dbPTM

PAPOG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PAPOG_HUMAN
UniProt AC	Q9BWT3
Protein Name	Poly(A) polymerase gamma
Gene Name	PAPOLG
Organism	Homo sapiens (Human).
Sequence Length	736
Subcellular Localization	Nucleus .
Protein Description	Responsible for the post-transcriptional adenylation of the 3'-terminal of mRNA precursors and several small RNAs including signal recognition particle (SRP) RNA, nuclear 7SK RNA, U2 small nuclear RNA, and ribosomal 5S RNA..
Protein Sequence	MKEMSANTVLDSQRQQKHYGITSPISLASPKEIDHIYTQKLIDAMKPFGVFEDEEELNHRLVVLGKLNNLVKEWISDVSESKNLPPSVVATVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVERSDFFQSFFEKLKHQDGIRNLRAVEDAFVPVIKFEFDGIEIDLVFARLAIQTISDNLDLRDDSRLRSLDIRCIRSLNGCRVTDEILHLVPNKETFRLTLRAVKLWAKRRGIYSNMLGFLGGVSWAMLVARTCQLYPNAAASTLVHKFFLVFSKWEWPNPVLLKQPEESNLNLPVWDPRVNPSDRYHLMPIITPAYPQQNSTYNVSTSTRTVMVEEFKQGLAVTDEILQGKSDWSKLLEPPNFFQKYRHYIVLTASASTEENHLEWVGLVESKIRVLVGNLERNEFITLAHVNPQSFPGNKEHHKDNNYVSMWFLGIIFRRVENAESVNIDLTYDIQSFTDTVYRQANNINMLKEGMKIEATHVKKKQLHHYLPAEILQKKKKQSLSDVNRSSGGLQSKRLSLDSSCLDSSRDTDNGTPFNSPASKSDSPSVGETERNSAEPAAVIVEKPLSVPPAQGLSIPVIGAKVDSTVKTVSPPTVCTIPTVVGRNVIPRITTPHNPAQGQPHLNGMSNITKTVTPKRSHSPSIDGTPKRLKDVEKFIRLESTFKDPRTAEERKRKSVDAIGGESMPIPTIDTSRKKRLPSKELPDSSSPVPANNIRVIKNSIRLTLNR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MKEMSANTV ------CCCCCCCHH	63.22	21406692
2	Methylation	------MKEMSANTV ------CCCCCCCHH	63.22	115974597
5	Phosphorylation	---MKEMSANTVLDS ---CCCCCCCHHCCH	21.32	21406692
8	Phosphorylation	MKEMSANTVLDSQRQ CCCCCCCHHCCHHHH	23.35	21406692
9	Ubiquitination	KEMSANTVLDSQRQQ CCCCCCHHCCHHHHH	5.84	-
12	Phosphorylation	SANTVLDSQRQQKHY CCCHHCCHHHHHHHH	24.09	21406692
19	Phosphorylation	SQRQQKHYGITSPIS HHHHHHHHCCCCCCC	19.77	20068231
22	Phosphorylation	QQKHYGITSPISLAS HHHHHCCCCCCCCCC	24.88	25159151
22	Ubiquitination	QQKHYGITSPISLAS HHHHHCCCCCCCCCC	24.88	-
23	Phosphorylation	QKHYGITSPISLASP HHHHCCCCCCCCCCH	20.51	25159151
26	Phosphorylation	YGITSPISLASPKEI HCCCCCCCCCCHHHC	22.67	22617229
29	Phosphorylation	TSPISLASPKEIDHI CCCCCCCCHHHCCCC	41.62	25159151
31	Ubiquitination	PISLASPKEIDHIYT CCCCCCHHHCCCCHH	65.88	29967540
40	Ubiquitination	IDHIYTQKLIDAMKP CCCCHHHHHHHHHCC	39.34	29967540
46	Ubiquitination	QKLIDAMKPFGVFED HHHHHHHCCCCCCCC	38.63	29967540
66	Ubiquitination	HRLVVLGKLNNLVKE HHHHHHHHHHHHHHH	43.83	29967540
72	Ubiquitination	GKLNNLVKEWISDVS HHHHHHHHHHHHCCH	50.96	29967540
87	Phosphorylation	ESKNLPPSVVATVGG HHCCCCCCEEEEECC	27.55	20068231
91	Phosphorylation	LPPSVVATVGGKIFT CCCCEEEEECCEEEE	14.20	20068231
98	Phosphorylation	TVGGKIFTFGSYRLG EECCEEEEECCEEEE	30.47	20068231
101	Phosphorylation	GKIFTFGSYRLGVHT CEEEEECCEEEECCC	11.68	20068231
102	Phosphorylation	KIFTFGSYRLGVHTK EEEEECCEEEECCCC	15.38	20068231
108	Phosphorylation	SYRLGVHTKGADIDA CEEEECCCCCCCCCE	28.85	27422710
109	Ubiquitination	YRLGVHTKGADIDAL EEEECCCCCCCCCEE	36.90	-
117	Glutathionylation	GADIDALCVAPRHVE CCCCCEEEECCCCHH	2.35	22555962
135	Ubiquitination	FFQSFFEKLKHQDGI HHHHHHHHHCCCCHH	58.65	-
137	Ubiquitination	QSFFEKLKHQDGIRN HHHHHHHCCCCHHCC	50.73	-
176	Phosphorylation	FARLAIQTISDNLDL HHHHHHHHHHHCCCC	19.14	23403867
178	Phosphorylation	RLAIQTISDNLDLRD HHHHHHHHHCCCCCC	24.67	23403867
231	Acetylation	RAVKLWAKRRGIYSN HHHHHHHHHHCHHHH	30.92	30591129
306	Phosphorylation	WDPRVNPSDRYHLMP CCCCCCHHHCCCEEE	29.53	24275569
309	Phosphorylation	RVNPSDRYHLMPIIT CCCHHHCCCEEEEEC	12.33	23403867
311	Ubiquitination	NPSDRYHLMPIITPA CHHHCCCEEEEECCC	3.02	24816145
316	Phosphorylation	YHLMPIITPAYPQQN CCEEEEECCCCCCCC	11.55	23403867
324	Phosphorylation	PAYPQQNSTYNVSTS CCCCCCCCCCCCCCC	28.12	23403867
331	Phosphorylation	STYNVSTSTRTVMVE CCCCCCCCCCEEEHH	14.37	23403867
332	Phosphorylation	TYNVSTSTRTVMVEE CCCCCCCCCEEEHHH	30.37	23403867
334	Phosphorylation	NVSTSTRTVMVEEFK CCCCCCCEEEHHHHH	17.03	23403867
341	Ubiquitination	TVMVEEFKQGLAVTD EEEHHHHHHCCCCCH	46.89	29967540
347	Phosphorylation	FKQGLAVTDEILQGK HHHCCCCCHHHHCCC	23.47	26714015
354	Ubiquitination	TDEILQGKSDWSKLL CHHHHCCCCCHHHHC	32.08	29967540
432	Phosphorylation	EHHKDNNYVSMWFLG HHCCCCCCCHHHHHH	10.52	25884760
477	Ubiquitination	ANNINMLKEGMKIEA HHCCCHHHHCCEEEE	41.26	-
481	Sumoylation	NMLKEGMKIEATHVK CHHHHCCEEEEEECC	48.53	-
481	Sumoylation	NMLKEGMKIEATHVK CHHHHCCEEEEEECC	48.53	-
488	Ubiquitination	KIEATHVKKKQLHHY EEEEEECCHHHHHHH	46.80	-
489	Ubiquitination	IEATHVKKKQLHHYL EEEEECCHHHHHHHC	44.67	29967540
490	Ubiquitination	EATHVKKKQLHHYLP EEEECCHHHHHHHCC	52.99	29967540
503	Ubiquitination	LPAEILQKKKKQSLS CCHHHHHHHHHCCHH	64.21	29967540
505	Ubiquitination	AEILQKKKKQSLSDV HHHHHHHHHCCHHHH	64.18	24816145
506	Ubiquitination	EILQKKKKQSLSDVN HHHHHHHHCCHHHHC	54.74	29967540
508	Phosphorylation	LQKKKKQSLSDVNRS HHHHHHCCHHHHCCC	38.43	25159151
510	Phosphorylation	KKKKQSLSDVNRSSG HHHHCCHHHHCCCCC	44.77	23663014
515	Phosphorylation	SLSDVNRSSGGLQSK CHHHHCCCCCCCCCC	28.29	23403867
516	Phosphorylation	LSDVNRSSGGLQSKR HHHHCCCCCCCCCCC	33.37	23403867
525	Phosphorylation	GLQSKRLSLDSSCLD CCCCCCEECCCHHHC	33.88	23401153
528	Phosphorylation	SKRLSLDSSCLDSSR CCCEECCCHHHCCCC	28.39	23927012
529	Phosphorylation	KRLSLDSSCLDSSRD CCEECCCHHHCCCCC	20.54	29978859
533	Phosphorylation	LDSSCLDSSRDTDNG CCCHHHCCCCCCCCC	17.83	23927012
534	Phosphorylation	DSSCLDSSRDTDNGT CCHHHCCCCCCCCCC	33.57	29116813
537	Phosphorylation	CLDSSRDTDNGTPFN HHCCCCCCCCCCCCC	30.19	26546556
541	Phosphorylation	SRDTDNGTPFNSPAS CCCCCCCCCCCCCCC	30.84	26546556
545	Phosphorylation	DNGTPFNSPASKSDS CCCCCCCCCCCCCCC	23.40	21815630
548	Phosphorylation	TPFNSPASKSDSPSV CCCCCCCCCCCCCCC	35.76	26546556
549	Ubiquitination	PFNSPASKSDSPSVG CCCCCCCCCCCCCCC	61.46	24816145
550	Phosphorylation	FNSPASKSDSPSVGE CCCCCCCCCCCCCCC	40.60	21815630
552	Phosphorylation	SPASKSDSPSVGETE CCCCCCCCCCCCCCC	26.60	25159151
554	Phosphorylation	ASKSDSPSVGETERN CCCCCCCCCCCCCCC	46.86	22199227
558	Phosphorylation	DSPSVGETERNSAEP CCCCCCCCCCCCCCC	34.02	22199227
562	Phosphorylation	VGETERNSAEPAAVI CCCCCCCCCCCCEEE	39.98	22199227
593	Phosphorylation	VIGAKVDSTVKTVSP EECEEECCCCCCCCC	37.78	23312004
594	Phosphorylation	IGAKVDSTVKTVSPP ECEEECCCCCCCCCC	22.89	23312004
597	Phosphorylation	KVDSTVKTVSPPTVC EECCCCCCCCCCEEE	23.14	30266825
599	Phosphorylation	DSTVKTVSPPTVCTI CCCCCCCCCCEEEEC	30.32	30266825
602	Phosphorylation	VKTVSPPTVCTIPTV CCCCCCCEEEECCCC	31.43	30266825
605	Phosphorylation	VSPPTVCTIPTVVGR CCCCEEEECCCCCCC	26.17	26552605
608	Phosphorylation	PTVCTIPTVVGRNVI CEEEECCCCCCCCCC	24.79	26552605
620	Phosphorylation	NVIPRITTPHNPAQG CCCCCCCCCCCCCCC	21.85	25159151
642	Phosphorylation	SNITKTVTPKRSHSP CCCCEECCCCCCCCC	28.46	24719451
646	Phosphorylation	KTVTPKRSHSPSIDG EECCCCCCCCCCCCC	34.15	23401153
648	Phosphorylation	VTPKRSHSPSIDGTP CCCCCCCCCCCCCCC	22.91	29255136
650	Phosphorylation	PKRSHSPSIDGTPKR CCCCCCCCCCCCCCC	36.00	30266825
654	Phosphorylation	HSPSIDGTPKRLKDV CCCCCCCCCCCHHHH	23.14	23927012
669	Phosphorylation	EKFIRLESTFKDPRT HHHHHHHHHCCCCCC	43.68	28555341
684	Phosphorylation	AEERKRKSVDAIGGE HHHHHHHCCCCCCCC	29.30	25159151
692	Phosphorylation	VDAIGGESMPIPTID CCCCCCCCCCCCCCC	32.88	20068231
697	Phosphorylation	GESMPIPTIDTSRKK CCCCCCCCCCCCCCC	32.00	20068231
700	Phosphorylation	MPIPTIDTSRKKRLP CCCCCCCCCCCCCCC	26.95	20068231
701	Phosphorylation	PIPTIDTSRKKRLPS CCCCCCCCCCCCCCC	38.05	20068231
708	Phosphorylation	SRKKRLPSKELPDSS CCCCCCCCCCCCCCC	43.27	23401153
709	Acetylation	RKKRLPSKELPDSSS CCCCCCCCCCCCCCC	62.42	26051181
714	Phosphorylation	PSKELPDSSSPVPAN CCCCCCCCCCCCCHH	30.67	23927012
715	Phosphorylation	SKELPDSSSPVPANN CCCCCCCCCCCCHHH	46.14	29255136
716	Phosphorylation	KELPDSSSPVPANNI CCCCCCCCCCCHHHC	33.59	29255136
729	Phosphorylation	NIRVIKNSIRLTLNR HCEEEECEEEEECCC	12.23	-
731	Methylation	RVIKNSIRLTLNR-- EEEECEEEEECCC--	22.80	115486395

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 PAPOG_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SYHC_HUMAN	HARS	physical	26344197
HNRPR_HUMAN	HNRNPR	physical	26344197

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 PAPOG_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-684, 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 THR-597 AND SER-599, 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-23; SER-648; THR-654 ANDSER-684, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599, AND MASSSPECTROMETRY.	18220336 [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-29, AND MASSSPECTROMETRY.	15302935 [Abstract]