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Protein

DNA repair protein RAD50

Gene

RAD50

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.6 Publications

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per homodimer.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi681 – 6811ZincPROSITE-ProRule annotation
Metal bindingi684 – 6841ZincPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi36 – 438ATPSequence Analysis

GO - Molecular functioni

  • ATPase activity Source: InterPro
  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • protein binding, bridging Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: MGI
  • chromosome organization involved in meiosis Source: Ensembl
  • DNA duplex unwinding Source: BHF-UCL
  • DNA recombination Source: UniProtKB
  • DNA repair Source: UniProtKB
  • double-strand break repair Source: UniProtKB
  • double-strand break repair via homologous recombination Source: Reactome
  • nucleic acid phosphodiester bond hydrolysis Source: GOC
  • positive regulation of kinase activity Source: BHF-UCL
  • positive regulation of protein autophosphorylation Source: BHF-UCL
  • reciprocal meiotic recombination Source: ProtInc
  • regulation of mitotic cell cycle Source: Ensembl
  • regulation of mitotic recombination Source: UniProtKB
  • telomere maintenance Source: BHF-UCL
  • telomere maintenance via telomerase Source: UniProtKB
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair, Host-virus interaction, Meiosis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_27271. Meiotic recombination.
REACT_486. Assembly of the RAD50-MRE11-NBS1 complex at DNA double-strand breaks.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein RAD50 (EC:3.6.-.-)
Short name:
hRAD50
Gene namesi
Name:RAD50
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:9816. RAD50.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
  • Mre11 complex Source: UniProtKB
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nucleoplasm Source: HPA
  • pronucleus Source: Ensembl
  • site of double-strand break Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Involvement in diseasei

Nijmegen breakage syndrome-like disorder (NBSLD)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:613078

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421K → N: Abolishes ability to degrade ATP. 1 Publication
Mutagenesisi1231 – 12311D → A: Abolishes ability to degrade ATP. 1 Publication

Organism-specific databases

MIMi613078. phenotype.
Orphaneti145. Hereditary breast and ovarian cancer syndrome.
240760. Nijmegen breakage syndrome-like disorder.
PharmGKBiPA34175.

Polymorphism and mutation databases

BioMutaiRAD50.
DMDMi60392986.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13121312DNA repair protein RAD50PRO_0000138641Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei635 – 6351Phosphoserine3 Publications
Modified residuei690 – 6901Phosphothreonine3 Publications
Modified residuei959 – 9591N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ92878.
PaxDbiQ92878.
PRIDEiQ92878.

PTM databases

PhosphoSiteiQ92878.

Expressioni

Tissue specificityi

Expressed at very low level in most tissues, except in testis where it is expressed at higher level. Expressed in fibroblasts.1 Publication

Gene expression databases

BgeeiQ92878.
CleanExiHS_RAD50.
ExpressionAtlasiQ92878. baseline and differential.
GenevisibleiQ92878. HS.

Organism-specific databases

HPAiCAB022103.
CAB024979.
HPA052291.

Interactioni

Subunit structurei

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. Interacts with herpes simplex virus 1 protein UL12 (PubMed:20943970).11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATRXP461005EBI-495494,EBI-396461
RAD17O759432EBI-495494,EBI-968231

Protein-protein interaction databases

BioGridi115417. 70 interactions.
DIPiDIP-33606N.
IntActiQ92878. 29 interactions.
MINTiMINT-100363.
STRINGi9606.ENSP00000265335.

Structurei

3D structure databases

ProteinModelPortaliQ92878.
SMRiQ92878. Positions 6-66.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini635 – 734100Zinc-hookPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili228 – 359132Sequence AnalysisAdd
BLAST
Coiled coili401 – 598198Sequence AnalysisAdd
BLAST
Coiled coili635 – 67339Sequence AnalysisAdd
BLAST
Coiled coili706 – 73429Sequence AnalysisAdd
BLAST
Coiled coili789 – 1079291Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1201 – 123838Ala/Asp-rich (DA-box)Add
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the SMC family. RAD50 subfamily.Curated
Contains 1 zinc-hook domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0419.
GeneTreeiENSGT00390000018781.
HOGENOMiHOG000090195.
HOVERGENiHBG058033.
InParanoidiQ92878.
KOiK10866.
OMAiRSMVCTQ.
OrthoDBiEOG725DGM.
PhylomeDBiQ92878.
TreeFamiTF101217.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR004584. Rad50_eukaryotes.
IPR013134. Zn_hook_RAD50.
[Graphical view]
PANTHERiPTHR18867. PTHR18867. 1 hit.
PfamiPF04423. Rad50_zn_hook. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00606. rad50. 1 hit.
PROSITEiPS51131. ZN_HOOK. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q92878-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSRIEKMSIL GVRSFGIEDK DKQIITFFSP LTILVGPNGA GKTTIIECLK
60 70 80 90 100
YICTGDFPPG TKGNTFVHDP KVAQETDVRA QIRLQFRDVN GELIAVQRSM
110 120 130 140 150
VCTQKSKKTE FKTLEGVITR TKHGEKVSLS SKCAEIDREM ISSLGVSKAV
160 170 180 190 200
LNNVIFCHQE DSNWPLSEGK ALKQKFDEIF SATRYIKALE TLRQVRQTQG
210 220 230 240 250
QKVKEYQMEL KYLKQYKEKA CEIRDQITSK EAQLTSSKEI VKSYENELDP
260 270 280 290 300
LKNRLKEIEH NLSKIMKLDN EIKALDSRKK QMEKDNSELE EKMEKVFQGT
310 320 330 340 350
DEQLNDLYHN HQRTVREKER KLVDCHRELE KLNKESRLLN QEKSELLVEQ
360 370 380 390 400
GRLQLQADRH QEHIRARDSL IQSLATQLEL DGFERGPFSE RQIKNFHKLV
410 420 430 440 450
RERQEGEAKT ANQLMNDFAE KETLKQKQID EIRDKKTGLG RIIELKSEIL
460 470 480 490 500
SKKQNELKNV KYELQQLEGS SDRILELDQE LIKAERELSK AEKNSNVETL
510 520 530 540 550
KMEVISLQNE KADLDRTLRK LDQEMEQLNH HTTTRTQMEM LTKDKADKDE
560 570 580 590 600
QIRKIKSRHS DELTSLLGYF PNKKQLEDWL HSKSKEINQT RDRLAKLNKE
610 620 630 640 650
LASSEQNKNH INNELKRKEE QLSSYEDKLF DVCGSQDFES DLDRLKEEIE
660 670 680 690 700
KSSKQRAMLA GATAVYSQFI TQLTDENQSC CPVCQRVFQT EAELQEVISD
710 720 730 740 750
LQSKLRLAPD KLKSTESELK KKEKRRDEML GLVPMRQSII DLKEKEIPEL
760 770 780 790 800
RNKLQNVNRD IQRLKNDIEE QETLLGTIMP EEESAKVCLT DVTIMERFQM
810 820 830 840 850
ELKDVERKIA QQAAKLQGID LDRTVQQVNQ EKQEKQHKLD TVSSKIELNR
860 870 880 890 900
KLIQDQQEQI QHLKSTTNEL KSEKLQISTN LQRRQQLEEQ TVELSTEVQS
910 920 930 940 950
LYREIKDAKE QVSPLETTLE KFQQEKEELI NKKNTSNKIA QDKLNDIKEK
960 970 980 990 1000
VKNIHGYMKD IENYIQDGKD DYKKQKETEL NKVIAQLSEC EKHKEKINED
1010 1020 1030 1040 1050
MRLMRQDIDT QKIQERWLQD NLTLRKRNEE LKEVEEERKQ HLKEMGQMQV
1060 1070 1080 1090 1100
LQMKSEHQKL EENIDNIKRN HNLALGRQKG YEEEIIHFKK ELREPQFRDA
1110 1120 1130 1140 1150
EEKYREMMIV MRTTELVNKD LDIYYKTLDQ AIMKFHSMKM EEINKIIRDL
1160 1170 1180 1190 1200
WRSTYRGQDI EYIEIRSDAD ENVSASDKRR NYNYRVVMLK GDTALDMRGR
1210 1220 1230 1240 1250
CSAGQKVLAS LIIRLALAET FCLNCGIIAL DEPTTNLDRE NIESLAHALV
1260 1270 1280 1290 1300
EIIKSRSQQR NFQLLVITHD EDFVELLGRS EYVEKFYRIK KNIDQCSEIV
1310
KCSVSSLGFN VH
Length:1,312
Mass (Da):153,892
Last modified:February 1, 1997 - v1
Checksum:i1F208C3817FC41FC
GO
Isoform 2 (identifier: Q92878-2) [UniParc]FASTAAdd to basket

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

Show »
Length:1,318
Mass (Da):154,587
Checksum:i54B578956FC29852
GO
Isoform 3 (identifier: Q92878-3) [UniParc]FASTAAdd to basket

Also known as: RAD50-3

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

Show »
Length:1,173
Mass (Da):138,432
Checksum:iD6734A4E4D898AAE
GO

Sequence cautioni

The sequence AAH62603.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti204 – 2041K → E in CAA99729 (Ref. 3) Curated
Sequence conflicti723 – 7231E → K in AAH62603 (PubMed:15489334).Curated
Sequence conflicti723 – 7231E → K in AAH73850 (PubMed:15489334).Curated
Sequence conflicti733 – 7331V → A in CAA99729 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti94 – 941I → L.1 Publication
Corresponds to variant rs28903085 [ dbSNP | Ensembl ].
VAR_025526
Natural varianti127 – 1271V → I.
Corresponds to variant rs28903086 [ dbSNP | Ensembl ].
VAR_029168
Natural varianti191 – 1911T → I.
Corresponds to variant rs2230017 [ dbSNP | Ensembl ].
VAR_022085
Natural varianti193 – 1931R → W.
Corresponds to variant rs28903087 [ dbSNP | Ensembl ].
VAR_029169
Natural varianti224 – 2241R → H.1 Publication
Corresponds to variant rs28903088 [ dbSNP | Ensembl ].
VAR_025527
Natural varianti315 – 3151V → L.
Corresponds to variant rs28903090 [ dbSNP | Ensembl ].
VAR_034436
Natural varianti469 – 4691G → A.
Corresponds to variant rs55653181 [ dbSNP | Ensembl ].
VAR_061779
Natural varianti616 – 6161K → E.1 Publication
Corresponds to variant rs1047380 [ dbSNP | Ensembl ].
VAR_020958
Natural varianti697 – 6971V → A.1 Publication
Corresponds to variant rs1047382 [ dbSNP | Ensembl ].
VAR_020959
Natural varianti842 – 8421V → A.
Corresponds to variant rs28903093 [ dbSNP | Ensembl ].
VAR_029170
Natural varianti964 – 9641Y → H.1 Publication
Corresponds to variant rs1047386 [ dbSNP | Ensembl ].
VAR_020960
Natural varianti973 – 9731K → M.1 Publication
Corresponds to variant rs1129482 [ dbSNP | Ensembl ].
VAR_020961
Natural varianti1038 – 10381R → G.
Corresponds to variant rs1047387 [ dbSNP | Ensembl ].
VAR_020962

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 139139Missing in isoform 3. 1 PublicationVSP_012590Add
BLAST
Alternative sequencei1 – 55MSRIE → MLIFSVRDMFA in isoform 2. 1 PublicationVSP_012591

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34233.1. [Q92878-1]
RefSeqiNP_005723.2. NM_005732.3. [Q92878-1]
UniGeneiHs.633509.

Genome annotation databases

EnsembliENST00000378823; ENSP00000368100; ENSG00000113522.
GeneIDi10111.
KEGGihsa:10111.
UCSCiuc003kxh.3. human. [Q92878-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34233.1. [Q92878-1]
RefSeqiNP_005723.2. NM_005732.3. [Q92878-1]
UniGeneiHs.633509.

3D structure databases

ProteinModelPortaliQ92878.
SMRiQ92878. Positions 6-66.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115417. 70 interactions.
DIPiDIP-33606N.
IntActiQ92878. 29 interactions.
MINTiMINT-100363.
STRINGi9606.ENSP00000265335.

PTM databases

PhosphoSiteiQ92878.

Polymorphism and mutation databases

BioMutaiRAD50.
DMDMi60392986.

Proteomic databases

MaxQBiQ92878.
PaxDbiQ92878.
PRIDEiQ92878.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378823; ENSP00000368100; ENSG00000113522.
GeneIDi10111.
KEGGihsa:10111.
UCSCiuc003kxh.3. human. [Q92878-1]

Organism-specific databases

CTDi10111.
GeneCardsiGC05P131920.
HGNCiHGNC:9816. RAD50.
HPAiCAB022103.
CAB024979.
HPA052291.
MIMi604040. gene.
613078. phenotype.
neXtProtiNX_Q92878.
Orphaneti145. Hereditary breast and ovarian cancer syndrome.
240760. Nijmegen breakage syndrome-like disorder.
PharmGKBiPA34175.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0419.
GeneTreeiENSGT00390000018781.
HOGENOMiHOG000090195.
HOVERGENiHBG058033.
InParanoidiQ92878.
KOiK10866.
OMAiRSMVCTQ.
OrthoDBiEOG725DGM.
PhylomeDBiQ92878.
TreeFamiTF101217.

Enzyme and pathway databases

ReactomeiREACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_27271. Meiotic recombination.
REACT_486. Assembly of the RAD50-MRE11-NBS1 complex at DNA double-strand breaks.

Miscellaneous databases

ChiTaRSiRAD50. human.
GeneWikiiRad50.
GenomeRNAii10111.
NextBioi38249.
PROiQ92878.
SOURCEiSearch...

Gene expression databases

BgeeiQ92878.
CleanExiHS_RAD50.
ExpressionAtlasiQ92878. baseline and differential.
GenevisibleiQ92878. HS.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR004584. Rad50_eukaryotes.
IPR013134. Zn_hook_RAD50.
[Graphical view]
PANTHERiPTHR18867. PTHR18867. 1 hit.
PfamiPF04423. Rad50_zn_hook. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00606. rad50. 1 hit.
PROSITEiPS51131. ZN_HOOK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635 AND THR-690, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. 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. "Physical interaction between the herpes simplex virus type 1 exonuclease, UL12, and the DNA double-strand break-sensing MRN complex."
    Balasubramanian N., Bai P., Buchek G., Korza G., Weller S.K.
    J. Virol. 84:12504-12514(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HERPES SIMPLEX VIRUS 1 UL12.
  28. "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.
  29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  31. "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.

Entry informationi

Entry nameiRAD50_HUMAN
AccessioniPrimary (citable) accession number: Q92878
Secondary accession number(s): B9EGF5
, O43254, Q6GMT7, Q6P5X3, Q9UP86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 1, 1997
Last modified: July 22, 2015
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.