RPC3_HUMAN - dbPTM
RPC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPC3_HUMAN
UniProt AC Q9BUI4
Protein Name DNA-directed RNA polymerase III subunit RPC3
Gene Name POLR3C
Organism Homo sapiens (Human).
Sequence Length 534
Subcellular Localization Nucleus.
Protein Description DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct with other members of the 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. Preferentially binds single-stranded DNA (ssDNA) in a sequence-independent manner. [PubMed: 21358628]
Protein Sequence MTQAEIKLCSLLLQEHFGEIVEKIGVHLIRTGSQPLRVIAHDTGTSLDQVKKALCVLVQHNLVSYQVHKRGVVEYEAQCSRVLRMLRYPRYIYTTKTLYSDTGELIVEELLLNGKLTMSAVVKKVADRLTETMEDGKTMDYAEVSNTFVRLADTHFVQRCPSVPTTENSDPGPPPPAPTLVINEKDMYLVPKLSLIGKGKRRRSSDEDAAGEPKAKRPKYTTDNKEPIPDDGIYWQANLDRFHQHFRDQAIVSAVANRMDQTSSEIVRTMLRMSEITTSSSAPFTQPLSSNEIFRSLPVGYNISKQVLDQYLTLLADDPLEFVGKSGDSGGGMYVINLHKALASLATATLESVVQERFGSRCARIFRLVLQKKHIEQKQVEDFAMIPAKEAKDMLYKMLSENFMSLQEIPKTPDHAPSRTFYLYTVNILSAARMLLHRCYKSIANLIERRQFETKENKRLLEKSQRVEAIIASMQATGAEEAQLQEIEEMITAPERQQLETLKRNVNKLDASEIQVDETIFLLESYIECTMKRQ
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
31PhosphorylationIGVHLIRTGSQPLRV
HCCEECCCCCCCCEE		33.9030266825
33PhosphorylationVHLIRTGSQPLRVIA
CEECCCCCCCCEEEE		28.1924719451
46PhosphorylationIAHDTGTSLDQVKKA
EEECCCCCHHHHHHH		31.15-
51UbiquitinationGTSLDQVKKALCVLV
CCCHHHHHHHHHHHH		27.0529967540
64UbiquitinationLVQHNLVSYQVHKRG
HHHCCCCCEEHHHCC		17.0229967540
75UbiquitinationHKRGVVEYEAQCSRV
HHCCCEEHHHHHHHH		12.6421890473
81UbiquitinationEYEAQCSRVLRMLRY
EHHHHHHHHHHHHCC		38.8323000965
99UbiquitinationIYTTKTLYSDTGELI
EEEECEECCCCCCHH		15.1024816145
108UbiquitinationDTGELIVEELLLNGK
CCCCHHHHHHHHCCC		35.6122817900
115UbiquitinationEELLLNGKLTMSAVV
HHHHHCCCCCHHHHH		39.45-
119PhosphorylationLNGKLTMSAVVKKVA
HCCCCCHHHHHHHHH		16.8128509920
138PhosphorylationETMEDGKTMDYAEVS
HHCCCCCCCCHHHHC		22.3221406692
141PhosphorylationEDGKTMDYAEVSNTF
CCCCCCCHHHHCCHH		8.2121406692
145PhosphorylationTMDYAEVSNTFVRLA
CCCHHHHCCHHHHHH		22.9721406692
147PhosphorylationDYAEVSNTFVRLADT
CHHHHCCHHHHHHHC		18.9221406692
154PhosphorylationTFVRLADTHFVQRCP
HHHHHHHCCHHHCCC		16.1721406692
162PhosphorylationHFVQRCPSVPTTENS
CHHHCCCCCCCCCCC		44.3421406692
165PhosphorylationQRCPSVPTTENSDPG
HCCCCCCCCCCCCCC		44.5821406692
166PhosphorylationRCPSVPTTENSDPGP
CCCCCCCCCCCCCCC		27.4021406692
169PhosphorylationSVPTTENSDPGPPPP
CCCCCCCCCCCCCCC		38.6621406692
188PhosphorylationVINEKDMYLVPKLSL
EECCCCCEEEECCHH		18.0626074081
192UbiquitinationKDMYLVPKLSLIGKG
CCCEEEECCHHCCCC		43.1423000965
194PhosphorylationMYLVPKLSLIGKGKR
CEEEECCHHCCCCCC		24.8621712546
198UbiquitinationPKLSLIGKGKRRRSS
ECCHHCCCCCCCCCC		55.0223000965
198AcetylationPKLSLIGKGKRRRSS
ECCHHCCCCCCCCCC		55.0225953088
204PhosphorylationGKGKRRRSSDEDAAG
CCCCCCCCCCCCCCC		40.0923401153
205PhosphorylationKGKRRRSSDEDAAGE
CCCCCCCCCCCCCCC		43.1129255136
205UbiquitinationKGKRRRSSDEDAAGE
CCCCCCCCCCCCCCC		43.1121890473
207PhosphorylationKRRRSSDEDAAGEPK
CCCCCCCCCCCCCCC		52.0420068231
211UbiquitinationSSDEDAAGEPKAKRP
CCCCCCCCCCCCCCC		54.1623000965
216UbiquitinationAAGEPKAKRPKYTTD
CCCCCCCCCCCCCCC		75.3024816145
217PhosphorylationAGEPKAKRPKYTTDN
CCCCCCCCCCCCCCC		37.4927251275
218PhosphorylationGEPKAKRPKYTTDNK
CCCCCCCCCCCCCCC		33.0433259812
225UbiquitinationPKYTTDNKEPIPDDG
CCCCCCCCCCCCCCC		68.6221906983
229UbiquitinationTDNKEPIPDDGIYWQ
CCCCCCCCCCCCEEE		44.3424816145
238UbiquitinationDGIYWQANLDRFHQH
CCCEEECCHHHHHHH		27.6322817900
269PhosphorylationTSSEIVRTMLRMSEI
CHHHHHHHHHHHCCC		15.0622210691
274PhosphorylationVRTMLRMSEITTSSS
HHHHHHHCCCCCCCC		21.2922210691
277PhosphorylationMLRMSEITTSSSAPF
HHHHCCCCCCCCCCC		19.3022210691
278PhosphorylationLRMSEITTSSSAPFT
HHHCCCCCCCCCCCC		32.0722210691
279PhosphorylationRMSEITTSSSAPFTQ
HHCCCCCCCCCCCCC		17.4122210691
280PhosphorylationMSEITTSSSAPFTQP
HCCCCCCCCCCCCCC		28.5522210691
281PhosphorylationSEITTSSSAPFTQPL
CCCCCCCCCCCCCCC		39.4622210691
296PhosphorylationSSNEIFRSLPVGYNI
CCCHHHHHCCCCCCC		26.6924719451
301PhosphorylationFRSLPVGYNISKQVL
HHHCCCCCCCCHHHH		15.0124719451
309PhosphorylationNISKQVLDQYLTLLA
CCCHHHHHHHHHHHC		35.90-
314PhosphorylationVLDQYLTLLADDPLE
HHHHHHHHHCCCCCE		3.24-
329PhosphorylationFVGKSGDSGGGMYVI
ECCCCCCCCCCEEEE		42.75-
334PhosphorylationGDSGGGMYVINLHKA
CCCCCCEEEEEHHHH		11.06-
340UbiquitinationMYVINLHKALASLAT
EEEEEHHHHHHHHHH		48.54-
341UbiquitinationYVINLHKALASLATA
EEEEHHHHHHHHHHH		9.5224816145
378UbiquitinationQKKHIEQKQVEDFAM
HHHCCHHHCHHHCCC		43.4529967540
385SulfoxidationKQVEDFAMIPAKEAK
HCHHHCCCCCHHHHH		3.6821406390
389UbiquitinationDFAMIPAKEAKDMLY
HCCCCCHHHHHHHHH		53.50-
389AcetylationDFAMIPAKEAKDMLY
HCCCCCHHHHHHHHH		53.5025953088
391UbiquitinationAMIPAKEAKDMLYKM
CCCCHHHHHHHHHHH		16.6729967540
392UbiquitinationMIPAKEAKDMLYKML
CCCHHHHHHHHHHHH		44.77-
396PhosphorylationKEAKDMLYKMLSENF
HHHHHHHHHHHHHHC		6.4229083192
405PhosphorylationMLSENFMSLQEIPKT
HHHHHCCCHHHCCCC		23.8229978859
411UbiquitinationMSLQEIPKTPDHAPS
CCHHHCCCCCCCCCC		77.63-
412PhosphorylationSLQEIPKTPDHAPSR
CHHHCCCCCCCCCCC		28.7018669648
418PhosphorylationKTPDHAPSRTFYLYT
CCCCCCCCCEEEEHH		44.7429978859
424UbiquitinationPSRTFYLYTVNILSA
CCCEEEEHHHHHHHH		9.39-
425PhosphorylationSRTFYLYTVNILSAA
CCEEEEHHHHHHHHH		12.4120068231
441UbiquitinationMLLHRCYKSIANLIE
HHHHHHHHHHHHHHH		38.73-
454UbiquitinationIERRQFETKENKRLL
HHHHHCCCHHHHHHH		44.97-
458UbiquitinationQFETKENKRLLEKSQ
HCCCHHHHHHHHHHH		45.5824816145
463UbiquitinationENKRLLEKSQRVEAI
HHHHHHHHHHHHHHH		52.4329967540
471UbiquitinationSQRVEAIIASMQATG
HHHHHHHHHHHHCCC		2.7524816145
476UbiquitinationAIIASMQATGAEEAQ
HHHHHHHCCCCHHHH		10.2029967540
501PhosphorylationPERQQLETLKRNVNK
HHHHHHHHHHHHHHH		46.28-
503UbiquitinationRQQLETLKRNVNKLD
HHHHHHHHHHHHHCC		49.7129967540
516UbiquitinationLDASEIQVDETIFLL
CCHHHCCCCHHHHHH		9.8629967540
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 RPC3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPC3_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 RPC3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TF3C5_HUMANGTF3C5physical
10373544
TF3C1_HUMANGTF3C1physical
10373544
TF3C2_HUMANGTF3C2physical
10373544
TF3C4_HUMANGTF3C4physical
10373544
TF3C3_HUMANGTF3C3physical
10373544
TF3C4_HUMANGTF3C4physical
10523658
RPC6_HUMANPOLR3Fphysical
9171375
RPC7_HUMANPOLR3Gphysical
9171375
TBP_HUMANTBPphysical
9171375
A4_HUMANAPPphysical
21832049
RPC6_HUMANPOLR3Fphysical
22939629
RPC7_HUMANPOLR3Gphysical
22939629
RPC8_HUMANPOLR3Hphysical
22939629
ROP1A_HUMANROPN1physical
25416956
CEP63_HUMANCEP63physical
25416956
PNMA5_HUMANPNMA5physical
25416956
RPC9_HUMANCRCPphysical
26344197
RPAC1_HUMANPOLR1Cphysical
26344197
RPAB3_HUMANPOLR2Hphysical
26344197
RPAB5_HUMANPOLR2Lphysical
26344197
RPC2_HUMANPOLR3Bphysical
26344197
RPC5_HUMANPOLR3Ephysical
26344197
RPC6_HUMANPOLR3Fphysical
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 RPC3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-194, AND MASSSPECTROMETRY.

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