CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018854
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA repair protein RAD50 
Protein Synonyms/Alias
 hRAD50 
Gene Name
 RAD50 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MSRIEKMSILGVRubiquitination[1]
62GDFPPGTKGNTFVHDubiquitination[2]
112KSKKTEFKTLEGVITubiquitination[1]
175EGKALKQKFDEIFSAubiquitination[1, 2]
187FSATRYIKALETLRQubiquitination[1, 2]
217LKYLKQYKEKACEIRubiquitination[2]
230IRDQITSKEAQLTSSubiquitination[3]
242TSSKEIVKSYENELDubiquitination[3]
256DPLKNRLKEIEHNLSubiquitination[1]
264EIEHNLSKIMKLDNEacetylation[4]
295ELEEKMEKVFQGTDEubiquitination[2]
461QNELKNVKYELQQLEubiquitination[2]
815KIAQQAAKLQGIDLDacetylation[5]
845KLDTVSSKIELNRKLubiquitination[2]
851SKIELNRKLIQDQQEubiquitination[2]
959KNIHGYMKDIENYIQacetylation[4, 5]
1068EENIDNIKRNHNLALubiquitination[1, 3]
1119RTTELVNKDLDIYYKubiquitination[2, 3]
1126KDLDIYYKTLDQAIMubiquitination[3]
1134TLDQAIMKFHSMKMEubiquitination[2]
1145MKMEEINKIIRDLWRubiquitination[3]
1190NYRVVMLKGDTALDMubiquitination[1, 3]
1285GRSEYVEKFYRIKKNacetylation[4]
1285GRSEYVEKFYRIKKNubiquitination[2]
1291EKFYRIKKNIDQCSEubiquitination[2]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional 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 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. 
Sequence Annotation
 DOMAIN 635 734 Zinc-hook.
 NP_BIND 36 43 ATP (Potential).
 METAL 681 681 Zinc (By similarity).
 METAL 684 684 Zinc (By similarity).
 MOD_RES 237 237 Phosphoserine (By similarity).
 MOD_RES 635 635 Phosphoserine.
 MOD_RES 690 690 Phosphothreonine.
 MOD_RES 959 959 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Cell cycle; Chromosome; Coiled coil; Complete proteome; DNA damage; DNA repair; Hydrolase; Meiosis; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Telomere; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1312 AA 
Protein Sequence
MSRIEKMSIL GVRSFGIEDK DKQIITFFSP LTILVGPNGA GKTTIIECLK YICTGDFPPG 60
TKGNTFVHDP KVAQETDVRA QIRLQFRDVN GELIAVQRSM VCTQKSKKTE FKTLEGVITR 120
TKHGEKVSLS SKCAEIDREM ISSLGVSKAV LNNVIFCHQE DSNWPLSEGK ALKQKFDEIF 180
SATRYIKALE TLRQVRQTQG QKVKEYQMEL KYLKQYKEKA CEIRDQITSK EAQLTSSKEI 240
VKSYENELDP LKNRLKEIEH NLSKIMKLDN EIKALDSRKK QMEKDNSELE EKMEKVFQGT 300
DEQLNDLYHN HQRTVREKER KLVDCHRELE KLNKESRLLN QEKSELLVEQ GRLQLQADRH 360
QEHIRARDSL IQSLATQLEL DGFERGPFSE RQIKNFHKLV RERQEGEAKT ANQLMNDFAE 420
KETLKQKQID EIRDKKTGLG RIIELKSEIL SKKQNELKNV KYELQQLEGS SDRILELDQE 480
LIKAERELSK AEKNSNVETL KMEVISLQNE KADLDRTLRK LDQEMEQLNH HTTTRTQMEM 540
LTKDKADKDE QIRKIKSRHS DELTSLLGYF PNKKQLEDWL HSKSKEINQT RDRLAKLNKE 600
LASSEQNKNH INNELKRKEE QLSSYEDKLF DVCGSQDFES DLDRLKEEIE KSSKQRAMLA 660
GATAVYSQFI TQLTDENQSC CPVCQRVFQT EAELQEVISD LQSKLRLAPD KLKSTESELK 720
KKEKRRDEML GLVPMRQSII DLKEKEIPEL RNKLQNVNRD IQRLKNDIEE QETLLGTIMP 780
EEESAKVCLT DVTIMERFQM ELKDVERKIA QQAAKLQGID LDRTVQQVNQ EKQEKQHKLD 840
TVSSKIELNR KLIQDQQEQI QHLKSTTNEL KSEKLQISTN LQRRQQLEEQ TVELSTEVQS 900
LYREIKDAKE QVSPLETTLE KFQQEKEELI NKKNTSNKIA QDKLNDIKEK VKNIHGYMKD 960
IENYIQDGKD DYKKQKETEL NKVIAQLSEC EKHKEKINED MRLMRQDIDT QKIQERWLQD 1020
NLTLRKRNEE LKEVEEERKQ HLKEMGQMQV LQMKSEHQKL EENIDNIKRN HNLALGRQKG 1080
YEEEIIHFKK ELREPQFRDA EEKYREMMIV MRTTELVNKD LDIYYKTLDQ AIMKFHSMKM 1140
EEINKIIRDL WRSTYRGQDI EYIEIRSDAD ENVSASDKRR NYNYRVVMLK GDTALDMRGR 1200
CSAGQKVLAS LIIRLALAET FCLNCGIIAL DEPTTNLDRE NIESLAHALV EIIKSRSQQR 1260
NFQLLVITHD EDFVELLGRS EYVEKFYRIK KNIDQCSEIV KCSVSSLGFN VH 1312 
Gene Ontology
 GO:0030870; C:Mre11 complex; IDA:UniProtKB.
 GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0045120; C:pronucleus; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IDA:BHF-UCL.
 GO:0004518; F:nuclease activity; IEA:InterPro.
 GO:0030674; F:protein binding, bridging; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0032508; P:DNA duplex unwinding; IMP:BHF-UCL.
 GO:0000724; P:double-strand break repair via homologous recombination; TAS:Reactome.
 GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
 GO:0033674; P:positive regulation of kinase activity; IDA:BHF-UCL.
 GO:0031954; P:positive regulation of protein autophosphorylation; IDA:BHF-UCL.
 GO:0007131; P:reciprocal meiotic recombination; TAS:ProtInc.
 GO:0000019; P:regulation of mitotic recombination; IDA:UniProtKB.
 GO:0007004; P:telomere maintenance via telomerase; IDA:UniProtKB. 
Interpro
 IPR027417; P-loop_NTPase.
 IPR004584; Rad50.
 IPR007517; Rad50_Zn_hook.
 IPR013134; Zn_hook_Rad50. 
Pfam
 PF04423; Rad50_zn_hook 
SMART
  
PROSITE
 PS51131; ZN_HOOK 
PRINTS