RAD52_HUMAN - dbPTM
RAD52_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAD52_HUMAN
UniProt AC P43351
Protein Name DNA repair protein RAD52 homolog
Gene Name RAD52
Organism Homo sapiens (Human).
Sequence Length 418
Subcellular Localization Nucleus .
Protein Description Involved in double-stranded break repair. Plays a central role in genetic recombination and DNA repair by promoting the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase..
Protein Sequence MSGTEEAILGGRDSHPAAGGGSVLCFGQCQYTAEEYQAIQKALRQRLGPEYISSRMAGGGQKVCYIEGHRVINLANEMFGYNGWAHSITQQNVDFVDLNNGKFYVGVCAFVRVQLKDGSYHEDVGYGVSEGLKSKALSLEKARKEAVTDGLKRALRSFGNALGNCILDKDYLRSLNKLPRQLPLEVDLTKAKRQDLEPSVEEARYNSCRPNMALGHPQLQQVTSPSRPSHAVIPADQDCSSRSLSSSAVESEATHQRKLRQKQLQQQFRERMEKQQVRVSTPSAEKSEAAPPAPPVTHSTPVTVSEPLLEKDFLAGVTQELIKTLEDNSEKWAVTPDAGDGVVKPSSRADPAQTSDTLALNNQMVTQNRTPHSVCHQKPQAKSGSWDLQTYSADQRTTGNWESHRKSQDMKKRKYDPS
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
2Phosphorylation------MSGTEEAIL
------CCCCHHHHC		55.1917192257
4Phosphorylation----MSGTEEAILGG
----CCCCHHHHCCC		24.2823186163
41UbiquitinationEEYQAIQKALRQRLG
HHHHHHHHHHHHHHC		43.19-
104PhosphorylationDLNNGKFYVGVCAFV
ECCCCEEEEEEEEEE		10.3614757045
129PhosphorylationEDVGYGVSEGLKSKA
CCCCCCCCHHHHHHC		22.91-
133AcetylationYGVSEGLKSKALSLE
CCCCHHHHHHCCCHH		61.85-
135UbiquitinationVSEGLKSKALSLEKA
CCHHHHHHCCCHHHH		52.32-
138PhosphorylationGLKSKALSLEKARKE
HHHHHCCCHHHHHHH		39.06-
141UbiquitinationSKALSLEKARKEAVT
HHCCCHHHHHHHHHH		59.80-
171PhosphorylationNCILDKDYLRSLNKL
HHHCCHHHHHHHHCC		15.1219664995
174PhosphorylationLDKDYLRSLNKLPRQ
CCHHHHHHHHCCCCC		33.4319664995
177AcetylationDYLRSLNKLPRQLPL
HHHHHHHCCCCCCCC		66.22-
177UbiquitinationDYLRSLNKLPRQLPL
HHHHHHHCCCCCCCC		66.22-
190AcetylationPLEVDLTKAKRQDLE
CCEEECCHHHHCCCC		60.24-
192AcetylationEVDLTKAKRQDLEPS
EEECCHHHHCCCCCC		52.74-
199PhosphorylationKRQDLEPSVEEARYN
HHCCCCCCHHHHHHH		32.5517192257
205PhosphorylationPSVEEARYNSCRPNM
CCHHHHHHHCCCCCC		20.62-
207PhosphorylationVEEARYNSCRPNMAL
HHHHHHHCCCCCCCC		11.54-
223PhosphorylationHPQLQQVTSPSRPSH
CCCHHCCCCCCCCCC		30.4927251275
224PhosphorylationPQLQQVTSPSRPSHA
CCHHCCCCCCCCCCE		23.2527251275
226PhosphorylationLQQVTSPSRPSHAVI
HHCCCCCCCCCCEEE		57.5028348404
229PhosphorylationVTSPSRPSHAVIPAD
CCCCCCCCCEEECCC		23.9828348404
251PhosphorylationLSSSAVESEATHQRK
CCCHHHHCHHHHHHH		26.40-
262AcetylationHQRKLRQKQLQQQFR
HHHHHHHHHHHHHHH		46.68-
274AcetylationQFRERMEKQQVRVST
HHHHHHHHHCCEECC		36.37-
281PhosphorylationKQQVRVSTPSAEKSE
HHCCEECCCCHHHHC		20.57-
286AcetylationVSTPSAEKSEAAPPA
ECCCCHHHHCCCCCC		54.00-
287PhosphorylationSTPSAEKSEAAPPAP
CCCCHHHHCCCCCCC		24.7921712546
297PhosphorylationAPPAPPVTHSTPVTV
CCCCCCCCCCCCEEC		18.8428348404
299PhosphorylationPAPPVTHSTPVTVSE
CCCCCCCCCCEECCC		25.6625159151
300PhosphorylationAPPVTHSTPVTVSEP
CCCCCCCCCEECCCC		17.7425159151
303PhosphorylationVTHSTPVTVSEPLLE
CCCCCCEECCCCHHH		21.3721712546
318PhosphorylationKDFLAGVTQELIKTL
CCHHHCHHHHHHHHH		18.5317525332
323AcetylationGVTQELIKTLEDNSE
CHHHHHHHHHHHCCC		60.73-
324PhosphorylationVTQELIKTLEDNSEK
HHHHHHHHHHHCCCC		28.5229759185
329PhosphorylationIKTLEDNSEKWAVTP
HHHHHHCCCCEEECC		53.5322199227
335PhosphorylationNSEKWAVTPDAGDGV
CCCCEEECCCCCCCC		14.0117192257
344AcetylationDAGDGVVKPSSRADP
CCCCCCCCCCCCCCC		36.45-
383PhosphorylationHQKPQAKSGSWDLQT
CCCCCCCCCCCEEEE		40.8628348404
385PhosphorylationKPQAKSGSWDLQTYS
CCCCCCCCCEEEEEC		25.2229507054
397PhosphorylationTYSADQRTTGNWESH
EECCCCCCCCCHHHH		33.16-
403PhosphorylationRTTGNWESHRKSQDM
CCCCCHHHHCCCHHH		21.8724719451
406AcetylationGNWESHRKSQDMKKR
CCHHHHCCCHHHHHH		47.23-
411SumoylationHRKSQDMKKRKYDPS
HCCCHHHHHHCCCCC		58.68-
411SumoylationHRKSQDMKKRKYDPS
HCCCHHHHHHCCCCC		58.68-
412SumoylationRKSQDMKKRKYDPS-
CCCHHHHHHCCCCC-		47.70-
412AcetylationRKSQDMKKRKYDPS-
CCCHHHHHHCCCCC-		47.70-
412SumoylationRKSQDMKKRKYDPS-
CCCHHHHHHCCCCC-		47.70-
414AcetylationSQDMKKRKYDPS---
CHHHHHHCCCCC---		63.99-
414SumoylationSQDMKKRKYDPS---
CHHHHHHCCCCC---		63.99-
414SumoylationSQDMKKRKYDPS---
CHHHHHHCCCCC---		63.99-
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
104YPhosphorylationKinaseBCR-ABL1A9UF07
PSP
104YPhosphorylationKinaseABLP00519
PSP
104YPhosphorylationKinaseABL-FAMILY-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAD52_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 RAD52_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAD51_HUMANRAD51physical
10212258
SUMO1_HUMANSUMO1physical
8812453
UBC9_HUMANUBE2Iphysical
8921390
WRN_HUMANWRNphysical
17118963
RAD51_HUMANRAD51physical
17118963
RAD52_HUMANRAD52physical
12750383
WRN_HUMANWRNphysical
12750383
ERCC3_HUMANERCC3physical
12372413
ERCC2_HUMANERCC2physical
12372413
RPB1_HUMANPOLR2Aphysical
12372413
RAD52_HUMANRAD52physical
19338310
GNAI1_HUMANGNAI1physical
19338310
RFA3_HUMANRPA3physical
19338310
PROF1_HUMANPFN1physical
19338310
ACTB_HUMANACTBphysical
19338310
1433Z_HUMANYWHAZphysical
19338310
1433E_HUMANYWHAEphysical
19338310
CH60_HUMANHSPD1physical
19338310
HSP74_HUMANHSPA4physical
19338310
HSP7C_HUMANHSPA8physical
19338310
HS90A_HUMANHSP90AA1physical
19338310
PRDX1_HUMANPRDX1physical
19338310
PRDX2_HUMANPRDX2physical
19338310
EF1A1_HUMANEEF1A1physical
19338310
EF1G_HUMANEEF1Gphysical
19338310
EF1D_HUMANEEF1Dphysical
19338310
LDHB_HUMANLDHBphysical
19338310
G3P_HUMANGAPDHphysical
19338310
KCRB_HUMANCKBphysical
19338310
ENOA_HUMANENO1physical
19338310
ALDOA_HUMANALDOAphysical
19338310
RS10_HUMANRPS10physical
19338310
RS19_HUMANRPS19physical
19338310
PPIA_HUMANPPIAphysical
19338310
ARFG1_HUMANARFGAP1physical
19338310
TBA1A_HUMANTUBA1Aphysical
19338310
DAZP1_HUMANDAZAP1physical
19338310
SEC13_HUMANSEC13physical
19338310
RAD51_HUMANRAD51physical
19338310
RAD52_HUMANRAD52physical
12659830
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 RAD52_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-199 AND THR-335,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 THR-318, AND MASSSPECTROMETRY.
"Regulation of ionizing radiation-induced Rad52 nuclear foci formationby c-Abl-mediated phosphorylation.";
Kitao H., Yuan Z.M.;
J. Biol. Chem. 277:48944-48948(2002).
Cited for: FUNCTION, INTERACTION WITH ABL1, AND PHOSPHORYLATION AT TYR-104.

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