RPC5_HUMAN - dbPTM
RPC5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPC5_HUMAN
UniProt AC Q9NVU0
Protein Name DNA-directed RNA polymerase III subunit RPC5
Gene Name POLR3E
Organism Homo sapiens (Human).
Sequence Length 708
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. Essential for efficient transcription from both the type 2 VAI and type 3 U6 RNA polymerase III promoters. 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 MANEEDDPVVQEIDVYLAKSLAEKLYLFQYPVRPASMTYDDIPHLSAKIKPKQQKVELEMAIDTLNPNYCRSKGEQIALNVDGACADETSTYSSKLMDKQTFCSSQTTSNTSRYAAALYRQGELHLTPLHGILQLRPSFSYLDKADAKHREREAANEAGDSSQDEAEDDVKQITVRFSRPESEQARQRRVQSYEFLQKKHAEEPWVHLHYYGLRDSRSEHERQYLLCPGSSGVENTELVKSPSEYLMMLMPPSQEEEKDKPVAPSNVLSMAQLRTLPLADQIKILMKNVKVMPFANLMSLLGPSIDSVAVLRGIQKVAMLVQGNWVVKSDILYPKDSSSPHSGVPAEVLCRGRDFVMWKFTQSRWVVRKEVATVTKLCAEDVKDFLEHMAVVRINKGWEFILPYDGEFIKKHPDVVQRQHMLWTGIQAKLEKVYNLVKETMPKKPDAQSGPAGLVCGDQRIQVAKTKAQQNHALLERELQRRKEQLRVPAVPPGVRIKEEPVSEEGEEDEEQEAEEEPMDTSPSGLHSKLANGLPLGRAAGTDSFNGHPPQGCASTPVARELKAFVEATFQRQFVLTLSELKRLFNLHLASLPPGHTLFSGISDRMLQDTVLAAGCKQILVPFPPQTAASPDEQKVFALWESGDMSDQHRQVLLEIFSKNYRVRRNMIQSRLTQECGEDLSKQEVDKVLKDCCVSYGGMWYLKGTVQS
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
20PhosphorylationIDVYLAKSLAEKLYL
HHHHHHHHHHHHHHH		27.4922210691
36PhosphorylationQYPVRPASMTYDDIP
CCCCCCCCCCCCCCC		17.8428348404
38PhosphorylationPVRPASMTYDDIPHL
CCCCCCCCCCCCCCC		22.7028348404
39PhosphorylationVRPASMTYDDIPHLS
CCCCCCCCCCCCCCC		11.7228122231
64PhosphorylationELEMAIDTLNPNYCR
HHEHHHHHCCHHHHC		23.4829759185
69PhosphorylationIDTLNPNYCRSKGEQ
HHHCCHHHHCCCCCE		7.1829759185
92PhosphorylationCADETSTYSSKLMDK
CCCCCCCCCCHHCCC		15.6630576142
95AcetylationETSTYSSKLMDKQTF
CCCCCCCHHCCCCCC		41.7230591449
104PhosphorylationMDKQTFCSSQTTSNT
CCCCCCCCCCCCCCH		22.6830576142
107PhosphorylationQTFCSSQTTSNTSRY
CCCCCCCCCCCHHHH		33.8525690035
108PhosphorylationTFCSSQTTSNTSRYA
CCCCCCCCCCHHHHH		16.6130576142
161PhosphorylationAANEAGDSSQDEAED
HHHHHCCCCHHHHHH		29.0529255136
162PhosphorylationANEAGDSSQDEAEDD
HHHHCCCCHHHHHHH		46.5229255136
171SumoylationDEAEDDVKQITVRFS
HHHHHHHHHHEEEEC		42.8728112733
174PhosphorylationEDDVKQITVRFSRPE
HHHHHHHEEEECCCH		11.7928111955
178PhosphorylationKQITVRFSRPESEQA
HHHEEEECCCHHHHH		36.0428509920
182PhosphorylationVRFSRPESEQARQRR
EEECCCHHHHHHHHH		37.3828509920
192PhosphorylationARQRRVQSYEFLQKK
HHHHHHHHHHHHHHH		24.6323186163
193PhosphorylationRQRRVQSYEFLQKKH
HHHHHHHHHHHHHHH		8.1323186163
224PhosphorylationRSEHERQYLLCPGSS
CCHHHCEEEECCCCC		14.0922817900
230PhosphorylationQYLLCPGSSGVENTE
EEEECCCCCCCCCCE		14.7328348404
231PhosphorylationYLLCPGSSGVENTEL
EEECCCCCCCCCCEE		53.4228348404
236PhosphorylationGSSGVENTELVKSPS
CCCCCCCCEECCCHH		19.7222817900
241PhosphorylationENTELVKSPSEYLMM
CCCEECCCHHHHHHH		26.6128348404
243PhosphorylationTELVKSPSEYLMMLM
CEECCCHHHHHHHHC		46.0628348404
245PhosphorylationLVKSPSEYLMMLMPP
ECCCHHHHHHHHCCC		12.3028348404
287UbiquitinationDQIKILMKNVKVMPF
HHHHHHHHCCCEECH		55.96-
376UbiquitinationKEVATVTKLCAEDVK
HHHHHHHHHHHHHHH		36.91-
383AcetylationKLCAEDVKDFLEHMA
HHHHHHHHHHHHHCC		55.9020167786
411UbiquitinationYDGEFIKKHPDVVQR
CCCHHHHHCCCHHHH		56.40-
432UbiquitinationGIQAKLEKVYNLVKE
HHHHHHHHHHHHHHH		61.53-
432SumoylationGIQAKLEKVYNLVKE
HHHHHHHHHHHHHHH		61.5328112733
434PhosphorylationQAKLEKVYNLVKETM
HHHHHHHHHHHHHHC		17.5330576142
440PhosphorylationVYNLVKETMPKKPDA
HHHHHHHHCCCCCCC		32.8130576142
443UbiquitinationLVKETMPKKPDAQSG
HHHHHCCCCCCCCCC		67.14-
465MethylationDQRIQVAKTKAQQNH
CHHHHHHHHHHHHHH		52.26115975363
467UbiquitinationRIQVAKTKAQQNHAL
HHHHHHHHHHHHHHH		43.41-
467MethylationRIQVAKTKAQQNHAL
HHHHHHHHHHHHHHH		43.41115975371
498SumoylationVPPGVRIKEEPVSEE
CCCCCCCCCCCCCCC		45.5225114211
498SumoylationVPPGVRIKEEPVSEE
CCCCCCCCCCCCCCC		45.52-
503PhosphorylationRIKEEPVSEEGEEDE
CCCCCCCCCCCCCHH		40.4223927012
521PhosphorylationAEEEPMDTSPSGLHS
HHCCCCCCCCCHHHH		35.9623401153
522PhosphorylationEEEPMDTSPSGLHSK
HCCCCCCCCCHHHHH		16.8930278072
524PhosphorylationEPMDTSPSGLHSKLA
CCCCCCCCHHHHHHC		54.4723927012
528PhosphorylationTSPSGLHSKLANGLP
CCCCHHHHHHCCCCC		34.1123927012
544PhosphorylationGRAAGTDSFNGHPPQ
CCCCCCCCCCCCCCC		22.0521712546
555PhosphorylationHPPQGCASTPVAREL
CCCCCCCCCHHHHHH		37.0025627689
556PhosphorylationPPQGCASTPVARELK
CCCCCCCCHHHHHHH		11.8525627689
603PhosphorylationHTLFSGISDRMLQDT
CCCCCCCCHHHHHHH		23.77-
616GlutathionylationDTVLAAGCKQILVPF
HHHHHCCCCEEEEEC		2.2222555962
653 (in isoform 2)Phosphorylation-2.4126471730
654 (in isoform 2)Phosphorylation-5.0826471730
658PhosphorylationQVLLEIFSKNYRVRR
HHHHHHHCCCHHHHH		26.1724719451
659 (in isoform 2)Phosphorylation-47.4526471730
659SumoylationVLLEIFSKNYRVRRN
HHHHHHCCCHHHHHH		47.4528112733
659SumoylationVLLEIFSKNYRVRRN
HHHHHHCCCHHHHHH		47.45-
670PhosphorylationVRRNMIQSRLTQECG
HHHHHHHHHHHHHHC		20.5227067055
673PhosphorylationNMIQSRLTQECGEDL
HHHHHHHHHHHCCCC		22.6327067055
682UbiquitinationECGEDLSKQEVDKVL
HHCCCCCHHHHHHHH		58.75-
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 RPC5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPC5_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 RPC5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPC4_HUMANPOLR3Dphysical
12391170
RPC1_HUMANPOLR3Aphysical
12391170
BCCIP_HUMANBCCIPphysical
26344197
RPC4_HUMANPOLR3Dphysical
26344197
RPC6_HUMANPOLR3Fphysical
26344197
RPC7_HUMANPOLR3Gphysical
26344197
RPC8_HUMANPOLR3Hphysical
26344197
ADT3_HUMANSLC25A6physical
26496610
RPC4_HUMANPOLR3Dphysical
26496610
FMNL1_HUMANFMNL1physical
26496610
TF3B_HUMANBRF1physical
26496610
PFD2_HUMANPFDN2physical
26496610
RPAB1_HUMANPOLR2Ephysical
26496610
RPAB3_HUMANPOLR2Hphysical
26496610
RPAB4_HUMANPOLR2Kphysical
26496610
SPT6H_HUMANSUPT6Hphysical
26496610
RMP_HUMANURI1physical
26496610
RPAC1_HUMANPOLR1Cphysical
26496610
KEAP1_HUMANKEAP1physical
26496610
PFD6_HUMANPFDN6physical
26496610
RPC6_HUMANPOLR3Fphysical
26496610
RPC7_HUMANPOLR3Gphysical
26496610
RPC3_HUMANPOLR3Cphysical
26496610
RUVB2_HUMANRUVBL2physical
26496610
RPC1_HUMANPOLR3Aphysical
26496610
GPN1_HUMANGPN1physical
26496610
RPC9_HUMANCRCPphysical
26496610
GPN3_HUMANGPN3physical
26496610
RPC10_HUMANPOLR3Kphysical
26496610
PIHD1_HUMANPIH1D1physical
26496610
RPC2_HUMANPOLR3Bphysical
26496610
BDP1_HUMANBDP1physical
26496610
TPC_HUMANSLC25A19physical
26496610
RPAP3_HUMANRPAP3physical
26496610
PDRG1_HUMANPDRG1physical
26496610
RPC7L_HUMANPOLR3GLphysical
26496610
TM263_HUMANTMEM263physical
26496610
AROS_HUMANRPS19BP1physical
26496610
WDR92_HUMANWDR92physical
26496610
RPC8_HUMANPOLR3Hphysical
26496610
RPC7_HUMANPOLR3Gphysical
28514442
RPC8_HUMANPOLR3Hphysical
28514442
RPC6_HUMANPOLR3Fphysical
28514442
RPC3_HUMANPOLR3Cphysical
28514442
RPC2_HUMANPOLR3Bphysical
28514442
RPC9_HUMANCRCPphysical
28514442
RPC1_HUMANPOLR3Aphysical
28514442
ACD11_HUMANACAD11physical
28514442
RPC10_HUMANPOLR3Kphysical
28514442
MCAT_HUMANSLC25A20physical
28514442
UCP5_HUMANSLC25A14physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
BAG5_HUMANBAG5physical
28514442
GBB2_HUMANGNB2physical
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 RPC5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; SER-162; TYR-224AND SER-503, AND MASS SPECTROMETRY.
"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 SER-161; SER-162; SER-503AND SER-522, AND MASS SPECTROMETRY.
"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-162, AND MASSSPECTROMETRY.

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