RPA49_HUMAN - dbPTM
RPA49_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPA49_HUMAN
UniProt AC Q9GZS1
Protein Name DNA-directed RNA polymerase I subunit RPA49
Gene Name POLR1E
Organism Homo sapiens (Human).
Sequence Length 481
Subcellular Localization Nucleus, nucleolus .
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. Appears to be involved in the formation of the initiation complex at the promoter by mediating the interaction between Pol I and UBTF/UBF (By similarity)..
Protein Sequence MYQASAVSLLPRDIPSCHSPSPGFSHLPTSSSQLAPDLLQFPLGQDPSFLAIPILTLPPSDSLVPPYIVWYIVWPSALISFLGCTLTVQFSNGKLQSPGNMRFTLYENKDSTNPRKRNQRILAAETDRLSYVGNNFGTGALKCNTLCRHFVGILNKTSGQMEVYDAELFNMQPLFSDVSVESELALESQTKTYREKMDSCIEAFGTTKQKRALNTRRMNRVGNESLNRAVAKAAETIIDTKGVTALVSDAIHNDLQDDSLYLPPCYDDAAKPEDVYKFEDLLSPAEYEALQSPSEAFRNVTSEEILKMIEENSHCTFVIEALKSLPSDVESRDRQARCIWFLDTLIKFRAHRVVKRKSALGPGVPHIINTKLLKHFTCLTYNNGRLRNLISDSMKAKITAYVIILALHIHDFQIDLTVLQRDLKLSEKRMMEIAKAMRLKISKRRVSVAAGSEEDHKLGTLSLPLPPAQTSDRLAKRRKIT
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
2Phosphorylation------MYQASAVSL
------CCCCCHHCC		16.8820068231
8 (in isoform 2)Phosphorylation-24.7320068231
8PhosphorylationMYQASAVSLLPRDIP
CCCCCHHCCCCCCCC		24.7320068231
29 (in isoform 2)Phosphorylation-47.8327174698
32 (in isoform 2)Ubiquitination-29.04-
35 (in isoform 2)Phosphorylation-6.4720068231
35PhosphorylationPTSSSQLAPDLLQFP
CCCHHHCCHHHHCCC		6.4723186163
47 (in isoform 2)Ubiquitination-21.06-
80 (in isoform 2)Ubiquitination-18.44-
94AcetylationTVQFSNGKLQSPGNM
EEEEECCEECCCCCE		47.8326051181
97PhosphorylationFSNGKLQSPGNMRFT
EECCEECCCCCEEEE		45.2526055452
102MethylationLQSPGNMRFTLYENK
ECCCCCEEEEEEECC		25.95115488133
104PhosphorylationSPGNMRFTLYENKDS
CCCCEEEEEEECCCC		20.3326074081
106PhosphorylationGNMRFTLYENKDSTN
CCEEEEEEECCCCCC		17.8826074081
109AcetylationRFTLYENKDSTNPRK
EEEEEECCCCCCCCH		40.9126051181
109UbiquitinationRFTLYENKDSTNPRK
EEEEEECCCCCCCCH		40.91-
111PhosphorylationTLYENKDSTNPRKRN
EEEECCCCCCCCHHH		31.5226074081
112PhosphorylationLYENKDSTNPRKRNQ
EEECCCCCCCCHHHH		60.4226074081
126PhosphorylationQRILAAETDRLSYVG
HHHHEEECCHHHHCC		22.9924667141
128MethylationILAAETDRLSYVGNN
HHEEECCHHHHCCCC		32.71115488125
134 (in isoform 2)Ubiquitination-30.52-
138PhosphorylationYVGNNFGTGALKCNT
HCCCCCCCCHHHHHH		18.3628555341
142MethylationNFGTGALKCNTLCRH
CCCCCHHHHHHHHHH		25.5582985949
142UbiquitinationNFGTGALKCNTLCRH
CCCCCHHHHHHHHHH		25.55-
148 (in isoform 2)Ubiquitination-29.41-
163PhosphorylationKTSGQMEVYDAELFN
CCCCCEEEEEHHHHC		4.3821406692
170 (in isoform 2)Ubiquitination-40.5821906983
193PhosphorylationLESQTKTYREKMDSC
HHHCCHHHHHHHHHH		20.5224719451
196AcetylationQTKTYREKMDSCIEA
CCHHHHHHHHHHHHH		38.7226051181
199PhosphorylationTYREKMDSCIEAFGT
HHHHHHHHHHHHHCC		17.3128555341
206PhosphorylationSCIEAFGTTKQKRAL
HHHHHHCCHHHHHHH		25.1124719451
207PhosphorylationCIEAFGTTKQKRALN
HHHHHCCHHHHHHHC		31.68-
225PhosphorylationMNRVGNESLNRAVAK
HHHHCHHHHHHHHHH		34.6423401153
232UbiquitinationSLNRAVAKAAETIID
HHHHHHHHHHHHHHH		41.342190698
232 (in isoform 1)Ubiquitination-41.3421906983
240PhosphorylationAAETIIDTKGVTALV
HHHHHHHCCCHHEEC		21.2024114839
283PhosphorylationYKFEDLLSPAEYEAL
CCHHHHCCHHHHHHH		29.3920873877
287PhosphorylationDLLSPAEYEALQSPS
HHCCHHHHHHHCCHH		14.4928102081
292PhosphorylationAEYEALQSPSEAFRN
HHHHHHCCHHHHHCC		31.1028102081
294PhosphorylationYEALQSPSEAFRNVT
HHHHCCHHHHHCCCC		46.9728102081
309 (in isoform 2)Ubiquitination-6.01-
312 (in isoform 2)Ubiquitination-25.02-
327PhosphorylationEALKSLPSDVESRDR
HHHHCCCCCHHHHHH		60.63-
357MethylationAHRVVKRKSALGPGV
HHHHHHCCCCCCCCC		34.07115975309
358PhosphorylationHRVVKRKSALGPGVP
HHHHHCCCCCCCCCC		32.5325159151
373AcetylationHIINTKLLKHFTCLT
EEECHHHHHHCEEEE		4.2819608861
374AcetylationIINTKLLKHFTCLTY
EECHHHHHHCEEEEE		47.2926051181
385PhosphorylationCLTYNNGRLRNLISD
EEEECCCHHHHHCCH		32.3720068231
390PhosphorylationNGRLRNLISDSMKAK
CCHHHHHCCHHHHHH		4.9920068231
391PhosphorylationGRLRNLISDSMKAKI
CHHHHHCCHHHHHHH		27.1421406692
393PhosphorylationLRNLISDSMKAKITA
HHHHCCHHHHHHHHH		18.5221406692
428AcetylationRDLKLSEKRMMEIAK
HHCCCCHHHHHHHHH		42.077851935
428UbiquitinationRDLKLSEKRMMEIAK
HHCCCCHHHHHHHHH		42.07-
435AcetylationKRMMEIAKAMRLKIS
HHHHHHHHHHHHHHH		48.6719608861
447PhosphorylationKISKRRVSVAAGSEE
HHHCCCEEEECCCCC		12.2920068231
452PhosphorylationRVSVAAGSEEDHKLG
CEEEECCCCCCCCCC		32.8420068231
457AcetylationAGSEEDHKLGTLSLP
CCCCCCCCCCCCCCC		62.0226051181
460PhosphorylationEEDHKLGTLSLPLPP
CCCCCCCCCCCCCCC		24.4921406692
462PhosphorylationDHKLGTLSLPLPPAQ
CCCCCCCCCCCCCCC		27.9821406692
470PhosphorylationLPLPPAQTSDRLAKR
CCCCCCCCHHHHHHH		34.4021406692
471PhosphorylationPLPPAQTSDRLAKRR
CCCCCCCHHHHHHHC		14.5121406692
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 RPA49_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
373KAcetylation

24207024
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 RPA49_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HNRL1_HUMANHNRNPUL1physical
17353931
DDX20_HUMANDDX20physical
17353931
DDX6_HUMANDDX6physical
17353931
QPCTL_HUMANQPCTLphysical
17353931
RPAC1_HUMANPOLR1Cphysical
17353931
RPAC1_HUMANPOLR1Cphysical
15226435
RPA34_HUMANCD3EAPphysical
15226435
UBF1_HUMANUBTFphysical
15226435
RPA1_HUMANPOLR1Aphysical
15226435
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 RPA49_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-225, AND MASSSPECTROMETRY.

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