Q92878 (RAD50_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA repair protein RAD50
Short name=hRAD50
EC=3.6.-.-

Gene names

Name:

RAD50

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1312 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7 Ref.8 Ref.9 Ref.13 Ref.15 Ref.19
Cofactor	Binds 1 zinc ion per homodimer By similarity.
Subunit structure	Component of the MRN complex composed of two heterodimers RAD50/MRE11A associated with a single NBN. Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50, MRE11A and NBN. Found in a complex with TERF2. Interacts with RINT1. Interacts with BRCA1 via its N-terminal domain. Interacts with DCLRE1C/Artemis. Ref.1 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.18 Ref.20
Subcellular location	Nucleus. Chromosome › telomere. Note: Localizes to discrete nuclear foci after treatment with genotoxic agents. Ref.10 Ref.11
Tissue specificity	Expressed at very low level in most tissues, except in testis where it is expressed at higher level. Expressed in fibroblasts. Ref.1
Domain	The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of the homodimer, which constitute the ATP-binding domain, interact with the MRE11A homodimer By similarity. Ref.15
Involvement in disease	Nijmegen breakage syndrome-like disorder (NBSLD) [MIM:613078]: A disorder similar to Nijmegen breakage syndrome and characterized by chromosomal instability, radiation sensitivity, microcephaly, growth retardation, short stature and bird-like face. Immunodeficiency is absent. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23
Miscellaneous	In case of infection by adenovirus E4, the MRN complex is inactivated and degraded by viral oncoproteins, thereby preventing concatenation of viral genomes in infected cells.
Sequence similarities	Belongs to the SMC family. RAD50 subfamily. Contains 1 zinc-hook domain.
Sequence caution	The sequence AAH62603.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA repair Meiosis
Cellular component	Chromosome Nucleus Telomere
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA duplex unwinding Inferred from mutant phenotype PubMed 15790808. Source: BHF-UCL double-strand break repair via homologous recombination Traceable author statement. Source: Reactome nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC positive regulation of kinase activity Inferred from direct assay PubMed 15790808. Source: BHF-UCL positive regulation of protein autophosphorylation Inferred from direct assay PubMed 15790808. Source: BHF-UCL reciprocal meiotic recombination Traceable author statement Ref.1. Source: ProtInc regulation of mitotic recombination Inferred from direct assay Ref.1. Source: UniProtKB telomere maintenance via telomerase Inferred from direct assay Ref.8. Source: UniProtKB
Cellular_component	Mre11 complex Inferred from direct assay Ref.7. Source: UniProtKB nuclear chromosome, telomeric region Inferred from direct assay Ref.13. Source: BHF-UCL nucleoplasm Traceable author statement. Source: Reactome pronucleus Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from direct assay PubMed 15790808. Source: BHF-UCL nuclease activity Inferred from electronic annotation. Source: InterPro protein binding, bridging Inferred from direct assay PubMed 12152085. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92878-1)

Also known as: RAD50-1; RAD50-2;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q92878-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MSRIE → MLIFSVRDMFA

Isoform 3 (identifier: Q92878-3)

Also known as: RAD50-3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-139: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1312	1312	DNA repair protein RAD50		PRO_0000138641
Regions
	Domain	635 – 734	100	Zinc-hook
	Nucleotide binding	36 – 43	8	ATP Potential
	Coiled coil	228 – 359	132	Potential
	Coiled coil	401 – 598	198	Potential
	Coiled coil	635 – 673	39	Potential
	Coiled coil	706 – 734	29	Potential
	Coiled coil	789 – 1079	291	Potential
	Compositional bias	1201 – 1238	38	Ala/Asp-rich (DA-box)
Sites
	Metal binding	681	1	Zinc By similarity
	Metal binding	684	1	Zinc By similarity
Amino acid modifications
	Modified residue	237	1	Phosphoserine By similarity
	Modified residue	635	1	Phosphoserine Ref.21 Ref.22 Ref.26
	Modified residue	690	1	Phosphothreonine Ref.22 Ref.24 Ref.26
	Modified residue	959	1	N6-acetyllysine Ref.25
Natural variations
	Alternative sequence	1 – 139	139	Missing in isoform 3.		VSP_012590
	Alternative sequence	1 – 5	5	MSRIE → MLIFSVRDMFA in isoform 2.		VSP_012591
	Natural variant	94	1	I → L. Ref.28 Corresponds to variant rs28903085 [ dbSNP | Ensembl ].		VAR_025526
	Natural variant	127	1	V → I. Corresponds to variant rs28903086 [ dbSNP | Ensembl ].		VAR_029168
	Natural variant	191	1	T → I. Corresponds to variant rs2230017 [ dbSNP | Ensembl ].		VAR_022085
	Natural variant	193	1	R → W. Corresponds to variant rs28903087 [ dbSNP | Ensembl ].		VAR_029169
	Natural variant	224	1	R → H. Ref.28 Corresponds to variant rs28903088 [ dbSNP | Ensembl ].		VAR_025527
	Natural variant	315	1	V → L. Corresponds to variant rs28903090 [ dbSNP | Ensembl ].		VAR_034436
	Natural variant	469	1	G → A. Corresponds to variant rs55653181 [ dbSNP | Ensembl ].		VAR_061779
	Natural variant	616	1	K → E. Ref.3 Corresponds to variant rs1047380 [ dbSNP | Ensembl ].		VAR_020958
	Natural variant	697	1	V → A. Ref.3 Corresponds to variant rs1047382 [ dbSNP | Ensembl ].		VAR_020959
	Natural variant	842	1	V → A. Corresponds to variant rs28903093 [ dbSNP | Ensembl ].		VAR_029170
	Natural variant	964	1	Y → H. Ref.3 Corresponds to variant rs1047386 [ dbSNP | Ensembl ].		VAR_020960
	Natural variant	973	1	K → M. Ref.3 Corresponds to variant rs1129482 [ dbSNP | Ensembl ].		VAR_020961
	Natural variant	1038	1	R → G. Corresponds to variant rs1047387 [ dbSNP | Ensembl ].		VAR_020962
Experimental info
	Mutagenesis	42	1	K → N: Abolishes ability to degrade ATP. Ref.9
	Mutagenesis	1231	1	D → A: Abolishes ability to degrade ATP. Ref.9
	Sequence conflict	204	1	K → E in CAA99729. Ref.3
	Sequence conflict	723	1	E → K in AAH62603. Ref.6
	Sequence conflict	723	1	E → K in AAH73850. Ref.6
	Sequence conflict	733	1	V → A in CAA99729. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (RAD50-1) (RAD50-2) [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 1F208C3817FC41FC	FASTA	1,312	153,892
	10 20 30 40 50 60 MSRIEKMSIL GVRSFGIEDK DKQIITFFSP LTILVGPNGA GKTTIIECLK YICTGDFPPG 70 80 90 100 110 120 TKGNTFVHDP KVAQETDVRA QIRLQFRDVN GELIAVQRSM VCTQKSKKTE FKTLEGVITR 130 140 150 160 170 180 TKHGEKVSLS SKCAEIDREM ISSLGVSKAV LNNVIFCHQE DSNWPLSEGK ALKQKFDEIF 190 200 210 220 230 240 SATRYIKALE TLRQVRQTQG QKVKEYQMEL KYLKQYKEKA CEIRDQITSK EAQLTSSKEI 250 260 270 280 290 300 VKSYENELDP LKNRLKEIEH NLSKIMKLDN EIKALDSRKK QMEKDNSELE EKMEKVFQGT 310 320 330 340 350 360 DEQLNDLYHN HQRTVREKER KLVDCHRELE KLNKESRLLN QEKSELLVEQ GRLQLQADRH 370 380 390 400 410 420 QEHIRARDSL IQSLATQLEL DGFERGPFSE RQIKNFHKLV RERQEGEAKT ANQLMNDFAE 430 440 450 460 470 480 KETLKQKQID EIRDKKTGLG RIIELKSEIL SKKQNELKNV KYELQQLEGS SDRILELDQE 490 500 510 520 530 540 LIKAERELSK AEKNSNVETL KMEVISLQNE KADLDRTLRK LDQEMEQLNH HTTTRTQMEM 550 560 570 580 590 600 LTKDKADKDE QIRKIKSRHS DELTSLLGYF PNKKQLEDWL HSKSKEINQT RDRLAKLNKE 610 620 630 640 650 660 LASSEQNKNH INNELKRKEE QLSSYEDKLF DVCGSQDFES DLDRLKEEIE KSSKQRAMLA 670 680 690 700 710 720 GATAVYSQFI TQLTDENQSC CPVCQRVFQT EAELQEVISD LQSKLRLAPD KLKSTESELK 730 740 750 760 770 780 KKEKRRDEML GLVPMRQSII DLKEKEIPEL RNKLQNVNRD IQRLKNDIEE QETLLGTIMP 790 800 810 820 830 840 EEESAKVCLT DVTIMERFQM ELKDVERKIA QQAAKLQGID LDRTVQQVNQ EKQEKQHKLD 850 860 870 880 890 900 TVSSKIELNR KLIQDQQEQI QHLKSTTNEL KSEKLQISTN LQRRQQLEEQ TVELSTEVQS 910 920 930 940 950 960 LYREIKDAKE QVSPLETTLE KFQQEKEELI NKKNTSNKIA QDKLNDIKEK VKNIHGYMKD 970 980 990 1000 1010 1020 IENYIQDGKD DYKKQKETEL NKVIAQLSEC EKHKEKINED MRLMRQDIDT QKIQERWLQD 1030 1040 1050 1060 1070 1080 NLTLRKRNEE LKEVEEERKQ HLKEMGQMQV LQMKSEHQKL EENIDNIKRN HNLALGRQKG 1090 1100 1110 1120 1130 1140 YEEEIIHFKK ELREPQFRDA EEKYREMMIV MRTTELVNKD LDIYYKTLDQ AIMKFHSMKM 1150 1160 1170 1180 1190 1200 EEINKIIRDL WRSTYRGQDI EYIEIRSDAD ENVSASDKRR NYNYRVVMLK GDTALDMRGR 1210 1220 1230 1240 1250 1260 CSAGQKVLAS LIIRLALAET FCLNCGIIAL DEPTTNLDRE NIESLAHALV EIIKSRSQQR 1270 1280 1290 1300 1310 NFQLLVITHD EDFVELLGRS EYVEKFYRIK KNIDQCSEIV KCSVSSLGFN VH
	Isoform 2 [UniParc]. Checksum: 54B578956FC29852	FASTA	1,318	154,587
	10 20 30 40 50 60 MLIFSVRDMF AKMSILGVRS FGIEDKDKQI ITFFSPLTIL VGPNGAGKTT IIECLKYICT 70 80 90 100 110 120 GDFPPGTKGN TFVHDPKVAQ ETDVRAQIRL QFRDVNGELI AVQRSMVCTQ KSKKTEFKTL 130 140 150 160 170 180 EGVITRTKHG EKVSLSSKCA EIDREMISSL GVSKAVLNNV IFCHQEDSNW PLSEGKALKQ 190 200 210 220 230 240 KFDEIFSATR YIKALETLRQ VRQTQGQKVK EYQMELKYLK QYKEKACEIR DQITSKEAQL 250 260 270 280 290 300 TSSKEIVKSY ENELDPLKNR LKEIEHNLSK IMKLDNEIKA LDSRKKQMEK DNSELEEKME 310 320 330 340 350 360 KVFQGTDEQL NDLYHNHQRT VREKERKLVD CHRELEKLNK ESRLLNQEKS ELLVEQGRLQ 370 380 390 400 410 420 LQADRHQEHI RARDSLIQSL ATQLELDGFE RGPFSERQIK NFHKLVRERQ EGEAKTANQL 430 440 450 460 470 480 MNDFAEKETL KQKQIDEIRD KKTGLGRIIE LKSEILSKKQ NELKNVKYEL QQLEGSSDRI 490 500 510 520 530 540 LELDQELIKA ERELSKAEKN SNVETLKMEV ISLQNEKADL DRTLRKLDQE MEQLNHHTTT 550 560 570 580 590 600 RTQMEMLTKD KADKDEQIRK IKSRHSDELT SLLGYFPNKK QLEDWLHSKS KEINQTRDRL 610 620 630 640 650 660 AKLNKELASS EQNKNHINNE LKRKEEQLSS YEDKLFDVCG SQDFESDLDR LKEEIEKSSK 670 680 690 700 710 720 QRAMLAGATA VYSQFITQLT DENQSCCPVC QRVFQTEAEL QEVISDLQSK LRLAPDKLKS 730 740 750 760 770 780 TESELKKKEK RRDEMLGLVP MRQSIIDLKE KEIPELRNKL QNVNRDIQRL KNDIEEQETL 790 800 810 820 830 840 LGTIMPEEES AKVCLTDVTI MERFQMELKD VERKIAQQAA KLQGIDLDRT VQQVNQEKQE 850 860 870 880 890 900 KQHKLDTVSS KIELNRKLIQ DQQEQIQHLK STTNELKSEK LQISTNLQRR QQLEEQTVEL 910 920 930 940 950 960 STEVQSLYRE IKDAKEQVSP LETTLEKFQQ EKEELINKKN TSNKIAQDKL NDIKEKVKNI 970 980 990 1000 1010 1020 HGYMKDIENY IQDGKDDYKK QKETELNKVI AQLSECEKHK EKINEDMRLM RQDIDTQKIQ 1030 1040 1050 1060 1070 1080 ERWLQDNLTL RKRNEELKEV EEERKQHLKE MGQMQVLQMK SEHQKLEENI DNIKRNHNLA 1090 1100 1110 1120 1130 1140 LGRQKGYEEE IIHFKKELRE PQFRDAEEKY REMMIVMRTT ELVNKDLDIY YKTLDQAIMK 1150 1160 1170 1180 1190 1200 FHSMKMEEIN KIIRDLWRST YRGQDIEYIE IRSDADENVS ASDKRRNYNY RVVMLKGDTA 1210 1220 1230 1240 1250 1260 LDMRGRCSAG QKVLASLIIR LALAETFCLN CGIIALDEPT TNLDRENIES LAHALVEIIK 1270 1280 1290 1300 1310 SRSQQRNFQL LVITHDEDFV ELLGRSEYVE KFYRIKKNID QCSEIVKCSV SSLGFNVH
	Isoform 3 (RAD50-3) [UniParc]. Checksum: D6734A4E4D898AAE	FASTA	1,173	138,432
	10 20 30 40 50 60 MISSLGVSKA VLNNVIFCHQ EDSNWPLSEG KALKQKFDEI FSATRYIKAL ETLRQVRQTQ 70 80 90 100 110 120 GQKVKEYQME LKYLKQYKEK ACEIRDQITS KEAQLTSSKE IVKSYENELD PLKNRLKEIE 130 140 150 160 170 180 HNLSKIMKLD NEIKALDSRK KQMEKDNSEL EEKMEKVFQG TDEQLNDLYH NHQRTVREKE 190 200 210 220 230 240 RKLVDCHREL EKLNKESRLL NQEKSELLVE QGRLQLQADR HQEHIRARDS LIQSLATQLE 250 260 270 280 290 300 LDGFERGPFS ERQIKNFHKL VRERQEGEAK TANQLMNDFA EKETLKQKQI DEIRDKKTGL 310 320 330 340 350 360 GRIIELKSEI LSKKQNELKN VKYELQQLEG SSDRILELDQ ELIKAERELS KAEKNSNVET 370 380 390 400 410 420 LKMEVISLQN EKADLDRTLR KLDQEMEQLN HHTTTRTQME MLTKDKADKD EQIRKIKSRH 430 440 450 460 470 480 SDELTSLLGY FPNKKQLEDW LHSKSKEINQ TRDRLAKLNK ELASSEQNKN HINNELKRKE 490 500 510 520 530 540 EQLSSYEDKL FDVCGSQDFE SDLDRLKEEI EKSSKQRAML AGATAVYSQF ITQLTDENQS 550 560 570 580 590 600 CCPVCQRVFQ TEAELQEVIS DLQSKLRLAP DKLKSTESEL KKKEKRRDEM LGLVPMRQSI 610 620 630 640 650 660 IDLKEKEIPE LRNKLQNVNR DIQRLKNDIE EQETLLGTIM PEEESAKVCL TDVTIMERFQ 670 680 690 700 710 720 MELKDVERKI AQQAAKLQGI DLDRTVQQVN QEKQEKQHKL DTVSSKIELN RKLIQDQQEQ 730 740 750 760 770 780 IQHLKSTTNE LKSEKLQIST NLQRRQQLEE QTVELSTEVQ SLYREIKDAK EQVSPLETTL 790 800 810 820 830 840 EKFQQEKEEL INKKNTSNKI AQDKLNDIKE KVKNIHGYMK DIENYIQDGK DDYKKQKETE 850 860 870 880 890 900 LNKVIAQLSE CEKHKEKINE DMRLMRQDID TQKIQERWLQ DNLTLRKRNE ELKEVEEERK 910 920 930 940 950 960 QHLKEMGQMQ VLQMKSEHQK LEENIDNIKR NHNLALGRQK GYEEEIIHFK KELREPQFRD 970 980 990 1000 1010 1020 AEEKYREMMI VMRTTELVNK DLDIYYKTLD QAIMKFHSMK MEEINKIIRD LWRSTYRGQD 1030 1040 1050 1060 1070 1080 IEYIEIRSDA DENVSASDKR RNYNYRVVML KGDTALDMRG RCSAGQKVLA SLIIRLALAE 1090 1100 1110 1120 1130 1140 TFCLNCGIIA LDEPTTNLDR ENIESLAHAL VEIIKSRSQQ RNFQLLVITH DEDFVELLGR 1150 1160 1170 SEYVEKFYRI KKNIDQCSEI VKCSVSSLGF NVH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human Rad50 is physically associated with human Mre11: identification of a conserved multiprotein complex implicated in recombinational DNA repair." Dolganov G.M., Maser R.S., Novikov A., Tosto L., Chong S., Bressan D.A., Petrini J.H.J. Mol. Cell. Biol. 16:4832-4841(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH MRE11A, TISSUE SPECIFICITY.
[2]	"Molecular cloning and characterization of splice variants of human RAD50 gene." Kim K.K., Shin B.A., Seo K.H., Kim P.N., Koh J.T., Kim J.H., Park B.R. Gene 235:59-67(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
[3]	Offenberg H.H. Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS GLU-616; ALA-697; HIS-964 AND MET-973. Tissue: Testis.
[4]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lymph.
[7]	"The hMre11/hRad50 protein complex and Nijmegen breakage syndrome: linkage of double-strand break repair to the cellular DNA damage response." Carney J.P., Maser R.S., Olivares H., Davis E.M., Le Beau M., Yates J.R. III, Hays L., Morgan W.F., Petrini J.H.J. Cell 93:477-486(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DSB REPAIR, IDENTIFICATION IN THE MRN COMPLEX WITH MRE11A AND NBN.
[8]	"Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, and p95." Trujillo K.M., Yuan S.-S.F., Lee E.Y.-H.P., Sung P. J. Biol. Chem. 273:21447-21450(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN DSB REPAIR, IDENTIFICATION IN THE MRN COMPLEX WITH MRE11A AND NBN.
[9]	"The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks." Paull T.T., Gellert M. Mol. Cell 1:969-979(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ATP-BINDING, MUTAGENESIS OF LYS-42 AND ASP-1231.
[10]	"Association of BRCA1 with the hRad50-hMre11-p95 complex and the DNA damage response." Zhong Q., Chen C.-F., Li S., Chen Y., Wang C.-C., Xiao J., Chen P.-L., Sharp Z.D., Lee W.-H. Science 285:747-750(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BRCA1.
[11]	"BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures." Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J. Genes Dev. 14:927-939(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE BASC COMPLEX WITH BRCA1; MSH2; MSH6; MLH1; ATM; BLM; MRE11A AND NBN.
[12]	"Functional link between ataxia-telangiectasia and Nijmegen breakage syndrome gene products." Zhao S., Weng Y.-C., Yuan S.-S.F., Lin Y.-T., Hsu H.-C., Lin S.-C., Gerbino E., Song M.-H., Zdzienicka M.Z., Gatti R.A., Shay J.W., Ziv Y., Shiloh Y., Lee E.Y.-H.P. Nature 405:473-477(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MRN COMPLEX WITH MRE11A AND NBN.
[13]	"Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres." Zhu X.-D., Kuester B., Mann M., Petrini J.H.J., de Lange T. Nat. Genet. 25:347-352(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TELOMERES, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE A COMPLEX WITH TERF2.
[14]	"RINT-1, a novel Rad50-interacting protein, participates in radiation-induced G2/M checkpoint control." Xiao J., Liu C.-C., Chen P.-L., Lee W.-H. J. Biol. Chem. 276:6105-6111(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RINT1.
[15]	"Human Rad50/Mre11 is a flexible complex that can tether DNA ends." de Jager M., van Noort J., van Gent D.C., Dekker C., Kanaar R., Wyman C. Mol. Cell 8:1129-1135(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTRAMOLECULAR COILED-COIL DOMAINS.
[16]	"Adenovirus oncoproteins inactivate the Mre11-Rad50-NBS1 DNA repair complex." Stracker T.H., Carson C.T., Weitzman M.D. Nature 418:348-352(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INACTIVATION BY ADENOVIRUS ONCOPROTEINS.
[17]	"DNA end-binding specificity of human Rad50/Mre11 is influenced by ATP." de Jager M., Wyman C., van Gent D.C., Kanaar R. Nucleic Acids Res. 30:4425-4431(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ATP-BINDING.
[18]	"Artemis is a phosphorylation target of ATM and ATR and is involved in the G2/M DNA damage checkpoint response." Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D., Legerski R.J. Mol. Cell. Biol. 24:9207-9220(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DCLRE1C.
[19]	"Direct activation of the ATM protein kinase by the Mre11/Rad50/Nbs1 complex." Lee J.-H., Paull T.T. Science 304:93-96(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ATM ACTIVATION.
[20]	"Ataxia-telangiectasia-mutated dependent phosphorylation of Artemis in response to DNA damage." Chen L., Morio T., Minegishi Y., Nakada S., Nagasawa M., Komatsu K., Chessa L., Villa A., Lecis D., Delia D., Mizutani S. Cancer Sci. 96:134-141(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DCLRE1C.
[21]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[22]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635 AND THR-690, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"Human RAD50 deficiency in a Nijmegen breakage syndrome-like disorder." Waltes R., Kalb R., Gatei M., Kijas A.W., Stumm M., Sobeck A., Wieland B., Varon R., Lerenthal Y., Lavin M.F., Schindler D., Doerk T. Am. J. Hum. Genet. 84:605-616(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN NBSLD.
[24]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-690, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[25]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-959, MASS SPECTROMETRY.
[26]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635 AND THR-690, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]	"Mutation screening of Mre11 complex genes: indication of RAD50 involvement in breast and ovarian cancer susceptibility." Heikkinen K., Karppinen S.-M., Soini Y., Maekinen M., Winqvist R. J. Med. Genet. 40:E131-E131(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LEU-94 AND HIS-224.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U63139 mRNA. Translation: AAB07119.1. AF057299 mRNA. Translation: AAD50325.1. AF057300 mRNA. Translation: AAD50326.1. Z75311 mRNA. Translation: CAA99729.1. AC116366 Genomic DNA. No translation available. AC004042 Genomic DNA. No translation available. CH471062 Genomic DNA. Translation: EAW62329.1. BC062603 mRNA. Translation: AAH62603.1. Sequence problems. BC073850 mRNA. Translation: AAH73850.1. BC136436 mRNA. Translation: AAI36437.1.
IPI	IPI00107531. IPI00305282. IPI00549205.
RefSeq	NP_005723.2. NM_005732.3.
UniGene	Hs.633509.
3D structure databases
ProteinModelPortal	Q92878.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-33606N.
IntAct	Q92878. 12 interactions.
MINT	MINT-100363.
STRING	9606.ENSP00000265335.
PTM databases
PhosphoSite	Q92878.
Polymorphism databases
DMDM	60392986.
Proteomic databases
PaxDb	Q92878.
PRIDE	Q92878.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000265335; ENSP00000265335; ENSG00000113522. ENST00000378823; ENSP00000368100; ENSG00000113522.
GeneID	10111.
KEGG	hsa:10111.
UCSC	uc003kxh.3. human.
Organism-specific databases
CTD	10111.
GeneCards	GC05P131920.
HGNC	HGNC:9816. RAD50.
HPA	CAB022103. CAB024979.
MIM	604040. gene. 613078. phenotype.
neXtProt	NX_Q92878.
Orphanet	145. Hereditary breast and ovarian cancer syndrome. 240760. Nijmegen breakage syndrome-like disorder.
PharmGKB	PA34175.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0419.
HOGENOM	HOG000090195.
HOVERGEN	HBG058033.
InParanoid	Q92878.
KO	K10866.
OMA	NDIEEQE.
OrthoDB	EOG45HRWK.
Enzyme and pathway databases
Pathway_Interaction_DB	bard1pathway. BARD1 signaling events. telomerasepathway. Regulation of Telomerase.
Reactome	REACT_111183. Meiosis. REACT_216. DNA Repair.
Gene expression databases
ArrayExpress	Q92878.
Bgee	Q92878.
CleanEx	HS_RAD50.
Genevestigator	Q92878.
GermOnline	ENSG00000113522. Homo sapiens.
Family and domain databases
InterPro	IPR004584. Rad50. IPR007517. Rad50_Zn_hook. IPR013134. Zn_hook_Rad50. [Graphical view]
PANTHER	PTHR18867. PTHR18867. 1 hit.
Pfam	PF04423. Rad50_zn_hook. 1 hit. [Graphical view]
TIGRFAMs	TIGR00606. rad50. 1 hit.
PROSITE	PS51131. ZN_HOOK. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RAD50. human.
GenomeRNAi	10111.
NextBio	38249.
SOURCE	Search...

Entry information

Entry name

RAD50_HUMAN

Accession

Primary (citable) accession number: Q92878
Secondary accession number(s): B9EGF5 , O43254, Q6GMT7, Q6P5X3, Q9UP86

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.