RPA1_HUMAN - dbPTM
RPA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPA1_HUMAN
UniProt AC O95602
Protein Name DNA-directed RNA polymerase I subunit RPA1
Gene Name POLR1A
Organism Homo sapiens (Human).
Sequence Length 1720
Subcellular Localization Nucleus, nucleolus.
Protein Description DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity)..
Protein Sequence MLISKNMPWRRLQGISFGMYSAEELKKLSVKSITNPRYLDSLGNPSANGLYDLALGPADSKEVCSTCVQDFSNCSGHLGHIELPLTVYNPLLFDKLYLLLRGSCLNCHMLTCPRAVIHLLLCQLRVLEVGALQAVYELERILNRFLEENPDPSASEIREELEQYTTEIVQNNLLGSQGAHVKNVCESKSKLIALFWKAHMNAKRCPHCKTGRSVVRKEHNSKLTITFPAMVHRTAGQKDSEPLGIEEAQIGKRGYLTPTSAREHLSALWKNEGFFLNYLFSGMDDDGMESRFNPSVFFLDFLVVPPSRYRPVSRLGDQMFTNGQTVNLQAVMKDVVLIRKLLALMAQEQKLPEEVATPTTDEEKDSLIAIDRSFLSTLPGQSLIDKLYNIWIRLQSHVNIVFDSEMDKLMMDKYPGIRQILEKKEGLFRKHMMGKRVDYAARSVICPDMYINTNEIGIPMVFATKLTYPQPVTPWNVQELRQAVINGPNVHPGASMVINEDGSRTALSAVDMTQREAVAKQLLTPATGAPKPQGTKIVCRHVKNGDILLLNRQPTLHRPSIQAHRARILPEEKVLRLHYANCKAYNADFDGDEMNAHFPQSELGRAEAYVLACTDQQYLVPKDGQPLAGLIQDHMVSGASMTTRGCFFTREHYMELVYRGLTDKVGRVKLLSPSILKPFPLWTGKQVVSTLLINIIPEDHIPLNLSGKAKITGKAWVKETPRSVPGFNPDSMCESQVIIREGELLCGVLDKAHYGSSAYGLVHCCYEIYGGETSGKVLTCLARLFTAYLQLYRGFTLGVEDILVKPKADVKRQRIIEESTHCGPQAVRAALNLPEAASYDEVRGKWQDAHLGKDQRDFNMIDLKFKEEVNHYSNEINKACMPFGLHRQFPENSLQMMVQSGAKGSTVNTMQISCLLGQIELEGRRPPLMASGKSLPCFEPYEFTPRAGGFVTGRFLTGIKPPEFFFHCMAGREGLVDTAVKTSRSGYLQRCIIKHLEGLVVQYDLTVRDSDGSVVQFLYGEDGLDIPKTQFLQPKQFPFLASNYEVIMKSQHLHEVLSRADPKKALHHFRAIKKWQSKHPNTLLRRGAFLSYSQKIQEAVKALKLESENRNGRSPGTQEMLRMWYELDEESRRKYQKKAAACPDPSLSVWRPDIYFASVSETFETKVDDYSQEWAAQTEKSYEKSELSLDRLRTLLQLKWQRSLCEPGEAVGLLAAQSIGEPSTQMTLNTFHFAGRGEMNVTLGIPRLREILMVASANIKTPMMSVPVLNTKKALKRVKSLKKQLTRVCLGEVLQKIDVQESFCMEEKQNKFQVYQLRFQFLPHAYYQQEKCLRPEDILRFMETRFFKLLMESIKKKNNKASAFRNVNTRRATQRDLDNAGELGRSRGEQEGDEEEEGHIVDAEAEEGDADASDAKRKEKQEEEVDYESEEEEEREGEENDDEDMQEERNPHREGARKTQEQDEEVGLGTEEDPSLPALLTQPRKPTHSQEPQGPEAMERRVQAVREIHPFIDDYQYDTEESLWCQVTVKLPLMKINFDMSSLVVSLAHGAVIYATKGITRCLLNETTNNKNEKELVLNTEGINLPELFKYAEVLDLRRLYSNDIHAIANTYGIEAALRVIEKEIKDVFAVYGIAVDPRHLSLVADYMCFEGVYKPLNRFGIRSNSSPLQQMTFETSFQFLKQATMLGSHDELRSPSACLVVGKVVRGGTGLFELKQPLR
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
5Acetylation---MLISKNMPWRRL
---CCCCCCCCHHHH
50.727927295
5Methylation---MLISKNMPWRRL
---CCCCCCCCHHHH
50.727927295
5Ubiquitination---MLISKNMPWRRL
---CCCCCCCCHHHH
50.7222505724
31UbiquitinationELKKLSVKSITNPRY
HHHHCCCCCCCCCHH
32.5327667366
164PhosphorylationIREELEQYTTEIVQN
HHHHHHHHHHHHHHC
13.2722210691
165PhosphorylationREELEQYTTEIVQNN
HHHHHHHHHHHHHCC
20.0427080861
166PhosphorylationEELEQYTTEIVQNNL
HHHHHHHHHHHHCCC
20.8427080861
176PhosphorylationVQNNLLGSQGAHVKN
HHCCCCCCCCCHHHH
25.9720068231
187PhosphorylationHVKNVCESKSKLIAL
HHHHHHHCHHHHHHH
36.7822210691
190UbiquitinationNVCESKSKLIALFWK
HHHHCHHHHHHHHHH
47.88-
222AcetylationVRKEHNSKLTITFPA
ECCCCCCCEEEEECE
55.7725953088
222UbiquitinationVRKEHNSKLTITFPA
ECCCCCCCEEEEECE
55.77-
234PhosphorylationFPAMVHRTAGQKDSE
ECEEHHCCCCCCCCC
21.9123186163
238UbiquitinationVHRTAGQKDSEPLGI
HHCCCCCCCCCCCCC
63.4021906983
240PhosphorylationRTAGQKDSEPLGIEE
CCCCCCCCCCCCCCC
48.4230108239
252AcetylationIEEAQIGKRGYLTPT
CCCHHCCCCCCCCCC
44.2525953088
252UbiquitinationIEEAQIGKRGYLTPT
CCCHHCCCCCCCCCC
44.2521906983
350UbiquitinationALMAQEQKLPEEVAT
HHHHHHCCCCHHHCC
66.3221906983
357PhosphorylationKLPEEVATPTTDEEK
CCCHHHCCCCCCHHH
26.7530266825
359PhosphorylationPEEVATPTTDEEKDS
CHHHCCCCCCHHHHH
42.3930266825
360PhosphorylationEEVATPTTDEEKDSL
HHHCCCCCCHHHHHE
42.4930266825
364UbiquitinationTPTTDEEKDSLIAID
CCCCCHHHHHEEEEE
51.0421906983
366PhosphorylationTTDEEKDSLIAIDRS
CCCHHHHHEEEEEHH
32.5130266825
408UbiquitinationVFDSEMDKLMMDKYP
EECHHHHHHHHHCCH
36.6522817900
413UbiquitinationMDKLMMDKYPGIRQI
HHHHHHHCCHHHHHH
35.1321906983
443PhosphorylationRVDYAARSVICPDMY
CCCHHHHHCCCCCCE
15.8823532336
505PhosphorylationINEDGSRTALSAVDM
ECCCCCCCHHHHCCC
33.3827134283
508PhosphorylationDGSRTALSAVDMTQR
CCCCCHHHHCCCHHH
24.6327134283
512SulfoxidationTALSAVDMTQREAVA
CHHHHCCCHHHHHHH
2.5021406390
513PhosphorylationALSAVDMTQREAVAK
HHHHCCCHHHHHHHH
21.7327134283
520UbiquitinationTQREAVAKQLLTPAT
HHHHHHHHHHCCCCC
34.5721963094
531UbiquitinationTPATGAPKPQGTKIV
CCCCCCCCCCCCEEE
49.8129967540
536UbiquitinationAPKPQGTKIVCRHVK
CCCCCCCEEEEEECC
39.71-
543UbiquitinationKIVCRHVKNGDILLL
EEEEEECCCCCEEEE
49.43-
573UbiquitinationARILPEEKVLRLHYA
CCCCCHHHHHHHHHC
44.9322817900
583UbiquitinationRLHYANCKAYNADFD
HHHHCCCEECCCCCC
54.4321963094
664UbiquitinationVYRGLTDKVGRVKLL
HHCCCCCCCCCEEEC
41.16-
669UbiquitinationTDKVGRVKLLSPSIL
CCCCCCEEECCHHHC
42.2027667366
674PhosphorylationRVKLLSPSILKPFPL
CEEECCHHHCCCCCC
36.8624719451
677UbiquitinationLLSPSILKPFPLWTG
ECCHHHCCCCCCCCC
42.8321963094
714UbiquitinationGKAKITGKAWVKETP
CCCEEECEEECCCCC
30.3529967540
718UbiquitinationITGKAWVKETPRSVP
EECEEECCCCCCCCC
45.2127667366
805UbiquitinationGVEDILVKPKADVKR
CHHHEEECCCCHHCH
37.0421906983
807UbiquitinationEDILVKPKADVKRQR
HHEEECCCCHHCHHH
52.0522817900
838PhosphorylationLNLPEAASYDEVRGK
HCCCHHCCHHHHCCC
39.9228796482
839PhosphorylationNLPEAASYDEVRGKW
CCCHHCCHHHHCCCC
16.0528796482
845UbiquitinationSYDEVRGKWQDAHLG
CHHHHCCCCHHHCCC
30.9929967540
853AcetylationWQDAHLGKDQRDFNM
CHHHCCCCCCCCCCC
57.9811925265
853UbiquitinationWQDAHLGKDQRDFNM
CHHHCCCCCCCCCCC
57.9829967540
864UbiquitinationDFNMIDLKFKEEVNH
CCCCCCHHHHHHHHH
51.1221906983
866AcetylationNMIDLKFKEEVNHYS
CCCCHHHHHHHHHHH
51.9123954790
866UbiquitinationNMIDLKFKEEVNHYS
CCCCHHHHHHHHHHH
51.9122817900
872PhosphorylationFKEEVNHYSNEINKA
HHHHHHHHHHHHHHH
14.1627642862
878UbiquitinationHYSNEINKACMPFGL
HHHHHHHHHHCCCCC
48.9329967540
893PhosphorylationHRQFPENSLQMMVQS
CCCCCCCHHHHHHHC
20.5129978859
900PhosphorylationSLQMMVQSGAKGSTV
HHHHHHHCCCCCCCC
29.3429978859
933AcetylationPPLMASGKSLPCFEP
CCCCCCCCCCCCCCC
46.4526051181
933UbiquitinationPPLMASGKSLPCFEP
CCCCCCCCCCCCCCC
46.45-
934PhosphorylationPLMASGKSLPCFEPY
CCCCCCCCCCCCCCC
40.86-
941PhosphorylationSLPCFEPYEFTPRAG
CCCCCCCCEECCCCC
19.24-
952PhosphorylationPRAGGFVTGRFLTGI
CCCCCEECCCCCCCC
22.0024719451
960UbiquitinationGRFLTGIKPPEFFFH
CCCCCCCCCCHHHHH
56.73-
981UbiquitinationGLVDTAVKTSRSGYL
CCCCHHHHHCCCCHH
38.0221906983
1028UbiquitinationEDGLDIPKTQFLQPK
CCCCCCCCCCCCCCC
56.1222817900
1042PhosphorylationKQFPFLASNYEVIMK
CCCCCHHCCCEEEEC
41.9325348772
1044PhosphorylationFPFLASNYEVIMKSQ
CCCHHCCCEEEECHH
14.7425348772
1049MethylationSNYEVIMKSQHLHEV
CCCEEEECHHHHHHH
35.52115975261
1058PhosphorylationQHLHEVLSRADPKKA
HHHHHHHHCCCHHHH
30.51-
1063UbiquitinationVLSRADPKKALHHFR
HHHCCCHHHHHHHHH
51.7529967540
1078UbiquitinationAIKKWQSKHPNTLLR
HHHHHHHCCCCHHHH
48.24-
1091PhosphorylationLRRGAFLSYSQKIQE
HHCCCCCCHHHHHHH
19.1129514088
1092PhosphorylationRRGAFLSYSQKIQEA
HCCCCCCHHHHHHHH
19.7829514088
1093PhosphorylationRGAFLSYSQKIQEAV
CCCCCCHHHHHHHHH
22.9429514088
1095UbiquitinationAFLSYSQKIQEAVKA
CCCCHHHHHHHHHHH
40.18-
1101UbiquitinationQKIQEAVKALKLESE
HHHHHHHHHHHHCCC
55.8621906983
1104UbiquitinationQEAVKALKLESENRN
HHHHHHHHHCCCCCC
55.8822817900
1125PhosphorylationQEMLRMWYELDEESR
HHHHHHHHHCCHHHH
9.4019658100
1180UbiquitinationEWAAQTEKSYEKSEL
HHHHHCCHHHHCCCC
62.8221906983
1184UbiquitinationQTEKSYEKSELSLDR
HCCHHHHCCCCCHHH
40.7821906983
1185PhosphorylationTEKSYEKSELSLDRL
CCHHHHCCCCCHHHH
31.6520860994
1191MethylationKSELSLDRLRTLLQL
CCCCCHHHHHHHHHH
31.22115488109
1199UbiquitinationLRTLLQLKWQRSLCE
HHHHHHHHHHHHCCC
28.4621963094
1242PhosphorylationGRGEMNVTLGIPRLR
CCCCCCEEECCCHHH
17.7922210691
1256PhosphorylationREILMVASANIKTPM
HHHHHHHCCCCCCCC
15.50-
1261PhosphorylationVASANIKTPMMSVPV
HHCCCCCCCCCCCCC
16.7820068231
1265PhosphorylationNIKTPMMSVPVLNTK
CCCCCCCCCCCCCHH
19.6030257219
1271PhosphorylationMSVPVLNTKKALKRV
CCCCCCCHHHHHHHH
29.7520068231
1273UbiquitinationVPVLNTKKALKRVKS
CCCCCHHHHHHHHHH
57.84-
1280PhosphorylationKALKRVKSLKKQLTR
HHHHHHHHHHHHHHH
42.4324719451
1283UbiquitinationKRVKSLKKQLTRVCL
HHHHHHHHHHHHHHH
56.7024816145
1308AcetylationESFCMEEKQNKFQVY
CCCCCHHHCCCCEEE
45.9526051181
1311AcetylationCMEEKQNKFQVYQLR
CCHHHCCCCEEEEHH
34.3826051181
1311UbiquitinationCMEEKQNKFQVYQLR
CCHHHCCCCEEEEHH
34.38-
1315PhosphorylationKQNKFQVYQLRFQFL
HCCCCEEEEHHHHHC
7.3425599653
1331UbiquitinationHAYYQQEKCLRPEDI
HHHHCHHCCCCHHHH
33.94-
1348AcetylationFMETRFFKLLMESIK
HHHHHHHHHHHHHHH
37.6919820035
1356UbiquitinationLLMESIKKKNNKASA
HHHHHHHHHCCCHHH
60.09-
1360UbiquitinationSIKKKNNKASAFRNV
HHHHHCCCHHHHHCC
53.7827667366
1373PhosphorylationNVNTRRATQRDLDNA
CCHHHHHHHHHHHCH
23.4824247654
1386PhosphorylationNAGELGRSRGEQEGD
CHHHHHHCCCCCCCC
42.7218669648
1413PhosphorylationEEGDADASDAKRKEK
HCCCCCHHHHHHHHH
38.35-
1416UbiquitinationDADASDAKRKEKQEE
CCCHHHHHHHHHHHH
69.8324816145
1427PhosphorylationKQEEEVDYESEEEEE
HHHHHCCCCCHHHHH
26.9123927012
1429PhosphorylationEEEVDYESEEEEERE
HHHCCCCCHHHHHHC
44.0423401153
1459PhosphorylationHREGARKTQEQDEEV
CHHHHHHCHHHHHCC
31.6122210691
1475PhosphorylationLGTEEDPSLPALLTQ
CCCCCCCCCCHHHCC
60.3422210691
1481PhosphorylationPSLPALLTQPRKPTH
CCCCHHHCCCCCCCC
37.0622210691
1485UbiquitinationALLTQPRKPTHSQEP
HHHCCCCCCCCCCCC
62.03-
1487PhosphorylationLTQPRKPTHSQEPQG
HCCCCCCCCCCCCCC
36.8823663014
1489PhosphorylationQPRKPTHSQEPQGPE
CCCCCCCCCCCCCHH
38.4225159151
1541PhosphorylationMKINFDMSSLVVSLA
EEEECCHHHHHHHHH
23.5120068231
1542PhosphorylationKINFDMSSLVVSLAH
EEECCHHHHHHHHHH
20.6720068231
1546PhosphorylationDMSSLVVSLAHGAVI
CHHHHHHHHHHCCHH
16.6220068231
1554PhosphorylationLAHGAVIYATKGITR
HHHCCHHHCCCCHHH
11.1320068231
1556PhosphorylationHGAVIYATKGITRCL
HCCHHHCCCCHHHHH
16.9020068231
1571UbiquitinationLNETTNNKNEKELVL
HCCCCCCCCHHEEEE
69.4321963094
1574UbiquitinationTTNNKNEKELVLNTE
CCCCCCHHEEEEECC
66.7821906983
1580PhosphorylationEKELVLNTEGINLPE
HHEEEEECCCCCHHH
31.2819060867
1695PhosphorylationGSHDELRSPSACLVV
CCCCCCCCCCCEEEE
35.5125159151
1697PhosphorylationHDELRSPSACLVVGK
CCCCCCCCCEEEEEE
32.6227251275
1704AcetylationSACLVVGKVVRGGTG
CCEEEEEEEEECCCC
26.4126051181
1704UbiquitinationSACLVVGKVVRGGTG
CCEEEEEEEEECCCC
26.4123000965
1707MethylationLVVGKVVRGGTGLFE
EEEEEEEECCCCHHE
40.59115488117
1716UbiquitinationGTGLFELKQPLR---
CCCHHEECCCCC---
42.5521906983

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 RPA1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPA1_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 RPA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPA2_HUMANPOLR1Bphysical
19214185
SSRP1_HUMANSSRP1physical
19214185
RPA34_HUMANCD3EAPphysical
19214185
RPA49_HUMANPOLR1Ephysical
19214185
RPAC1_HUMANPOLR1Cphysical
19214185
RPAB1_HUMANPOLR2Ephysical
19214185
RPAB3_HUMANPOLR2Hphysical
19214185
RPAB5_HUMANPOLR2Lphysical
19214185
SP16H_HUMANSUPT16Hphysical
19214185
SIR7_HUMANSIRT7physical
16618798
SIR7_HUMANSIRT7physical
22147730
UBF1_HUMANUBTFphysical
22147730
MBB1A_HUMANMYBBP1Aphysical
22147730
SMCA5_HUMANSMARCA5physical
22147730
SIR7_HUMANSIRT7physical
22586326
MBB1A_HUMANMYBBP1Aphysical
22586326
SMCA5_HUMANSMARCA5physical
22586326
UBF1_HUMANUBTFphysical
22586326
RPA2_HUMANPOLR1Bphysical
22939629
RPAB3_HUMANPOLR2Hphysical
22939629
RPAC1_HUMANPOLR1Cphysical
22939629
RPAB1_HUMANPOLR2Ephysical
22939629
RPC1_HUMANPOLR3Aphysical
22939629
KAT2B_HUMANKAT2Bphysical
23667505
EF1A1_HUMANEEF1A1physical
26344197
EF1A2_HUMANEEF1A2physical
26344197
RPAB1_HUMANPOLR2Ephysical
26344197
RPC1_HUMANPOLR3Aphysical
26344197
RPC3_HUMANPOLR3Cphysical
26344197
RL10A_HUMANRPL10Aphysical
26344197
RL9_HUMANRPL9physical
26344197
CIP4_HUMANTRIP10physical
26344197
RPA43_HUMANTWISTNBphysical
26344197
DIAP2_HUMANDIAPH2physical
26496610
PFD2_HUMANPFDN2physical
26496610
RPAB1_HUMANPOLR2Ephysical
26496610
RPAB2_HUMANPOLR2Fphysical
26496610
RPAB3_HUMANPOLR2Hphysical
26496610
RPAB4_HUMANPOLR2Kphysical
26496610
SPT6H_HUMANSUPT6Hphysical
26496610
RUVB1_HUMANRUVBL1physical
26496610
RMP_HUMANURI1physical
26496610
TAF1C_HUMANTAF1Cphysical
26496610
TAF1B_HUMANTAF1Bphysical
26496610
RPAC1_HUMANPOLR1Cphysical
26496610
PFD6_HUMANPFDN6physical
26496610
RPA34_HUMANCD3EAPphysical
26496610
RUVB2_HUMANRUVBL2physical
26496610
GPN1_HUMANGPN1physical
26496610
RPA12_HUMANZNRD1physical
26496610
RRN3_HUMANRRN3physical
26496610
PIHD1_HUMANPIH1D1physical
26496610
K1522_HUMANKIAA1522physical
26496610
NCK5L_HUMANNCKAP5Lphysical
26496610
RPA49_HUMANPOLR1Ephysical
26496610
RPAP3_HUMANRPAP3physical
26496610
PDRG1_HUMANPDRG1physical
26496610
RPA2_HUMANPOLR1Bphysical
26496610
WDR92_HUMANWDR92physical
26496610
RPA43_HUMANTWISTNBphysical
26496610
NOP58_HUMANNOP58physical
26399832
KBTB8_HUMANKBTBD8physical
26399832
RPA2_HUMANPOLR1Bphysical
26399832
CSK21_HUMANCSNK2A1physical
26399832
SHPRH_HUMANSHPRHphysical
28400511
UBF1_HUMANUBTFphysical
28400511

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 RPA1_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-1386, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1580, AND MASSSPECTROMETRY.

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