RAD50_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAD50_RAT
• UniProt AC: Q9JIL8
• Protein Name: DNA repair protein RAD50
• Gene Name: Rad50
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 1312
• Subcellular Localization: Nucleus. Chromosome, telomere. Localizes to discrete nuclear foci after treatment with genotoxic agents.
• Protein Description: Component of the 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 MRE11. 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 MRE11 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 (By similarity)..
• Protein Sequence: MSRIEKMSTLGVRSFGIEDKDKQIISFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGNTFVHDPKVAQETDVRAQIRLQFRDVNGEMVLVQRSMLCSQKSKKTEFKTLEGVITRIKHGEKVSLSSKCAEIDREMISCLGVSKSVLNNVIFCHQEDSNWPLSEGKALKQKFDEIFSATRYIKALDTLRQVRQTQGQKVKECQTELKYLRQNKEKACEIRDQITSKEAQLASSREIVKAYENELEPLKNRLKEIEHNLSKIMRLDNEIKALDSRKKQMEKDNSELEQKMEKVFQGTDEQLNDLYHNHQRTVREKERRLVDCQRELEKLSKEARLLNQERAELLVEQGRLQLQADRHQEHIRARDSLIQSLAAHLELDGFERGPFSERQIKNFHELVRERQEREAKTASQLLSDLTDKEALKQRQMDEMRDKKSGLGRMIELKTEILTKKQTELRNVRNELQQLEGSSDRILELDQELTKAERELSKAEKNSSIETLKAEILNLQSEKADLDRNLRKLDQEMEQLNHHTTTRTQMEMLTKDKTDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASAEQNKNHINNELKKKEEQLSSYEDKLFDVCGSQDFESDLDRLKEDIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPGCQRVFQTEAELQEVISDLQSKLRLAPDKLKSTESELKKKERRRDEMLGLVPMRQSIIDLKEKEIPELRNRLQSVNRDIQRLKNDIEEQETLLGTVMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGVDLDRTVQQVNQEKQEKQHKLDTVSSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIATNLQRRQQMEEQTVELSTEVQSLNREIKDAKEQINPLEIALEKLQQEKEELIHRKNTSNKMAQDKINDIKEKVKNIHGYMKDIENYIQDGKDDYKKQKETELNEVVIQLNECDKHKEKINKEMGTMRQDIDTKKIQERWLQDNLTLRKRREELKEVEEERKQHLKEMGQMQVLQMKNEHQKLEENIDTIKRNHSLALGRQKGYEEEILHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDHAIMKFHSMKMEEINKIIRDLWRSTYRGQDIEYIEIRSDADENVSASDKRRNYNYRVVMLKGDTALDMRGRCSAGQKVLASLIIRLALAETFCLNCGILALDEPTTNLDRENIESLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGRSEYVEKFYRVKKNIDQCSEIVKSSINSLGSYVH

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
635	Phosphorylation	KLFDVCGSQDFESDL HHHHHHCCCCHHHHH	22.81	23984901
640	Phosphorylation	CGSQDFESDLDRLKE HCCCCHHHHHHHHHH	43.39	23984901
690	Phosphorylation	GCQRVFQTEAELQEV CHHHHHCCHHHHHHH	26.21	23984901
959	Acetylation	KNIHGYMKDIENYIQ HHHHHHHHHHHHHHH	47.25	-
1089	Acetylation	EEEILHFKKELREPQ HHHHHHHHHHHCCCC	34.29	22902405
1134	Acetylation	TLDHAIMKFHSMKME HHHHHHHHHHCCCHH	33.54	22902405
1137	Phosphorylation	HAIMKFHSMKMEEIN HHHHHHHCCCHHHHH	24.19	23984901

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RAD50_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RAD50_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RAD50_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of RAD50_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.