dbPTM

RPAP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPAP1_HUMAN
UniProt AC	Q9BWH6
Protein Name	RNA polymerase II-associated protein 1
Gene Name	RPAP1
Organism	Homo sapiens (Human).
Sequence Length	1393
Subcellular Localization	Nucleus.
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. Required for interaction of the RNA polymerase II complex with acetylated histone H3..
Protein Sequence	MLSRPKPGESEVDLLHFQSQFLAAGAAPAVQLVKKGNRGGGDANSDRPPLQDHRDVVMLDNLPDLPPALVPSPPKRARPSPGHCLPEDEDPEERLRRHDQHITAVLTKIIERDTSSVAVNLPVPSGVAFPAVFLRSRDTQGKSATSGKRSIFAQEIAARRIAEAKGPSVGEVVPNVGPPEGAVTCETPTPRNQGCQLPGSSHSFQGPNLVTGKGLRDQEAEQEAQTIHEENIARLQAMAPEEILQEQQRLLAQLDPSLVAFLRSHSHTQEQTGETASEEQRPGGPSANVTKEEPLMSAFASEPRKRDKLEPEAPALALPVTPQKEWLHMDTVELEKLHWTQDLPPVRRQQTQERMQARFSLQGELLAPDVDLPTHLGLHHHGEEAERAGYSLQELFHLTRSQVSQQRALALHVLAQVISRAQAGEFGDRLAGSVLSLLLDAGFLFLLRFSLDDRVDGVIATAIRALRALLVAPGDEELLDSTFSWYHGALTFPLMPSQEDKEDEDEDEECPAGKAKRKSPEEESRPPPDLARHDVIKGLLATSLLPRLRYVLEVTYPGPAVVLDILAVLIRLARHSLESATRVLECPRLIETIVREFLPTSWSPVGAGPTPSLYKVPCATAMKLLRVLASAGRNIAARLLSSFDLRSRLCRIIAEAPQELALPPEEAEMLSTEALRLWAVAASYGQGGYLYRELYPVLMRALQVVPRELSTHPPQPLSMQRIASLLTLLTQLTLAAGSTPAETISDSAEASLSATPSLVTWTQVSGLQPLVEPCLRQTLKLLSRPEMWRAVGPVPVACLLFLGAYYQAWSQQPSSCPEDWLQDMQRLSEELLLPLLSQPTLGSLWDSLRHCSLLCNPLSCVPALEAPPSLVSLGCSGGCPRLSLAGSASPFPFLTALLSLLNTLAQIHKGLCGQLAAILAAPGLQNYFLQCVAPGAAPHLTPFSAWALRHEYHLQYLALALAQKAAALQPLPATHAALYHGMALALLSRLLPGSEYLTHELLLSCVFRLEFLPERTSGGPEAADFSDQLSLGSSRVPRCGQGTLLAQACQDLPSIRNCYLTHCSPARASLLASQALHRGELQRVPTLLLPMPTEPLLPTDWPFLPLIRLYHRASDTPSGLSPTDTMGTAMRVLQWVLVLESWRPQALWAVPPAARLARLMCVFLVDSELFRESPVQHLVAALLAQLCQPQVLPNLNLDCRLPGLTSFPDLYANFLDHFEAVSFGDHLFGALVLLPLQRRFSVTLRLALFGEHVGALRALSLPLTQLPVSLECYTVPPEDNLALLQLYFRTLVTGALRPRWCPVLYAVAVAHVNSFIFSQDPQSSDEVKAARRSMLQKTWLLADEGLRQHLLHYKLPNSTLPEGFELYSQLPPLRQHYLQRLTSTVLQNGVSET

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MLSRPKPGES -----CCCCCCCCCC	59.40	20068231
38	Methylation	QLVKKGNRGGGDANS HHHHCCCCCCCCCCC	54.52	115491519
72	Phosphorylation	LPPALVPSPPKRARP CCCHHCCCCCCCCCC	46.48	30266825
80	Phosphorylation	PPKRARPSPGHCLPE CCCCCCCCCCCCCCC	37.65	30266825
107	Phosphorylation	QHITAVLTKIIERDT HHHHHHHHHHHHCCC	17.38	28674151
114	Phosphorylation	TKIIERDTSSVAVNL HHHHHCCCCCEEEEC	29.17	21406692
115	Phosphorylation	KIIERDTSSVAVNLP HHHHCCCCCEEEECC	27.40	21406692
116	Phosphorylation	IIERDTSSVAVNLPV HHHCCCCCEEEECCC	19.05	21406692
125	Phosphorylation	AVNLPVPSGVAFPAV EEECCCCCCCCCCEE	46.24	21406692
136	Phosphorylation	FPAVFLRSRDTQGKS CCEEEEECCCCCCCC	36.33	21406692
139	Phosphorylation	VFLRSRDTQGKSATS EEEECCCCCCCCCCC	37.80	21406692
143	Phosphorylation	SRDTQGKSATSGKRS CCCCCCCCCCCCCCC	43.53	30576142
145	Phosphorylation	DTQGKSATSGKRSIF CCCCCCCCCCCCCHH	45.14	30576142
150	Phosphorylation	SATSGKRSIFAQEIA CCCCCCCCHHHHHHH	26.08	23898821
168	Phosphorylation	IAEAKGPSVGEVVPN HHHHHCCCCCEECCC	51.96	29978859
184	Phosphorylation	GPPEGAVTCETPTPR CCCCCCEEECCCCCC	12.23	21815630
187	Phosphorylation	EGAVTCETPTPRNQG CCCEEECCCCCCCCC	34.31	21815630
189	Phosphorylation	AVTCETPTPRNQGCQ CEEECCCCCCCCCCC	42.15	25850435
200	Phosphorylation	QGCQLPGSSHSFQGP CCCCCCCCCCCCCCC	23.96	25627689
201	Phosphorylation	GCQLPGSSHSFQGPN CCCCCCCCCCCCCCC	29.12	25627689
203	Phosphorylation	QLPGSSHSFQGPNLV CCCCCCCCCCCCCCC	22.63	25627689
213	Acetylation	GPNLVTGKGLRDQEA CCCCCCCCCCCHHHH	45.46	26051181
213	Ubiquitination	GPNLVTGKGLRDQEA CCCCCCCCCCCHHHH	45.46	-
238	Sulfoxidation	NIARLQAMAPEEILQ HHHHHHHHCHHHHHH	4.05	21406390
264	Phosphorylation	SLVAFLRSHSHTQEQ HHHHHHHCCCCCCCC	31.33	26657352
266	Phosphorylation	VAFLRSHSHTQEQTG HHHHHCCCCCCCCCC	29.49	25159151
268	Phosphorylation	FLRSHSHTQEQTGET HHHCCCCCCCCCCCC	36.49	19413330
272	Phosphorylation	HSHTQEQTGETASEE CCCCCCCCCCCCCHH	35.91	29978859
275	Phosphorylation	TQEQTGETASEEQRP CCCCCCCCCCHHCCC	36.51	21406692
277	Phosphorylation	EQTGETASEEQRPGG CCCCCCCCHHCCCCC	49.43	21406692
286	Phosphorylation	EQRPGGPSANVTKEE HCCCCCCCCCCCCCC	35.43	21406692
290	Phosphorylation	GGPSANVTKEEPLMS CCCCCCCCCCCCCHH	32.33	28464451
297	Phosphorylation	TKEEPLMSAFASEPR CCCCCCHHHHCCCCC	28.11	29396449
301	Phosphorylation	PLMSAFASEPRKRDK CCHHHHCCCCCCCCC	41.50	21815630
308	Ubiquitination	SEPRKRDKLEPEAPA CCCCCCCCCCCCCCC	59.80	-
321	Phosphorylation	PALALPVTPQKEWLH CCCCCCCCCCCCEEC	20.33	19664994
324	Ubiquitination	ALPVTPQKEWLHMDT CCCCCCCCCEECCCC	52.65	-
401	Phosphorylation	ELFHLTRSQVSQQRA HHHHHHHHHHHHHHH	29.69	22210691
419	Phosphorylation	HVLAQVISRAQAGEF HHHHHHHHHHHCCCH	23.78	22210691
518	Ubiquitination	PAGKAKRKSPEEESR CCCCCCCCCCCHHCC	70.43	-
519	Phosphorylation	AGKAKRKSPEEESRP CCCCCCCCCCHHCCC	41.39	28348404
537	Ubiquitination	LARHDVIKGLLATSL HHHHHHHHHHHHHHH	43.27	-
600	Phosphorylation	IVREFLPTSWSPVGA HHHHHCCCCCCCCCC	45.00	28857561
601	Phosphorylation	VREFLPTSWSPVGAG HHHHCCCCCCCCCCC	24.50	28857561
603	Phosphorylation	EFLPTSWSPVGAGPT HHCCCCCCCCCCCCC	14.96	21082442
610	Phosphorylation	SPVGAGPTPSLYKVP CCCCCCCCCCCCCCC	25.29	27732954
615	Ubiquitination	GPTPSLYKVPCATAM CCCCCCCCCCHHHHH	45.02	-
623	Ubiquitination	VPCATAMKLLRVLAS CCHHHHHHHHHHHHH	41.74	-
647	Phosphorylation	LSSFDLRSRLCRIIA HHCCCHHHHHHHHHH	36.58	23403867
716 (in isoform 3)	Ubiquitination	-	31.98	21906983
778	Phosphorylation	VEPCLRQTLKLLSRP HHHHHHHHHHHHHCH	21.30	24043423
780	Ubiquitination	PCLRQTLKLLSRPEM HHHHHHHHHHHCHHH	51.25	21890473
783	Phosphorylation	RQTLKLLSRPEMWRA HHHHHHHHCHHHHHH	57.11	24043423
994	Phosphorylation	LSRLLPGSEYLTHEL HHHHCCCCHHHHHHH	22.56	22210691
998	Phosphorylation	LPGSEYLTHELLLSC CCCCHHHHHHHHHHH	16.65	22210691
1033	Phosphorylation	SDQLSLGSSRVPRCG CHHHCCCCCCCCCCC	21.92	22210691
1054	Phosphorylation	QACQDLPSIRNCYLT HHHCCCHHHCCEEEC	41.29	24719451
1064	Phosphorylation	NCYLTHCSPARASLL CEEECCCCHHHHHHH	17.62	-
1086	Phosphorylation	GELQRVPTLLLPMPT CCCCCCCEEEECCCC	27.47	-
1093	Phosphorylation	TLLLPMPTEPLLPTD EEEECCCCCCCCCCC	43.94	-
1114	Phosphorylation	IRLYHRASDTPSGLS HHHHHHCCCCCCCCC	41.81	15345747
1116	Phosphorylation	LYHRASDTPSGLSPT HHHHCCCCCCCCCCC	19.50	29255136
1118	Phosphorylation	HRASDTPSGLSPTDT HHCCCCCCCCCCCCH	55.23	29255136
1121	Phosphorylation	SDTPSGLSPTDTMGT CCCCCCCCCCCHHHH	29.31	29255136
1123	Phosphorylation	TPSGLSPTDTMGTAM CCCCCCCCCHHHHHH	40.50	25850435
1125	Phosphorylation	SGLSPTDTMGTAMRV CCCCCCCHHHHHHHH	21.70	27732954
1128	Phosphorylation	SPTDTMGTAMRVLQW CCCCHHHHHHHHHHH	13.37	27732954
1241	Phosphorylation	LPLQRRFSVTLRLAL HHHHHHHHHHHHHHH	16.63	23312004
1243	Phosphorylation	LQRRFSVTLRLALFG HHHHHHHHHHHHHHH	12.64	24719451
1271 (in isoform 2)	Phosphorylation	-	20.26	22617229
1337	Acetylation	ARRSMLQKTWLLADE HHHHHHHHHHHHCCH	37.39	25953088
1337 (in isoform 1)	Ubiquitination	-	37.39	21906983
1337	Ubiquitination	ARRSMLQKTWLLADE HHHHHHHHHHHHCCH	37.39	2190698
1367	Phosphorylation	LPEGFELYSQLPPLR CCCCCHHHHHCCHHH	6.28	27642862
1377	Phosphorylation	LPPLRQHYLQRLTST CCHHHHHHHHHHHHH	9.01	-
1382	Phosphorylation	QHYLQRLTSTVLQNG HHHHHHHHHHHHHCC	25.25	28857561
1383	Phosphorylation	HYLQRLTSTVLQNGV HHHHHHHHHHHHCCC	22.55	28555341
1384	Phosphorylation	YLQRLTSTVLQNGVS HHHHHHHHHHHCCCC	21.72	28555341

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 RPAP1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RPAP1_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 RPAP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RHG23_HUMAN	ARHGAP23	physical	17643375
ROA1_HUMAN	HNRNPA1	physical	17643375
IF2B1_HUMAN	IGF2BP1	physical	17643375
GPN1_HUMAN	GPN1	physical	17643375
RPB2_HUMAN	POLR2B	physical	17643375
CH60_HUMAN	HSPD1	physical	17643375
RPB3_HUMAN	POLR2C	physical	17643375
SRP72_HUMAN	SRP72	physical	17643375
U5S1_HUMAN	EFTUD2	physical	17643375
ZFR_HUMAN	ZFR	physical	17643375
RPC1_HUMAN	POLR3A	physical	17643375
ELAV1_HUMAN	ELAVL1	physical	17643375
CENPC_HUMAN	CENPC	physical	17643375
ILF3_HUMAN	ILF3	physical	17643375
RPC2_HUMAN	POLR3B	physical	17643375
HSP7C_HUMAN	HSPA8	physical	17643375
BAG6_HUMAN	BAG6	physical	17643375
KIF11_HUMAN	KIF11	physical	17643375
TCPZ_HUMAN	CCT6A	physical	17643375
DDX3Y_HUMAN	DDX3Y	physical	17643375
PHF8_HUMAN	PHF8	physical	17643375
NUMA1_HUMAN	NUMA1	physical	17643375
IPO9_HUMAN	IPO9	physical	17643375
SLN11_HUMAN	SLFN11	physical	17643375
CSK2B_HUMAN	CSNK2B	physical	17643375
MAGD2_HUMAN	MAGED2	physical	17643375
HLTF_HUMAN	HLTF	physical	17643375
MCM10_HUMAN	MCM10	physical	17643375
SYTL2_HUMAN	SYTL2	physical	17643375
ERBIN_HUMAN	ERBB2IP	physical	17643375
APC1_HUMAN	ANAPC1	physical	17643375

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 RPAP1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-266 AND THR-268, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-80 AND THR-321,AND MASS SPECTROMETRY.	18691976 [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-603, AND MASSSPECTROMETRY.	15302935 [Abstract]