RPC2_HUMAN - dbPTM
RPC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPC2_HUMAN
UniProt AC Q9NW08
Protein Name DNA-directed RNA polymerase III subunit RPC2
Gene Name POLR3B
Organism Homo sapiens (Human).
Sequence Length 1133
Subcellular Localization Nucleus.
Protein Description DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and RPC2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity). 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..
Protein Sequence MDVLAEEFGNLTPEQLAAPIPTVEEKWRLLPAFLKVKGLVKQHIDSFNYFINVEIKKIMKANEKVTSDADPMWYLKYLNIYVGLPDVEESFNVTRPVSPHECRLRDMTYSAPITVDIEYTRGSQRIIRNALPIGRMPIMLRSSNCVLTGKTPAEFAKLNECPLDPGGYFIVKGVEKVILIQEQLSKNRIIVEADRKGAVGASVTSSTHEKKSRTNMAVKQGRFYLRHNTLSEDIPIVIIFKAMGVESDQEIVQMIGTEEHVMAAFGPSLEECQKAQIFTQMQALKYIGNKVRRQRMWGGGPKKTKIEEARELLASTILTHVPVKEFNFRAKCIYTAVMVRRVILAQGDNKVDDRDYYGNKRLELAGQLLSLLFEDLFKKFNSEMKKIADQVIPKQRAAQFDVVKHMRQDQITNGMVNAISTGNWSLKRFKMDRQGVTQVLSRLSYISALGMMTRISSQFEKTRKVSGPRSLQPSQWGMLCPSDTPEGEACGLVKNLALMTHITTDMEDGPIVKLASNLGVEDVNLLCGEELSYPNVFLVFLNGNILGVIRDHKKLVNTFRLMRRAGYINEFVSISTNLTDRCVYISSDGGRLCRPYIIVKKQKPAVTNKHMEELAQGYRNFEDFLHESLVEYLDVNEENDCNIALYEHTINKDTTHLEIEPFTLLGVCAGLIPYPHHNQSPRNTYQCAMGKQAMGTIGYNQRNRIDTLMYLLAYPQKPMVKTKTIELIEFEKLPAGQNATVAVMSYSGYDIEDALVLNKASLDRGFGRCLVYKNAKCTLKRYTNQTFDKVMGPMLDAATRKPIWRHEILDADGICSPGEKVENKQVLVNKSMPTVTQIPLEGSNVPQQPQYKDVPITYKGATDSYIEKVMISSNAEDAFLIKMLLRQTRRPEIGDKFSSRHGQKGVCGLIVPQEDMPFCDSGICPDIIMNPHGFPSRMTVGKLIELLAGKAGVLDGRFHYGTAFGGSKVKDVCEDLVRHGYNYLGKDYVTSGITGEPLEAYIYFGPVYYQKLKHMVLDKMHARARGPRAVLTRQPTEGRSRDGGLRLGEMERDCLIGYGASMLLLERLMISSDAFEVDVCGQCGLLGYSGWCHYCKSSCHVSSLRIPYACKLLFQELQSMNIIPRLKLSKYNE
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
12PhosphorylationAEEFGNLTPEQLAAP
HHHHCCCCHHHHCCC		28.8728464451
35UbiquitinationRLLPAFLKVKGLVKQ
HHHHHHHHHHHHHHH		35.13-
37UbiquitinationLPAFLKVKGLVKQHI
HHHHHHHHHHHHHHH		44.96-
64UbiquitinationKIMKANEKVTSDADP
HHHHCCCCCCCCCCH		51.09-
109PhosphorylationCRLRDMTYSAPITVD
EECCCCCCCCCEEEE		9.0126503892
110PhosphorylationRLRDMTYSAPITVDI
ECCCCCCCCCEEEEE		20.5726503892
119PhosphorylationPITVDIEYTRGSQRI
CEEEEEEEECCCCHH		11.3226503892
120PhosphorylationITVDIEYTRGSQRII
EEEEEEEECCCCHHH		18.7626503892
150UbiquitinationSNCVLTGKTPAEFAK
CCEEEECCCHHHHHH		46.21-
157UbiquitinationKTPAEFAKLNECPLD
CCHHHHHHHCCCCCC		58.11-
172UbiquitinationPGGYFIVKGVEKVIL
CCCEEEEECCCEEEE		53.04-
186UbiquitinationLIQEQLSKNRIIVEA
EEEHHHHCCCEEEEE		59.86-
196UbiquitinationIIVEADRKGAVGASV
EEEEECCCCCCCCCC		52.33-
202PhosphorylationRKGAVGASVTSSTHE
CCCCCCCCCCCCCCC		21.7223403867
204PhosphorylationGAVGASVTSSTHEKK
CCCCCCCCCCCCCCC		17.9222210691
205PhosphorylationAVGASVTSSTHEKKS
CCCCCCCCCCCCCCC		30.9622210691
206PhosphorylationVGASVTSSTHEKKSR
CCCCCCCCCCCCCCC		25.1523403867
207PhosphorylationGASVTSSTHEKKSRT
CCCCCCCCCCCCCCC		33.5523403867
210UbiquitinationVTSSTHEKKSRTNMA
CCCCCCCCCCCCCCH		48.7421890473
281SulfoxidationKAQIFTQMQALKYIG
HHHHHHHHHHHHHHH		1.9821406390
290UbiquitinationALKYIGNKVRRQRMW
HHHHHHHHHHHHHCC		31.72-
304PhosphorylationWGGGPKKTKIEEARE
CCCCCCCCCHHHHHH		43.30-
324UbiquitinationILTHVPVKEFNFRAK
HHHCCCHHHCCHHHH		50.9821890473
324UbiquitinationILTHVPVKEFNFRAK
HHHCCCHHHCCHHHH		50.9821890473
360UbiquitinationDRDYYGNKRLELAGQ
CCCCHHHHHHHHHHH		54.73-
394UbiquitinationIADQVIPKQRAAQFD
HHHHHCCHHHHHHCH		41.09-
404UbiquitinationAAQFDVVKHMRQDQI
HHHCHHHHHHCHHCC		31.37-
437PhosphorylationKMDRQGVTQVLSRLS
CCCHHHHHHHHHHHH		21.5624732914
447PhosphorylationLSRLSYISALGMMTR
HHHHHHHHHHHHHHH		14.8124719451
456PhosphorylationLGMMTRISSQFEKTR
HHHHHHHHHHHHHHC		18.1324719451
457O-linked_GlycosylationGMMTRISSQFEKTRK
HHHHHHHHHHHHHCC		36.2030379171
461UbiquitinationRISSQFEKTRKVSGP
HHHHHHHHHCCCCCC		55.72-
516PhosphorylationGPIVKLASNLGVEDV
CCCHHHCCCCCCCCH		42.9222210691
532PhosphorylationLLCGEELSYPNVFLV
HHCCCCCCCCCEEEE		41.6522210691
533PhosphorylationLCGEELSYPNVFLVF
HCCCCCCCCCEEEEE		16.0822210691
601UbiquitinationRPYIIVKKQKPAVTN
EEEEEEECCCCCCCH		53.30-
609UbiquitinationQKPAVTNKHMEELAQ
CCCCCCHHHHHHHHH		34.66-
680PhosphorylationPYPHHNQSPRNTYQC
CCCCCCCCCCCCCHH		31.0125159151
691UbiquitinationTYQCAMGKQAMGTIG
CCHHHCCCCCCCCCC		23.07-
707PhosphorylationNQRNRIDTLMYLLAY
CCCCHHHHHHHHHHC		15.8521214269
710PhosphorylationNRIDTLMYLLAYPQK
CHHHHHHHHHHCCCC		11.1521214269
714PhosphorylationTLMYLLAYPQKPMVK
HHHHHHHCCCCCCCC		13.2321214269
722PhosphorylationPQKPMVKTKTIELIE
CCCCCCCCEEEEEEE		23.2421214269
723UbiquitinationQKPMVKTKTIELIEF
CCCCCCCEEEEEEEE		41.6121890473
816PhosphorylationLDADGICSPGEKVEN
CCCCCCCCCCCCCCC		33.7425159151
820AcetylationGICSPGEKVENKQVL
CCCCCCCCCCCCEEE		61.8426051181
820UbiquitinationGICSPGEKVENKQVL
CCCCCCCCCCCCEEE		61.84-
824UbiquitinationPGEKVENKQVLVNKS
CCCCCCCCEEEEECC		28.42-
830UbiquitinationNKQVLVNKSMPTVTQ
CCEEEEECCCCCEEE		40.42-
852UbiquitinationVPQQPQYKDVPITYK
CCCCCCCCCCCCCCC		47.1821890473
859AcetylationKDVPITYKGATDSYI
CCCCCCCCCCCHHHH		33.1626051181
859MethylationKDVPITYKGATDSYI
CCCCCCCCCCCHHHH		33.1682986105
859UbiquitinationKDVPITYKGATDSYI
CCCCCCCCCCCHHHH		33.16-
872PhosphorylationYIEKVMISSNAEDAF
HHEEEECCCCHHHHH		10.23-
873PhosphorylationIEKVMISSNAEDAFL
HEEEECCCCHHHHHH		29.18-
896UbiquitinationRRPEIGDKFSSRHGQ
CCCCCHHHHHHCCCC		41.77-
950UbiquitinationLIELLAGKAGVLDGR
HHHHHHHCCCCCCCC		36.0421890473
968UbiquitinationGTAFGGSKVKDVCED
CCCCCCCHHHHHHHH		57.49-
970UbiquitinationAFGGSKVKDVCEDLV
CCCCCHHHHHHHHHH		48.45-
1013MethylationPVYYQKLKHMVLDKM
HHHHHHHHHHHHHHH		36.3723644510
1019UbiquitinationLKHMVLDKMHARARG
HHHHHHHHHHHHHCC		28.5521890473
1036PhosphorylationAVLTRQPTEGRSRDG
EEEECCCCCCCCCCC		42.61-
1102PhosphorylationCKSSCHVSSLRIPYA
CCCCCCHHHCCHHHH		10.4524719451
1103PhosphorylationKSSCHVSSLRIPYAC
CCCCCHHHCCHHHHH		22.1524719451
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 RPC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPC2_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 RPC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPC4_HUMANPOLR3Dphysical
22939629
RPC8_HUMANPOLR3Hphysical
22939629
RPC9_HUMANCRCPphysical
22939629
TSR1_HUMANTSR1physical
22939629
RPC9_HUMANCRCPphysical
26344197
EF1A1_HUMANEEF1A1physical
26344197
IPO9_HUMANIPO9physical
26344197
RM17_HUMANMRPL17physical
26344197
NOB1_HUMANNOB1physical
26344197
RPA1_HUMANPOLR1Aphysical
26344197
RPA2_HUMANPOLR1Bphysical
26344197
RPAC1_HUMANPOLR1Cphysical
26344197
RPB1_HUMANPOLR2Aphysical
26344197
RPAB1_HUMANPOLR2Ephysical
26344197
RPAB3_HUMANPOLR2Hphysical
26344197
RPC4_HUMANPOLR3Dphysical
26344197
RPC5_HUMANPOLR3Ephysical
26344197
RPC6_HUMANPOLR3Fphysical
26344197
RPC7_HUMANPOLR3Gphysical
26344197
RPC8_HUMANPOLR3Hphysical
26344197
RPC10_HUMANPOLR3Kphysical
26344197
RL30_HUMANRPL30physical
26344197
RRS1_HUMANRRS1physical
26344197
SMCA5_HUMANSMARCA5physical
26344197
TSR1_HUMANTSR1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614381Leukodystrophy, hypomyelinating, 8, with or without oligodontia and/or hypogonadotropic hypogonadism (HLD8)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RPC2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-206, ANDMASS SPECTROMETRY.

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