGSSQGRNSP CCCCCCCCCCCCCCC	22.80	28450419
553	Phosphorylation	PLNSSGSSQGRNSPA CCCCCCCCCCCCCCC	39.93	23927012
558	Phosphorylation	GSSQGRNSPAPAVTA CCCCCCCCCCCCCEE	22.52	25332170
569	Phosphorylation	AVTAASVTNIQATEV CCEEEEEEEEEEEEE	24.90	24275569
586	Phosphorylation	PQVNSSESSGGTSSE CCCCCCCCCCCCCCC	35.91	25332170
605	Phosphorylation	TATQPAISPPPKPTV CCCCCCCCCCCCCCC	33.20	24719451
617	Phosphorylation	PTVSRVVSSTRLVNP CCCEEEEECCEECCC	24.12	22199227
618	Phosphorylation	TVSRVVSSTRLVNPP CCEEEEECCEECCCC	13.11	26699800
619	Phosphorylation	VSRVVSSTRLVNPPP CEEEEECCEECCCCC	22.10	27273156
628	Phosphorylation	LVNPPPRSSGNAATS ECCCCCCCCCCCCCC	48.66	29116813
629	Phosphorylation	VNPPPRSSGNAATSG CCCCCCCCCCCCCCC	37.03	29116813
634	Phosphorylation	RSSGNAATSGNAATK CCCCCCCCCCCCCCC	34.45	29116813
635	Phosphorylation	SSGNAATSGNAATKI CCCCCCCCCCCCCCC	25.89	29116813
640	Phosphorylation	ATSGNAATKIPTPIV CCCCCCCCCCCCCCE	27.39	23312004
641	Acetylation	TSGNAATKIPTPIVG CCCCCCCCCCCCCEE	41.80	25953088
644	Phosphorylation	NAATKIPTPIVGVKR CCCCCCCCCCEEEEC	29.17	22985185
650	Acetylation	PTPIVGVKRTSSPHK CCCCEEEECCCCCCC	43.99	23954790
652	Phosphorylation	PIVGVKRTSSPHKEE CCEEEECCCCCCCCC	28.04	28176443
653	Phosphorylation	IVGVKRTSSPHKEES CEEEECCCCCCCCCC	46.00	28176443
654	Phosphorylation	VGVKRTSSPHKEESP EEEECCCCCCCCCCC	30.34	28176443
660	Phosphorylation	SSPHKEESPKKTKTE CCCCCCCCCCCCCCC	43.01	26055452
662	Sumoylation	PHKEESPKKTKTEED CCCCCCCCCCCCCCC	80.50	-
662	Sumoylation	PHKEESPKKTKTEED CCCCCCCCCCCCCCC	80.50	-
663	Sumoylation	HKEESPKKTKTEEDE CCCCCCCCCCCCCCC	59.65	-
663	Sumoylation	HKEESPKKTKTEEDE CCCCCCCCCCCCCCC	59.65	-
664	Phosphorylation	KEESPKKTKTEEDET CCCCCCCCCCCCCCC	49.69	28450419
666	Phosphorylation	ESPKKTKTEEDETSE CCCCCCCCCCCCCCC	50.25	30576142
671	Phosphorylation	TKTEEDETSEDANCL CCCCCCCCCCHHCCC	50.14	25849741
672	Phosphorylation	KTEEDETSEDANCLA CCCCCCCCCHHCCCH	31.28	30108239
681	Phosphorylation	DANCLALSGHDKTEA HHCCCHHCCCCHHHH	28.60	30108239
685	Acetylation	LALSGHDKTEAKEQL CHHCCCCHHHHHHHH	42.46	26051181
686	Phosphorylation	ALSGHDKTEAKEQLD HHCCCCHHHHHHHHC	47.43	30108239
698	O-linked_Glycosylation	QLDTETSTTQSETIQ HHCCCCCCCHHHHHH	35.95	28510447
699	O-linked_Glycosylation	LDTETSTTQSETIQT HCCCCCCCHHHHHHH	29.84	28510447
701	O-linked_Glycosylation	TETSTTQSETIQTAA CCCCCCHHHHHHHHH	34.32	28510447
713	Phosphorylation	TAASLLASQKTSSTD HHHHHHHCCCCCCCC	31.98	-
716	Phosphorylation	SLLASQKTSSTDLSD HHHHCCCCCCCCHHH	21.92	26846344
717	Phosphorylation	LLASQKTSSTDLSDI HHHCCCCCCCCHHHC	37.97	26846344
718	Phosphorylation	LASQKTSSTDLSDIP HHCCCCCCCCHHHCC	31.04	26846344
719	Phosphorylation	ASQKTSSTDLSDIPA HCCCCCCCCHHHCCC	40.50	26846344
722	Phosphorylation	KTSSTDLSDIPALPA CCCCCCHHHCCCCCC	35.98	26846344
736	Acetylation	ANPIPVIKNSIKLRL CCCCCCCCCEEEEEC	44.89	17172643
738	Phosphorylation	PIPVIKNSIKLRLNR CCCCCCCEEEEECCC	18.99	23401153
740	Acetylation	PVIKNSIKLRLNR-- CCCCCEEEEECCC--	27.63	17172643

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

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HDAC1_HUMAN	HDAC1	physical	17172643
HDAC3_HUMAN	HDAC3	physical	17172643
HDA10_HUMAN	HDAC10	physical	17172643
SIR1_HUMAN	SIRT1	physical	17172643
SIR2_HUMAN	SIRT2	physical	17172643
CPSF6_HUMAN	CPSF6	physical	17172643
CPSF5_HUMAN	NUDT21	physical	17172643
IMB1_HUMAN	KPNB1	physical	17172643
PP1B_HUMAN	PPP1CB	physical	22939629
GNA11_HUMAN	GNA11	physical	26186194
ARBK1_HUMAN	ADRBK1	physical	26344197
CSTF2_HUMAN	CSTF2	physical	26344197
CSTFT_HUMAN	CSTF2T	physical	26344197
CSTF3_HUMAN	CSTF3	physical	26344197
ROA1_HUMAN	HNRNPA1	physical	26344197
SPT5H_HUMAN	SUPT5H	physical	26344197
CIRBP_HUMAN	CIRBP	physical	26496610
RSRC1_HUMAN	RSRC1	physical	26496610
RASN_HUMAN	NRAS	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PAPOA_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND MASSSPECTROMETRY.	19690332 [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 SER-534 AND SER-537, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND MASSSPECTROMETRY.	18669648 [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 SER-24, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553, AND MASSSPECTROMETRY.	15302935 [Abstract]