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Q92878 (RAD50_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein RAD50

Short name=hRAD50
EC=3.6.-.-
Gene names
Name:RAD50
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1312 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Chromosometelomere. Note: Localizes to discrete nuclear foci after treatment with genotoxic agents. Ref.10 Ref.11 Ref.21

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.24

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 processCell cycle
DNA damage
DNA repair
Meiosis
   Cellular componentChromosome
Nucleus
Telomere
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionHydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Inferred from direct assay Ref.8. Source: GOC

DNA duplex unwinding

Inferred from mutant phenotype PubMed 15790808. Source: BHF-UCL

DNA recombination

Inferred from direct assay Ref.8. Source: UniProtKB

DNA repair

Inferred from direct assay Ref.8. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from direct assay PubMed 17500065. Source: MGI

double-strand break repair

Inferred from mutant phenotype Ref.7. Source: UniProtKB

double-strand break repair via homologous recombination

Traceable author statement. Source: Reactome

nucleic acid phosphodiester bond hydrolysis

Inferred from direct assay Ref.8. 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

Traceable author statement Ref.13. Source: BHF-UCL

telomere maintenance via telomerase

Inferred from direct assay Ref.8. Source: UniProtKB

   Cellular_componentMre11 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

nucleus

Inferred from direct assay. Source: HPA

pronucleus

Inferred from electronic annotation. Source: Ensembl

site of double-strand break

Inferred from direct assay Ref.21. Source: UniProtKB

   Molecular_functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13121312DNA repair protein RAD50
PRO_0000138641

Regions

Domain635 – 734100Zinc-hook
Nucleotide binding36 – 438ATP Potential
Coiled coil228 – 359132 Potential
Coiled coil401 – 598198 Potential
Coiled coil635 – 67339 Potential
Coiled coil706 – 73429 Potential
Coiled coil789 – 1079291 Potential
Compositional bias1201 – 123838Ala/Asp-rich (DA-box)

Sites

Metal binding6811Zinc By similarity
Metal binding6841Zinc By similarity

Amino acid modifications

Modified residue6351Phosphoserine Ref.22 Ref.23 Ref.27
Modified residue6901Phosphothreonine Ref.23 Ref.25 Ref.27
Modified residue9591N6-acetyllysine Ref.26

Natural variations

Alternative sequence1 – 139139Missing in isoform 3.
VSP_012590
Alternative sequence1 – 55MSRIE → MLIFSVRDMFA in isoform 2.
VSP_012591
Natural variant941I → L. Ref.29
Corresponds to variant rs28903085 [ dbSNP | Ensembl ].
VAR_025526
Natural variant1271V → I.
Corresponds to variant rs28903086 [ dbSNP | Ensembl ].
VAR_029168
Natural variant1911T → I.
Corresponds to variant rs2230017 [ dbSNP | Ensembl ].
VAR_022085
Natural variant1931R → W.
Corresponds to variant rs28903087 [ dbSNP | Ensembl ].
VAR_029169
Natural variant2241R → H. Ref.29
Corresponds to variant rs28903088 [ dbSNP | Ensembl ].
VAR_025527
Natural variant3151V → L.
Corresponds to variant rs28903090 [ dbSNP | Ensembl ].
VAR_034436
Natural variant4691G → A.
Corresponds to variant rs55653181 [ dbSNP | Ensembl ].
VAR_061779
Natural variant6161K → E. Ref.3
Corresponds to variant rs1047380 [ dbSNP | Ensembl ].
VAR_020958
Natural variant6971V → A. Ref.3
Corresponds to variant rs1047382 [ dbSNP | Ensembl ].
VAR_020959
Natural variant8421V → A.
Corresponds to variant rs28903093 [ dbSNP | Ensembl ].
VAR_029170
Natural variant9641Y → H. Ref.3
Corresponds to variant rs1047386 [ dbSNP | Ensembl ].
VAR_020960
Natural variant9731K → M. Ref.3
Corresponds to variant rs1129482 [ dbSNP | Ensembl ].
VAR_020961
Natural variant10381R → G.
Corresponds to variant rs1047387 [ dbSNP | Ensembl ].
VAR_020962

Experimental info

Mutagenesis421K → N: Abolishes ability to degrade ATP. Ref.9
Mutagenesis12311D → A: Abolishes ability to degrade ATP. Ref.9
Sequence conflict2041K → E in CAA99729. Ref.3
Sequence conflict7231E → K in AAH62603. Ref.6
Sequence conflict7231E → K in AAH73850. Ref.6
Sequence conflict7331V → A in CAA99729. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (RAD50-1) (RAD50-2) [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 1F208C3817FC41FC

FASTA1,312153,892
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 54B578956FC29852
Show »

FASTA1,318154,587
Isoform 3 (RAD50-3) [UniParc].

Checksum: D6734A4E4D898AAE
Show »

FASTA1,173138,432

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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-dependent phosphorylation of ATF2 is required for the DNA damage response."
Bhoumik A., Takahashi S., Breitweiser W., Shiloh Y., Jones N., Ronai Z.
Mol. Cell 18:577-587(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[22]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[23]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"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.
[25]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[26]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"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].
[29]"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.
RefSeqNP_005723.2. NM_005732.3.
UniGeneHs.633509.

3D structure databases

ProteinModelPortalQ92878.
SMRQ92878. Positions 3-101, 1200-1291.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115417. 55 interactions.
DIPDIP-33606N.
IntActQ92878. 24 interactions.
MINTMINT-100363.
STRING9606.ENSP00000265335.

PTM databases

PhosphoSiteQ92878.

Polymorphism databases

DMDM60392986.

Proteomic databases

PaxDbQ92878.
PRIDEQ92878.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265335; ENSP00000265335; ENSG00000113522. [Q92878-1]
ENST00000378823; ENSP00000368100; ENSG00000113522. [Q92878-3]
GeneID10111.
KEGGhsa:10111.
UCSCuc003kxh.3. human. [Q92878-1]

Organism-specific databases

CTD10111.
GeneCardsGC05P131920.
HGNCHGNC:9816. RAD50.
HPACAB022103.
CAB024979.
HPA052291.
MIM604040. gene.
613078. phenotype.
neXtProtNX_Q92878.
Orphanet145. Hereditary breast and ovarian cancer syndrome.
240760. Nijmegen breakage syndrome-like disorder.
PharmGKBPA34175.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0419.
HOGENOMHOG000090195.
HOVERGENHBG058033.
InParanoidQ92878.
KOK10866.
OMASLGSYVH.
OrthoDBEOG725DGM.
PhylomeDBQ92878.
TreeFamTF101217.

Enzyme and pathway databases

ReactomeREACT_111183. Meiosis.
REACT_120956. Cellular responses to stress.
REACT_216. DNA Repair.

Gene expression databases

ArrayExpressQ92878.
BgeeQ92878.
CleanExHS_RAD50.
GenevestigatorQ92878.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR027417. P-loop_NTPase.
IPR004584. Rad50_eukaryotes.
IPR007517. Rad50_Zn_hook.
IPR013134. Zn_hook_Rad50.
[Graphical view]
PANTHERPTHR18867. PTHR18867. 1 hit.
PfamPF04423. Rad50_zn_hook. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 3 hits.
TIGRFAMsTIGR00606. rad50. 1 hit.
PROSITEPS51131. ZN_HOOK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAD50. human.
GeneWikiRad50.
GenomeRNAi10111.
NextBio38249.
PROQ92878.
SOURCESearch...

Entry information

Entry nameRAD50_HUMAN
AccessionPrimary (citable) accession number: Q92878
Secondary accession number(s): B9EGF5 expand/collapse secondary AC list , O43254, Q6GMT7, Q6P5X3, Q9UP86
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM