Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

DNA repair protein RAD50 (hRAD50) (EC 3.6.-.-)

 RAD50_HUMAN             Reviewed;        1312 AA.
Q92878; B9EGF5; O43254; Q6GMT7; Q6P5X3; Q9UP86;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
25-OCT-2017, entry version 164.
RecName: Full=DNA repair protein RAD50;
Short=hRAD50;
EC=3.6.-.-;
Name=RAD50;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH MRE11, AND
TISSUE SPECIFICITY.
PubMed=8756642; DOI=10.1128/MCB.16.9.4832;
Dolganov G.M., Maser R.S., Novikov A., Tosto L., Chong S.,
Bressan D.A., Petrini J.H.J.;
"Human Rad50 is physically associated with human Mre11: identification
of a conserved multiprotein complex implicated in recombinational DNA
repair.";
Mol. Cell. Biol. 16:4832-4841(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
PubMed=10415333; DOI=10.1016/S0378-1119(99)00215-2;
Kim K.K., Shin B.A., Seo K.H., Kim P.N., Koh J.T., Kim J.H.,
Park B.R.;
"Molecular cloning and characterization of splice variants of human
RAD50 gene.";
Gene 235:59-67(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS GLU-616; ALA-697;
HIS-964 AND MET-973.
TISSUE=Testis;
Offenberg H.H.;
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
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.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION IN DSB REPAIR, AND IDENTIFICATION IN THE MRN COMPLEX WITH
MRE11 AND NBN.
PubMed=9590181; DOI=10.1016/S0092-8674(00)81175-7;
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.;
"The hMre11/hRad50 protein complex and Nijmegen breakage syndrome:
linkage of double-strand break repair to the cellular DNA damage
response.";
Cell 93:477-486(1998).
[8]
FUNCTION IN DSB REPAIR, AND IDENTIFICATION IN THE MRN COMPLEX WITH
MRE11 AND NBN.
PubMed=9705271; DOI=10.1074/jbc.273.34.21447;
Trujillo K.M., Yuan S.-S.F., Lee E.Y.-H.P., Sung P.;
"Nuclease activities in a complex of human recombination and DNA
repair factors Rad50, Mre11, and p95.";
J. Biol. Chem. 273:21447-21450(1998).
[9]
FUNCTION, ATP-BINDING, AND MUTAGENESIS OF LYS-42 AND ASP-1231.
PubMed=9651580; DOI=10.1016/S1097-2765(00)80097-0;
Paull T.T., Gellert M.;
"The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA
double-strand breaks.";
Mol. Cell 1:969-979(1998).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH BRCA1.
PubMed=10426999; DOI=10.1126/science.285.5428.747;
Zhong Q., Chen C.-F., Li S., Chen Y., Wang C.-C., Xiao J., Chen P.-L.,
Sharp Z.D., Lee W.-H.;
"Association of BRCA1 with the hRad50-hMre11-p95 complex and the DNA
damage response.";
Science 285:747-750(1999).
[11]
SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE BASC COMPLEX WITH
BRCA1; MSH2; MSH6; MLH1; ATM; BLM; MRE11 AND NBN.
PubMed=10783165;
Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., Qin J.;
"BASC, a super complex of BRCA1-associated proteins involved in the
recognition and repair of aberrant DNA structures.";
Genes Dev. 14:927-939(2000).
[12]
IDENTIFICATION IN THE MRN COMPLEX WITH MRE11 AND NBN.
PubMed=10839544; DOI=10.1038/35013083;
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.;
"Functional link between ataxia-telangiectasia and Nijmegen breakage
syndrome gene products.";
Nature 405:473-477(2000).
[13]
FUNCTION IN TELOMERES, IDENTIFICATION BY MASS SPECTROMETRY,
IDENTIFICATION IN THE A COMPLEX WITH TERF2, AND SUBCELLULAR LOCATION.
PubMed=10888888; DOI=10.1038/77139;
Zhu X.-D., Kuester B., Mann M., Petrini J.H.J., de Lange T.;
"Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and
human telomeres.";
Nat. Genet. 25:347-352(2000).
[14]
INTERACTION WITH RINT1.
PubMed=11096100; DOI=10.1074/jbc.M008893200;
Xiao J., Liu C.-C., Chen P.-L., Lee W.-H.;
"RINT-1, a novel Rad50-interacting protein, participates in radiation-
induced G2/M checkpoint control.";
J. Biol. Chem. 276:6105-6111(2001).
[15]
FUNCTION, AND INTRAMOLECULAR COILED-COIL DOMAINS.
PubMed=11741547; DOI=10.1016/S1097-2765(01)00381-1;
de Jager M., van Noort J., van Gent D.C., Dekker C., Kanaar R.,
Wyman C.;
"Human Rad50/Mre11 is a flexible complex that can tether DNA ends.";
Mol. Cell 8:1129-1135(2001).
[16]
INACTIVATION BY ADENOVIRUS ONCOPROTEINS.
PubMed=12124628; DOI=10.1038/nature00863;
Stracker T.H., Carson C.T., Weitzman M.D.;
"Adenovirus oncoproteins inactivate the Mre11-Rad50-NBS1 DNA repair
complex.";
Nature 418:348-352(2002).
[17]
ATP-BINDING.
PubMed=12384589; DOI=10.1093/nar/gkf574;
de Jager M., Wyman C., van Gent D.C., Kanaar R.;
"DNA end-binding specificity of human Rad50/Mre11 is influenced by
ATP.";
Nucleic Acids Res. 30:4425-4431(2002).
[18]
INTERACTION WITH DCLRE1C.
PubMed=15456891; DOI=10.1128/MCB.24.20.9207-9220.2004;
Zhang X., Succi J., Feng Z., Prithivirajsingh S., Story M.D.,
Legerski R.J.;
"Artemis is a phosphorylation target of ATM and ATR and is involved in
the G2/M DNA damage checkpoint response.";
Mol. Cell. Biol. 24:9207-9220(2004).
[19]
FUNCTION IN ATM ACTIVATION.
PubMed=15064416; DOI=10.1126/science.1091496;
Lee J.-H., Paull T.T.;
"Direct activation of the ATM protein kinase by the Mre11/Rad50/Nbs1
complex.";
Science 304:93-96(2004).
[20]
INTERACTION WITH DCLRE1C.
PubMed=15723659; DOI=10.1111/j.1349-7006.2005.00019.x;
Chen L., Morio T., Minegishi Y., Nakada S., Nagasawa M., Komatsu K.,
Chessa L., Villa A., Lecis D., Delia D., Mizutani S.;
"Ataxia-telangiectasia-mutated dependent phosphorylation of Artemis in
response to DNA damage.";
Cancer Sci. 96:134-141(2005).
[21]
SUBCELLULAR LOCATION.
PubMed=15916964; DOI=10.1016/j.molcel.2005.04.015;
Bhoumik A., Takahashi S., Breitweiser W., Shiloh Y., Jones N.,
Ronai Z.;
"ATM-dependent phosphorylation of ATF2 is required for the DNA damage
response.";
Mol. Cell 18:577-587(2005).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
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.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635 AND THR-690, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
INVOLVEMENT IN NBSLD.
PubMed=19409520; DOI=10.1016/j.ajhg.2009.04.010;
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.;
"Human RAD50 deficiency in a Nijmegen breakage syndrome-like
disorder.";
Am. J. Hum. Genet. 84:605-616(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-690, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-959, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[27]
INTERACTION WITH HERPES SIMPLEX VIRUS 1 UL12.
PubMed=20943970; DOI=10.1128/JVI.01506-10;
Balasubramanian N., Bai P., Buchek G., Korza G., Weller S.K.;
"Physical interaction between the herpes simplex virus type 1
exonuclease, UL12, and the DNA double-strand break-sensing MRN
complex.";
J. Virol. 84:12504-12514(2010).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635 AND THR-690, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635 AND THR-690, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[32]
INTERACTION WITH MRNIP.
PubMed=27568553; DOI=10.1016/j.celrep.2016.07.087;
Staples C.J., Barone G., Myers K.N., Ganesh A., Gibbs-Seymour I.,
Patil A.A., Beveridge R.D., Daye C., Beniston R., Maslen S., Ahel I.,
Skehel J.M., Collis S.J.;
"MRNIP/C5orf45 interacts with the MRN complex and contributes to the
DNA damage response.";
Cell Rep. 16:2565-2575(2016).
[33]
VARIANTS LEU-94 AND HIS-224.
PubMed=14684699; DOI=10.1136/jmg.40.12.e131;
Heikkinen K., Karppinen S.-M., Soini Y., Maekinen M., Winqvist R.;
"Mutation screening of Mre11 complex genes: indication of RAD50
involvement in breast and ovarian cancer susceptibility.";
J. Med. Genet. 40:E131-E131(2003).
-!- 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 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 (PubMed:11741547, PubMed:9590181, PubMed:9705271,
PubMed:9651580). The complex may also be required for DNA damage
signaling via activation of the ATM kinase (PubMed:15064416). In
telomeres the MRN complex may modulate t-loop formation
(PubMed:10888888). {ECO:0000269|PubMed:10888888,
ECO:0000269|PubMed:11741547, ECO:0000269|PubMed:15064416,
ECO:0000269|PubMed:9590181, ECO:0000269|PubMed:9651580,
ECO:0000269|PubMed:9705271}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per homodimer. {ECO:0000250};
-!- SUBUNIT: Component of the MRN complex composed of two heterodimers
RAD50/MRE11 associated with a single NBN (PubMed:8756642,
PubMed:9590181, PubMed:9705271, PubMed:10839544). Component of the
BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM,
BLM, RAD50, MRE11 and NBN (PubMed:10783165). Found in a complex
with TERF2 (PubMed:10888888). Interacts with RINT1
(PubMed:11096100). Interacts with BRCA1 via its N-terminal domain
(PubMed:10426999). Interacts with DCLRE1C/Artemis
(PubMed:15456891, PubMed:15723659). Interacts with MRNIP
(PubMed:27568553). {ECO:0000269|PubMed:10426999,
ECO:0000269|PubMed:10783165, ECO:0000269|PubMed:10839544,
ECO:0000269|PubMed:10888888, ECO:0000269|PubMed:11096100,
ECO:0000269|PubMed:15456891, ECO:0000269|PubMed:15723659,
ECO:0000269|PubMed:27568553, ECO:0000269|PubMed:8756642,
ECO:0000269|PubMed:9590181, ECO:0000269|PubMed:9705271}.
-!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus
1 protein UL12 (PubMed:20943970). {ECO:0000269|PubMed:20943970}.
-!- INTERACTION:
P46100:ATRX; NbExp=5; IntAct=EBI-495494, EBI-396461;
O75943:RAD17; NbExp=2; IntAct=EBI-495494, EBI-968231;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10783165,
ECO:0000269|PubMed:15916964}. Chromosome, telomere
{ECO:0000269|PubMed:10888888}. Note=Localizes to discrete nuclear
foci after treatment with genotoxic agents.
{ECO:0000269|PubMed:10783165, ECO:0000269|PubMed:15916964}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=RAD50-1, RAD50-2;
IsoId=Q92878-1; Sequence=Displayed;
Name=2;
IsoId=Q92878-2; Sequence=VSP_012591;
Name=3; Synonyms=RAD50-3;
IsoId=Q92878-3; Sequence=VSP_012590;
-!- TISSUE SPECIFICITY: Expressed at very low level in most tissues,
except in testis where it is expressed at higher level. Expressed
in fibroblasts. {ECO:0000269|PubMed:8756642}.
-!- 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 MRE11 homodimer (By
similarity). {ECO:0000250}.
-!- 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. {ECO:0000269|PubMed:19409520}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- 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.
-!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH62603.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U63139; AAB07119.1; -; mRNA.
EMBL; AF057299; AAD50325.1; -; mRNA.
EMBL; AF057300; AAD50326.1; -; mRNA.
EMBL; Z75311; CAA99729.1; -; mRNA.
EMBL; AC116366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC004042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471062; EAW62329.1; -; Genomic_DNA.
EMBL; BC062603; AAH62603.1; ALT_SEQ; mRNA.
EMBL; BC073850; AAH73850.1; -; mRNA.
EMBL; BC136436; AAI36437.1; -; mRNA.
CCDS; CCDS34233.1; -. [Q92878-1]
RefSeq; NP_005723.2; NM_005732.3. [Q92878-1]
UniGene; Hs.633509; -.
PDB; 5GOX; X-ray; 2.40 A; A/B=585-766.
PDBsum; 5GOX; -.
ProteinModelPortal; Q92878; -.
SMR; Q92878; -.
BioGrid; 115417; 113.
CORUM; Q92878; -.
DIP; DIP-33606N; -.
IntAct; Q92878; 54.
MINT; MINT-100363; -.
STRING; 9606.ENSP00000265335; -.
iPTMnet; Q92878; -.
PhosphoSitePlus; Q92878; -.
BioMuta; RAD50; -.
DMDM; 60392986; -.
EPD; Q92878; -.
MaxQB; Q92878; -.
PaxDb; Q92878; -.
PeptideAtlas; Q92878; -.
PRIDE; Q92878; -.
Ensembl; ENST00000378823; ENSP00000368100; ENSG00000113522. [Q92878-1]
GeneID; 10111; -.
KEGG; hsa:10111; -.
UCSC; uc003kxi.4; human. [Q92878-1]
CTD; 10111; -.
DisGeNET; 10111; -.
EuPathDB; HostDB:ENSG00000113522.13; -.
GeneCards; RAD50; -.
HGNC; HGNC:9816; RAD50.
HPA; CAB022103; -.
HPA; CAB024979; -.
HPA; HPA052291; -.
MalaCards; RAD50; -.
MIM; 604040; gene.
MIM; 613078; phenotype.
neXtProt; NX_Q92878; -.
OpenTargets; ENSG00000113522; -.
Orphanet; 145; Hereditary breast and ovarian cancer syndrome.
Orphanet; 240760; Nijmegen breakage syndrome-like disorder.
PharmGKB; PA34175; -.
eggNOG; KOG0962; Eukaryota.
eggNOG; COG0419; LUCA.
GeneTree; ENSGT00390000018781; -.
HOGENOM; HOG000090195; -.
HOVERGEN; HBG058033; -.
InParanoid; Q92878; -.
KO; K10866; -.
OMA; RSMVCTQ; -.
OrthoDB; EOG091G01KA; -.
PhylomeDB; Q92878; -.
TreeFam; TF101217; -.
Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-HSA-5685939; HDR through MMEJ (alt-NHEJ).
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5693548; Sensing of DNA Double Strand Breaks.
Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
Reactome; R-HSA-912446; Meiotic recombination.
SIGNOR; Q92878; -.
ChiTaRS; RAD50; human.
GeneWiki; Rad50; -.
GenomeRNAi; 10111; -.
PRO; PR:Q92878; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113522; -.
CleanEx; HS_RAD50; -.
ExpressionAtlas; Q92878; baseline and differential.
Genevisible; Q92878; HS.
GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0030870; C:Mre11 complex; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IDA:BHF-UCL.
GO; GO:0003691; F:double-stranded telomeric DNA binding; IBA:GO_Central.
GO; GO:0051880; F:G-quadruplex DNA binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030674; F:protein binding, bridging; IDA:UniProtKB.
GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
GO; GO:0000729; P:DNA double-strand break processing; TAS:Reactome.
GO; GO:0032508; P:DNA duplex unwinding; IMP:BHF-UCL.
GO; GO:0006310; P:DNA recombination; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
GO; GO:0006260; P:DNA replication; TAS:Reactome.
GO; GO:0000731; P:DNA synthesis involved in DNA repair; TAS:Reactome.
GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
GO; GO:1904354; P:negative regulation of telomere capping; IDA:BHF-UCL.
GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
GO; GO:0033674; P:positive regulation of kinase activity; IDA:BHF-UCL.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:BHF-UCL.
GO; GO:0032206; P:positive regulation of telomere maintenance; IMP:BHF-UCL.
GO; GO:0007131; P:reciprocal meiotic recombination; TAS:ProtInc.
GO; GO:0000019; P:regulation of mitotic recombination; IDA:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0000732; P:strand displacement; TAS:Reactome.
GO; GO:0000723; P:telomere maintenance; TAS:BHF-UCL.
GO; GO:0000722; P:telomere maintenance via recombination; IBA:GO_Central.
GO; GO:0007004; P:telomere maintenance via telomerase; IDA:UniProtKB.
GO; GO:0031860; P:telomeric 3' overhang formation; IMP:BHF-UCL.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR004584; Rad50_eukaryotes.
InterPro; IPR013134; Zn_hook_RAD50.
Pfam; PF04423; Rad50_zn_hook; 1.
SUPFAM; SSF52540; SSF52540; 3.
TIGRFAMs; TIGR00606; rad50; 1.
PROSITE; PS51131; ZN_HOOK; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Cell cycle; Chromosome; Coiled coil; Complete proteome; DNA damage;
DNA repair; Host-virus interaction; Hydrolase; Meiosis; Metal-binding;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Telomere; Zinc.
CHAIN 1 1312 DNA repair protein RAD50.
/FTId=PRO_0000138641.
DOMAIN 635 734 Zinc-hook. {ECO:0000255|PROSITE-
ProRule:PRU00471}.
NP_BIND 36 43 ATP. {ECO:0000255}.
COILED 228 359 {ECO:0000255}.
COILED 401 598 {ECO:0000255}.
COILED 635 673 {ECO:0000255}.
COILED 706 734 {ECO:0000255}.
COILED 789 1079 {ECO:0000255}.
COMPBIAS 1201 1238 Ala/Asp-rich (DA-box).
METAL 681 681 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00471}.
METAL 684 684 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00471}.
MOD_RES 635 635 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 690 690 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 959 959 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 139 Missing (in isoform 3).
{ECO:0000303|PubMed:10415333}.
/FTId=VSP_012590.
VAR_SEQ 1 5 MSRIE -> MLIFSVRDMFA (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_012591.
VARIANT 94 94 I -> L (in dbSNP:rs28903085).
{ECO:0000269|PubMed:14684699}.
/FTId=VAR_025526.
VARIANT 127 127 V -> I (in dbSNP:rs28903086).
/FTId=VAR_029168.
VARIANT 191 191 T -> I (in dbSNP:rs2230017).
/FTId=VAR_022085.
VARIANT 193 193 R -> W (in dbSNP:rs28903087).
/FTId=VAR_029169.
VARIANT 224 224 R -> H (in dbSNP:rs28903088).
{ECO:0000269|PubMed:14684699}.
/FTId=VAR_025527.
VARIANT 315 315 V -> L (in dbSNP:rs28903090).
/FTId=VAR_034436.
VARIANT 469 469 G -> A (in dbSNP:rs55653181).
/FTId=VAR_061779.
VARIANT 616 616 K -> E (in dbSNP:rs1047380).
{ECO:0000269|Ref.3}.
/FTId=VAR_020958.
VARIANT 697 697 V -> A (in dbSNP:rs1047382).
{ECO:0000269|Ref.3}.
/FTId=VAR_020959.
VARIANT 842 842 V -> A (in dbSNP:rs28903093).
/FTId=VAR_029170.
VARIANT 964 964 Y -> H (in dbSNP:rs1047386).
{ECO:0000269|Ref.3}.
/FTId=VAR_020960.
VARIANT 973 973 K -> M (in dbSNP:rs1129482).
{ECO:0000269|Ref.3}.
/FTId=VAR_020961.
VARIANT 1038 1038 R -> G (in dbSNP:rs1047387).
/FTId=VAR_020962.
MUTAGEN 42 42 K->N: Abolishes ability to degrade ATP.
{ECO:0000269|PubMed:9651580}.
MUTAGEN 1231 1231 D->A: Abolishes ability to degrade ATP.
{ECO:0000269|PubMed:9651580}.
CONFLICT 204 204 K -> E (in Ref. 3; CAA99729).
{ECO:0000305}.
CONFLICT 723 723 E -> K (in Ref. 6; AAH62603/AAH73850).
{ECO:0000305}.
CONFLICT 733 733 V -> A (in Ref. 3; CAA99729).
{ECO:0000305}.
HELIX 586 632 {ECO:0000244|PDB:5GOX}.
HELIX 638 673 {ECO:0000244|PDB:5GOX}.
TURN 674 676 {ECO:0000244|PDB:5GOX}.
STRAND 682 684 {ECO:0000244|PDB:5GOX}.
HELIX 691 704 {ECO:0000244|PDB:5GOX}.
TURN 705 707 {ECO:0000244|PDB:5GOX}.
HELIX 708 731 {ECO:0000244|PDB:5GOX}.
HELIX 733 744 {ECO:0000244|PDB:5GOX}.
HELIX 746 764 {ECO:0000244|PDB:5GOX}.
SEQUENCE 1312 AA; 153892 MW; 1F208C3817FC41FC CRC64;
MSRIEKMSIL GVRSFGIEDK DKQIITFFSP LTILVGPNGA GKTTIIECLK YICTGDFPPG
TKGNTFVHDP KVAQETDVRA QIRLQFRDVN GELIAVQRSM VCTQKSKKTE FKTLEGVITR
TKHGEKVSLS SKCAEIDREM ISSLGVSKAV LNNVIFCHQE DSNWPLSEGK ALKQKFDEIF
SATRYIKALE TLRQVRQTQG QKVKEYQMEL KYLKQYKEKA CEIRDQITSK EAQLTSSKEI
VKSYENELDP LKNRLKEIEH NLSKIMKLDN EIKALDSRKK QMEKDNSELE EKMEKVFQGT
DEQLNDLYHN HQRTVREKER KLVDCHRELE KLNKESRLLN QEKSELLVEQ GRLQLQADRH
QEHIRARDSL IQSLATQLEL DGFERGPFSE RQIKNFHKLV RERQEGEAKT ANQLMNDFAE
KETLKQKQID EIRDKKTGLG RIIELKSEIL SKKQNELKNV KYELQQLEGS SDRILELDQE
LIKAERELSK AEKNSNVETL KMEVISLQNE KADLDRTLRK LDQEMEQLNH HTTTRTQMEM
LTKDKADKDE QIRKIKSRHS DELTSLLGYF PNKKQLEDWL HSKSKEINQT RDRLAKLNKE
LASSEQNKNH INNELKRKEE QLSSYEDKLF DVCGSQDFES DLDRLKEEIE KSSKQRAMLA
GATAVYSQFI TQLTDENQSC CPVCQRVFQT EAELQEVISD LQSKLRLAPD KLKSTESELK
KKEKRRDEML GLVPMRQSII DLKEKEIPEL RNKLQNVNRD IQRLKNDIEE QETLLGTIMP
EEESAKVCLT DVTIMERFQM ELKDVERKIA QQAAKLQGID LDRTVQQVNQ EKQEKQHKLD
TVSSKIELNR KLIQDQQEQI QHLKSTTNEL KSEKLQISTN LQRRQQLEEQ TVELSTEVQS
LYREIKDAKE QVSPLETTLE KFQQEKEELI NKKNTSNKIA QDKLNDIKEK VKNIHGYMKD
IENYIQDGKD DYKKQKETEL NKVIAQLSEC EKHKEKINED MRLMRQDIDT QKIQERWLQD
NLTLRKRNEE LKEVEEERKQ HLKEMGQMQV LQMKSEHQKL EENIDNIKRN HNLALGRQKG
YEEEIIHFKK ELREPQFRDA EEKYREMMIV MRTTELVNKD LDIYYKTLDQ AIMKFHSMKM
EEINKIIRDL WRSTYRGQDI EYIEIRSDAD ENVSASDKRR NYNYRVVMLK GDTALDMRGR
CSAGQKVLAS LIIRLALAET FCLNCGIIAL DEPTTNLDRE NIESLAHALV EIIKSRSQQR
NFQLLVITHD EDFVELLGRS EYVEKFYRIK KNIDQCSEIV KCSVSSLGFN VH


Related products :

Catalog number Product name Quantity
EIAAB33656 DNA repair protein RAD50,Homo sapiens,hRAD50,Human,RAD50
DL-RAD50-Mu Mouse DNA Repair Protein RAD50 (RAD50) ELISA Kit 96T
DL-RAD50-Hu Human DNA Repair Protein RAD50 (RAD50) ELISA Kit 96T
RAD50_HUMAN ELISA Kit FOR DNA repair protein RAD50; organism: Human; gene name: RAD50 96T
SEK111Hu ELISA Kit for DNA Repair Protein RAD50 (RAD50) Homo sapiens (Human) 96T
E99111Mu ELISA Kit for DNA Repair Protein RAD50 (RAD50) Organism: Mus musculus (Mouse) 96T
RAD50_MOUSE ELISA Kit FOR DNA repair protein RAD50; organism: Mouse; gene name: Rad50 96T
SEK111Mu ELISA Kit for DNA Repair Protein RAD50 (RAD50) Mus musculus (Mouse) 96T
CSB-EL019262HU Human DNA repair protein RAD50(RAD50) ELISA kit SpeciesHuman 96T
CSB-EL019262MO Mouse DNA repair protein RAD50(RAD50) ELISA kit SpeciesMouse 96T
EIAAB33654 DNA repair protein RAD50,Mouse,mRad50,Mus musculus,Rad50
CSB-EL019262HU Human DNA repair protein RAD50(RAD50) ELISA kit 96T
CSB-EL019262MO Mouse DNA repair protein RAD50(RAD50) ELISA kit 96T
CSB-EL019262RA Rat DNA repair protein RAD50(RAD50) ELISA kit SpeciesRat 96T
EIAAB33655 DNA repair protein RAD50,Rad50,Rat,Rattus norvegicus
201-02-1074 Mouse DNA Repair Protein RAD50(RAD50)ELISA Kit 96T
P99111Hu01 DNA Repair Protein RAD50 (RAD50) Organism: Homo sapiens (Human) Source: Escherichia coli 100ug
E99111Mu ELISA Kit for DNA Repair Protein RAD50 (RAD50), Organism Mus musculus (Mouse), Detection range 0.312-20ng_mL 96T/Kit
P99111Hu01 DNA Repair Protein RAD50 (RAD50) Organism: Homo sapiens (Human) Source: Escherichia coli 50ug
P99111Hu01 DNA Repair Protein RAD50 (RAD50) Organism: Homo sapiens (Human) Source: Escherichia coli 10ug
E99111Mu ELISA Kit for DNA Repair Protein RAD50 (RAD50) 96T/Kit
CSB-EL019262RA Rat DNA repair protein RAD50(RAD50) ELISA kit 96T
A99111Hu01 Antibody to DNA Repair Protein RAD50 (RAD50) Organism: Homo sapiens (Human) Type: Polyclonal Source: Rabbit 100ug
A99111Hu01 Antibody to DNA Repair Protein RAD50 (RAD50) Organism: Homo sapiens (Human) Type: Polyclonal Source: Rabbit 50ug
A99111Hu01-B Biotin-linked Antibody to DNA Repair Protein RAD50 (RAD50); Reactivity: Homo sapiens (Human) Clonality: Polyclonal Source: Rabbit 50ug


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur