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Protein Page:
Rad52 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
Rad52 a protein involved in DNA double strand breaks and recombination. Associates with and is phosphorylated by c-Abl. Belongs to the RAD52/RAD22 family. Note: This description may include information from UniProtKB.
Protein type: DNA repair, damage
Cellular Component: nucleoplasm; nucleus
Molecular Function: identical protein binding; protein binding; DNA binding
Biological Process: DNA recombinase assembly; double-strand break repair; DNA repair; double-strand break repair via homologous recombination; DNA recombination
Reference #:  P43351 (UniProtKB)
Alt. Names/Synonyms: DNA repair protein RAD52 homolog; RAD52; RAD52 homolog (S. cerevisiae); recombination protein RAD52; rhabdomyosarcoma antigen MU-RMS-40.23
Gene Symbols: RAD52
Molecular weight: 46,169 Da
Basal Isoelectric point: 8.49  Predict pI for various phosphorylation states
CST Pathways:  G2/M DNA Damage Checkpoint
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Rad52

Protein Structure Not Found.


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Sites Implicated In
DNA repair, induced: Y104‑p
activity, induced: Y104‑p
intracellular localization: Y104‑p
molecular association, regulation: Y104‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S2-p ______MsGTEEAIL
3 0 Y104-p DLNNGKFyVGVCAFV
0 1 S129-p EDVGYGVsEGLKSKA
0 1 S138-p GLKSKALsLEKARKE
0 2 K144 LsLEKARKEAVTDGL
0 2 K152 EAVTDGLKRALRSFG
0 1 Y171-p NCILDKDyLRsLNKL
0 1 S174-p LDKDyLRsLNKLPRQ
0 1 S199-p KRQDLEPsVEEARyN
0 1 Y205-p PsVEEARyNsCRPNM
0 1 S207-p VEEARyNsCRPNMAL
0 1 T223-p HPQLQQVtsPSRPSH
0 1 S224-p PQLQQVtsPSRPSHA
0 1 S251-p LSSSAVEsEATHQRK
0 1 T281-p KQQVRVStPSAEKsE
0 1 S287-p StPSAEKsEAAPPAP
0 1 S299-p PAPPVTHsTPVtVSE
0 1 T303-p VTHsTPVtVSEPLLE
0 1 T318-p KDFLAGVtQELIKTL
0 1 T335-p NSEKWAVtPDAGDGV
0 1 T397-p TYSADQRtTGNWESH
1 0 K411-sm HRKSQDMkkRkYDPS
1 0 K412-sm RKSQDMkkRkYDPS_
1 0 K414-sm SQDMkkRkYDPS___
  mouse

 
A2 ______MAGPEEAVH
Y105 DLNNGKFYVGVCAFV
S130 EDVGYGVSEGLRSKA
S139 GLRSKALSLEKARkE
K145-ac LSLEKARkEAVTDGL
K153-ac EAVTDGLkRALRSFG
Y172 NCILDKDYLRSLNKL
S175 LDKDYLRSLNKLPRQ
S200 KREDFEPSVEQARYN
Y206 PSVEQARYNSCRQNE
S208 VEQARYNSCRQNEAL
T224 LPKPQEVTSPCRSSP
S225 PKPQEVTSPCRSSPP
S257 SLAATLESDATHQRK
- gap
K297 PAEEVAAKHAAVLPA
S309 LPAPPKHSTPVTAAS
T313 PKHSTPVTAASELLQ
- gap
T339 NLEMWDLTPDLEDII
- gap
K413 HRKSQDLKKRKLDPS
K414 RKSQDLKKRKLDPS_
K416 SQDLKKRKLDPS___
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