RPB3_HUMAN - dbPTM
RPB3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPB3_HUMAN
UniProt AC P19387
Protein Name DNA-directed RNA polymerase II subunit RPB3 {ECO:0000305}
Gene Name POLR2C {ECO:0000312|HGNC:HGNC:9189}
Organism Homo sapiens (Human).
Sequence Length 275
Subcellular Localization Nucleus .
Protein Description DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB3 is part of the core element with the central large cleft and the clamp element that moves to open and close the cleft (By similarity)..
Protein Sequence MPYANQPTVRITELTDENVKFIIENTDLAVANSIRRVFIAEVPIIAIDWVQIDANSSVLHDEFIAHRLGLIPLISDDIVDKLQYSRDCTCEEFCPECSVEFTLDVRCNEDQTRHVTSRDLISNSPRVIPVTSRNRDNDPNDYVEQDDILIVKLRKGQELRLRAYAKKGFGKEHAKWNPTAGVAFEYDPDNALRHTVYPKPEEWPKSEYSELDEDESQAPYDPNGKPERFYYNVESCGSLRPETIVLSALSGLKKKLSDLQTQLSHEIQSDVLTIN
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
3Phosphorylation-----MPYANQPTVR
-----CCCCCCCEEE		19.5227174698
8PhosphorylationMPYANQPTVRITELT
CCCCCCCEEEEEECC		16.8027174698
12PhosphorylationNQPTVRITELTDENV
CCCEEEEEECCCCCC		17.8724719451
15PhosphorylationTVRITELTDENVKFI
EEEEEECCCCCCEEE		34.7327174698
20UbiquitinationELTDENVKFIIENTD
ECCCCCCEEEEECCC		42.2921906983
26PhosphorylationVKFIIENTDLAVANS
CEEEEECCCHHHHHH		21.4324719451
33PhosphorylationTDLAVANSIRRVFIA
CCHHHHHHHHEEEEE		14.0327174698
81UbiquitinationISDDIVDKLQYSRDC
CCHHHHHHHHHCCCC		26.9621906983
122PhosphorylationVTSRDLISNSPRVIP
ECHHHHHHCCCCEEE		38.2525159151
124PhosphorylationSRDLISNSPRVIPVT
HHHHHHCCCCEEECC		13.8029255136
142PhosphorylationRDNDPNDYVEQDDIL
CCCCCCCCCCCCCEE		16.7228796482
152UbiquitinationQDDILIVKLRKGQEL
CCCEEEEEECCCCCC		35.26-
175SumoylationGFGKEHAKWNPTAGV
CCCHHHCCCCCCCCE		49.78-
175UbiquitinationGFGKEHAKWNPTAGV
CCCHHHCCCCCCCCE		49.7821906983
175SumoylationGFGKEHAKWNPTAGV
CCCHHHCCCCCCCCE		49.78-
199UbiquitinationLRHTVYPKPEEWPKS
CCCCCCCCCCCCCHH		47.58-
199SumoylationLRHTVYPKPEEWPKS
CCCCCCCCCCCCCHH		47.58-
205SumoylationPKPEEWPKSEYSELD
CCCCCCCHHHCCCCC		57.92-
205UbiquitinationPKPEEWPKSEYSELD
CCCCCCCHHHCCCCC		57.9221906983
206PhosphorylationKPEEWPKSEYSELDE
CCCCCCHHHCCCCCC		37.37-
208PhosphorylationEEWPKSEYSELDEDE
CCCCHHHCCCCCCCC		17.9728796482
209PhosphorylationEWPKSEYSELDEDES
CCCHHHCCCCCCCCC		27.8627642862
220PhosphorylationEDESQAPYDPNGKPE
CCCCCCCCCCCCCCC		47.23-
225AcetylationAPYDPNGKPERFYYN
CCCCCCCCCCCEEEE		50.8026051181
225UbiquitinationAPYDPNGKPERFYYN
CCCCCCCCCCCEEEE		50.8021906983
235PhosphorylationRFYYNVESCGSLRPE
CEEEEHHHCCCCCHH		21.35-
253UbiquitinationLSALSGLKKKLSDLQ
HHHHHHHHHHHHHHH		51.92-
254UbiquitinationSALSGLKKKLSDLQT
HHHHHHHHHHHHHHH		65.08-
255UbiquitinationALSGLKKKLSDLQTQ
HHHHHHHHHHHHHHH		52.192190698
257PhosphorylationSGLKKKLSDLQTQLS
HHHHHHHHHHHHHHH		45.1922617229
261PhosphorylationKKLSDLQTQLSHEIQ
HHHHHHHHHHHHHHH		38.4828348404
264PhosphorylationSDLQTQLSHEIQSDV
HHHHHHHHHHHHHCC		14.8428348404
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 RPB3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPB3_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 RPB3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBE2W_HUMANUBE2Wphysical
16169070
ERG28_HUMANC14orf1physical
16169070
EF1A1_HUMANEEF1A1physical
16169070
SMRC2_HUMANSMARCC2physical
16169070
STC2_HUMANSTC2physical
16169070
LRIF1_HUMANLRIF1physical
16169070
RPB1_HUMANPOLR2Aphysical
9201987
RPB2_HUMANPOLR2Bphysical
9201987
RPB3_HUMANPOLR2Cphysical
9201987
RPAB1_HUMANPOLR2Ephysical
9201987
RPAB2_HUMANPOLR2Fphysical
9201987
RPB7_HUMANPOLR2Gphysical
9201987
RPAB3_HUMANPOLR2Hphysical
9201987
RPAB4_HUMANPOLR2Kphysical
9201987
RPAB5_HUMANPOLR2Lphysical
9201987
RPB11_HUMANPOLR2Jphysical
9201987
MYOG_HUMANMYOGphysical
12207009
RPB11_HUMANPOLR2Jphysical
12207009
CCHCR_HUMANCCHCR1physical
16141233
CTR9_HUMANCTR9physical
18469135
MCAF1_MOUSEAtf7ipphysical
10777215
ZN326_HUMANZNF326physical
22446626
RPB4_HUMANPOLR2Dphysical
22939629
RPB9_HUMANPOLR2Iphysical
22939629
RPC7_HUMANPOLR3Gphysical
22939629
RPB1_HUMANPOLR2Aphysical
18562274
RPB2_HUMANPOLR2Bphysical
18562274
CTDP1_HUMANCTDP1physical
18562274
ANM5_HUMANPRMT5physical
18562274
T2FA_HUMANGTF2F1physical
18562274
MEP50_HUMANWDR77physical
18562274
RPB3_HUMANPOLR2Cphysical
18562274
T2FB_HUMANGTF2F2physical
18562274
RPAB1_HUMANPOLR2Ephysical
18562274
RPAB3_HUMANPOLR2Hphysical
18562274
RPB4_HUMANPOLR2Dphysical
18562274
RPB11_HUMANPOLR2Jphysical
18562274
WNT1_HUMANWNT1physical
18562274
SPT6H_HUMANSUPT6Hphysical
18562274
SPT5H_HUMANSUPT5Hphysical
18562274
FGF3_HUMANFGF3physical
18562274
EIF3E_HUMANEIF3Ephysical
18562274
RECQ5_HUMANRECQL5physical
18562274
DHX15_HUMANDHX15physical
18562274
ERCC3_HUMANERCC3physical
18562274
INT10_HUMANINTS10physical
18562274
MED17_HUMANMED17physical
18562274
NELFA_HUMANNELFAphysical
18562274
NELFB_HUMANNELFBphysical
18562274
TF2H1_HUMANGTF2H1physical
18562274
NELFD_HUMANNELFCDphysical
18562274
INT12_HUMANINTS12physical
18562274
NELFE_HUMANNELFEphysical
18562274
TCEA1_HUMANTCEA1physical
18562274
TF2B_HUMANGTF2Bphysical
18562274
MED27_HUMANMED27physical
18562274
H2A2C_HUMANHIST2H2ACphysical
18562274
EH1L1_HUMANEHBP1L1physical
22863883
HNRPR_HUMANHNRNPRphysical
22863883
MAP4_HUMANMAP4physical
22863883
PP4R1_HUMANPPP4R1physical
22863883
ESR1_HUMANESR1physical
16957778
SRC_HUMANSRCphysical
16957778
PSB9_HUMANPSMB9physical
16957778
ELOA1_HUMANTCEB3physical
16957778
RPAC1_HUMANPOLR1Cphysical
26344197
RPB1_HUMANPOLR2Aphysical
26344197
RPB4_HUMANPOLR2Dphysical
26344197
RPAB1_HUMANPOLR2Ephysical
26344197
RPAB2_HUMANPOLR2Fphysical
26344197
RPB7_HUMANPOLR2Gphysical
26344197
RPAB3_HUMANPOLR2Hphysical
26344197
RPB11_HUMANPOLR2Jphysical
26344197
RPAB4_HUMANPOLR2Kphysical
26344197
RPAB5_HUMANPOLR2Lphysical
26344197
RS9_HUMANRPS9physical
26344197
SPT5H_HUMANSUPT5Hphysical
26344197
NECA2_HUMANNECAB2physical
21516116
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 RPB3_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-124, AND MASSSPECTROMETRY.

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