RFC4_HUMAN - dbPTM
RFC4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RFC4_HUMAN
UniProt AC P35249
Protein Name Replication factor C subunit 4
Gene Name RFC4
Organism Homo sapiens (Human).
Sequence Length 363
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. This subunit may be involved in the elongation of the multiprimed DNA template..
Protein Sequence MQAFLKGTSISTKPPLTKDRGVAASAGSSGENKKAKPVPWVEKYRPKCVDEVAFQEEVVAVLKKSLEGADLPNLLFYGPPGTGKTSTILAAARELFGPELFRLRVLELNASDERGIQVVREKVKNFAQLTVSGSRSDGKPCPPFKIVILDEADSMTSAAQAALRRTMEKESKTTRFCLICNYVSRIIEPLTSRCSKFRFKPLSDKIQQQRLLDIAKKENVKISDEGIAYLVKVSEGDLRKAITFLQSATRLTGGKEITEKVITDIAGVIPAEKIDGVFAACQSGSFDKLEAVVKDLIDEGHAATQLVNQLHDVVVENNLSDKQKSIITEKLAEVDKCLADGADEHLQLISLCATVMQQLSQNC
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-------MQAFLKGT
-------CCCCCCCC		6.1422814378
6Methylation--MQAFLKGTSISTK
--CCCCCCCCCCCCC		54.4022636065
6Ubiquitination--MQAFLKGTSISTK
--CCCCCCCCCCCCC		54.4019608861
6Acetylation--MQAFLKGTSISTK
--CCCCCCCCCCCCC		54.4019608861
8PhosphorylationMQAFLKGTSISTKPP
CCCCCCCCCCCCCCC		22.6920068231
9PhosphorylationQAFLKGTSISTKPPL
CCCCCCCCCCCCCCC		24.1820068231
11PhosphorylationFLKGTSISTKPPLTK
CCCCCCCCCCCCCCC		30.1020068231
12PhosphorylationLKGTSISTKPPLTKD
CCCCCCCCCCCCCCC		45.9920068231
13AcetylationKGTSISTKPPLTKDR
CCCCCCCCCCCCCCC		37.5419608861
13UbiquitinationKGTSISTKPPLTKDR
CCCCCCCCCCCCCCC		37.5424816145
17PhosphorylationISTKPPLTKDRGVAA
CCCCCCCCCCCCCCC		36.3520068231
18UbiquitinationSTKPPLTKDRGVAAS
CCCCCCCCCCCCCCC		53.7832015554
20MethylationKPPLTKDRGVAASAG
CCCCCCCCCCCCCCC		42.94115491183
25PhosphorylationKDRGVAASAGSSGEN
CCCCCCCCCCCCCCC		24.3520068231
28PhosphorylationGVAASAGSSGENKKA
CCCCCCCCCCCCCCC		34.5825159151
29PhosphorylationVAASAGSSGENKKAK
CCCCCCCCCCCCCCC		49.5625159151
33AcetylationAGSSGENKKAKPVPW
CCCCCCCCCCCCCCC		50.2125953088
34UbiquitinationGSSGENKKAKPVPWV
CCCCCCCCCCCCCCH		73.5429967540
36UbiquitinationSGENKKAKPVPWVEK
CCCCCCCCCCCCHHH		56.2629967540
43UbiquitinationKPVPWVEKYRPKCVD
CCCCCHHHHCCCCCC		36.6229967540
47AcetylationWVEKYRPKCVDEVAF
CHHHHCCCCCCHHHC		37.5826051181
47UbiquitinationWVEKYRPKCVDEVAF
CHHHHCCCCCCHHHC		37.5829967540
48GlutathionylationVEKYRPKCVDEVAFQ
HHHHCCCCCCHHHCH		5.3022555962
63UbiquitinationEEVVAVLKKSLEGAD
HHHHHHHHHHCCCCC		33.4522817900
64UbiquitinationEVVAVLKKSLEGADL
HHHHHHHHHCCCCCC		56.9921890473
64UbiquitinationEVVAVLKKSLEGADL
HHHHHHHHHCCCCCC		56.9921906983
84UbiquitinationYGPPGTGKTSTILAA
ECCCCCCHHHHHHHH		38.8621890473
84UbiquitinationYGPPGTGKTSTILAA
ECCCCCCHHHHHHHH		38.8621906983
114MethylationELNASDERGIQVVRE
ECCCCCCCCCHHHHH		53.13115491189
124UbiquitinationQVVREKVKNFAQLTV
HHHHHHHHCCEEEEE		58.37-
139UbiquitinationSGSRSDGKPCPPFKI
CCCCCCCCCCCCEEE		48.7333845483
154PhosphorylationVILDEADSMTSAAQA
EEEECHHHHHHHHHH		30.8928060719
156PhosphorylationLDEADSMTSAAQAAL
EECHHHHHHHHHHHH		21.1128060719
157PhosphorylationDEADSMTSAAQAALR
ECHHHHHHHHHHHHH		16.9928060719
166PhosphorylationAQAALRRTMEKESKT
HHHHHHHHHHHCCCC		24.2128060719
172UbiquitinationRTMEKESKTTRFCLI
HHHHHCCCCHHHHHH		55.8224816145
174PhosphorylationMEKESKTTRFCLICN
HHHCCCCHHHHHHHH		26.03-
182PhosphorylationRFCLICNYVSRIIEP
HHHHHHHHHHHHHHH		8.7328152594
184PhosphorylationCLICNYVSRIIEPLT
HHHHHHHHHHHHHHH		13.8528152594
191PhosphorylationSRIIEPLTSRCSKFR
HHHHHHHHHCCCCCC		25.49-
192PhosphorylationRIIEPLTSRCSKFRF
HHHHHHHHCCCCCCC		38.68-
200UbiquitinationRCSKFRFKPLSDKIQ
CCCCCCCCCCCHHHH		40.5724816145
205UbiquitinationRFKPLSDKIQQQRLL
CCCCCCHHHHHHHHH		38.7533845483
205AcetylationRFKPLSDKIQQQRLL
CCCCCCHHHHHHHHH		38.7525953088
216UbiquitinationQRLLDIAKKENVKIS
HHHHHHHHHCCCCCC		62.0429967540
2162-HydroxyisobutyrylationQRLLDIAKKENVKIS
HHHHHHHHHCCCCCC		62.04-
216AcetylationQRLLDIAKKENVKIS
HHHHHHHHHCCCCCC		62.0425953088
217AcetylationRLLDIAKKENVKISD
HHHHHHHHCCCCCCC		45.5619816155
221UbiquitinationIAKKENVKISDEGIA
HHHHCCCCCCCCCEE		48.3429967540
229PhosphorylationISDEGIAYLVKVSEG
CCCCCEEEEEECCCH		15.3128152594
232UbiquitinationEGIAYLVKVSEGDLR
CCEEEEEECCCHHHH		37.1321906983
240UbiquitinationVSEGDLRKAITFLQS
CCCHHHHHHHHHHHH		51.9821890473
240UbiquitinationVSEGDLRKAITFLQS
CCCHHHHHHHHHHHH		51.9821906983
243PhosphorylationGDLRKAITFLQSATR
HHHHHHHHHHHHHHH		24.1329759185
247PhosphorylationKAITFLQSATRLTGG
HHHHHHHHHHHHHCC		33.4829759185
249PhosphorylationITFLQSATRLTGGKE
HHHHHHHHHHHCCHH		31.3029759185
252O-linked_GlycosylationLQSATRLTGGKEITE
HHHHHHHHCCHHHHH		40.3730379171
252PhosphorylationLQSATRLTGGKEITE
HHHHHHHHCCHHHHH		40.3729759185
2552-HydroxyisobutyrylationATRLTGGKEITEKVI
HHHHHCCHHHHHHHH		47.49-
255UbiquitinationATRLTGGKEITEKVI
HHHHHCCHHHHHHHH		47.4927667366
255AcetylationATRLTGGKEITEKVI
HHHHHCCHHHHHHHH		47.4926051181
258PhosphorylationLTGGKEITEKVITDI
HHCCHHHHHHHHHHH		30.7429759185
260UbiquitinationGGKEITEKVITDIAG
CCHHHHHHHHHHHCC		30.2229967540
283PhosphorylationGVFAACQSGSFDKLE
CEEEECCCCCHHHHH		35.9728348404
285PhosphorylationFAACQSGSFDKLEAV
EEECCCCCHHHHHHH		35.2028348404
288UbiquitinationCQSGSFDKLEAVVKD
CCCCCHHHHHHHHHH		46.3332015554
289 (in isoform 2)Phosphorylation-5.7122617229
290 (in isoform 2)Phosphorylation-45.2022617229
294UbiquitinationDKLEAVVKDLIDEGH
HHHHHHHHHHHHHHH		39.97-
322UbiquitinationVENNLSDKQKSIITE
HHCCCCHHHHHHHHH		57.1421906983
324UbiquitinationNNLSDKQKSIITEKL
CCCCHHHHHHHHHHH		49.7322817900
330UbiquitinationQKSIITEKLAEVDKC
HHHHHHHHHHHHHHH		44.3329967540
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 RFC4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RFC4_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 RFC4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RFC5_HUMANRFC5physical
16189514
RFC5_HUMANRFC5physical
9228079
RFC5_HUMANRFC5physical
9488738
RFC5_HUMANRFC5physical
22939629
RFC2_HUMANRFC2physical
9092549
RFC3_HUMANRFC3physical
9092549
RFC1_HUMANRFC1physical
9092549
RFC5_HUMANRFC5physical
9092549
ABCF1_HUMANABCF1physical
22863883
HNRPM_HUMANHNRNPMphysical
22863883
HNRPU_HUMANHNRNPUphysical
22863883
IF2B3_HUMANIGF2BP3physical
22863883
ILF2_HUMANILF2physical
22863883
MRE11_HUMANMRE11Aphysical
22863883
NMT1_HUMANNMT1physical
22863883
SYQ_HUMANQARSphysical
22863883
RFC5_HUMANRFC5physical
25416956
RNF41_HUMANRNF41physical
25416956
RFC2_HUMANRFC2physical
26344197
RFC5_HUMANRFC5physical
26344197
TRI33_HUMANTRIM33physical
26344197
ATAD5_HUMANATAD5physical
28514442
CTF18_HUMANCHTF18physical
28514442
RFC1_HUMANRFC1physical
28514442
CTF8_HUMANCHTF8physical
28514442
RFC2_HUMANRFC2physical
28514442
RFC3_HUMANRFC3physical
28514442
RAD1_HUMANRAD1physical
28514442
TAF12_HUMANTAF12physical
28514442
EPHA4_HUMANEPHA4physical
28514442
TAF2_HUMANTAF2physical
28514442
TAF9B_HUMANTAF9Bphysical
28514442
TAF6_HUMANTAF6physical
28514442
LFA3_HUMANCD58physical
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 RFC4_HUMAN

loading...

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 MET-1; LYS-6 AND LYS-13, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory