Home

Rad50 (human)

Overview Rad50 a component of the Mre11-Rad50-NBS1 (MRN) complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11A. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11A to prevent nucleolytic degradation past a given point. The complex may also be required for DNA damage signaling via activation of the ATM kinase. In telomeres the MRN complex may modulate t-loop formation. Three alternatively spliced isoforms have been described. Note: This description may include information from UniProtKB. Protein type: DNA repair; Adaptor/scaffold; EC 3.6.-.-; Hydrolase Cellular Component: nucleoplasm; Mre11 complex; nuclear chromosome, telomeric region; pronucleus Molecular Function: protein binding, bridging; ATP-dependent DNA helicase activity; protein binding; DNA binding; single-stranded DNA specific endodeoxyribonuclease activity; zinc ion binding; 3'-5' exonuclease activity; ATP binding Biological Process: meiotic recombination; double-strand break repair; positive regulation of kinase activity; telomere maintenance via telomerase; regulation of mitotic recombination; DNA repair; positive regulation of protein amino acid autophosphorylation; response to DNA damage stimulus; telomere maintenance; double-strand break repair via homologous recombination; DNA duplex unwinding; DNA recombination Reference #:  Q92878 (UniProtKB) Alt. Names/Synonyms: DNA repair protein RAD50; hRAD50; NBSLD; RAD50; RAD50 homolog (S. cerevisiae); RAD50-2 Gene Symbols: RAD50 Molecular weight: 153,892 Da Basal Isoelectric point: 6.47  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 Rad50

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  ENZYME  |  DISEASE  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	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		T54	ECLKYICTGDFPPGT
0	1		T61	TGDFPPGTkGNTFVH
0	1		K62-u	GDFPPGTkGNTFVHD
0	1		T119	KTLEGVITRTKHGEK
0	1		K175-u	EGKALKQkFDEIFSA
0	1		K187-u	FSATRYIkALETLRQ
0	1		T198-p	TLRQVRQtQGQKVKE
0	1		K211-u	KEYQMELkYLKQYKE
0	1		K230-u	IRDQITSkEAQLTSS
0	1		K242-u	TSSKEIVkSYENELD
0	1		K264-a	EIEHNLSkIMKLDNE
0	1		K284-u	SRKKQMEkDNSELEE
0	1		K295-u	ELEEKMEkVFQGTDE
0	1		K331	DCHRELEKLNKESRL
0	1		K398-a	RQIKNFHkLVRERQE
0	1		K453-a	KSEILSKkQNELKNV
0	1		K461-u	QNELKNVkYELQQLE
0	1		S560	RKIKSRHSDELTSLL
0	1		S565	RHSDELTSLLGYFPN
0	1		S603	KLNKELASSEQNKNH
0	14		S635-p	KLFDVCGsQDFEsDL
0	1		S640-p	CGsQDFEsDLDRLKE
0	34		T690-p	VCQRVFQtEAELQEV
0	1		K704	VISDLQSKLRLAPDK
0	4		R797-m2	TDVTIMErFQMELKD
0	1		K845-u	KLDTVSSkIELNRKL
0	1		K950	KLNDIKEKVKNIHGY
0	2		K959-a	KNIHGYMkDIENYIQ
0	1		K1032-a	RKRNEELkEVEEERK
0	1		T1113-p	EMMIVMRttELVNkD
0	1		T1114-p	MMIVMRttELVNkDL
0	1		K1119-u	RttELVNkDLDIYyk
0	2		Y1125-p	NkDLDIYykTLDQAI
0	1		K1126-u	kDLDIYykTLDQAIM
0	1		K1134-u	TLDQAIMkFHSMKME
0	2		K1190-u	NYRVVMLkGDTALDM
0	1		K1285-a	GRSEYVEkFYRIKKN
0	1		K1285-u	GRSEYVEkFYRIKKN

	mouse
T54-p	ECLKYICtGDFPPGt
T61-p	tGDFPPGtKGNTFVH
K62	GDFPPGtKGNTFVHD
T119-p	KTLEGVItRMKHGEK
K175	EGKALKQKFDEIFSA
K187	FSATRYIKALDTLRQ
T198	TLRQVRQTQGQKVKE
K211	KECQTELKYLKQNKE
K230	IRDQITSKEAQLASS
R242	ASSQEIVRSYEDELE
K264	EIEHNLSKIMKLDNE
K284-u	SRKKQMEkDNSELEQ
K295	ELEQKMEKVFQGTDE
K331-a	DCQRELEkLNKEARL
E398	RQIKNFHELVKERQE
K453	KTEILTKKQSELRHV
R461	QSELRHVRSELQQLE
S560-p	RKIKSRHsDELTsLL
S565-p	RHsDELTsLLGYFPN
S603-p	KLNKELAsAEQNKNH
S635-p	KLFDVCGsQDLESDL
S640	CGsQDLESDLGRLKE
T690-p	VCQRVFQtEAELQEV
K704-u	VISDLQSkLRLAPDK
R797-m2	TDVTIMErFQMELKD
K845	RLDTVTSKIELNRKL
K950-a	KINDIKEkVKNIHGY
K959	KNIHGYMKDIENYIQ
K1032	RKRRDELKEVEEEPK
T1113	EMMIVMRTTELVNKD
T1114	MMIVMRTTELVNKDL
K1119	RTTELVNKDLDIYYK
Y1125	NKDLDIYYKTLDQAI
K1126	KDLDIYYKTLDQAIM
K1134	TLDQAIMKFHSMKME
K1190	NYRVVMLKGDTALDM
K1285	GRSEYVEKFYRVKKN
K1285	GRSEYVEKFYRVKKN

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E Produced by 3rd Millennium  |  Design by Digizyme ©2003-2013 Cell Signaling Technology, Inc.