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Rad52 (human)

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 Cellular Component: nucleoplasm; nucleus Molecular Function: protein binding; DNA binding Biological Process: mitotic recombination; DNA recombinase assembly; meiotic recombination; double-strand break repair; DNA repair; double-strand break repair via homologous 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:  Cell Cycle: G2/M DNA Damage Checkpoint Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below Rad52 1H2I - A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=1-209 (human) 1KN0 - A/B/C/D/E/F/G/H/I/J/K=1-212 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1H2I 1KN0  |  Phospho3D  |  DISEASE  |  Source  |  InnateDB  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Sites Implicated In
activation: 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

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
2	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		T318-p	KDFLAGVtQELIKTL
0	1		T335-p	NSEKWAVtPDAGDGV
0	1		T397-p	TYSADQRtTGNWESH
1	0		K411-s	HRKSQDMkkRkYDPS
1	0		K412-s	RKSQDMkkRkYDPS_
1	0		K414-s	SQDMkkRkYDPS___

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

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