RPC4_HUMAN - dbPTM
RPC4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPC4_HUMAN
UniProt AC P05423
Protein Name DNA-directed RNA polymerase III subunit RPC4
Gene Name POLR3D
Organism Homo sapiens (Human).
Sequence Length 398
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. 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 (By similarity)..
Protein Sequence MSEGNAAGEPSTPGGPRPLLTGARGLIGRRPAPPLTPGRLPSIRSRDLTLGGVKKKTFTPNIISRKIKEEPKEEVTVKKEKRERDRDRQREGHGRGRGRPEVIQSHSIFEQGPAEMMKKKGNWDKTVDVSDMGPSHIINIKKEKRETDEETKQILRMLEKDDFLDDPGLRNDTRNMPVQLPLAHSGWLFKEENDEPDVKPWLAGPKEEDMEVDIPAVKVKEEPRDEEEEAKMKAPPKAARKTPGLPKDVSVAELLRELSLTKEEELLFLQLPDTLPGQPPTQDIKPIKTEVQGEDGQVVLIKQEKDREAKLAENACTLADLTEGQVGKLLIRKSGRVQLLLGKVTLDVTMGTACSFLQELVSVGLGDSRTGEMTVLGHVKHKLVCSPDFESLLDHKHR
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------MSEGNAAGE
------CCCCCCCCC		54.9622814378
2Phosphorylation------MSEGNAAGE
------CCCCCCCCC		54.9628857561
11PhosphorylationGNAAGEPSTPGGPRP
CCCCCCCCCCCCCCC		42.8228857561
12PhosphorylationNAAGEPSTPGGPRPL
CCCCCCCCCCCCCCC		36.3527050516
17MethylationPSTPGGPRPLLTGAR
CCCCCCCCCCCCCCC		37.46115384065
21PhosphorylationGGPRPLLTGARGLIG
CCCCCCCCCCCCCCC		36.1627050516
24MethylationRPLLTGARGLIGRRP
CCCCCCCCCCCCCCC		41.62115384071
29MethylationGARGLIGRRPAPPLT
CCCCCCCCCCCCCCC		34.12115488199
30MethylationARGLIGRRPAPPLTP
CCCCCCCCCCCCCCC		26.90115488193
36PhosphorylationRRPAPPLTPGRLPSI
CCCCCCCCCCCCCCH		29.4821712546
42PhosphorylationLTPGRLPSIRSRDLT
CCCCCCCCHHCCCCC		34.9122617229
57PhosphorylationLGGVKKKTFTPNIIS
CCCCCCCCCCHHHHH		41.4428555341
59PhosphorylationGVKKKTFTPNIISRK
CCCCCCCCHHHHHHH		22.2121815630
68SumoylationNIISRKIKEEPKEEV
HHHHHHHCCCCCCCC		60.0928112733
72UbiquitinationRKIKEEPKEEVTVKK
HHHCCCCCCCCEECH		70.5524816145
78SumoylationPKEEVTVKKEKRERD
CCCCCEECHHHHHHH		45.94-
78SumoylationPKEEVTVKKEKRERD
CCCCCEECHHHHHHH		45.9428112733
90MethylationERDRDRQREGHGRGR
HHHHHHHHHCCCCCC		53.40115488187
95MethylationRQREGHGRGRGRPEV
HHHHCCCCCCCCCHH		26.4324129315
97MethylationREGHGRGRGRPEVIQ
HHCCCCCCCCCHHHH		36.2624129315
99MethylationGHGRGRGRPEVIQSH
CCCCCCCCCHHHHCC		23.8924129315
105PhosphorylationGRPEVIQSHSIFEQG
CCCHHHHCCCHHHHC		14.21-
107PhosphorylationPEVIQSHSIFEQGPA
CHHHHCCCHHHHCHH		33.93-
125UbiquitinationKKKGNWDKTVDVSDM
HHCCCCCCCCCHHHC		41.9032015554
130PhosphorylationWDKTVDVSDMGPSHI
CCCCCCHHHCCHHHE		19.8824719451
141SumoylationPSHIINIKKEKRETD
HHHEEEECHHHCCCH		50.85-
141UbiquitinationPSHIINIKKEKRETD
HHHEEEECHHHCCCH		50.8529967540
141SumoylationPSHIINIKKEKRETD
HHHEEEECHHHCCCH		50.8528112733
147PhosphorylationIKKEKRETDEETKQI
ECHHHCCCHHHHHHH		53.3928985074
152UbiquitinationRETDEETKQILRMLE
CCCHHHHHHHHHHHH		38.3232015554
152SumoylationRETDEETKQILRMLE
CCCHHHHHHHHHHHH		38.3228112733
160SumoylationQILRMLEKDDFLDDP
HHHHHHHHCCCCCCC		59.6528112733
160UbiquitinationQILRMLEKDDFLDDP
HHHHHHHHCCCCCCC		59.6524816145
190SumoylationAHSGWLFKEENDEPD
CCCCCCEECCCCCCC		63.0528112733
199SumoylationENDEPDVKPWLAGPK
CCCCCCCCCCCCCCC		37.5428112733
199SumoylationENDEPDVKPWLAGPK
CCCCCCCCCCCCCCC		37.54-
199UbiquitinationENDEPDVKPWLAGPK
CCCCCCCCCCCCCCC		37.5432015554
206SumoylationKPWLAGPKEEDMEVD
CCCCCCCCHHHCCCC		73.2028112733
206SumoylationKPWLAGPKEEDMEVD
CCCCCCCCHHHCCCC		73.20-
218UbiquitinationEVDIPAVKVKEEPRD
CCCCCEEECCCCCCC		50.0932015554
220SumoylationDIPAVKVKEEPRDEE
CCCEEECCCCCCCHH		51.12-
220SumoylationDIPAVKVKEEPRDEE
CCCEEECCCCCCCHH		51.1228112733
247UbiquitinationRKTPGLPKDVSVAEL
HCCCCCCCCCCHHHH		75.6629967540
250PhosphorylationPGLPKDVSVAELLRE
CCCCCCCCHHHHHHH		26.2420068231
259PhosphorylationAELLRELSLTKEEEL
HHHHHHHCCCCHHEE		29.2824719451
285SumoylationQPPTQDIKPIKTEVQ
CCCCCCCCCCEEEEE		49.3228112733
285UbiquitinationQPPTQDIKPIKTEVQ
CCCCCCCCCCEEEEE		49.3229967540
288SumoylationTQDIKPIKTEVQGED
CCCCCCCEEEEECCC		47.35-
302SumoylationDGQVVLIKQEKDREA
CCCEEEEECCHHHHH		48.5228112733
302SumoylationDGQVVLIKQEKDREA
CCCEEEEECCHHHHH		48.52-
302UbiquitinationDGQVVLIKQEKDREA
CCCEEEEECCHHHHH		48.5222817900
305UbiquitinationVVLIKQEKDREAKLA
EEEEECCHHHHHHHH		60.6422817900
310UbiquitinationQEKDREAKLAENACT
CCHHHHHHHHHHHCH		43.4029967540
310SumoylationQEKDREAKLAENACT
CCHHHHHHHHHHHCH		43.4028112733
328UbiquitinationLTEGQVGKLLIRKSG
CCCCCHHHEEEECCC		41.0629967540
334PhosphorylationGKLLIRKSGRVQLLL
HHEEEECCCCEEEEE		23.2222210691
380UbiquitinationMTVLGHVKHKLVCSP
EEEEEEEEEEEEECC		29.3729967540
382UbiquitinationVLGHVKHKLVCSPDF
EEEEEEEEEEECCCH		36.5829967540
386PhosphorylationVKHKLVCSPDFESLL
EEEEEEECCCHHHHH		21.7425159151
396UbiquitinationFESLLDHKHR-----
HHHHHCCCCC-----		40.5232015554
396SumoylationFESLLDHKHR-----
HHHHHCCCCC-----		40.5228112733
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 RPC4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPC4_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 RPC4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPC1_HUMANPOLR3Aphysical
12391170
RPC2_HUMANPOLR3Bphysical
12391170
RPC5_HUMANPOLR3Ephysical
12391170
HSP7C_HUMANHSPA8physical
12391170
RPC3_HUMANPOLR3Cphysical
12391170
RPAC1_HUMANPOLR1Cphysical
12391170
RPC6_HUMANPOLR3Fphysical
12391170
RPC7_HUMANPOLR3Gphysical
12391170
RPC8_HUMANPOLR3Hphysical
12391170
RPAB1_HUMANPOLR2Ephysical
12391170
RPAB2_HUMANPOLR2Fphysical
12391170
RPAB3_HUMANPOLR2Hphysical
12391170
RPC10_HUMANPOLR3Kphysical
12391170
ROAA_HUMANHNRNPABphysical
20211142
HXA10_HUMANHOXA10physical
20211142
HXC9_HUMANHOXC9physical
20211142
MSX2_HUMANMSX2physical
20211142
NR2E3_HUMANNR2E3physical
20211142
RFOX2_HUMANRBFOX2physical
20211142
RHXF2_HUMANRHOXF2physical
20211142
ZN496_HUMANZNF496physical
20211142
RPC8_HUMANPOLR3Hphysical
22939629
RPC8_HUMANPOLR3Hphysical
26186194
RPC10_HUMANPOLR3Kphysical
26186194
RPC1_HUMANPOLR3Aphysical
26186194
RPC5_HUMANPOLR3Ephysical
26186194
RPC3_HUMANPOLR3Cphysical
26186194
RPC2_HUMANPOLR3Bphysical
26186194
RPC7_HUMANPOLR3Gphysical
26186194
RPC9_HUMANCRCPphysical
26186194
RPAC1_HUMANPOLR1Cphysical
26186194
RPC6_HUMANPOLR3Fphysical
26186194
RPAB5_HUMANPOLR2Lphysical
26186194
RPAC1_HUMANPOLR1Cphysical
26344197
RPC3_HUMANPOLR3Cphysical
26344197
RPC7_HUMANPOLR3Gphysical
26344197
TSR1_HUMANTSR1physical
26344197
RPC5_HUMANPOLR3Ephysical
28514442
RPC6_HUMANPOLR3Fphysical
28514442
RPC9_HUMANCRCPphysical
28514442
RPC3_HUMANPOLR3Cphysical
28514442
RPC8_HUMANPOLR3Hphysical
28514442
RPC7_HUMANPOLR3Gphysical
28514442
RPC10_HUMANPOLR3Kphysical
28514442
RPC2_HUMANPOLR3Bphysical
28514442
RPC1_HUMANPOLR3Aphysical
28514442
RPAB5_HUMANPOLR2Lphysical
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.
Regulatory Network of RPC4_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory