dbPTM

RPAB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPAB1_HUMAN
UniProt AC	P19388
Protein Name	DNA-directed RNA polymerases I, II, and III subunit RPABC1
Gene Name	POLR2E
Organism	Homo sapiens (Human).
Sequence Length	210
Subcellular Localization	Nucleus .
Protein Description	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2E/RPB5 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. Seems to be the major component in this process (By similarity)..
Protein Sequence	MDDEEETYRLWKIRKTIMQLCHDRGYLVTQDELDQTLEEFKAQSGDKPSEGRPRRTDLTVLVAHNDDPTDQMFVFFPEEPKVGIKTIKVYCQRMQEENITRALIVVQQGMTPSAKQSLVDMAPKYILEQFLQQELLINITEHELVPEHVVMTKEEVTELLARYKLRENQLPRIQAGDPVARYFGIKRGQVVKIIRPSETAGRYITYRLVQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDDEEETY -------CCHHHHHH	15.36	22814378
8	Phosphorylation	MDDEEETYRLWKIRK CCHHHHHHHHHHHHH	13.64	29496907
9	Methylation	DDEEETYRLWKIRKT CHHHHHHHHHHHHHH	41.30	115488165
15	Ubiquitination	YRLWKIRKTIMQLCH HHHHHHHHHHHHHHH	45.97	-
29	Phosphorylation	HDRGYLVTQDELDQT HHCCCEEEHHHHHHH	27.92	-
56	Phosphorylation	SEGRPRRTDLTVLVA CCCCCCCCCEEEEEE	36.32	18452278
59	Phosphorylation	RPRRTDLTVLVAHND CCCCCCEEEEEECCC	18.01	18452278
81	Ubiquitination	VFFPEEPKVGIKTIK EEECCCCCCCEEHHH	57.27	-
81	Sumoylation	VFFPEEPKVGIKTIK EEECCCCCCCEEHHH	57.27	28112733
85	Ubiquitination	EEPKVGIKTIKVYCQ CCCCCCEEHHHHHHH	37.96	-
88	Ubiquitination	KVGIKTIKVYCQRMQ CCCEEHHHHHHHHHC	32.17	21890473
88	Acetylation	KVGIKTIKVYCQRMQ CCCEEHHHHHHHHHC	32.17	26051181
90	Phosphorylation	GIKTIKVYCQRMQEE CEEHHHHHHHHHCCC	4.28	29496907
110	Sulfoxidation	LIVVQQGMTPSAKQS EEEHHCCCCHHHHHH	4.29	21406390
111	Phosphorylation	IVVQQGMTPSAKQSL EEHHCCCCHHHHHHH	22.40	21815630
113	Phosphorylation	VQQGMTPSAKQSLVD HHCCCCHHHHHHHHH	38.64	26270265
115	Ubiquitination	QGMTPSAKQSLVDMA CCCCHHHHHHHHHHC	44.77	21890473
157	Phosphorylation	VMTKEEVTELLARYK ECCHHHHHHHHHHHH	24.97	26852163
186	Ubiquitination	VARYFGIKRGQVVKI HHHHHCCCCCCEEEE	51.35	-
192	Ubiquitination	IKRGQVVKIIRPSET CCCCCEEEEECCCCC	33.29	2190698
192	2-Hydroxyisobutyrylation	IKRGQVVKIIRPSET CCCCCEEEEECCCCC	33.29	-
192	Acetylation	IKRGQVVKIIRPSET CCCCCEEEEECCCCC	33.29	26051181
197	Phosphorylation	VVKIIRPSETAGRYI EEEEECCCCCCCCEE	37.42	28787133
199	Phosphorylation	KIIRPSETAGRYITY EEECCCCCCCCEEEE	38.46	28787133

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 RPAB1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RPAB1_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 RPAB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RMP_HUMAN	URI1	physical	14615539
RPB1_HUMAN	POLR2A	physical	9201987
RPB2_HUMAN	POLR2B	physical	9201987
RPB3_HUMAN	POLR2C	physical	9201987
RPAB1_HUMAN	POLR2E	physical	9201987
RPB7_HUMAN	POLR2G	physical	9201987
RPAB3_HUMAN	POLR2H	physical	9201987
RPAB5_HUMAN	POLR2L	physical	9201987
LZTR1_HUMAN	LZTR1	physical	20211142
NEMO_HUMAN	IKBKG	physical	20211142
TRI29_HUMAN	TRIM29	physical	20211142
ZSCA1_HUMAN	ZSCAN1	physical	20211142
ENPL_HUMAN	HSP90B1	physical	21900206
FOS_HUMAN	FOS	physical	21900206
SYT5_HUMAN	SYT5	physical	21900206
FKB14_HUMAN	FKBP14	physical	21900206
RPB3_HUMAN	POLR2C	physical	22939629
RPB1_HUMAN	POLR2A	physical	22939629
RPB2_HUMAN	POLR2B	physical	22939629
RPB9_HUMAN	POLR2I	physical	22939629
RPC1_HUMAN	POLR3A	physical	22939629
RPC8_HUMAN	POLR3H	physical	22939629
RPC6_HUMAN	POLR3F	physical	22939629
RPAC1_HUMAN	POLR1C	physical	22939629
RPC3_HUMAN	POLR3C	physical	22939629
TF2B_HUMAN	GTF2B	physical	9054408
TTI1_HUMAN	TTI1	physical	20371770
RUVB2_HUMAN	RUVBL2	physical	20371770
HTSF1_HUMAN	HTATSF1	physical	22863883
PAAF1_HUMAN	PAAF1	physical	22863883
TIF1B_HUMAN	TRIM28	physical	22863883
ESR1_HUMAN	ESR1	physical	16957778
SRC_HUMAN	SRC	physical	16957778
PSB9_HUMAN	PSMB9	physical	16957778
ELOA1_HUMAN	TCEB3	physical	16957778
T2FB_HUMAN	GTF2F2	physical	26344197
RPB4_HUMAN	POLR2D	physical	26344197
RPAB2_HUMAN	POLR2F	physical	26344197
RPB7_HUMAN	POLR2G	physical	26344197
RPAB4_HUMAN	POLR2K	physical	26344197
RPAB5_HUMAN	POLR2L	physical	26344197
RPC4_HUMAN	POLR3D	physical	26344197
RPC8_HUMAN	POLR3H	physical	26344197
RPC10_HUMAN	POLR3K	physical	26344197
RS5_HUMAN	RPS5	physical	26344197
SPT5H_HUMAN	SUPT5H	physical	26344197
RPC8_HUMAN	POLR3H	physical	28514442
RPC7_HUMAN	POLR3G	physical	28514442
RPC6_HUMAN	POLR3F	physical	28514442
RPC4_HUMAN	POLR3D	physical	28514442
RPC5_HUMAN	POLR3E	physical	28514442
ZN589_HUMAN	ZNF589	physical	28514442
RPC10_HUMAN	POLR3K	physical	28514442
RPA49_HUMAN	POLR1E	physical	28514442
RPC3_HUMAN	POLR3C	physical	28514442
RPC2_HUMAN	POLR3B	physical	28514442
RPA34_HUMAN	CD3EAP	physical	28514442
HELB_HUMAN	HELB	physical	28514442
RPC1_HUMAN	POLR3A	physical	28514442
MYZAP_HUMAN	POLR2M	physical	28514442
GRL1A_HUMAN	POLR2M	physical	28514442
GL1AD_HUMAN	POLR2M	physical	28514442
RPAP2_HUMAN	RPAP2	physical	28514442
GPN3_HUMAN	GPN3	physical	28514442
RECQ5_HUMAN	RECQL5	physical	28514442
RPA1_HUMAN	POLR1A	physical	28514442
RPA2_HUMAN	POLR1B	physical	28514442
RPB9_HUMAN	POLR2I	physical	28514442
CSK22_HUMAN	CSNK2A2	physical	28514442
PIHD1_HUMAN	PIH1D1	physical	28514442
RPB1_HUMAN	POLR2A	physical	28514442
RPB7_HUMAN	POLR2G	physical	28514442
PP1A_HUMAN	PPP1CA	physical	28514442
CK084_HUMAN	C11orf84	physical	28514442
RMP_HUMAN	URI1	physical	28514442
RPAC1_HUMAN	POLR1C	physical	28514442
RPAB5_HUMAN	POLR2L	physical	28514442
BRMS1_HUMAN	BRMS1	physical	28514442
CSK2B_HUMAN	CSNK2B	physical	28514442
CSK21_HUMAN	CSNK2A1	physical	28514442
ST7_HUMAN	ST7	physical	28514442
SPT6H_HUMAN	SUPT6H	physical	28514442
PP1R7_HUMAN	PPP1R7	physical	27173435

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 RPAB1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]