RPC7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RPC7_HUMAN
• UniProt AC: O15318
• Protein Name: DNA-directed RNA polymerase III subunit RPC7
• Gene Name: POLR3G
• Organism: Homo sapiens (Human).
• Sequence Length: 223
• Subcellular Localization: Nucleus . Cytoplasm . Excluded from nucleoli (PubMed:21898682). In zygotes and the 2-cell stage embryos, mainly in the cytoplasm. Starts to localize to the nucleus in the 8-16 cell stage embryo and early blastocysts (By similarity).
• Protein Description: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. [PubMed: 20154270 May direct with other members of the RPC3/POLR3C-RPC6/POLR3F-RPC7/POLR3G subcomplex RNA Pol III binding to the TFIIIB-DNA complex via the interactions between TFIIIB and POLR3F. May be involved either in the recruitment and stabilization of the subcomplex within RNA polymerase III, or in stimulating catalytic functions of other subunits during initiation. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs), induce type I interferon and NF- Kappa-B through the RIG-I pathway]
• Protein Sequence: MAGNKGRGRAAYTFNIEAVGFSKGEKLPDVVLKPPPLFPDTDYKPVPLKTGEGEEYMLALKQELRETMKRMPYFIETPEERQDIERYSKRYMKVYKEEWIPDWRRLPREMMPRNKCKKAGPKPKKAKDAGKGTPLTNTEDVLKKMEELEKRGDGEKSDEENEEKEGSKEKSKEGDDDDDDDAAEQEEYDEEEQEEENDYINSYFEDGDDFGADSDDNMDEATY

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
7	Methylation	-MAGNKGRGRAAYTF -CCCCCCCCCEEEEE	32.79	115383475
9	Methylation	AGNKGRGRAAYTFNI CCCCCCCCEEEEEEE	18.06	115383483
33	Ubiquitination	KLPDVVLKPPPLFPD CCCCEECCCCCCCCC	43.82	21906983
44	Ubiquitination	LFPDTDYKPVPLKTG CCCCCCCCCCCCCCC	42.20	21906983
56	Phosphorylation	KTGEGEEYMLALKQE CCCCCHHHHHHHHHH	7.98	27642862
61	Ubiquitination	EEYMLALKQELRETM HHHHHHHHHHHHHHH	35.80	21906983
67	Phosphorylation	LKQELRETMKRMPYF HHHHHHHHHHHCCCC	22.89	24719451
73	Phosphorylation	ETMKRMPYFIETPEE HHHHHCCCCCCCHHH	14.08	24719451
77	Phosphorylation	RMPYFIETPEERQDI HCCCCCCCHHHHHHH	31.05	24719451
89	Acetylation	QDIERYSKRYMKVYK HHHHHHHHHHHHHHH	38.32	20167786
118	Acetylation	MPRNKCKKAGPKPKK CCHHHHHCCCCCCCC	68.96	164371
122	Acetylation	KCKKAGPKPKKAKDA HHHCCCCCCCCCHHC	69.43	164375
131	Acetylation	KKAKDAGKGTPLTNT CCCHHCCCCCCCCCH	62.42	26051181
133	Phosphorylation	AKDAGKGTPLTNTED CHHCCCCCCCCCHHH	20.72	25159151
136	Phosphorylation	AGKGTPLTNTEDVLK CCCCCCCCCHHHHHH	41.10	29396449
138	Phosphorylation	KGTPLTNTEDVLKKM CCCCCCCHHHHHHHH	28.47	29396449
157	Phosphorylation	KRGDGEKSDEENEEK HCCCCCCCHHHHHHH	46.05	29255136
167	Phosphorylation	ENEEKEGSKEKSKEG HHHHHCCCHHHCCCC	38.44	26074081

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

Oops, there are no upstream regulatory protein records of RPC7_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RPC7_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 RPC7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RPC8_HUMAN	POLR3H	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

Phosphorylation

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND MASSSPECTROMETRY.
PubMed: 17287340

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-133, AND MASSSPECTROMETRY.
PubMed: 18669648