RPB9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RPB9_HUMAN
• UniProt AC: P36954
• Protein Name: DNA-directed RNA polymerase II subunit RPB9
• Gene Name: POLR2I
• Organism: Homo sapiens (Human).
• Sequence Length: 125
• Subcellular Localization: Nucleus, nucleolus .
• 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. RPB9 is part of the upper jaw surrounding the central large cleft and thought to grab the incoming DNA template (By similarity)..
• Protein Sequence: MEPDGTYEPGFVGIRFCQECNNMLYPKEDKENRILLYACRNCDYQQEADNSCIYVNKITHEVDELTQIIADVSQDPTLPRTEDHPCQKCGHKEAVFFQSHSARAEDAMRLYYVCTAPHCGHRWTE

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
1	Acetylation	-------MEPDGTYE -------CCCCCCCC	17.79	22814378
7	Phosphorylation	-MEPDGTYEPGFVGI -CCCCCCCCCCCCEE	26.17	27642862
27	Ubiquitination	CNNMLYPKEDKENRI HCCCEECCCCCCCCE	66.06	24816145
37	Phosphorylation	KENRILLYACRNCDY CCCCEEEEECCCCCC	10.54	29978859
51	Phosphorylation	YQQEADNSCIYVNKI CCHHHCCCCEEEECC	11.48	28985074
54	Phosphorylation	EADNSCIYVNKITHE HHCCCCEEEECCCCC	11.42	28796482
59	Phosphorylation	CIYVNKITHEVDELT CEEEECCCCCHHHHH	17.37	20068231
66	Phosphorylation	THEVDELTQIIADVS CCCHHHHHHHHHHHH	18.70	20068231
73	Phosphorylation	TQIIADVSQDPTLPR HHHHHHHHCCCCCCC	29.43	17525332
77	Phosphorylation	ADVSQDPTLPRTEDH HHHHCCCCCCCCCCC	58.65	20068231
81	Phosphorylation	QDPTLPRTEDHPCQK CCCCCCCCCCCCCCC	43.77	20068231
101	Phosphorylation	AVFFQSHSARAEDAM EEEEECCCCCHHHHH	25.38	26329039
111	Phosphorylation	AEDAMRLYYVCTAPH HHHHHHHHEEECCCC	5.40	28152594
112	Phosphorylation	EDAMRLYYVCTAPHC HHHHHHHEEECCCCC	8.14	28152594
115	Phosphorylation	MRLYYVCTAPHCGHR HHHHEEECCCCCCCC	32.93	28152594

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

Oops, there are no upstream regulatory protein records of RPB9_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RPB9_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 RPB9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TBCD_HUMAN	TBCD	physical	21988832
ESR1_HUMAN	ESR1	physical	16957778
SRC_HUMAN	SRC	physical	16957778
PSB9_HUMAN	PSMB9	physical	16957778
ELOA1_HUMAN	TCEB3	physical	16957778
CSN5_HUMAN	COPS5	physical	26344197
RPB3_HUMAN	POLR2C	physical	26344197
RPB4_HUMAN	POLR2D	physical	26344197
RPAB1_HUMAN	POLR2E	physical	26344197
RPAB4_HUMAN	POLR2K	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.

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 MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASSSPECTROMETRY.
PubMed: 17525332