RFC2_HUMAN - dbPTM
RFC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RFC2_HUMAN
UniProt AC P35250
Protein Name Replication factor C subunit 2
Gene Name RFC2
Organism Homo sapiens (Human).
Sequence Length 354
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 binds ATP (By similarity)..
Protein Sequence MEVEAVCGGAGEVEAQDSDPAPAFSKAPGSAGHYELPWVEKYRPVKLNEIVGNEDTVSRLEVFAREGNVPNIIIAGPPGTGKTTSILCLARALLGPALKDAMLELNASNDRGIDVVRNKIKMFAQQKVTLPKGRHKIIILDEADSMTDGAQQALRRTMEIYSKTTRFALACNASDKIIEPIQSRCAVLRYTKLTDAQILTRLMNVIEKERVPYTDDGLEAIIFTAQGDMRQALNNLQSTFSGFGFINSENVFKVCDEPHPLLVKEMIQHCVNANIDEAYKILAHLWHLGYSPEDIIGNIFRVCKTFQMAEYLKLEFIKEIGYTHMKIAEGVNSLLQMAGLLARLCQKTMAPVAS
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-------MEVEAVCG
-------CCCEEECC		13.5322223895
18PhosphorylationGEVEAQDSDPAPAFS
CCCEECCCCCCCCCC		33.1526074081
25PhosphorylationSDPAPAFSKAPGSAG
CCCCCCCCCCCCCCC		29.9826074081
28AcetylationAPAFSKAPGSAGHYE
CCCCCCCCCCCCCCC		40.7919608861
28UbiquitinationAPAFSKAPGSAGHYE
CCCCCCCCCCCCCCC		40.7919608861
30PhosphorylationAFSKAPGSAGHYELP
CCCCCCCCCCCCCCC		29.9830266825
34PhosphorylationAPGSAGHYELPWVEK
CCCCCCCCCCCHHHE		20.4628796482
41UbiquitinationYELPWVEKYRPVKLN
CCCCHHHEECCCCHH		36.62-
42PhosphorylationELPWVEKYRPVKLNE
CCCHHHEECCCCHHH		13.4725367160
46AcetylationVEKYRPVKLNEIVGN
HHEECCCCHHHCCCC		48.5625953088
46UbiquitinationVEKYRPVKLNEIVGN
HHEECCCCHHHCCCC		48.5621906983
46 (in isoform 2)Ubiquitination-48.5621890473
46 (in isoform 1)Ubiquitination-48.5621890473
56PhosphorylationEIVGNEDTVSRLEVF
HCCCCCCHHHHHHHH		17.7520873877
58PhosphorylationVGNEDTVSRLEVFAR
CCCCCHHHHHHHHHC		32.9920873877
62AcetylationDTVSRLEVFAREGNV
CHHHHHHHHHCCCCC		5.5619608861
62UbiquitinationDTVSRLEVFAREGNV
CHHHHHHHHHCCCCC		5.5619608861
82UbiquitinationAGPPGTGKTTSILCL
ECCCCCCHHHHHHHH		48.76-
88GlutathionylationGKTTSILCLARALLG
CHHHHHHHHHHHHHC		2.3822555962
99 (in isoform 1)Ubiquitination-45.6121890473
99UbiquitinationALLGPALKDAMLELN
HHHCHHHHHHHHHHH		45.6121906983
99 (in isoform 2)Ubiquitination-45.6121890473
102SulfoxidationGPALKDAMLELNASN
CHHHHHHHHHHHCCC		4.2421406390
108PhosphorylationAMLELNASNDRGIDV
HHHHHHCCCCCCHHH		37.88-
111MethylationELNASNDRGIDVVRN
HHHCCCCCCHHHHHH		48.49115491171
121AcetylationDVVRNKIKMFAQQKV
HHHHHHHHHHHHCCC		29.5825953088
121UbiquitinationDVVRNKIKMFAQQKV
HHHHHHHHHHHHCCC		29.58-
127UbiquitinationIKMFAQQKVTLPKGR
HHHHHHCCCCCCCCC		25.71-
129 (in isoform 2)Ubiquitination-44.3621890473
129PhosphorylationMFAQQKVTLPKGRHK
HHHHCCCCCCCCCCE		44.3623312004
145PhosphorylationIILDEADSMTDGAQQ
EEEECHHHCCHHHHH		30.5430174305
157PhosphorylationAQQALRRTMEIYSKT
HHHHHHHHHHHHCCH		16.8430174305
158 (in isoform 2)Ubiquitination-2.5321890473
161PhosphorylationLRRTMEIYSKTTRFA
HHHHHHHHCCHHHHH		7.2730174305
162PhosphorylationRRTMEIYSKTTRFAL
HHHHHHHCCHHHHHH		29.23-
163 (in isoform 1)Ubiquitination-36.6221890473
163UbiquitinationRTMEIYSKTTRFALA
HHHHHHCCHHHHHHH		36.6221906983
163AcetylationRTMEIYSKTTRFALA
HHHHHHCCHHHHHHH		36.6219608861
164PhosphorylationTMEIYSKTTRFALAC
HHHHHCCHHHHHHHC		19.77-
165PhosphorylationMEIYSKTTRFALACN
HHHHCCHHHHHHHCC		27.76-
169AcetylationSKTTRFALACNASDK
CCHHHHHHHCCCCCH		5.2619608861
174 (in isoform 2)Ubiquitination-25.9921890473
174PhosphorylationFALACNASDKIIEPI
HHHHCCCCCHHHHHH		25.99-
176AcetylationLACNASDKIIEPIQS
HHCCCCCHHHHHHHH		42.9923954790
176UbiquitinationLACNASDKIIEPIQS
HHCCCCCHHHHHHHH		42.99-
184MethylationIIEPIQSRCAVLRYT
HHHHHHHCCHHHHHC		8.95115491177
190PhosphorylationSRCAVLRYTKLTDAQ
HCCHHHHHCCCCHHH		12.2220068231
191PhosphorylationRCAVLRYTKLTDAQI
CCHHHHHCCCCHHHH		17.1020068231
1922-HydroxyisobutyrylationCAVLRYTKLTDAQIL
CHHHHHCCCCHHHHH		40.22-
192 (in isoform 1)Ubiquitination-40.2221890473
192AcetylationCAVLRYTKLTDAQIL
CHHHHHCCCCHHHHH		40.2223749302
192UbiquitinationCAVLRYTKLTDAQIL
CHHHHHCCCCHHHHH		40.2221890473
194PhosphorylationVLRYTKLTDAQILTR
HHHHCCCCHHHHHHH		30.7420068231
200PhosphorylationLTDAQILTRLMNVIE
CCHHHHHHHHHHHHH		24.3220068231
203AcetylationAQILTRLMNVIEKER
HHHHHHHHHHHHHHC		3.2019608861
208AcetylationRLMNVIEKERVPYTD
HHHHHHHHHCCCCCC		39.4325953088
208UbiquitinationRLMNVIEKERVPYTD
HHHHHHHHHCCCCCC		39.432190698
208 (in isoform 1)Ubiquitination-39.4321890473
255S-nitrosylationSENVFKVCDEPHPLL
CCCEEECCCCCCCHH		5.1719483679
255S-nitrosocysteineSENVFKVCDEPHPLL
CCCEEECCCCCCCHH		5.17-
264AcetylationEPHPLLVKEMIQHCV
CCCCHHHHHHHHHHH		41.3526051181
264UbiquitinationEPHPLLVKEMIQHCV
CCCCHHHHHHHHHHH		41.35-
304AcetylationGNIFRVCKTFQMAEY
HHHHHHHHHHHHHHH		49.9019608861
318AcetylationYLKLEFIKEIGYTHM
HHCHHHHHHHCCCHH		48.9126051181
318UbiquitinationYLKLEFIKEIGYTHM
HHCHHHHHHHCCCHH		48.91-
322NitrationEFIKEIGYTHMKIAE
HHHHHHCCCHHHHHH		10.11-
347UbiquitinationLLARLCQKTMAPVAS
HHHHHHHHHCCCCCC		38.99-
348PhosphorylationLARLCQKTMAPVAS-
HHHHHHHHCCCCCC-		7.8420860994
354PhosphorylationKTMAPVAS-------
HHCCCCCC-------		40.7728102081
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
-KUbiquitinationE3 ubiquitin ligaseRAD18Q9NS91
PMID:18245774
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RFC2_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 RFC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RFC4_HUMANRFC4physical
9228079
RFC5_HUMANRFC5physical
9228079
RFC4_HUMANRFC4physical
9751713
RFC5_HUMANRFC5physical
22939629
RFC4_HUMANRFC4physical
22939629
RFC3_HUMANRFC3physical
22939629
KAP0_HUMANPRKAR1Aphysical
16582606
RFC4_HUMANRFC4physical
16582606
PRKDC_HUMANPRKDCphysical
22863883
PSF3_HUMANGINS3physical
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 RFC2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
"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-163 AND LYS-304, AND MASSSPECTROMETRY.

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