ID A0A494C1B7_HUMAN Unreviewed; 894 AA.
AC A0A494C1B7;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=RAD50 double strand break repair protein {ECO:0000313|Ensembl:ENSP00000498973.1};
DE Flags: Fragment;
GN Name=RAD50 {ECO:0000313|Ensembl:ENSP00000498973.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000498973.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000498973.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2] {ECO:0000313|Ensembl:ENSP00000498973.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000256|ARBA:ARBA00009439}.
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DR EMBL; AC004041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF457995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF458010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A494C1B7; -.
DR SMR; A0A494C1B7; -.
DR MassIVE; A0A494C1B7; -.
DR PeptideAtlas; A0A494C1B7; -.
DR Antibodypedia; 14460; 536 antibodies from 35 providers.
DR Ensembl; ENST00000652485.1; ENSP00000498973.1; ENSG00000113522.14.
DR HGNC; HGNC:9816; RAD50.
DR VEuPathDB; HostDB:ENSG00000113522; -.
DR GeneTree; ENSGT00390000018781; -.
DR ChiTaRS; RAD50; human.
DR Proteomes; UP000005640; Chromosome 5.
DR Bgee; ENSG00000113522; Expressed in corpus callosum and 113 other cell types or tissues.
DR ExpressionAtlas; A0A494C1B7; baseline and differential.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR004584; Rad50_eukaryotes.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR NCBIfam; TIGR00606; rad50; 1.
DR PANTHER; PTHR18867:SF12; DNA REPAIR PROTEIN RAD50; 1.
DR PANTHER; PTHR18867; RAD50; 1.
DR Pfam; PF13476; AAA_23; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromosome {ECO:0000256|ARBA:ARBA00022895};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00471}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proteomics identification {ECO:0007829|EPD:A0A494C1B7,
KW ECO:0007829|MaxQB:A0A494C1B7};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00471}.
FT DOMAIN 646..745
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT COILED 241..349
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 501..673
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 723..884
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 692
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 695
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT NON_TER 894
FT /evidence="ECO:0000313|Ensembl:ENSP00000498973.1"
SQ SEQUENCE 894 AA; 104099 MW; 6B3E97597B5EA4CE 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
LIKASVLLLH ISITKERELS KAEKNSNVET LKMEVISLQN EKADLDRTLR KLDQEMEQLN
HHTTTRTQME MLTKDKADKD EQIRKIKSRH SDELTSLLGY FPNKKQLEDW LHSKSKEINQ
TRDRLAKLNK ELASSEQNKN HINNELKRKE EQLSSYEDKL FDVCGSQDFE SDLDRLKEEI
EKSSKQRAML AGATAVYSQF ITQLTDENQS CCPVCQRVFQ TEAELQEVIS DLQSKLRLAP
DKLKSTESEL KKKEKRRDEM LGLVPMRQSI IDLKEKEIPE LRNKLQNVNR DIQRLKNDIE
EQETLLGTIM PEEESAKVCL TDVTIMERFQ MELKDVERKI AQQAAKLQGI DLDRTVQQVN
QEKQEKQHKL DTVSSKIELN RKLIQDQQEQ IQHLKSTTNE LKSEKLQIST NLQR
//
