RFC5_HUMAN - dbPTM
RFC5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RFC5_HUMAN
UniProt AC P40937
Protein Name Replication factor C subunit 5
Gene Name RFC5
Organism Homo sapiens (Human).
Sequence Length 340
Subcellular Localization Nucleus .
Protein Description The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1..
Protein Sequence METSALKQQEQPAATKIRNLPWVEKYRPQTLNDLISHQDILSTIQKFINEDRLPHLLLYGPPGTGKTSTILACAKQLYKDKEFGSMVLELNASDDRGIDIIRGPILSFASTRTIFKKGFKLVILDEADAMTQDAQNALRRVIEKFTENTRFCLICNYLSKIIPALQSRCTRFRFGPLTPELMVPRLEHVVEEEKVDISEDGMKALVTLSSGDMRRALNILQSTNMAFGKVTEETVYTCTGHPLKSDIANILDWMLNQDFTTAYRNITELKTLKGLALHDILTEIHLFVHRVDFPSSVRIHLLTKMADIEYRLSVGTNEKIQLSSLIAAFQVTRDLIVAEA
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-------METSALKQ
-------CCCHHHHH
13.1522814378
7Ubiquitination-METSALKQQEQPAA
-CCCHHHHHCCCCHH
50.04-
7Acetylation-METSALKQQEQPAA
-CCCHHHHHCCCCHH
50.0425953088
7Sumoylation-METSALKQQEQPAA
-CCCHHHHHCCCCHH
50.04-
16AcetylationQEQPAATKIRNLPWV
CCCCHHHHHCCCCHH
34.6425953088
16UbiquitinationQEQPAATKIRNLPWV
CCCCHHHHHCCCCHH
34.6421906983
25UbiquitinationRNLPWVEKYRPQTLN
CCCCHHHHHCCCCHH
36.6221906983
26PhosphorylationNLPWVEKYRPQTLND
CCCHHHHHCCCCHHH
17.6429496907
52MethylationQKFINEDRLPHLLLY
HHHHCCCCCCEEEEE
43.89115491195
59PhosphorylationRLPHLLLYGPPGTGK
CCCEEEEECCCCCCH
27.7921406692
64PhosphorylationLLYGPPGTGKTSTIL
EEECCCCCCHHHHHH
41.0821406692
66UbiquitinationYGPPGTGKTSTILAC
ECCCCCCHHHHHHHH
38.86-
75AcetylationSTILACAKQLYKDKE
HHHHHHHHHHHCCCC
40.4926051181
75UbiquitinationSTILACAKQLYKDKE
HHHHHHHHHHHCCCC
40.49-
96MethylationELNASDDRGIDIIRG
EECCCCCCCCCEECC
49.29115491203
107PhosphorylationIIRGPILSFASTRTI
EECCCCCHHHCCHHH
21.3421406692
110PhosphorylationGPILSFASTRTIFKK
CCCCHHHCCHHHHHC
19.1921406692
111PhosphorylationPILSFASTRTIFKKG
CCCHHHCCHHHHHCC
28.5321406692
120UbiquitinationTIFKKGFKLVILDEA
HHHHCCCEEEEECCH
50.98-
144AcetylationALRRVIEKFTENTRF
HHHHHHHHHHCCCHH
46.6025953088
144UbiquitinationALRRVIEKFTENTRF
HHHHHHHHHHCCCHH
46.6021906983
157PhosphorylationRFCLICNYLSKIIPA
HHHHHHHHHHHHHHH
14.1328152594
159PhosphorylationCLICNYLSKIIPALQ
HHHHHHHHHHHHHHH
16.0828152594
178PhosphorylationRFRFGPLTPELMVPR
CCCCCCCCHHHHHHH
20.1827273156
194UbiquitinationEHVVEEEKVDISEDG
HHHHHHHCCCCCHHH
48.7821906983
194AcetylationEHVVEEEKVDISEDG
HHHHHHHCCCCCHHH
48.7826051181
203UbiquitinationDISEDGMKALVTLSS
CCCHHHHHHEEEECH
44.0621906983
213SulfoxidationVTLSSGDMRRALNIL
EEECHHHHHHHHHHH
3.4021406390
222PhosphorylationRALNILQSTNMAFGK
HHHHHHHHCCCCCCC
20.5021406692
223PhosphorylationALNILQSTNMAFGKV
HHHHHHHCCCCCCCC
18.9521406692
225SulfoxidationNILQSTNMAFGKVTE
HHHHHCCCCCCCCCE
3.1121406390
231PhosphorylationNMAFGKVTEETVYTC
CCCCCCCCEEEEEEE
31.4329396449
234PhosphorylationFGKVTEETVYTCTGH
CCCCCEEEEEEECCC
16.7529396449
236PhosphorylationKVTEETVYTCTGHPL
CCCEEEEEEECCCCC
11.9725159151
237PhosphorylationVTEETVYTCTGHPLK
CCEEEEEEECCCCCH
10.1529396449
238S-nitrosylationTEETVYTCTGHPLKS
CEEEEEEECCCCCHH
2.0519483679
238S-nitrosocysteineTEETVYTCTGHPLKS
CEEEEEEECCCCCHH
2.05-
239PhosphorylationEETVYTCTGHPLKSD
EEEEEEECCCCCHHH
30.6329396449
2702-HydroxyisobutyrylationYRNITELKTLKGLAL
HHHHHHHHHCHHHHH
45.65-
270UbiquitinationYRNITELKTLKGLAL
HHHHHHHHHCHHHHH
45.652190698
273UbiquitinationITELKTLKGLALHDI
HHHHHHCHHHHHHHH
58.05-
304UbiquitinationVRIHLLTKMADIEYR
HHHHHHHHHCCCEEE
31.87-
313PhosphorylationADIEYRLSVGTNEKI
CCCEEEECCCCCCCC
14.9821406692
316PhosphorylationEYRLSVGTNEKIQLS
EEEECCCCCCCCCHH
37.7421406692

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 RFC5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RFC5_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 RFC5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MED31_HUMANMED31physical
16169070
CSN6_HUMANCOPS6physical
16169070
RBM48_HUMANRBM48physical
16169070
EF1A1_HUMANEEF1A1physical
16169070
LRIF1_HUMANLRIF1physical
16169070
U119A_HUMANUNC119physical
16169070
PCNA_HUMANPCNAphysical
8999859
RFC4_HUMANRFC4physical
9751713
RFC2_HUMANRFC2physical
9751713
TRI38_HUMANTRIM38physical
25416956
RFC2_HUMANRFC2physical
26344197
RAD17_HUMANRAD17physical
28514442
DCC1_HUMANDSCC1physical
28514442
RFC4_HUMANRFC4physical
28514442
ATAD5_HUMANATAD5physical
28514442
CTF8_HUMANCHTF8physical
28514442
CTF18_HUMANCHTF18physical
28514442
RFC1_HUMANRFC1physical
28514442
RFC2_HUMANRFC2physical
28514442
RFC3_HUMANRFC3physical
28514442
RB_HUMANRB1physical
28514442

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 RFC5_HUMAN

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Related Literatures of Post-Translational Modification

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