P70388 (RAD50_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA repair protein RAD50
Short name=mRad50
EC=3.6.-.-

Gene names

Name:

Rad50

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1312 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity. Ref.4 Ref.5
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 By similarity.
Subcellular location	Nucleus By similarity. Chromosome › telomere By similarity. Note: Localizes to discrete nuclear foci after treatment with genotoxic agents By similarity.
Tissue specificity	In adult, it is expressed at very low level in most tissues, except in heart, lung and aorta. Expressed at high level in testis. Ref.1
Developmental stage	Widely expressed. Expressed at higher level in heart, liver and thymus from E18. By neonatal day 1.5, it decreases in brain, liver, gut and skin, while it is expressed in spleen. 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.
Disruption phenotype	Defects cause embryonic stem cell lethality, abnormal embryonic development and sensitivity to ionizing radiation. Ref.4
Sequence similarities	Belongs to the SMC family. RAD50 subfamily. Contains 1 zinc-hook domain.

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA repair Meiosis
Cellular component	Chromosome Nucleus Telomere
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW meiosis Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC response to DNA damage stimulus Inferred from sequence orthology PubMed 17500065. Source: MGI
Cellular_component	Mre11 complex Inferred from electronic annotation. Source: InterPro chromosome, telomeric region Inferred from electronic annotation. Source: UniProtKB-SubCell pronucleus Inferred from direct assay PubMed 17982445. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nuclease activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P70388-1)

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: P70388-2)

The sequence of this isoform differs from the canonical sequence as follows:
     485-545: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: P70388-3)

Also known as: 3.1 kb splice variant;

The sequence of this isoform differs from the canonical sequence as follows:
     1-886: Missing.

Isoform 4 (identifier: P70388-4)

Also known as: 1.6 kb splice variant;

The sequence of this isoform differs from the canonical sequence as follows:
     485-496: ERELSKAEKNSS → IYFLELVRWLSG
     497-1312: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1312	1312	DNA repair protein RAD50		PRO_0000138642
Regions
	Domain	635 – 734	100	Zinc-hook
	Nucleotide binding	36 – 43	8	ATP Potential
	Coiled coil	200 – 532	333	Potential
	Coiled coil	635 – 673	39	Potential
	Coiled coil	706 – 734	29	Potential
	Coiled coil	776 – 942	167	Potential
	Coiled coil	1043 – 1075	33	Potential
	Compositional bias	1201 – 1238	38	Ala/Asp-rich (DA-box)
Sites
	Metal binding	681	1	Zinc By similarity
	Metal binding	684	1	Zinc By similarity
Amino acid modifications
	Modified residue	237	1	Phosphoserine Ref.6
	Modified residue	635	1	Phosphoserine By similarity
	Modified residue	690	1	Phosphothreonine By similarity
	Modified residue	959	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	1 – 886	886	Missing in isoform 3.		VSP_012592
	Alternative sequence	485 – 545	61	Missing in isoform 2.		VSP_012593
	Alternative sequence	485 – 496	12	ERELS…EKNSS → IYFLELVRWLSG in isoform 4.		VSP_012594
	Alternative sequence	497 – 1312	816	Missing in isoform 4.		VSP_012595
Experimental info
	Mutagenesis	22	1	K → M in Rad50S; hypomorphic allele that induces growth defects and cancer predisposition. Homozygous individuals die with complete bone marrow depletion as a result of progressive hematopoietic stem cell failure. Ref.5
	Sequence conflict	97	1	H → Q in BAB31030. Ref.2
	Sequence conflict	200	1	G → V in AAH58180. Ref.3
	Sequence conflict	474	1	I → V in BAC40074. Ref.2
	Sequence conflict	718	1	E → A in BAC40074. Ref.2
	Sequence conflict	719	1	L → K in AAH58180. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 4AF9AF9AD9E1D7A2	FASTA	1,312	153,488
	10 20 30 40 50 60 MSRIEKMSIL GVRSFGIEDK DKQIISFFSP LTILVGPNGA GKTTIIECLK YICTGDFPPG 70 80 90 100 110 120 TKGNTFVHDP KVAQETDVRA QIRLQFRDVN GEMVAVHRSM LCSQKNKKTE FKTLEGVITR 130 140 150 160 170 180 MKHGEKVSLS SKCAEIDREM ISCLGVSKSV LNNVIFCHQE DSNWPLSEGK ALKQKFDEIF 190 200 210 220 230 240 SATRYIKALD TLRQVRQTQG QKVKECQTEL KYLKQNKEKA CEIRDQITSK EAQLASSQEI 250 260 270 280 290 300 VRSYEDELEP LKNRLKEIEH NLSKIMKLDN EIKALESRKK QMEKDNSELE QKMEKVFQGT 310 320 330 340 350 360 DEQLNDLYHN HQRTVREKER RLVDCQRELE KLNKEARLLN QEKAELLVEQ GRLQLQADRH 370 380 390 400 410 420 QEHIRARDSL IQSLATHLEL DGFERGPFSE RQIKNFHELV KERQEREAKT ASQLLSDLTD 430 440 450 460 470 480 KEALKQRQLD ELRDRKSGLG RTIELKTEIL TKKQSELRHV RSELQQLEGS SDRILELDQE 490 500 510 520 530 540 LTKAERELSK AEKNSSIETL KAEVMSLQNE KADLDRSLRK LDQEMEQLNH HTTTRTQMEM 550 560 570 580 590 600 LTKDKTDKDE QIRKIKSRHS DELTSLLGYF PNKKQLEDWL HSKSKEINQT RDRLAKLNKE 610 620 630 640 650 660 LASAEQNKNH INNELKKKEE QLSSYEDKLF DVCGSQDLES DLGRLKEEIE KSSKQRAMLA 670 680 690 700 710 720 GATAVYSQFI TQLTDENQSC CPVCQRVFQT EAELQEVISD LQSKLRLAPD KLKSTESELK 730 740 750 760 770 780 KKERRRDEML GLVPVRQSII DLKEKEIPEL RNRLQSVNRD IQRLKNDIEE QETLLGTIMP 790 800 810 820 830 840 EEESAKVCLT DVTIMERFQM ELKDVERKIA QQAAKLQGVD LDRTVQQVNQ EKQEKQHRLD 850 860 870 880 890 900 TVTSKIELNR KLIQDQQEQI QHLKSKTNEL KSEKLQIATN LQRRQQMEEQ SVELSTEVQS 910 920 930 940 950 960 LNREIKDAKE QISPLETALE KLQQEKEELI HRKHTSNKMA QDKINDIKEK VKNIHGYMKD 970 980 990 1000 1010 1020 IENYIQDGKD DYKKQKETEL NGVAVQLNEC EKHREKINKD MGTMRQDIDT QKIQERWLQD 1030 1040 1050 1060 1070 1080 NLTLRKRRDE LKEVEEEPKQ HLKEMGQMQV LQMKNEHQKL EENIDTIKRN HSLALGRQKG 1090 1100 1110 1120 1130 1140 YEDEILHFKK 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 FCLNCGILAL DEPTTNLDRE NIESLAHALV EIIKSRSQQR 1270 1280 1290 1300 1310 NFQLLVITHD EDFVELLGRS EYVEKFYRVK KNMDQCSEIV KCSISSLGSY VH
	Isoform 2 [UniParc]. Checksum: C8583CBF04603CD5	FASTA	1,251	146,317
	10 20 30 40 50 60 MSRIEKMSIL GVRSFGIEDK DKQIISFFSP LTILVGPNGA GKTTIIECLK YICTGDFPPG 70 80 90 100 110 120 TKGNTFVHDP KVAQETDVRA QIRLQFRDVN GEMVAVHRSM LCSQKNKKTE FKTLEGVITR 130 140 150 160 170 180 MKHGEKVSLS SKCAEIDREM ISCLGVSKSV LNNVIFCHQE DSNWPLSEGK ALKQKFDEIF 190 200 210 220 230 240 SATRYIKALD TLRQVRQTQG QKVKECQTEL KYLKQNKEKA CEIRDQITSK EAQLASSQEI 250 260 270 280 290 300 VRSYEDELEP LKNRLKEIEH NLSKIMKLDN EIKALESRKK QMEKDNSELE QKMEKVFQGT 310 320 330 340 350 360 DEQLNDLYHN HQRTVREKER RLVDCQRELE KLNKEARLLN QEKAELLVEQ GRLQLQADRH 370 380 390 400 410 420 QEHIRARDSL IQSLATHLEL DGFERGPFSE RQIKNFHELV KERQEREAKT ASQLLSDLTD 430 440 450 460 470 480 KEALKQRQLD ELRDRKSGLG RTIELKTEIL TKKQSELRHV RSELQQLEGS SDRILELDQE 490 500 510 520 530 540 LTKATDKDEQ IRKIKSRHSD ELTSLLGYFP NKKQLEDWLH SKSKEINQTR DRLAKLNKEL 550 560 570 580 590 600 ASAEQNKNHI NNELKKKEEQ LSSYEDKLFD VCGSQDLESD LGRLKEEIEK SSKQRAMLAG 610 620 630 640 650 660 ATAVYSQFIT QLTDENQSCC PVCQRVFQTE AELQEVISDL QSKLRLAPDK LKSTESELKK 670 680 690 700 710 720 KERRRDEMLG LVPVRQSIID LKEKEIPELR NRLQSVNRDI QRLKNDIEEQ ETLLGTIMPE 730 740 750 760 770 780 EESAKVCLTD VTIMERFQME LKDVERKIAQ QAAKLQGVDL DRTVQQVNQE KQEKQHRLDT 790 800 810 820 830 840 VTSKIELNRK LIQDQQEQIQ HLKSKTNELK SEKLQIATNL QRRQQMEEQS VELSTEVQSL 850 860 870 880 890 900 NREIKDAKEQ ISPLETALEK LQQEKEELIH RKHTSNKMAQ DKINDIKEKV KNIHGYMKDI 910 920 930 940 950 960 ENYIQDGKDD YKKQKETELN GVAVQLNECE KHREKINKDM GTMRQDIDTQ KIQERWLQDN 970 980 990 1000 1010 1020 LTLRKRRDEL KEVEEEPKQH LKEMGQMQVL QMKNEHQKLE ENIDTIKRNH SLALGRQKGY 1030 1040 1050 1060 1070 1080 EDEILHFKKE LREPQFRDAE EKYREMMIVM RTTELVNKDL DIYYKTLDQA IMKFHSMKME 1090 1100 1110 1120 1130 1140 EINKIIRDLW RSTYRGQDIE YIEIRSDADE NVSASDKRRN YNYRVVMLKG DTALDMRGRC 1150 1160 1170 1180 1190 1200 SAGQKVLASL IIRLALAETF CLNCGILALD EPTTNLDREN IESLAHALVE IIKSRSQQRN 1210 1220 1230 1240 1250 FQLLVITHDE DFVELLGRSE YVEKFYRVKK NMDQCSEIVK CSISSLGSYV H
	Isoform 3 (3.1 kb splice variant) [UniParc]. Checksum: D52552F467A47A85	FASTA	426	50,408
	10 20 30 40 50 60 MEEQSVELST EVQSLNREIK DAKEQISPLE TALEKLQQEK EELIHRKHTS NKMAQDKIND 70 80 90 100 110 120 IKEKVKNIHG YMKDIENYIQ DGKDDYKKQK ETELNGVAVQ LNECEKHREK INKDMGTMRQ 130 140 150 160 170 180 DIDTQKIQER WLQDNLTLRK RRDELKEVEE EPKQHLKEMG QMQVLQMKNE HQKLEENIDT 190 200 210 220 230 240 IKRNHSLALG RQKGYEDEIL HFKKELREPQ FRDAEEKYRE MMIVMRTTEL VNKDLDIYYK 250 260 270 280 290 300 TLDQAIMKFH SMKMEEINKI IRDLWRSTYR GQDIEYIEIR SDADENVSAS DKRRNYNYRV 310 320 330 340 350 360 VMLKGDTALD MRGRCSAGQK VLASLIIRLA LAETFCLNCG ILALDEPTTN LDRENIESLA 370 380 390 400 410 420 HALVEIIKSR SQQRNFQLLV ITHDEDFVEL LGRSEYVEKF YRVKKNMDQC SEIVKCSISS LGSYVH
	Isoform 4 (1.6 kb splice variant) [UniParc]. Checksum: 8D296981D5BD922F	FASTA	496	57,589
	10 20 30 40 50 60 MSRIEKMSIL GVRSFGIEDK DKQIISFFSP LTILVGPNGA GKTTIIECLK YICTGDFPPG 70 80 90 100 110 120 TKGNTFVHDP KVAQETDVRA QIRLQFRDVN GEMVAVHRSM LCSQKNKKTE FKTLEGVITR 130 140 150 160 170 180 MKHGEKVSLS SKCAEIDREM ISCLGVSKSV LNNVIFCHQE DSNWPLSEGK ALKQKFDEIF 190 200 210 220 230 240 SATRYIKALD TLRQVRQTQG QKVKECQTEL KYLKQNKEKA CEIRDQITSK EAQLASSQEI 250 260 270 280 290 300 VRSYEDELEP LKNRLKEIEH NLSKIMKLDN EIKALESRKK QMEKDNSELE QKMEKVFQGT 310 320 330 340 350 360 DEQLNDLYHN HQRTVREKER RLVDCQRELE KLNKEARLLN QEKAELLVEQ GRLQLQADRH 370 380 390 400 410 420 QEHIRARDSL IQSLATHLEL DGFERGPFSE RQIKNFHELV KERQEREAKT ASQLLSDLTD 430 440 450 460 470 480 KEALKQRQLD ELRDRKSGLG RTIELKTEIL TKKQSELRHV RSELQQLEGS SDRILELDQE 490 LTKAIYFLEL VRWLSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mouse RAD50 has limited epitopic homology to p53 and is expressed in the adult myocardium." Kim K.K., Daud A.I., Wong S.C., Pajak L., Tsai S.-C., Wang H., Henzel W.J., Field L.J. J. Biol. Chem. 271:29255-29264(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), PROTEIN SEQUENCE OF 113-120; 132-140; 175-202; 230-248; 295-310; 815-832; 840-845; 1012-1026 AND 1079-1089, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-214 AND 443-743 (ISOFORM 1). Strain: C57BL/6J and NOD. Tissue: Thymus.
[3]	"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] OF 1-722 (ISOFORM 2). Strain: NMRI. Tissue: Mammary tumor.
[4]	"Disruption of mRad50 causes embryonic stem cell lethality, abnormal embryonic development, and sensitivity to ionizing radiation." Luo G., Yao M.S., Bender C.F., Mills M., Bladl A.R., Bradley A., Petrini J.H.J. Proc. Natl. Acad. Sci. U.S.A. 96:7376-7381(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]	"Cancer predisposition and hematopoietic failure in Rad50(S/S) mice." Bender C.F., Sikes M.L., Sullivan R., Huye L.E., Le Beau M.M., Roth D.B., Mirzoeva O.K., Oltz E.M., Petrini J.H.J. Genes Dev. 16:2237-2251(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LYS-22.
[6]	"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-237, MASS SPECTROMETRY. Tissue: Embryonic kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U66887 mRNA. Translation: AAC52894.1. AK018001 mRNA. Translation: BAB31030.1. AK087982 mRNA. Translation: BAC40074.1. BC058180 mRNA. Translation: AAH58180.1.
IPI	IPI00108335. IPI00551249. IPI00551329. IPI00551367.
PIR	T30845.
UniGene	Mm.4888.
3D structure databases
ProteinModelPortal	P70388.
SMR	P70388. Positions 7-67.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-46805N.
IntAct	P70388. 2 interactions.
PTM databases
PhosphoSite	P70388.
Proteomic databases
PaxDb	P70388.
PRIDE	P70388.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	uc011xus.1. mouse.
Organism-specific databases
MGI	MGI:109292. Rad50.
Phylogenomic databases
eggNOG	COG0419.
HOGENOM	HOG000090195.
HOVERGEN	HBG058033.
InParanoid	P70388.
OrthoDB	EOG45HRWK.
Gene expression databases
CleanEx	MM_RAD50.
Genevestigator	P70388.
GermOnline	ENSMUSG00000020380. Mus musculus.
Family and domain databases
InterPro	IPR004584. Rad50. IPR007517. Rad50_Zn_hook. IPR013134. Zn_hook_Rad50. [Graphical view]
PANTHER	PTHR18867. PTHR18867. 1 hit.
Pfam	PF04423. Rad50_zn_hook. 1 hit. [Graphical view]
TIGRFAMs	TIGR00606. rad50. 1 hit.
PROSITE	PS51131. ZN_HOOK. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

RAD50_MOUSE

Accession

Primary (citable) accession number: P70388
Secondary accession number(s): Q6PEB0, Q8C2T7, Q9CU59

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program