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

 RAD50_RAT               Reviewed;        1312 AA.
Q9JIL8;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
10-MAY-2017, entry version 106.
RecName: Full=DNA repair protein RAD50;
EC=3.6.-.-;
Name=Rad50;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=10908350; DOI=10.1093/nar/28.15.2882;
Lanson N.A. Jr., Egeland D.B., Royals B.A., Claycomb W.C.;
"The MRE11-NBS1-RAD50 pathway is perturbed in SV40 large T antigen-
immortalized AT-1, AT-2 and HL-1 cardiomyocytes.";
Nucleic Acids Res. 28:2882-2892(2000).
[2]
PROTEIN SEQUENCE OF 454-458; 726-736; 824-832 AND 1127-1134, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
-!- 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. 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 (By similarity).
{ECO:0000250}.
-!- 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. Component of the BASC
complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM,
RAD50, MRE11 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 MRNIP.
{ECO:0000250|UniProtKB:Q92878}.
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere.
Note=Localizes to discrete nuclear foci after treatment with
genotoxic agents.
-!- TISSUE SPECIFICITY: Present at low levels in the heart at fetal-
day 17, at relatively constant levels at postnatal days 10, 17 and
21 and at slightly lower levels in the adult heart. Detected in
liver, kidney and lung. Barely detectable in skeletal muscle with
slightly higher levels observed in brain and the ventricles of the
heart (at protein level). {ECO:0000269|PubMed:10908350}.
-!- 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}.
-!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
{ECO:0000305}.
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EMBL; AF218576; AAF91229.1; -; mRNA.
RefSeq; NP_071582.1; NM_022246.1.
UniGene; Rn.51136; -.
ProteinModelPortal; Q9JIL8; -.
SMR; Q9JIL8; -.
BioGrid; 248931; 1.
STRING; 10116.ENSRNOP00000062378; -.
iPTMnet; Q9JIL8; -.
PhosphoSitePlus; Q9JIL8; -.
PaxDb; Q9JIL8; -.
PRIDE; Q9JIL8; -.
GeneID; 64012; -.
KEGG; rno:64012; -.
UCSC; RGD:621542; rat.
CTD; 10111; -.
RGD; 621542; Rad50.
eggNOG; KOG0962; Eukaryota.
eggNOG; COG0419; LUCA.
HOGENOM; HOG000090195; -.
HOVERGEN; HBG058033; -.
InParanoid; Q9JIL8; -.
KO; K10866; -.
PhylomeDB; Q9JIL8; -.
PRO; PR:Q9JIL8; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0000794; C:condensed nuclear chromosome; IDA:RGD.
GO; GO:0016234; C:inclusion body; IDA:RGD.
GO; GO:0030870; C:Mre11 complex; ISS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:RGD.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
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:0003690; F:double-stranded DNA binding; IDA:RGD.
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; ISS:UniProtKB.
GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:RGD.
GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
GO; GO:0006310; P:DNA recombination; ISS:UniProtKB.
GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
GO; GO:0007507; P:heart development; IEP:RGD.
GO; GO:0046597; P:negative regulation of viral entry into host cell; IMP:RGD.
GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GO_Central.
GO; GO:0051291; P:protein heterooligomerization; IDA:RGD.
GO; GO:0007131; P:reciprocal meiotic recombination; TAS:RGD.
GO; GO:0000019; P:regulation of mitotic recombination; ISS:UniProtKB.
GO; GO:0044752; P:response to human chorionic gonadotropin; IEP:RGD.
GO; GO:0016233; P:telomere capping; IBA:GO_Central.
GO; GO:0000723; P:telomere maintenance; TAS:RGD.
GO; GO:0000722; P:telomere maintenance via recombination; IBA:GO_Central.
GO; GO:0007004; P:telomere maintenance via telomerase; ISS:UniProtKB.
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;
Acetylation; ATP-binding; Cell cycle; Chromosome; Coiled coil;
Complete proteome; Direct protein sequencing; DNA damage; DNA repair;
Hydrolase; Meiosis; Metal-binding; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Telomere; Zinc.
CHAIN 1 1312 DNA repair protein RAD50.
/FTId=PRO_0000138643.
DOMAIN 635 734 Zinc-hook. {ECO:0000255|PROSITE-
ProRule:PRU00471}.
NP_BIND 36 43 ATP. {ECO:0000255}.
COILED 200 534 {ECO:0000255}.
COILED 635 673 {ECO:0000255}.
COILED 706 734 {ECO:0000255}.
COILED 754 954 {ECO:0000255}.
COILED 1019 1075 {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:0000250|UniProtKB:Q92878}.
MOD_RES 690 690 Phosphothreonine.
{ECO:0000250|UniProtKB:Q92878}.
MOD_RES 959 959 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q92878}.
SEQUENCE 1312 AA; 153784 MW; F13C041BD2C05932 CRC64;
MSRIEKMSTL GVRSFGIEDK DKQIISFFSP LTILVGPNGA GKTTIIECLK YICTGDFPPG
TKGNTFVHDP KVAQETDVRA QIRLQFRDVN GEMVLVQRSM LCSQKSKKTE FKTLEGVITR
IKHGEKVSLS SKCAEIDREM ISCLGVSKSV LNNVIFCHQE DSNWPLSEGK ALKQKFDEIF
SATRYIKALD TLRQVRQTQG QKVKECQTEL KYLRQNKEKA CEIRDQITSK EAQLASSREI
VKAYENELEP LKNRLKEIEH NLSKIMRLDN EIKALDSRKK QMEKDNSELE QKMEKVFQGT
DEQLNDLYHN HQRTVREKER RLVDCQRELE KLSKEARLLN QERAELLVEQ GRLQLQADRH
QEHIRARDSL IQSLAAHLEL DGFERGPFSE RQIKNFHELV RERQEREAKT ASQLLSDLTD
KEALKQRQMD EMRDKKSGLG RMIELKTEIL TKKQTELRNV RNELQQLEGS SDRILELDQE
LTKAERELSK AEKNSSIETL KAEILNLQSE KADLDRNLRK LDQEMEQLNH HTTTRTQMEM
LTKDKTDKDE QIRKIKSRHS DELTSLLGYF PNKKQLEDWL HSKSKEINQT RDRLAKLNKE
LASAEQNKNH INNELKKKEE QLSSYEDKLF DVCGSQDFES DLDRLKEDIE KSSKQRAMLA
GATAVYSQFI TQLTDENQSC CPGCQRVFQT EAELQEVISD LQSKLRLAPD KLKSTESELK
KKERRRDEML GLVPMRQSII DLKEKEIPEL RNRLQSVNRD IQRLKNDIEE QETLLGTVMP
EEESAKVCLT DVTIMERFQM ELKDVERKIA QQAAKLQGVD LDRTVQQVNQ EKQEKQHKLD
TVSSKIELNR KLIQDQQEQI QHLKSKTNEL KSEKLQIATN LQRRQQMEEQ TVELSTEVQS
LNREIKDAKE QINPLEIALE KLQQEKEELI HRKNTSNKMA QDKINDIKEK VKNIHGYMKD
IENYIQDGKD DYKKQKETEL NEVVIQLNEC DKHKEKINKE MGTMRQDIDT KKIQERWLQD
NLTLRKRREE LKEVEEERKQ HLKEMGQMQV LQMKNEHQKL EENIDTIKRN HSLALGRQKG
YEEEILHFKK ELREPQFRDA EEKYREMMIV MRTTELVNKD LDIYYKTLDH AIMKFHSMKM
EEINKIIRDL WRSTYRGQDI EYIEIRSDAD ENVSASDKRR NYNYRVVMLK GDTALDMRGR
CSAGQKVLAS LIIRLALAET FCLNCGILAL DEPTTNLDRE NIESLAHALV EIIKSRSQQR
NFQLLVITHD EDFVELLGRS EYVEKFYRVK KNIDQCSEIV KSSINSLGSY VH


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