dbPTM

RPAP3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPAP3_HUMAN
UniProt AC	Q9H6T3
Protein Name	RNA polymerase II-associated protein 3
Gene Name	RPAP3
Organism	Homo sapiens (Human).
Sequence Length	665
Subcellular Localization
Protein Description	Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation..
Protein Sequence	MTSANKAIELQLQVKQNAEELQDFMRDLENWEKDIKQKDMELRRQNGVPEENLPPIRNGNFRKKKKGKAKESSKKTREENTKNRIKSYDYEAWAKLDVDRILDELDKDDSTHESLSQESESEEDGIHVDSQKALVLKEKGNKYFKQGKYDEAIDCYTKGMDADPYNPVLPTNRASAYFRLKKFAVAESDCNLAVALNRSYTKAYSRRGAARFALQKLEEAKKDYERVLELEPNNFEATNELRKISQALASKENSYPKEADIVIKSTEGERKQIEAQQNKQQAISEKDRGNGFFKEGKYERAIECYTRGIAADGANALLPANRAMAYLKIQKYEEAEKDCTQAILLDGSYSKAFARRGTARTFLGKLNEAKQDFETVLLLEPGNKQAVTELSKIKKELIEKGHWDDVFLDSTQRQNVVKPIDNPPHPGSTKPLKKVIIEETGNLIQTIDVPDSTTAAAPENNPINLANVIAATGTTSKKNSSQDDLFPTSDTPRAKVLKIEEVSDTSSLQPQASLKQDVCQSYSEKMPIEIEQKPAQFATTVLPPIPANSFQLESDFRQLKSSPDMLYQYLKQIEPSLYPKLFQKNLDPDVFNQIVKILHDFYIEKEKPLLIFEILQRLSELKRFDMAVMFMSETEKKIARALFNHIDKSGLKDSSVEELKKRYGG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MTSANKAIE ------CCCHHHHHH	36.22	22814378
15	Ubiquitination	IELQLQVKQNAEELQ HHHHHHHHCCHHHHH	25.52	32015554
33	Ubiquitination	RDLENWEKDIKQKDM HHHHHHHHHHHHHHH	57.26	29967540
57	Acetylation	EENLPPIRNGNFRKK HHHCCCCCCCCHHHC	51.26	19608861
63	Ubiquitination	IRNGNFRKKKKGKAK CCCCCHHHCCCCCCC	65.88	24816145
81	Phosphorylation	KKTREENTKNRIKSY HHHHHHHHCHHHHHC	32.73	-
84	Ubiquitination	REENTKNRIKSYDYE HHHHHCHHHHHCCHH	38.99	29967540
86	Ubiquitination	ENTKNRIKSYDYEAW HHHCHHHHHCCHHHH	39.46	29967540
87	Phosphorylation	NTKNRIKSYDYEAWA HHCHHHHHCCHHHHH	22.36	25159151
88	Phosphorylation	TKNRIKSYDYEAWAK HCHHHHHCCHHHHHC	19.97	28796482
90	Phosphorylation	NRIKSYDYEAWAKLD HHHHHCCHHHHHCCC	10.18	25159151
92	Ubiquitination	IKSYDYEAWAKLDVD HHHCCHHHHHCCCHH	12.80	29967540
110	Phosphorylation	DELDKDDSTHESLSQ HHHCCCCCCCHHHHC	41.62	30266825
111	Phosphorylation	ELDKDDSTHESLSQE HHCCCCCCCHHHHCC	36.34	30266825
114	Phosphorylation	KDDSTHESLSQESES CCCCCCHHHHCCCCC	26.22	30266825
116	Phosphorylation	DSTHESLSQESESEE CCCCHHHHCCCCCCC	40.98	22167270
119	Phosphorylation	HESLSQESESEEDGI CHHHHCCCCCCCCCC	38.49	22167270
120	Ubiquitination	ESLSQESESEEDGIH HHHHCCCCCCCCCCC	62.51	24816145
121	Phosphorylation	SLSQESESEEDGIHV HHHCCCCCCCCCCCC	56.41	22167270
130	Phosphorylation	EDGIHVDSQKALVLK CCCCCCCCCCEEEEE	32.27	30266825
137	Malonylation	SQKALVLKEKGNKYF CCCEEEEEECCCCHH	50.31	26320211
137	Acetylation	SQKALVLKEKGNKYF CCCEEEEEECCCCHH	50.31	25953088
149	Phosphorylation	KYFKQGKYDEAIDCY CHHHCCCCCHHHHHC	26.32	-
158	Ubiquitination	EAIDCYTKGMDADPY HHHHHCCCCCCCCCC	26.26	32015554
160	Sulfoxidation	IDCYTKGMDADPYNP HHHCCCCCCCCCCCC	4.01	30846556
165	Phosphorylation	KGMDADPYNPVLPTN CCCCCCCCCCCCCCC	32.42	27642862
171	Phosphorylation	PYNPVLPTNRASAYF CCCCCCCCCCHHHHH	32.93	28555341
177	Phosphorylation	PTNRASAYFRLKKFA CCCCHHHHHHHCHHE	6.17	-
198	Methylation	NLAVALNRSYTKAYS CHHHHCCCCCHHHHH	31.71	115491535
211	Ubiquitination	YSRRGAARFALQKLE HHHHHHHHHHHHHHH	19.48	29967540
216	Acetylation	AARFALQKLEEAKKD HHHHHHHHHHHHHHH	59.73	19608861
222	Ubiquitination	QKLEEAKKDYERVLE HHHHHHHHHHHHHHH	73.01	24816145
224	Phosphorylation	LEEAKKDYERVLELE HHHHHHHHHHHHHCC	17.95	-
243	Ubiquitination	EATNELRKISQALAS HHHHHHHHHHHHHHH	60.37	29967540
251	Ubiquitination	ISQALASKENSYPKE HHHHHHHCCCCCCCC	56.14	29967540
254	Phosphorylation	ALASKENSYPKEADI HHHHCCCCCCCCCCE	43.85	24719451
271	Acetylation	KSTEGERKQIEAQQN ECCHHHHHHHHHHHH	51.86	19827715
279	Ubiquitination	QIEAQQNKQQAISEK HHHHHHHHHHHHHHH	39.18	24816145
284	Phosphorylation	QNKQQAISEKDRGNG HHHHHHHHHHHCCCC	41.43	-
307	Methylation	RAIECYTRGIAADGA HHHHHHHHCCCCCCH	14.19	115491527
326	Phosphorylation	PANRAMAYLKIQKYE CHHHHHHHHHHHCHH	8.74	20068231
328	Acetylation	NRAMAYLKIQKYEEA HHHHHHHHHHCHHHH	30.34	25953088
328	Malonylation	NRAMAYLKIQKYEEA HHHHHHHHHHCHHHH	30.34	26320211
349	Phosphorylation	AILLDGSYSKAFARR HHHHCCCHHHHHHHH	21.51	28555341
356	Ubiquitination	YSKAFARRGTARTFL HHHHHHHHHHHHHHH	43.30	32015554
358	Phosphorylation	KAFARRGTARTFLGK HHHHHHHHHHHHHHH	15.91	22210691
370	Ubiquitination	LGKLNEAKQDFETVL HHHHHHHHCCCEEEE	44.19	29967540
388	Phosphorylation	PGNKQAVTELSKIKK CCCHHHHHHHHHHHH	33.94	21406692
391	Phosphorylation	KQAVTELSKIKKELI HHHHHHHHHHHHHHH	26.55	21406692
410	Phosphorylation	WDDVFLDSTQRQNVV CCCCCCCCCCCCCCC	28.69	21406692
411	Phosphorylation	DDVFLDSTQRQNVVK CCCCCCCCCCCCCCC	27.69	21406692
452	Phosphorylation	QTIDVPDSTTAAAPE EEEECCCCCCCCCCC	22.91	26074081
453	Phosphorylation	TIDVPDSTTAAAPEN EEECCCCCCCCCCCC	28.03	26074081
454	Phosphorylation	IDVPDSTTAAAPENN EECCCCCCCCCCCCC	20.46	26074081
472	Phosphorylation	LANVIAATGTTSKKN HHHHHHHHCCCCCCC	26.49	26074081
474	Phosphorylation	NVIAATGTTSKKNSS HHHHHHCCCCCCCCC	24.44	26074081
475	Phosphorylation	VIAATGTTSKKNSSQ HHHHHCCCCCCCCCC	39.63	26074081
476	Phosphorylation	IAATGTTSKKNSSQD HHHHCCCCCCCCCCC	41.28	26074081
480	Phosphorylation	GTTSKKNSSQDDLFP CCCCCCCCCCCCCCC	37.95	30266825
481	Phosphorylation	TTSKKNSSQDDLFPT CCCCCCCCCCCCCCC	47.20	29255136
481	Ubiquitination	TTSKKNSSQDDLFPT CCCCCCCCCCCCCCC	47.20	32015554
488	Phosphorylation	SQDDLFPTSDTPRAK CCCCCCCCCCCCCCE	31.72	30266825
489	Phosphorylation	QDDLFPTSDTPRAKV CCCCCCCCCCCCCEE	39.46	30266825
491	Phosphorylation	DLFPTSDTPRAKVLK CCCCCCCCCCCEEEE	17.91	30266825
498	Sumoylation	TPRAKVLKIEEVSDT CCCCEEEEEEEECCC	51.57	28112733
498	Sumoylation	TPRAKVLKIEEVSDT CCCCEEEEEEEECCC	51.57	-
503	Phosphorylation	VLKIEEVSDTSSLQP EEEEEEECCCCCCCC	38.15	28555341
505	Phosphorylation	KIEEVSDTSSLQPQA EEEEECCCCCCCCCC	16.83	28555341
506	Phosphorylation	IEEVSDTSSLQPQAS EEEECCCCCCCCCCC	33.76	25627689
507	Phosphorylation	EEVSDTSSLQPQASL EEECCCCCCCCCCCC	32.87	25627689
513	Phosphorylation	SSLQPQASLKQDVCQ CCCCCCCCCCHHHHH	30.74	25159151
515	Ubiquitination	LQPQASLKQDVCQSY CCCCCCCCHHHHHHH	41.79	32015554
521	Phosphorylation	LKQDVCQSYSEKMPI CCHHHHHHHHHCCCC	26.04	25627689
567	Phosphorylation	KSSPDMLYQYLKQIE HCCHHHHHHHHHHHC	6.62	-
607	Acetylation	DFYIEKEKPLLIFEI HHHHCCCCCCHHHHH	52.62	20167786

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 RPAP3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RPAP3_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 RPAP3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RMP_HUMAN	URI1	physical	17643375
PIHD1_HUMAN	PIH1D1	physical	17643375
RPB2_HUMAN	POLR2B	physical	17643375
GPN1_HUMAN	GPN1	physical	17643375
RPAB1_HUMAN	POLR2E	physical	17643375
RPC1_HUMAN	POLR3A	physical	17643375
RPB1_HUMAN	POLR2A	physical	17643375
PP1A_HUMAN	PPP1CA	physical	17643375
UXT_HUMAN	UXT	physical	17643375
RFC5_HUMAN	RFC5	physical	17643375
U5S1_HUMAN	EFTUD2	physical	17643375
PDRG1_HUMAN	PDRG1	physical	17643375
TCPE_HUMAN	CCT5	physical	17643375
RPA1_HUMAN	POLR1A	physical	17643375
HS90B_HUMAN	HSP90AB1	physical	17643375
PFD2_HUMAN	PFDN2	physical	17643375
IF4A1_HUMAN	EIF4A1	physical	17643375
HSP76_HUMAN	HSPA6	physical	17643375
PFD6_HUMAN	PFDN6	physical	17643375
LRCH2_HUMAN	LRCH2	physical	17643375
INT1_HUMAN	INTS1	physical	17643375
APC1_HUMAN	ANAPC1	physical	17643375
HELLS_HUMAN	HELLS	physical	17643375
RGPD1_HUMAN	RGPD1	physical	17643375
NEMO_HUMAN	IKBKG	physical	21184742
RMP_HUMAN	URI1	physical	19450687
RUVB1_HUMAN	RUVBL1	physical	19450687
RUVB2_HUMAN	RUVBL2	physical	19450687
WDR92_HUMAN	WDR92	physical	19450687
PIHD1_HUMAN	PIH1D1	physical	19450687
RPAB1_HUMAN	POLR2E	physical	19450687
PFD2_HUMAN	PFDN2	physical	19450687
UXT_HUMAN	UXT	physical	19450687
PDRG1_HUMAN	PDRG1	physical	19450687
PFD6_HUMAN	PFDN6	physical	19450687
A4_HUMAN	APP	physical	21832049
UXT_HUMAN	UXT	physical	25036637
PDRG1_HUMAN	PDRG1	physical	25036637
CYBP_HUMAN	CACYBP	physical	25036637
RUVB1_HUMAN	RUVBL1	physical	25036637
ZNHI2_HUMAN	ZNHIT2	physical	25036637
SERA_HUMAN	PHGDH	physical	25036637
RUVB2_HUMAN	RUVBL2	physical	25036637
UBP19_HUMAN	USP19	physical	25036637
DPCD_HUMAN	DPCD	physical	25036637
RMP_HUMAN	URI1	physical	25036637
WDR92_HUMAN	WDR92	physical	25036637
PFD2_HUMAN	PFDN2	physical	25036637
SGT1_HUMAN	SUGT1	physical	25036637
PIHD1_HUMAN	PIH1D1	physical	25036637
RPAB1_HUMAN	POLR2E	physical	25036637
PRPS1_HUMAN	PRPS1	physical	25036637
PIHD1_HUMAN	PIH1D1	physical	21078300
PIHD1_HUMAN	PIH1D1	physical	26344197
RMP_HUMAN	URI1	physical	26344197
WDR92_HUMAN	WDR92	physical	26344197
HS90A_HUMAN	HSP90AA1	physical	24794838
CTRO_HUMAN	CIT	physical	28561026
HSP74_HUMAN	HSPA4	physical	28561026
LC7L2_HUMAN	LUC7L2	physical	28561026
PFD2_HUMAN	PFDN2	physical	28561026
PIHD1_HUMAN	PIH1D1	physical	28561026
RPAC1_HUMAN	POLR1C	physical	28561026
RPB1_HUMAN	POLR2A	physical	28561026
RPB2_HUMAN	POLR2B	physical	28561026
RPAB1_HUMAN	POLR2E	physical	28561026
RPC1_HUMAN	POLR3A	physical	28561026
PP1G_HUMAN	PPP1CC	physical	28561026
RPAP3_HUMAN	RPAP3	physical	28561026
RUVB1_HUMAN	RUVBL1	physical	28561026
RUVB2_HUMAN	RUVBL2	physical	28561026
TNG6_HUMAN	TANGO6	physical	28561026
RMP_HUMAN	URI1	physical	28561026
WDR92_HUMAN	WDR92	physical	28561026

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 RPAP3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-87; THR-111; SER-116;SER-119; SER-121 AND SER-481, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-119 ANDSER-121, AND MASS SPECTROMETRY.	17081983 [Abstract]