RFC1_HUMAN - dbPTM
RFC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RFC1_HUMAN
UniProt AC P35251
Protein Name Replication factor C subunit 1
Gene Name RFC1
Organism Homo sapiens (Human).
Sequence Length 1148
Subcellular Localization Nucleus.
Protein Description The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Could play a role in DNA transcription regulation as well as DNA replication and/or repair. Can bind single- or double-stranded DNA.; Interacts with C-terminus of PCNA. 5' phosphate residue is required for binding of the N-terminal DNA-binding domain to duplex DNA, suggesting a role in recognition of non-primer template DNA structures during replication and/or repair..
Protein Sequence MDIRKFFGVIPSGKKLVSETVKKNEKTKSDEETLKAKKGIKEIKVNSSRKEDDFKQKQPSKKKRIIYDSDSESEETLQVKNAKKPPEKLPVSSKPGKISRQDPVTYISETDEEDDFMCKKAASKSKENGRSTNSHLGTSNMKKNEENTKTKNKPLSPIKLTPTSVLDYFGTGSVQRSNKKMVASKRKELSQNTDESGLNDEAIAKQLQLDEDAELERQLHEDEEFARTLAMLDEEPKTKKARKDTEAGETFSSVQANLSKAEKHKYPHKVKTAQVSDERKSYSPRKQSKYESSKESQQHSKSSADKIGEVSSPKASSKLAIMKRKEESSYKEIEPVASKRKENAIKLKGETKTPKKTKSSPAKKESVSPEDSEKKRTNYQAYRSYLNREGPKALGSKEIPKGAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAALGTKIIDEDGLLNLIRTMPGKKSKYEIAVETEMKKESKLERTPQKNVQGKRKISPSKKESESKKSRPTSKRDSLAKTIKKETDVFWKSLDFKEQVAEETSGDSKARNLADDSSENKVENLLWVDKYKPTSLKTIIGQQGDQSCANKLLRWLRNWQKSSSEDKKHAAKFGKFSGKDDGSSFKAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSKSSLKAIVAESLNNTSIKGFYSNGAASSVSTKHALIMDEVDGMAGNEDRGGIQELIGLIKHTKIPIICMCNDRNHPKIRSLVHYCFDLRFQRPRVEQIKGAMMSIAFKEGLKIPPPAMNEIILGANQDIRQVLHNLSMWCARSKALTYDQAKADSHRAKKDIKMGPFDVARKVFAAGEETAHMSLVDKSDLFFHDYSIAPLFVQENYIHVKPVAAGGDMKKHLMLLSRAADSICDGDLVDSQIRSKQNWSLLPAQAIYASVLPGELMRGYMTQFPTFPSWLGKHSSTGKHDRIVQDLALHMSLRTYSSKRTVNMDYLSLLRDALVQPLTSQGVDGVQDVVALMDTYYLMKEDFENIMEISSWGGKPSPFSKLDPKVKAAFTRAYNKEAHLTPYSLQAIKASRHSTSPSLDSEYNEELNEDDSQSDEKDQDAIETDAMIKKKTKSSKPSKPEKDKEPRKGKGKSSKK
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
12PhosphorylationKFFGVIPSGKKLVSE
HHCCCCCCCCCHHHH
52.7125159151
142-HydroxyisobutyrylationFGVIPSGKKLVSETV
CCCCCCCCCHHHHHH
47.47-
14AcetylationFGVIPSGKKLVSETV
CCCCCCCCCHHHHHH
47.4725953088
14UbiquitinationFGVIPSGKKLVSETV
CCCCCCCCCHHHHHH
47.4727667366
15AcetylationGVIPSGKKLVSETVK
CCCCCCCCHHHHHHH
58.6125953088
27PhosphorylationTVKKNEKTKSDEETL
HHHHCCCCCCHHHHH
29.6028176443
29PhosphorylationKKNEKTKSDEETLKA
HHCCCCCCHHHHHHH
56.3325849741
33PhosphorylationKTKSDEETLKAKKGI
CCCCHHHHHHHHHCC
31.3528176443
41AcetylationLKAKKGIKEIKVNSS
HHHHHCCCEEECCCC
63.1525953088
50SumoylationIKVNSSRKEDDFKQK
EECCCCCCCCCCCCC
68.4025772364
55UbiquitinationSRKEDDFKQKQPSKK
CCCCCCCCCCCCCCC
64.6824816145
60PhosphorylationDFKQKQPSKKKRIIY
CCCCCCCCCCCCEEE
55.3926074081
67PhosphorylationSKKKRIIYDSDSESE
CCCCCEEECCCCCCH
13.6629255136
67 (in isoform 2)Phosphorylation-13.66-
69PhosphorylationKKRIIYDSDSESEET
CCCEEECCCCCCHHH
26.5129255136
69 (in isoform 2)Phosphorylation-26.51-
71PhosphorylationRIIYDSDSESEETLQ
CEEECCCCCCHHHHC
47.1529255136
71 (in isoform 2)Phosphorylation-47.15-
73PhosphorylationIYDSDSESEETLQVK
EECCCCCCHHHHCCC
44.6929255136
73 (in isoform 2)Phosphorylation-44.69-
76PhosphorylationSDSESEETLQVKNAK
CCCCCHHHHCCCCCC
20.5930266825
76 (in isoform 2)Phosphorylation-20.59-
92PhosphorylationPPEKLPVSSKPGKIS
CCHHCCCCCCCCCCC
30.6125627689
93PhosphorylationPEKLPVSSKPGKISR
CHHCCCCCCCCCCCC
43.0028555341
94AcetylationEKLPVSSKPGKISRQ
HHCCCCCCCCCCCCC
50.7325953088
97AcetylationPVSSKPGKISRQDPV
CCCCCCCCCCCCCCC
46.1425953088
97UbiquitinationPVSSKPGKISRQDPV
CCCCCCCCCCCCCCC
46.1429967540
99PhosphorylationSSKPGKISRQDPVTY
CCCCCCCCCCCCCCE
27.6320068231
99 (in isoform 2)Phosphorylation-27.63-
105PhosphorylationISRQDPVTYISETDE
CCCCCCCCEEECCCC
22.1130266825
105 (in isoform 2)Phosphorylation-22.11-
106PhosphorylationSRQDPVTYISETDEE
CCCCCCCEEECCCCC
11.5930266825
108PhosphorylationQDPVTYISETDEEDD
CCCCCEEECCCCCCC
24.8322167270
108 (in isoform 2)Phosphorylation-24.83-
110PhosphorylationPVTYISETDEEDDFM
CCCEEECCCCCCCHH
41.7522167270
110 (in isoform 2)Phosphorylation-41.75-
123PhosphorylationFMCKKAASKSKENGR
HHHHHHHHCCHHCCC
42.1820860994
131PhosphorylationKSKENGRSTNSHLGT
CCHHCCCCCCCCCCC
33.08-
134PhosphorylationENGRSTNSHLGTSNM
HCCCCCCCCCCCCCC
21.8530576142
138PhosphorylationSTNSHLGTSNMKKNE
CCCCCCCCCCCCCCC
24.2425627689
139PhosphorylationTNSHLGTSNMKKNEE
CCCCCCCCCCCCCCC
32.8825159151
142AcetylationHLGTSNMKKNEENTK
CCCCCCCCCCCCCCC
57.6125953088
148PhosphorylationMKKNEENTKTKNKPL
CCCCCCCCCCCCCCC
43.2930576142
149AcetylationKKNEENTKTKNKPLS
CCCCCCCCCCCCCCC
69.9130585933
150PhosphorylationKNEENTKTKNKPLSP
CCCCCCCCCCCCCCC
37.5026074081
153AcetylationENTKTKNKPLSPIKL
CCCCCCCCCCCCCCC
49.2230585939
156PhosphorylationKTKNKPLSPIKLTPT
CCCCCCCCCCCCCCC
32.8625159151
156 (in isoform 2)Phosphorylation-32.86-
161PhosphorylationPLSPIKLTPTSVLDY
CCCCCCCCCCCHHHH
21.3723927012
161 (in isoform 2)Phosphorylation-21.37-
163PhosphorylationSPIKLTPTSVLDYFG
CCCCCCCCCHHHHHC
26.6523927012
163 (in isoform 2)Phosphorylation-26.65-
164PhosphorylationPIKLTPTSVLDYFGT
CCCCCCCCHHHHHCC
23.1425159151
164 (in isoform 2)Phosphorylation-23.14-
168PhosphorylationTPTSVLDYFGTGSVQ
CCCCHHHHHCCCCCC
10.3523927012
168 (in isoform 2)Phosphorylation-10.35-
171PhosphorylationSVLDYFGTGSVQRSN
CHHHHHCCCCCCCCC
19.1823927012
171 (in isoform 2)Phosphorylation-19.18-
173PhosphorylationLDYFGTGSVQRSNKK
HHHHCCCCCCCCCHH
18.2125159151
173 (in isoform 2)Phosphorylation-18.21-
177PhosphorylationGTGSVQRSNKKMVAS
CCCCCCCCCHHHHHH
35.5925159151
185UbiquitinationNKKMVASKRKELSQN
CHHHHHHHHHHHHCC
58.7224816145
190PhosphorylationASKRKELSQNTDESG
HHHHHHHHCCCCCCC
23.6029255136
190 (in isoform 2)Phosphorylation-23.60-
193PhosphorylationRKELSQNTDESGLND
HHHHHCCCCCCCCCH
33.2430266825
193 (in isoform 2)Phosphorylation-33.24-
196PhosphorylationLSQNTDESGLNDEAI
HHCCCCCCCCCHHHH
51.9330266825
217UbiquitinationDEDAELERQLHEDEE
CCHHHHHHHHHCCHH
57.9221963094
234UbiquitinationRTLAMLDEEPKTKKA
HHHHHHCCCCCCCCC
72.7022817900
237UbiquitinationAMLDEEPKTKKARKD
HHHCCCCCCCCCCCC
76.0221906983
237 (in isoform 1)Ubiquitination-76.0221890473
237 (in isoform 2)Ubiquitination-76.0221890473
239UbiquitinationLDEEPKTKKARKDTE
HCCCCCCCCCCCCCC
51.0322817900
240UbiquitinationDEEPKTKKARKDTEA
CCCCCCCCCCCCCCC
59.6722817900
243UbiquitinationPKTKKARKDTEAGET
CCCCCCCCCCCCHHC
74.0821906983
243 (in isoform 1)Ubiquitination-74.0821890473
243 (in isoform 2)Ubiquitination-74.0821890473
245PhosphorylationTKKARKDTEAGETFS
CCCCCCCCCCHHCHH
30.6726133373
245UbiquitinationTKKARKDTEAGETFS
CCCCCCCCCCHHCHH
30.6727667366
250PhosphorylationKDTEAGETFSSVQAN
CCCCCHHCHHHHHHH
28.0928555341
253PhosphorylationEAGETFSSVQANLSK
CCHHCHHHHHHHHHH
17.6628555341
259PhosphorylationSSVQANLSKAEKHKY
HHHHHHHHHHHHCCC
29.6321712546
260AcetylationSVQANLSKAEKHKYP
HHHHHHHHHHHCCCC
64.8325953088
260UbiquitinationSVQANLSKAEKHKYP
HHHHHHHHHHHCCCC
64.8321906983
260 (in isoform 1)Ubiquitination-64.8321890473
260 (in isoform 2)Ubiquitination-64.8321890473
263UbiquitinationANLSKAEKHKYPHKV
HHHHHHHHCCCCCCC
50.7022817900
265UbiquitinationLSKAEKHKYPHKVKT
HHHHHHCCCCCCCEE
72.1122817900
271UbiquitinationHKYPHKVKTAQVSDE
CCCCCCCEECCCCCC
42.8427667366
272PhosphorylationKYPHKVKTAQVSDER
CCCCCCEECCCCCCC
25.8821712546
276PhosphorylationKVKTAQVSDERKSYS
CCEECCCCCCCCCCC
22.9821712546
281PhosphorylationQVSDERKSYSPRKQS
CCCCCCCCCCCCHHH
36.7426055452
281 (in isoform 2)Phosphorylation-36.74-
282PhosphorylationVSDERKSYSPRKQSK
CCCCCCCCCCCHHHH
26.2320068231
283PhosphorylationSDERKSYSPRKQSKY
CCCCCCCCCCHHHHH
25.8926055452
283 (in isoform 2)Phosphorylation-25.89-
302PhosphorylationESQQHSKSSADKIGE
HHHHHCHHHHHHHHC
33.5024732914
303PhosphorylationSQQHSKSSADKIGEV
HHHHCHHHHHHHHCC
44.2024732914
306AcetylationHSKSSADKIGEVSSP
HCHHHHHHHHCCCCC
52.9425953088
306UbiquitinationHSKSSADKIGEVSSP
HCHHHHHHHHCCCCC
52.94-
311PhosphorylationADKIGEVSSPKASSK
HHHHHCCCCCCHHHH
36.3023401153
312PhosphorylationDKIGEVSSPKASSKL
HHHHCCCCCCHHHHH
35.2829255136
312 (in isoform 2)Phosphorylation-35.28-
313UbiquitinationKIGEVSSPKASSKLA
HHHCCCCCCHHHHHH
28.8224816145
316PhosphorylationEVSSPKASSKLAIMK
CCCCCCHHHHHHHHH
33.8526074081
317PhosphorylationVSSPKASSKLAIMKR
CCCCCHHHHHHHHHC
36.2326074081
318AcetylationSSPKASSKLAIMKRK
CCCCHHHHHHHHHCC
39.1725953088
318UbiquitinationSSPKASSKLAIMKRK
CCCCHHHHHHHHHCC
39.1729967540
323MethylationSSKLAIMKRKEESSY
HHHHHHHHCCCCCCC
54.96116252259
325UbiquitinationKLAIMKRKEESSYKE
HHHHHHCCCCCCCCC
61.38-
328PhosphorylationIMKRKEESSYKEIEP
HHHCCCCCCCCCCCC
39.8128796482
329PhosphorylationMKRKEESSYKEIEPV
HHCCCCCCCCCCCCC
43.4328796482
330PhosphorylationKRKEESSYKEIEPVA
HCCCCCCCCCCCCCC
23.1728796482
331AcetylationRKEESSYKEIEPVAS
CCCCCCCCCCCCCCC
54.9126051181
331UbiquitinationRKEESSYKEIEPVAS
CCCCCCCCCCCCCCC
54.91-
339AcetylationEIEPVASKRKENAIK
CCCCCCCCCHHHCCC
58.7225953088
339UbiquitinationEIEPVASKRKENAIK
CCCCCCCCCHHHCCC
58.7224816145
353PhosphorylationKLKGETKTPKKTKSS
CCCCCCCCCCCCCCC
48.0024719451
357PhosphorylationETKTPKKTKSSPAKK
CCCCCCCCCCCCCCC
42.1426074081
359PhosphorylationKTPKKTKSSPAKKES
CCCCCCCCCCCCCCC
46.9518669648
359 (in isoform 2)Phosphorylation-46.95-
360PhosphorylationTPKKTKSSPAKKESV
CCCCCCCCCCCCCCC
30.3628985074
366PhosphorylationSSPAKKESVSPEDSE
CCCCCCCCCCHHHHH
36.4530266825
368PhosphorylationPAKKESVSPEDSEKK
CCCCCCCCHHHHHHH
31.6729255136
368 (in isoform 2)Phosphorylation-31.67-
372PhosphorylationESVSPEDSEKKRTNY
CCCCHHHHHHHHHHH
50.0522167270
379PhosphorylationSEKKRTNYQAYRSYL
HHHHHHHHHHHHHHH
8.23-
382PhosphorylationKRTNYQAYRSYLNRE
HHHHHHHHHHHHCCC
5.65-
384PhosphorylationTNYQAYRSYLNREGP
HHHHHHHHHHCCCCC
22.6928555341
396PhosphorylationEGPKALGSKEIPKGA
CCCCCCCCCCCCCCH
28.1520363803
432UbiquitinationEAKSLIERYGGKVTG
HHHHHHHHHCCEEEC
28.5322817900
435UbiquitinationSLIERYGGKVTGNVS
HHHHHHCCEEECCCC
16.6022817900
436UbiquitinationLIERYGGKVTGNVSK
HHHHHCCEEECCCCC
32.06-
442UbiquitinationGKVTGNVSKKTNYLV
CEEECCCCCCCCEEE
32.2233845483
443AcetylationKVTGNVSKKTNYLVM
EEECCCCCCCCEEEE
60.3712656497
447PhosphorylationNVSKKTNYLVMGRDS
CCCCCCCEEEEECCC
13.1022210691
454PhosphorylationYLVMGRDSGQSKSDK
EEEEECCCCCCHHHH
37.0522210691
457PhosphorylationMGRDSGQSKSDKAAA
EECCCCCCHHHHHHH
37.3422210691
458UbiquitinationGRDSGQSKSDKAAAL
ECCCCCCHHHHHHHH
55.5822817900
459PhosphorylationRDSGQSKSDKAAALG
CCCCCCHHHHHHHHC
49.9827251275
461AcetylationSGQSKSDKAAALGTK
CCCCHHHHHHHHCCE
47.1925953088
461UbiquitinationSGQSKSDKAAALGTK
CCCCHHHHHHHHCCE
47.1922817900
461 (in isoform 1)Ubiquitination-47.1921890473
461 (in isoform 2)Ubiquitination-47.1921890473
467PhosphorylationDKAAALGTKIIDEDG
HHHHHHCCEEECCCC
21.6627251275
468UbiquitinationKAAALGTKIIDEDGL
HHHHHCCEEECCCCH
35.5521906983
468 (in isoform 1)Ubiquitination-35.5521890473
468 (in isoform 2)Ubiquitination-35.5521890473
486AcetylationIRTMPGKKSKYEIAV
HHCCCCCCCHHEEEE
59.087261903
488AcetylationTMPGKKSKYEIAVET
CCCCCCCHHEEEEEC
56.647261913
488UbiquitinationTMPGKKSKYEIAVET
CCCCCCCHHEEEEEC
56.6424816145
489PhosphorylationMPGKKSKYEIAVETE
CCCCCCHHEEEEECH
21.4720068231
498SumoylationIAVETEMKKESKLER
EEEECHHHHHHHCCC
47.35-
498UbiquitinationIAVETEMKKESKLER
EEEECHHHHHHHCCC
47.35-
506PhosphorylationKESKLERTPQKNVQG
HHHHCCCCCCCCCCC
22.2423401153
506 (in isoform 2)Phosphorylation-22.24-
509AcetylationKLERTPQKNVQGKRK
HCCCCCCCCCCCCCC
61.367664335
514AcetylationPQKNVQGKRKISPSK
CCCCCCCCCCCCCCH
33.172380553
514UbiquitinationPQKNVQGKRKISPSK
CCCCCCCCCCCCCCH
33.1724816145
518PhosphorylationVQGKRKISPSKKESE
CCCCCCCCCCHHHCC
26.5928102081
518 (in isoform 2)Phosphorylation-26.59-
520PhosphorylationGKRKISPSKKESESK
CCCCCCCCHHHCCCC
49.9623403867
520 (in isoform 2)Phosphorylation-49.96-
525UbiquitinationSPSKKESESKKSRPT
CCCHHHCCCCCCCCC
68.6121890473
530UbiquitinationESESKKSRPTSKRDS
HCCCCCCCCCCHHHH
47.6022817900
537PhosphorylationRPTSKRDSLAKTIKK
CCCCHHHHHHHHHHH
33.9728176443
542UbiquitinationRDSLAKTIKKETDVF
HHHHHHHHHHHHHHH
6.2233845483
551UbiquitinationKETDVFWKSLDFKEQ
HHHHHHHHHCCHHHH
29.6722817900
551 (in isoform 1)Ubiquitination-29.6721890473
551 (in isoform 2)Ubiquitination-29.6721890473
552PhosphorylationETDVFWKSLDFKEQV
HHHHHHHHCCHHHHH
24.6229978859
556SumoylationFWKSLDFKEQVAEET
HHHHCCHHHHHHHHC
47.07-
556UbiquitinationFWKSLDFKEQVAEET
HHHHCCHHHHHHHHC
47.0721906983
556 (in isoform 1)Ubiquitination-47.0721890473
556 (in isoform 2)Ubiquitination-47.0721890473
563PhosphorylationKEQVAEETSGDSKAR
HHHHHHHCCCCHHHH
29.5225850435
564PhosphorylationEQVAEETSGDSKARN
HHHHHHCCCCHHHHH
43.8325849741
567PhosphorylationAEETSGDSKARNLAD
HHHCCCCHHHHHCCC
31.5725850435
568SumoylationEETSGDSKARNLADD
HHCCCCHHHHHCCCC
56.98-
568SumoylationEETSGDSKARNLADD
HHCCCCHHHHHCCCC
56.98-
568UbiquitinationEETSGDSKARNLADD
HHCCCCHHHHHCCCC
56.9821906983
568 (in isoform 1)Ubiquitination-56.9821890473
568 (in isoform 2)Ubiquitination-56.9821890473
572UbiquitinationGDSKARNLADDSSEN
CCHHHHHCCCCCCCC
4.6321890473
576PhosphorylationARNLADDSSENKVEN
HHHCCCCCCCCCHHH
39.8520873877
577PhosphorylationRNLADDSSENKVENL
HHCCCCCCCCCHHHH
52.7820873877
580AcetylationADDSSENKVENLLWV
CCCCCCCCHHHHEEE
47.0426051181
580UbiquitinationADDSSENKVENLLWV
CCCCCCCCHHHHEEE
47.0429967540
589UbiquitinationENLLWVDKYKPTSLK
HHHEEECCCCCCCHH
45.6229967540
596UbiquitinationKYKPTSLKTIIGQQG
CCCCCCHHHHCCCCC
37.1329967540
597PhosphorylationYKPTSLKTIIGQQGD
CCCCCHHHHCCCCCC
24.1027732954
606PhosphorylationIGQQGDQSCANKLLR
CCCCCCHHHHHHHHH
21.6727732954
610AcetylationGDQSCANKLLRWLRN
CCHHHHHHHHHHHHH
30.3023749302
610UbiquitinationGDQSCANKLLRWLRN
CCHHHHHHHHHHHHH
30.30-
618UbiquitinationLLRWLRNWQKSSSED
HHHHHHHHHHCCHHH
10.6721890473
619UbiquitinationLRWLRNWQKSSSEDK
HHHHHHHHHCCHHHH
39.0221890473
633AcetylationKKHAAKFGKFSGKDD
HHHHHHHHCCCCCCC
29.4119608861
633 (in isoform 2)Acetylation-29.41-
634AcetylationKHAAKFGKFSGKDDG
HHHHHHHCCCCCCCC
39.2219608861
636PhosphorylationAAKFGKFSGKDDGSS
HHHHHCCCCCCCCCC
48.7128555341
638AcetylationKFGKFSGKDDGSSFK
HHHCCCCCCCCCCHH
51.9923749302
638UbiquitinationKFGKFSGKDDGSSFK
HHHCCCCCCCCCCHH
51.9929967540
644UbiquitinationGKDDGSSFKAALLSG
CCCCCCCHHHHHHHC
7.1721890473
644 (in isoform 2)Ubiquitination-7.1721890473
645MethylationKDDGSSFKAALLSGP
CCCCCCHHHHHHHCC
34.4042366681
645UbiquitinationKDDGSSFKAALLSGP
CCCCCCHHHHHHHCC
34.4022817900
645 (in isoform 1)Ubiquitination-34.4021890473
656UbiquitinationLSGPPGVGKTTTASL
HHCCCCCCHHHHHHH
27.7527667366
664UbiquitinationKTTTASLVCQELGYS
HHHHHHHHHHHHCCC
2.6824816145
670PhosphorylationLVCQELGYSYVELNA
HHHHHHCCCEEEECC
14.9517053785
672PhosphorylationCQELGYSYVELNASD
HHHHCCCEEEECCCC
6.8917053785
675UbiquitinationLGYSYVELNASDTRS
HCCCEEEECCCCCCC
4.6524816145
687UbiquitinationTRSKSSLKAIVAESL
CCCHHHHHHHHHHHC
37.71-
693PhosphorylationLKAIVAESLNNTSIK
HHHHHHHHCCCCCCC
27.0221406692
697PhosphorylationVAESLNNTSIKGFYS
HHHHCCCCCCCCCCC
30.6521406692
698PhosphorylationAESLNNTSIKGFYSN
HHHCCCCCCCCCCCC
25.1521406692
700UbiquitinationSLNNTSIKGFYSNGA
HCCCCCCCCCCCCCC
42.61-
703PhosphorylationNTSIKGFYSNGAASS
CCCCCCCCCCCCCCC
15.1922210691
709PhosphorylationFYSNGAASSVSTKHA
CCCCCCCCCCCCCCE
30.6422210691
710PhosphorylationYSNGAASSVSTKHAL
CCCCCCCCCCCCCEE
18.5022210691
713PhosphorylationGAASSVSTKHALIMD
CCCCCCCCCCEEEEC
25.3725367160
715UbiquitinationASSVSTKHALIMDEV
CCCCCCCCEEEECCC
26.3421890473
716UbiquitinationSSVSTKHALIMDEVD
CCCCCCCEEEECCCC
10.5921890473
741UbiquitinationIQELIGLIKHTKIPI
HHHHHHHHHCCCCCE
2.3121890473
741 (in isoform 2)Ubiquitination-2.3121890473
742AcetylationQELIGLIKHTKIPII
HHHHHHHHCCCCCEE
50.7125953088
742UbiquitinationQELIGLIKHTKIPII
HHHHHHHHCCCCCEE
50.7121890473
742 (in isoform 1)Ubiquitination-50.7121890473
799UbiquitinationGLKIPPPAMNEIILG
CCCCCCCHHHHHHHC
21.1427667366
800UbiquitinationLKIPPPAMNEIILGA
CCCCCCHHHHHHHCC
5.9627667366
807UbiquitinationMNEIILGANQDIRQV
HHHHHHCCCHHHHHH
13.6824816145
808UbiquitinationNEIILGANQDIRQVL
HHHHHCCCHHHHHHH
37.9524816145
818UbiquitinationIRQVLHNLSMWCARS
HHHHHHHHHHHHHHC
2.3024816145
819UbiquitinationRQVLHNLSMWCARSK
HHHHHHHHHHHHHCC
18.6324816145
825UbiquitinationLSMWCARSKALTYDQ
HHHHHHHCCCCCHHH
12.0727667366
826UbiquitinationSMWCARSKALTYDQA
HHHHHHCCCCCHHHH
41.6927667366
833UbiquitinationKALTYDQAKADSHRA
CCCCHHHHHHHHHHH
13.2024816145
834UbiquitinationALTYDQAKADSHRAK
CCCHHHHHHHHHHHH
47.2824816145
844UbiquitinationSHRAKKDIKMGPFDV
HHHHHCCCCCCHHHH
4.5524816145
845UbiquitinationHRAKKDIKMGPFDVA
HHHHCCCCCCHHHHH
48.1924816145
909PhosphorylationKKHLMLLSRAADSIC
HHHHHHHHHHHHHHC
18.86-
914PhosphorylationLLSRAADSICDGDLV
HHHHHHHHHCCCCCC
22.0120873877
932PhosphorylationIRSKQNWSLLPAQAI
HHHHCCCCCCCHHHH
27.81-
952PhosphorylationPGELMRGYMTQFPTF
CHHHHCCHHCCCCCC
6.1422210691
958PhosphorylationGYMTQFPTFPSWLGK
CHHCCCCCCHHHCCC
49.8422210691
958UbiquitinationGYMTQFPTFPSWLGK
CHHCCCCCCHHHCCC
49.8423503661
961UbiquitinationTQFPTFPSWLGKHSS
CCCCCCHHHCCCCCC
30.6425015289
964UbiquitinationPTFPSWLGKHSSTGK
CCCHHHCCCCCCCCC
21.2623503661
966UbiquitinationFPSWLGKHSSTGKHD
CHHHCCCCCCCCCCH
25.7825015289
968PhosphorylationSWLGKHSSTGKHDRI
HHCCCCCCCCCCHHH
40.6822210691
969PhosphorylationWLGKHSSTGKHDRIV
HCCCCCCCCCCHHHH
53.9522210691
970UbiquitinationLGKHSSTGKHDRIVQ
CCCCCCCCCCHHHHH
27.5223503661
986DimethylationLALHMSLRTYSSKRT
HHHHHHHHCCCCCCC
25.06-
986MethylationLALHMSLRTYSSKRT
HHHHHHHHCCCCCCC
25.06115372793
991AcetylationSLRTYSSKRTVNMDY
HHHCCCCCCCCCHHH
46.2630585945
1047UbiquitinationEISSWGGKPSPFSKL
HHHHCCCCCCCHHHC
38.08-
1053UbiquitinationGKPSPFSKLDPKVKA
CCCCCHHHCCHHHHH
58.24-
1057UbiquitinationPFSKLDPKVKAAFTR
CHHHCCHHHHHHHHH
56.91-
1063PhosphorylationPKVKAAFTRAYNKEA
HHHHHHHHHHHCCCC
15.0620068231
1073PhosphorylationYNKEAHLTPYSLQAI
HCCCCCCCHHHHHHH
15.4325159151
1075PhosphorylationKEAHLTPYSLQAIKA
CCCCCCHHHHHHHHH
19.4428122231
1076PhosphorylationEAHLTPYSLQAIKAS
CCCCCHHHHHHHHHH
18.4025159151
1080UbiquitinationTPYSLQAIKASRHST
CHHHHHHHHHHCCCC
2.1829967540
1081AcetylationPYSLQAIKASRHSTS
HHHHHHHHHHCCCCC
43.2425953088
1081UbiquitinationPYSLQAIKASRHSTS
HHHHHHHHHHCCCCC
43.2429967540
1083PhosphorylationSLQAIKASRHSTSPS
HHHHHHHHCCCCCCC
26.0628555341
1086PhosphorylationAIKASRHSTSPSLDS
HHHHHCCCCCCCCCH
29.4830576142
1087PhosphorylationIKASRHSTSPSLDSE
HHHHCCCCCCCCCHH
38.2318452278
1087 (in isoform 2)Phosphorylation-38.23-
1088PhosphorylationKASRHSTSPSLDSEY
HHHCCCCCCCCCHHH
18.5930576142
1089 (in isoform 2)Phosphorylation-38.71-
1090PhosphorylationSRHSTSPSLDSEYNE
HCCCCCCCCCHHHHH
44.5727362937
1092 (in isoform 2)Phosphorylation-43.70-
1093PhosphorylationSTSPSLDSEYNEELN
CCCCCCCHHHHHHHC
47.4728450419
1094 (in isoform 2)Phosphorylation-52.63-
1095PhosphorylationSPSLDSEYNEELNED
CCCCCHHHHHHHCCC
31.6528450419
1101UbiquitinationEYNEELNEDDSQSDE
HHHHHHCCCCCCCCH
75.6723503661
1102UbiquitinationYNEELNEDDSQSDEK
HHHHHCCCCCCCCHH
60.8423503661
1103 (in isoform 2)Phosphorylation-42.26-
1104PhosphorylationEELNEDDSQSDEKDQ
HHHCCCCCCCCHHHH
43.8620164059
1104UbiquitinationEELNEDDSQSDEKDQ
HHHCCCCCCCCHHHH
43.8625015289
1105UbiquitinationELNEDDSQSDEKDQD
HHCCCCCCCCHHHHH
62.9925015289
1105 (in isoform 2)Phosphorylation-62.99-
1106PhosphorylationLNEDDSQSDEKDQDA
HCCCCCCCCHHHHHH
52.2525159151
1107UbiquitinationNEDDSQSDEKDQDAI
CCCCCCCCHHHHHHH
60.3723503661
1108UbiquitinationEDDSQSDEKDQDAIE
CCCCCCCHHHHHHHH
64.8723503661
1109UbiquitinationDDSQSDEKDQDAIET
CCCCCCHHHHHHHHH
66.7225015289
1110UbiquitinationDSQSDEKDQDAIETD
CCCCCHHHHHHHHHH
49.9325015289
1113UbiquitinationSDEKDQDAIETDAMI
CCHHHHHHHHHHHHH
8.9023503661
1114UbiquitinationDEKDQDAIETDAMIK
CHHHHHHHHHHHHHH
8.6723503661
1116PhosphorylationKDQDAIETDAMIKKK
HHHHHHHHHHHHHHH
23.9720873877
1127UbiquitinationIKKKTKSSKPSKPEK
HHHHCCCCCCCCCCC
50.5723503661
1128UbiquitinationKKKTKSSKPSKPEKD
HHHCCCCCCCCCCCC
61.4723503661
1130UbiquitinationKTKSSKPSKPEKDKE
HCCCCCCCCCCCCCC
65.6625015289
1131UbiquitinationTKSSKPSKPEKDKEP
CCCCCCCCCCCCCCC
66.7725015289
1133UbiquitinationSSKPSKPEKDKEPRK
CCCCCCCCCCCCCCC
77.0823503661
1133 (in isoform 2)Ubiquitination-77.08-
1134UbiquitinationSKPSKPEKDKEPRKG
CCCCCCCCCCCCCCC
80.6823503661
1135UbiquitinationKPSKPEKDKEPRKGK
CCCCCCCCCCCCCCC
59.9125015289
1136UbiquitinationPSKPEKDKEPRKGKG
CCCCCCCCCCCCCCC
79.3425015289
1139UbiquitinationPEKDKEPRKGKGKSS
CCCCCCCCCCCCCCC
62.5423503661
1140UbiquitinationEKDKEPRKGKGKSSK
CCCCCCCCCCCCCCC
75.5723503661
1145PhosphorylationPRKGKGKSSKK----
CCCCCCCCCCC----
56.93-
1146PhosphorylationRKGKGKSSKK-----
CCCCCCCCCC-----
48.20-

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
506TPhosphorylationKinaseCDK1P06493
PSP
506TPhosphorylationKinaseCDK-FAMILY-GPS
518SPhosphorylationKinaseCDK1P06493
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RFC1_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 RFC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HDAC1_HUMANHDAC1physical
12045192
BRD4_HUMANBRD4physical
12192049
PCNA_HUMANPCNAphysical
12192049
PCNA_HUMANPCNAphysical
8861969
PCNA_HUMANPCNAphysical
8999859
P53_HUMANTP53physical
12509469
TF65_HUMANRELAphysical
12509469
RAD17_HUMANRAD17physical
18245774
CTF18_HUMANCHTF18physical
18245774
RFC2_HUMANRFC2physical
18245774
RFC3_HUMANRFC3physical
18245774
RFC4_HUMANRFC4physical
18245774
RFC5_HUMANRFC5physical
18245774
SSBP3_HUMANSSBP3physical
20211142
ZSCA1_HUMANZSCAN1physical
20211142
RAD17_HUMANRAD17physical
12400013
RFC3_HUMANRFC3physical
22939629
RFC2_HUMANRFC2physical
22939629
RFC4_HUMANRFC4physical
22939629
RFC5_HUMANRFC5physical
22939629
WDR18_HUMANWDR18physical
22939629
PCNA_HUMANPCNAphysical
9092549
PCNA_HUMANPCNAphysical
15225546
GLYR1_HUMANGLYR1physical
26344197
PCNA_HUMANPCNAphysical
26344197
PDS5A_HUMANPDS5Aphysical
26344197
RGAP1_HUMANRACGAP1physical
26344197
RFC2_HUMANRFC2physical
26344197
RFC3_HUMANRFC3physical
26344197
RFC4_HUMANRFC4physical
26344197
RFC5_HUMANRFC5physical
26344197
SMC1A_HUMANSMC1Aphysical
26344197
SMC2_HUMANSMC2physical
26344197
SMC4_HUMANSMC4physical
26344197
XRCC5_HUMANXRCC5physical
26344197
XRCC6_HUMANXRCC6physical
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 RFC1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-634, AND MASS 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-69; SER-71; SER-156;THR-161; THR-163; SER-164 AND SER-173, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67; SER-69; SER-71;SER-73 AND SER-312, AND MASS 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-69; SER-71; SER-73;SER-108; THR-110; SER-156; THR-161; SER-164; THR-171; SER-173;SER-190; SER-281; SER-283 AND SER-312, 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-190, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161 AND SER-173, ANDMASS SPECTROMETRY.
"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-69; SER-71 AND SER-73,AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-73 AND SER-156,AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-71; SER-108 ANDSER-190, AND MASS SPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-670 AND TYR-672, ANDMASS SPECTROMETRY.

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