RPA34_HUMAN - dbPTM
RPA34_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPA34_HUMAN
UniProt AC O15446
Protein Name DNA-directed RNA polymerase I subunit RPA34
Gene Name CD3EAP
Organism Homo sapiens (Human).
Sequence Length 510
Subcellular Localization Nucleus, nucleolus . Chromosome . Found at the fibrillar centers of the nucleolus in interphase and during cell division it is localized to the nucleolus organizer regions of the chromosomes.
Protein Description DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Isoform 1 is involved in UBTF-activated transcription, presumably at a step following PIC formation.; Isoform 2 has been described as a component of preformed T-cell receptor (TCR) complex..
Protein Sequence MEEPQAGDAARFSCPPNFTAKPPASESPRFSLEALTGPDTELWLIQAPADFAPECFNGRHVPLSGSQIVKGKLAGKRHRYRVLSSCPQAGEATLLAPSTEAGGGLTCASAPQGTLRILEGPQQSLSGSPLQPIPASPPPQIPPGLRPRFCAFGGNPPVTGPRSALAPNLLTSGKKKKEMQVTEAPVTQEAVNGHGALEVDMALGSPEMDVRKKKKKKNQQLKEPEAAGPVGTEPTVETLEPLGVLFPSTTKKRKKPKGKETFEPEDKTVKQEQINTEPLEDTVLSPTKKRKRQKGTEGMEPEEGVTVESQPQVKVEPLEEAIPLPPTKKRKKEKGQMAMMEPGTEAMEPVEPEMKPLESPGGTMAPQQPEGAKPQAQAALAAPKKKTKKEKQQDATVEPETEVVGPELPDDLEPQAAPTSTKKKKKKKERGHTVTEPIQPLEPELPGEGQPEARATPGSTKKRKKQSQESRMPETVPQEEMPGPPLNSESGEEAPTGRDKKRKQQQQQPV
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
1Acetylation-------MEEPQAGD
-------CCCCCCCC		13.6922814378
13PhosphorylationAGDAARFSCPPNFTA
CCCCCCCCCCCCCCC		21.8423927012
19PhosphorylationFSCPPNFTAKPPASE
CCCCCCCCCCCCCCC		40.1730108239
25PhosphorylationFTAKPPASESPRFSL
CCCCCCCCCCCCEEE		44.3622167270
27PhosphorylationAKPPASESPRFSLEA
CCCCCCCCCCEEEEE		20.9122167270
29PhosphorylationPPASESPRFSLEALT
CCCCCCCCEEEEEHH		42.9632142685
31PhosphorylationASESPRFSLEALTGP
CCCCCCEEEEEHHCC		26.9526074081
64PhosphorylationNGRHVPLSGSQIVKG
CCCCCCCCCCHHCCC		30.2620068231
66PhosphorylationRHVPLSGSQIVKGKL
CCCCCCCCHHCCCEE		17.2320068231
70AcetylationLSGSQIVKGKLAGKR
CCCCHHCCCEECCCH		52.5425953088
70UbiquitinationLSGSQIVKGKLAGKR
CCCCHHCCCEECCCH		52.5429967540
72UbiquitinationGSQIVKGKLAGKRHR
CCHHCCCEECCCHHH		29.4629967540
80PhosphorylationLAGKRHRYRVLSSCP
ECCCHHHEEEHHCCC		10.0310373416
124PhosphorylationILEGPQQSLSGSPLQ
EEECCCCCCCCCCCC		21.1830266825
126PhosphorylationEGPQQSLSGSPLQPI
ECCCCCCCCCCCCCC		42.3323927012
126 (in isoform 2)Phosphorylation-42.3321406692
128PhosphorylationPQQSLSGSPLQPIPA
CCCCCCCCCCCCCCC		21.0423927012
128 (in isoform 2)Phosphorylation-21.0421406692
130 (in isoform 2)Phosphorylation-11.5021406692
136PhosphorylationPLQPIPASPPPQIPP
CCCCCCCCCCCCCCC		32.3623927012
138 (in isoform 2)Phosphorylation-30.8221406692
159PhosphorylationFGGNPPVTGPRSALA
CCCCCCCCCCHHHHC		47.4428387310
162MethylationNPPVTGPRSALAPNL
CCCCCCCHHHHCCCC		35.59-
162DimethylationNPPVTGPRSALAPNL
CCCCCCCHHHHCCCC		35.59-
163PhosphorylationPPVTGPRSALAPNLL
CCCCCCHHHHCCCCC		30.6725159151
171PhosphorylationALAPNLLTSGKKKKE
HHCCCCCCCCCCCCC		38.3030266825
172PhosphorylationLAPNLLTSGKKKKEM
HCCCCCCCCCCCCCE		48.8930266825
174AcetylationPNLLTSGKKKKEMQV
CCCCCCCCCCCCEEE		62.2725953088
174UbiquitinationPNLLTSGKKKKEMQV
CCCCCCCCCCCCEEE		62.2733845483
176UbiquitinationLLTSGKKKKEMQVTE
CCCCCCCCCCEEEEE		58.4133845483
182PhosphorylationKKKEMQVTEAPVTQE
CCCCEEEEECCCCHH		14.9926552605
187PhosphorylationQVTEAPVTQEAVNGH
EEEECCCCHHHHCCC		21.4526552605
205PhosphorylationEVDMALGSPEMDVRK
EHHHHCCCCCHHHHH		20.6618669648
248PhosphorylationPLGVLFPSTTKKRKK
CCCCCCCCCCCCCCC		41.1818669648
249PhosphorylationLGVLFPSTTKKRKKP
CCCCCCCCCCCCCCC		42.7618669648
250PhosphorylationGVLFPSTTKKRKKPK
CCCCCCCCCCCCCCC		38.6229496963
268PhosphorylationTFEPEDKTVKQEQIN
CCCCCCCCCCHHHHC		45.3023403867
270SumoylationEPEDKTVKQEQINTE
CCCCCCCCHHHHCCC		54.04-
270SumoylationEPEDKTVKQEQINTE
CCCCCCCCHHHHCCC		54.0425114211
276PhosphorylationVKQEQINTEPLEDTV
CCHHHHCCCCCCCCC		40.3823927012
278 (in isoform 2)Phosphorylation-38.7221406692
282PhosphorylationNTEPLEDTVLSPTKK
CCCCCCCCCCCCCCH		17.6130266825
284 (in isoform 2)Phosphorylation-5.7221406692
285PhosphorylationPLEDTVLSPTKKRKR
CCCCCCCCCCCHHHC		26.6219664994
287PhosphorylationEDTVLSPTKKRKRQK
CCCCCCCCCHHHCCC		45.9119664994
287 (in isoform 2)Phosphorylation-45.9121406692
288AcetylationDTVLSPTKKRKRQKG
CCCCCCCCHHHCCCC		54.7025953088
289 (in isoform 2)Phosphorylation-66.6821406692
299SulfoxidationRQKGTEGMEPEEGVT
CCCCCCCCCCCCCCC		6.7221406390
309PhosphorylationEEGVTVESQPQVKVE
CCCCCCCCCCCCEEE		42.7123663014
314SumoylationVESQPQVKVEPLEEA
CCCCCCCEEEEHHHH		35.32-
314SumoylationVESQPQVKVEPLEEA
CCCCCCCEEEEHHHH		35.3225114211
327PhosphorylationEAIPLPPTKKRKKEK
HHCCCCCCCCCHHHH		47.4628555341
344PhosphorylationMAMMEPGTEAMEPVE
CCCCCCCCCCCCCCC		31.1426074081
359PhosphorylationPEMKPLESPGGTMAP
CCCCCCCCCCCCCCC		36.2128674151
363PhosphorylationPLESPGGTMAPQQPE
CCCCCCCCCCCCCCC		18.9727050516
419PhosphorylationLEPQAAPTSTKKKKK
CCCCCCCCCCCCHHH		44.2830576142
420PhosphorylationEPQAAPTSTKKKKKK
CCCCCCCCCCCHHHH		36.8530576142
421PhosphorylationPQAAPTSTKKKKKKK
CCCCCCCCCCHHHHH		49.7329496963
433PhosphorylationKKKERGHTVTEPIQP
HHHHCCCCCCCCCCC		31.7621712546
435PhosphorylationKERGHTVTEPIQPLE
HHCCCCCCCCCCCCC		36.8821712546
456PhosphorylationGQPEARATPGSTKKR
CCCCCCCCCCCHHHH		23.7230576142
459PhosphorylationEARATPGSTKKRKKQ
CCCCCCCCHHHHHHH		37.9530576142
460PhosphorylationARATPGSTKKRKKQS
CCCCCCCHHHHHHHC		46.6430576142
467PhosphorylationTKKRKKQSQESRMPE
HHHHHHHCHHHCCCC		44.8126074081
470PhosphorylationRKKQSQESRMPETVP
HHHHCHHHCCCCCCC		26.6626074081
475PhosphorylationQESRMPETVPQEEMP
HHHCCCCCCCHHHCC		31.4530576142
488PhosphorylationMPGPPLNSESGEEAP
CCCCCCCCCCCCCCC		40.6030266825
490PhosphorylationGPPLNSESGEEAPTG
CCCCCCCCCCCCCCC		51.8625159151
492PhosphorylationPLNSESGEEAPTGRD
CCCCCCCCCCCCCHH		61.3333259812
492 (in isoform 2)Phosphorylation-61.3321406692
496PhosphorylationESGEEAPTGRDKKRK
CCCCCCCCCHHHHHH		52.4730266825
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
285SPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPA34_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 RPA34_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPAC1_HUMANPOLR1Cphysical
15226435
RPA49_HUMANPOLR1Ephysical
15226435
TBP_HUMANTBPphysical
15226435
TAF1C_HUMANTAF1Cphysical
15226435
RPA1_HUMANPOLR1Aphysical
15226435
TF3C1_HUMANGTF3C1physical
22939629
RPA49_HUMANPOLR1Ephysical
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 RPA34_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-128; SER-136; SER-285; THR-287 AND SER-488, ANDMASS SPECTROMETRY.
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-136; SER-285 ANDSER-490, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-128; SER-136; SER-285; THR-287 AND SER-488, ANDMASS 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-27; SER-128; SER-136;SER-172; SER-205; SER-285 AND THR-287, 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-309, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, AND MASSSPECTROMETRY.
"RNA polymerase I-specific subunit CAST/hPAF49 has a role in theactivation of transcription by upstream binding factor.";
Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J.,Zomerdijk J.C.B.M.;
Mol. Cell. Biol. 26:5436-5448(2006).
Cited for: IDENTIFICATION IN THE RNA POL I COMPLEX, MASS SPECTROMETRY, FUNCTION,INTERACTION WITH TAF1A AND UBTF, AND PHOSPHORYLATION AT TYR-80.

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