dbPTM

RPAB3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPAB3_HUMAN
UniProt AC	P52434
Protein Name	DNA-directed RNA polymerases I, II, and III subunit RPABC3
Gene Name	POLR2H
Organism	Homo sapiens (Human).
Sequence Length	150
Subcellular Localization	Nucleus, nucleolus .
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..
Protein Sequence	MAGILFEDIFDVKDIDPEGKKFDRVSRLHCESESFKMDLILDVNIQIYPVDLGDKFRLVIASTLYEDGTLDDGEYNPTDDRPSRADQFEYVMYGKVYRIEGDETSTEAATRLSAYVSYGGLLMRLQGDANNLHGFEVDSRVYLLMKKLAF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGILFEDI ------CCCCEEEEC	17.46	22223895
13	Ubiquitination	FEDIFDVKDIDPEGK EEECCCCCCCCCCCC	51.30	29967540
13	Sumoylation	FEDIFDVKDIDPEGK EEECCCCCCCCCCCC	51.30	-
20	Ubiquitination	KDIDPEGKKFDRVSR CCCCCCCCCCCCEEE	48.91	33845483
20	Acetylation	KDIDPEGKKFDRVSR CCCCCCCCCCCCEEE	48.91	23749302
20	Ubiquitination	KDIDPEGKKFDRVSR CCCCCCCCCCCCEEE	48.91	-
20	Acetylation	KDIDPEGKKFDRVSR CCCCCCCCCCCCEEE	48.91	-
21	Ubiquitination	DIDPEGKKFDRVSRL CCCCCCCCCCCEEEE	64.45	33845483
21	Ubiquitination	DIDPEGKKFDRVSRL CCCCCCCCCCCEEEE	64.45	-
47 (in isoform 5)	Phosphorylation	-	3.58	27732954
48 (in isoform 5)	Phosphorylation	-	4.84	27732954
49 (in isoform 5)	Phosphorylation	-	18.12	27732954
51 (in isoform 5)	Phosphorylation	-	40.19	27732954
53 (in isoform 5)	Phosphorylation	-	31.44	27732954
54 (in isoform 5)	Phosphorylation	-	54.97	27732954
59	Ubiquitination	LGDKFRLVIASTLYE CCCCEEEEEEEEEEC	2.75	21890473
59	Ubiquitination	LGDKFRLVIASTLYE CCCCEEEEEEEEEEC	2.75	21963094
65	Phosphorylation	LVIASTLYEDGTLDD EEEEEEEECCCCCCC	16.44	-
75	Phosphorylation	GTLDDGEYNPTDDRP CCCCCCCCCCCCCCC	31.78	22817900
78	Phosphorylation	DDGEYNPTDDRPSRA CCCCCCCCCCCCCHH	47.06	-
82	Ubiquitination	YNPTDDRPSRADQFE CCCCCCCCCHHHCCE	34.85	21890473
82	Ubiquitination	YNPTDDRPSRADQFE CCCCCCCCCHHHCCE	34.85	21890473
83	Ubiquitination	NPTDDRPSRADQFEY CCCCCCCCHHHCCEE	40.78	21890473
83 (in isoform 2)	Phosphorylation	-	40.78	27732954
83	Ubiquitination	NPTDDRPSRADQFEY CCCCCCCCHHHCCEE	40.78	21890473
84 (in isoform 2)	Phosphorylation	-	44.88	27732954
85 (in isoform 2)	Phosphorylation	-	21.21	27732954
87 (in isoform 2)	Phosphorylation	-	31.89	27732954
89 (in isoform 2)	Phosphorylation	-	31.42	27732954
90 (in isoform 2)	Phosphorylation	-	7.57	27732954
90	Phosphorylation	SRADQFEYVMYGKVY CHHHCCEEEEEEEEE	7.57	-
92	Sulfoxidation	ADQFEYVMYGKVYRI HHCCEEEEEEEEEEE	3.41	30846556
95	Ubiquitination	FEYVMYGKVYRIEGD CEEEEEEEEEEEECC	20.71	21963094
104	Phosphorylation	YRIEGDETSTEAATR EEEECCCCCHHHHHH	45.77	21712546
105	Phosphorylation	RIEGDETSTEAATRL EEECCCCCHHHHHHH	23.39	23532336
110	Ubiquitination	ETSTEAATRLSAYVS CCCHHHHHHHHHEEE	38.91	21890473
110	Ubiquitination	ETSTEAATRLSAYVS CCCHHHHHHHHHEEE	38.91	21890473
111	Ubiquitination	TSTEAATRLSAYVSY CCHHHHHHHHHEEEH	23.17	21890473
111	Ubiquitination	TSTEAATRLSAYVSY CCHHHHHHHHHEEEH	23.17	21890473
118	Ubiquitination	RLSAYVSYGGLLMRL HHHHEEEHHCEEEEE	12.74	21890473
118	Ubiquitination	RLSAYVSYGGLLMRL HHHHEEEHHCEEEEE	12.74	21890473
118	Phosphorylation	RLSAYVSYGGLLMRL HHHHEEEHHCEEEEE	12.74	-
119	Ubiquitination	LSAYVSYGGLLMRLQ HHHEEEHHCEEEEEE	16.86	21890473
119	Ubiquitination	LSAYVSYGGLLMRLQ HHHEEEHHCEEEEEE	16.86	21890473
142	Phosphorylation	FEVDSRVYLLMKKLA CCCHHHHHHHHHHHC	7.94	22817900
146	Ubiquitination	SRVYLLMKKLAF--- HHHHHHHHHHCC---	44.60	21906983
147	Ubiquitination	RVYLLMKKLAF---- HHHHHHHHHCC----	30.96	21906983

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
-	K	Ubiquitination	E3 ubiquitin ligase	BARD1	Q99728	PMID:17283126
-	K	Ubiquitination	E3 ubiquitin ligase	BRCA1	P38398	PMID:17283126

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RPAB3_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 RPAB3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
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
BARD1_HUMAN	BARD1	physical	17283126
RPB1_HUMAN	POLR2A	physical	17283126
RPC1_HUMAN	POLR3A	physical	17283126
MCAF1_MOUSE	Atf7ip	physical	10777215
RPC8_HUMAN	POLR3H	physical	22939629
RPC4_HUMAN	POLR3D	physical	22939629
RPAC1_HUMAN	POLR1C	physical	22939629
RPC2_HUMAN	POLR3B	physical	22939629
RPC1_HUMAN	POLR3A	physical	22939629
RPAB1_HUMAN	POLR2E	physical	22863883
SART3_HUMAN	SART3	physical	22863883
ESR1_HUMAN	ESR1	physical	16957778
SRC_HUMAN	SRC	physical	16957778
PSB9_HUMAN	PSMB9	physical	16957778
ELOA1_HUMAN	TCEB3	physical	16957778
RPC9_HUMAN	CRCP	physical	26344197
RPA1_HUMAN	POLR1A	physical	26344197
RPB2_HUMAN	POLR2B	physical	26344197
RPAB1_HUMAN	POLR2E	physical	26344197
RPB9_HUMAN	POLR2I	physical	26344197
RPAB5_HUMAN	POLR2L	physical	26344197
SPT5H_HUMAN	SUPT5H	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 RPAB3_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 ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]