RPC6_HUMAN - dbPTM
RPC6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPC6_HUMAN
UniProt AC Q9H1D9
Protein Name DNA-directed RNA polymerase III subunit RPC6
Gene Name POLR3F
Organism Homo sapiens (Human).
Sequence Length 316
Subcellular Localization Nucleus.
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. May direct RNA Pol III binding to the TFIIIB-DNA complex. 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. Preferentially binds double-stranded DNA (dsDNA). [PubMed: 21358628]
Protein Sequence MAEVKVKVQPPDADPVEIENRIIELCHQFPHGITDQVIQNEMPHIEAQQRAVAINRLLSMGQLDLLRSNTGLLYRIKDSQNAGKMKGSDNQEKLVYQIIEDAGNKGIWSRDIRYKSNLPLTEINKILKNLESKKLIKAVKSVAASKKKVYMLYNLQPDRSVTGGAWYSDQDFESEFVEVLNQQCFKFLQSKAETARESKQNPMIQRNSSFASSHEVWKYICELGISKVELSMEDIETILNTLIYDGKVEMTIIAAKEGTVGSVDGHMKLYRAVNPIIPPTGLVRAPCGLCPVFDDCHEGGEISPSNCIYMTEWLEF
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 Orthologous
Protein Cluster
2Acetylation------MAEVKVKVQ
------CCEEEEEEC
30.2322814378
5Sumoylation---MAEVKVKVQPPD
---CCEEEEEECCCC
28.0428112733
7Sumoylation-MAEVKVKVQPPDAD
-CCEEEEEECCCCCC
29.45-
7Sumoylation-MAEVKVKVQPPDAD
-CCEEEEEECCCCCC
29.4528112733
59PhosphorylationVAINRLLSMGQLDLL
HHHHHHHHHCHHHHH
26.0124719451
60SulfoxidationAINRLLSMGQLDLLR
HHHHHHHHCHHHHHH
3.9121406390
79PhosphorylationLLYRIKDSQNAGKMK
CEEEEECCCCCCCCC
21.97-
93UbiquitinationKGSDNQEKLVYQIIE
CCCCCHHHHHHHHHH
33.23-
96PhosphorylationDNQEKLVYQIIEDAG
CCHHHHHHHHHHHHC
12.3927642862
114PhosphorylationIWSRDIRYKSNLPLT
CCCCCCCCCCCCCHH
21.0728152594
116PhosphorylationSRDIRYKSNLPLTEI
CCCCCCCCCCCHHHH
34.3628152594
128UbiquitinationTEINKILKNLESKKL
HHHHHHHHHHHHHHH
64.06-
140AcetylationKKLIKAVKSVAASKK
HHHHHHHHHHHHCCC
44.0324888495
146AcetylationVKSVAASKKKVYMLY
HHHHHHCCCEEEEEE
52.4624888503
150PhosphorylationAASKKKVYMLYNLQP
HHCCCEEEEEEECCC
7.1222817900
191UbiquitinationCFKFLQSKAETARES
HHHHHHHHHHHHHHH
36.96-
199UbiquitinationAETARESKQNPMIQR
HHHHHHHCCCCCHHC
49.71-
208PhosphorylationNPMIQRNSSFASSHE
CCCHHCCCCCCCHHH
29.0829083192
209PhosphorylationPMIQRNSSFASSHEV
CCHHCCCCCCCHHHH
28.5129083192
212PhosphorylationQRNSSFASSHEVWKY
HCCCCCCCHHHHHHH
30.1629083192
213PhosphorylationRNSSFASSHEVWKYI
CCCCCCCHHHHHHHH
21.9029083192
219PhosphorylationSSHEVWKYICELGIS
CHHHHHHHHHHHCCC
8.6222210691
226PhosphorylationYICELGISKVELSME
HHHHHCCCEEEECHH
28.9322210691
256UbiquitinationEMTIIAAKEGTVGSV
EEEEEEECCCCCCEE
47.88-

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 RPC6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPC6_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 RPC6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF3C4_HUMANGTF3C4physical
10523658
WDR89_HUMANWDR89physical
16169070
PRP4B_HUMANPRPF4Bphysical
16169070
KAT5_HUMANKAT5physical
16169070
STC2_HUMANSTC2physical
16169070
ERG28_HUMANC14orf1physical
16169070
LRIF1_HUMANLRIF1physical
16169070
TBP_HUMANTBPphysical
9171375
RPC7_HUMANPOLR3Gphysical
22939629
RRP12_HUMANRRP12physical
22939629
UB2G2_HUMANUBE2G2physical
21988832
SUV92_HUMANSUV39H2physical
23455924
RPC4_HUMANPOLR3Dphysical
26344197
RPC7_HUMANPOLR3Gphysical
26344197
RPC8_HUMANPOLR3Hphysical
26344197
RPC10_HUMANPOLR3Kphysical
26344197
SMCA4_HUMANSMARCA4physical
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 RPC6_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP