RPB4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RPB4_HUMAN
• UniProt AC: O15514
• Protein Name: DNA-directed RNA polymerase II subunit RPB4
• Gene Name: POLR2D
• Organism: Homo sapiens (Human).
• Sequence Length: 142
• Subcellular Localization: Nucleus .
• Protein Description: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB4 is part of a subcomplex with RPB7 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA (By similarity)..
• Protein Sequence: MAAGGSDPRAGDVEEDASQLIFPKEFETAETLLNSEVHMLLEHRKQQNESAEDEQELSEVFMKTLNYTARFSRFKNRETIASVRSLLLQKKLHKFELACLANLCPETAEESKALIPSLEGRFEDEELQQILDDIQTKRSFQY

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAGGSDPR ------CCCCCCCCC	18.14	-
28	Phosphorylation	IFPKEFETAETLLNS CCCCCHHHHHHHHHH	34.80	20068231
35	Phosphorylation	TAETLLNSEVHMLLE HHHHHHHHHHHHHHH	40.75	20068231
67	Phosphorylation	VFMKTLNYTARFSRF HHHHHHHHHHHHHHC	12.61	22817900
72	Phosphorylation	LNYTARFSRFKNRET HHHHHHHHHCCCHHH	31.11	29116813
91	Ubiquitination	RSLLLQKKLHKFELA HHHHHHHHHHHHHHH	42.75	29967540
94	Acetylation	LLQKKLHKFELACLA HHHHHHHHHHHHHHH	51.47	26051181
112	Ubiquitination	PETAEESKALIPSLE HHCHHHHHHHHHHCC	50.95	29967540
137	Ubiquitination	ILDDIQTKRSFQY-- HHHHHHHHHHHCC--	29.66	21906983

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RPB4_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RPB4_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RPB4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NEMO_HUMAN	IKBKG	physical	20211142
TRI29_HUMAN	TRIM29	physical	20211142
ZSCA1_HUMAN	ZSCAN1	physical	20211142
RPB1_HUMAN	POLR2A	physical	10567706
RPB2_HUMAN	POLR2B	physical	10567706
RPB3_HUMAN	POLR2C	physical	10567706
RPAB1_HUMAN	POLR2E	physical	10567706
RPB7_HUMAN	POLR2G	physical	10567706
RPAB3_HUMAN	POLR2H	physical	10567706
RPAB5_HUMAN	POLR2L	physical	10567706
MCAF1_MOUSE	Atf7ip	physical	10777215
RPB7_HUMAN	POLR2G	physical	22939629
RPB9_HUMAN	POLR2I	physical	22939629
T2FA_HUMAN	GTF2F1	physical	22939629
SMRD3_HUMAN	SMARCD3	physical	22939629
RPAB5_HUMAN	POLR2L	physical	21988832
ESR1_HUMAN	ESR1	physical	16957778
SRC_HUMAN	SRC	physical	16957778
PSB9_HUMAN	PSMB9	physical	16957778
ELOA1_HUMAN	TCEB3	physical	16957778
ELP2_HUMAN	ELP2	physical	26344197
MCFD2_HUMAN	MCFD2	physical	26344197
RPB1_HUMAN	POLR2A	physical	26344197
RPB7_HUMAN	POLR2G	physical	26344197
RPB1_HUMAN	POLR2A	physical	26700805
MYZAP_HUMAN	POLR2M	physical	28514442
GRL1A_HUMAN	POLR2M	physical	28514442
GL1AD_HUMAN	POLR2M	physical	28514442
RPR1B_HUMAN	RPRD1B	physical	28514442
RPB7_HUMAN	POLR2G	physical	28514442
RECQ5_HUMAN	RECQL5	physical	28514442
RPAP2_HUMAN	RPAP2	physical	28514442
GPN3_HUMAN	GPN3	physical	28514442
RPR1A_HUMAN	RPRD1A	physical	28514442
RPB1_HUMAN	POLR2A	physical	28514442
RPB11_HUMAN	POLR2J	physical	28514442
RPAB5_HUMAN	POLR2L	physical	28514442
RPB2_HUMAN	POLR2B	physical	28514442
RPAB1_HUMAN	POLR2E	physical	28514442

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.

Related Literatures of Post-Translational Modification

Acetylation

"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.
PubMed: 19413330