dbPTM

RPC9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPC9_HUMAN
UniProt AC	O75575
Protein Name	DNA-directed RNA polymerase III subunit RPC9
Gene Name	CRCP
Organism	Homo sapiens (Human).
Sequence Length	148
Subcellular Localization	Nucleus. Cell membrane Peripheral membrane protein Cytoplasmic side.
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. 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 induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity).; Accessory protein for the calcitonin gene-related peptide (CGRP) receptor. It modulates CGRP responsiveness in a variety of tissues..
Protein Sequence	MEVKDANSALLSNYEVFQLLTDLKEQRKESGKNKHSSGQQNLNTITYETLKYISKTPCRHQSPEIVREFLTALKSHKLTKAEKLQLLNHRPVTAVEIQLMVEESEERLTEEQIEALLHTVTSILPAEPEAEQKKNTNSNVAMDEEDPA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	NSALLSNYEVFQLLT HHHHHHHHHHHHHHH	15.30	29116813
21	Phosphorylation	YEVFQLLTDLKEQRK HHHHHHHHHHHHHHH	48.13	29116813
24	Ubiquitination	FQLLTDLKEQRKESG HHHHHHHHHHHHHHC	55.39	-
34	Ubiquitination	RKESGKNKHSSGQQN HHHHCCCCCCCCCCC	48.64	-
34	Malonylation	RKESGKNKHSSGQQN HHHHCCCCCCCCCCC	48.64	26320211
34	Acetylation	RKESGKNKHSSGQQN HHHHCCCCCCCCCCC	48.64	25953088
36	Phosphorylation	ESGKNKHSSGQQNLN HHCCCCCCCCCCCHH	37.46	30624053
37	Phosphorylation	SGKNKHSSGQQNLNT HCCCCCCCCCCCHHH	40.10	25159151
44	Phosphorylation	SGQQNLNTITYETLK CCCCCHHHHHHHHHH	20.19	23186163
46	Phosphorylation	QQNLNTITYETLKYI CCCHHHHHHHHHHHH	17.17	28796482
47	Phosphorylation	QNLNTITYETLKYIS CCHHHHHHHHHHHHC	11.76	28152594
49	Phosphorylation	LNTITYETLKYISKT HHHHHHHHHHHHCCC	20.38	28796482
51	Acetylation	TITYETLKYISKTPC HHHHHHHHHHCCCCC	48.21	19608861
55	Ubiquitination	ETLKYISKTPCRHQS HHHHHHCCCCCCCCC	47.10	-
56	Phosphorylation	TLKYISKTPCRHQSP HHHHHCCCCCCCCCH	22.34	25159151
62	Phosphorylation	KTPCRHQSPEIVREF CCCCCCCCHHHHHHH	20.55	20068231
74	Ubiquitination	REFLTALKSHKLTKA HHHHHHHHHCCCCHH	48.31	-
101 (in isoform 2)	Ubiquitination	-	11.39	21906983
104	Phosphorylation	IQLMVEESEERLTEE EEEEHHHHHHHCCHH	31.11	28270605
134 (in isoform 1)	Ubiquitination	-	69.56	21906983
134	Ubiquitination	EPEAEQKKNTNSNVA CCHHHHHCCCCCCCC	69.56	2190698
142	Sulfoxidation	NTNSNVAMDEEDPA- CCCCCCCCCCCCCC-	6.08	21406390

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 RPC9_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RPC9_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 RPC9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZMIZ2_HUMAN	ZMIZ2	physical	25416956
RPC5_HUMAN	POLR3E	physical	26344197
RPC6_HUMAN	POLR3F	physical	26344197
RPC10_HUMAN	POLR3K	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 RPC9_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-47, AND MASSSPECTROMETRY.	15592455 [Abstract]