Reviewed, UniProtKB/Swiss-Prot Q9QWZ1 (RAD1_MOUSE)

Names and origin

Protein names

Recommended name:
    Cell cycle checkpoint protein RAD1
      Short name=mRAD1
    EC=3.1.11.2
Alternative name(s):
    DNA repair exonuclease rad1 homolog
    Rad1-like DNA damage checkpoint protein

Gene names

Name:	Rad1
Synonyms:	Rec1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	280 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. Isoform 1 possesses 3'->5' double stranded DNA exonuclease activity By similarity.
Catalytic activity	Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Subunit structure	Component of the toroidal 9-1-1 (RAD9-RAD1-HUS1) complex, composed of RAD9A, RAD1 and HUS1. The 9-1-1 complex associates with LIG1, POLB, FEN1, RAD17, HDAC1, RPA1 and RPA2. The 9-1-1 complex associates with the RAD17-RFC complex. RAD1 interacts with POLB, FEN1, HUS1, HUS1B, RAD9A and RAD9B By similarity.
Subcellular location	Nucleus By similarity.
Tissue specificity	Expressed in testis, uterus, bladder, spleen, ovaries, lung, brain and muscle (at protein level). Expressed in brain, testis, kidney, heart, liver and lung. Ref.1 Ref.2 Ref.4
Sequence similarities	Belongs to the rad1 family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Exonuclease Hydrolase Nuclease
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3'-5' exonuclease activity Inferred from sequence or structural similarity. Source: UniProtKB damaged DNA binding Inferred from electronic annotation. Source: InterPro exodeoxyribonuclease III activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9QWZ1-1)

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: Q9QWZ1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     223-280: YKLSLLKPST...CCPDEEVPES → ISDVKYSCKT...QWVNVVPVQA

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 280	280	Cell cycle checkpoint protein RAD1		PRO_0000225006
Natural variations
	Alternative sequence	223 – 280	58	YKLSL…EVPES → ISDVKYSCKTWLQLPEGVGY DPLSGLEWTLSERDGEQEVA QWVNVVPVQA in isoform 2.		VSP_017337
Experimental info
	Sequence conflict	28	1	S → F Ref.3
	Sequence conflict	28	1	S → F Ref.4
	Sequence conflict	28	1	S → F Ref.6
	Sequence conflict	28	1	S → F Ref.7
	Sequence conflict	71	1	Q → E in BAE28343. Ref.8
	Sequence conflict	118	1	P → T in BAE40457. Ref.8
	Sequence conflict	198	1	N → S in AAC95465. Ref.2
	Sequence conflict	216	1	D → N in AAC27248. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: F9D6ED292C5D4361	FASTA	280	31,610
	10 20 30 40 50 60 MPLLTQYNEE EYEQYCLVAS LDNVRNLSTV LKAIHFREHA TCFATKNGIK VTVENAKCVQ 70 80 90 100 110 120 ANAFIQADVF QEFVIQEESV TFRINLTILL DCLSIFGSSP TPGTLTALRM CYQGYGHPLM 130 140 150 160 170 180 LFLEEGGVVT VCKITTQEPE ETLDFDFCST NVMNKIILQS EGLREAFSEL DMTGDVLQIT 190 200 210 220 230 240 VSPDKPYFRL STFGNAGNSH LDYPKDSDLV EAFHCDKTQV NRYKLSLLKP STKALALSCK 250 260 270 280 VSIRTDNRGF LSLQYMIRNE DGQICFVEYY CCPDEEVPES
	Isoform 2. Checksum: 36207A21BA05BCF8	FASTA	272	30,565
	10 20 30 40 50 60 MPLLTQYNEE EYEQYCLVAS LDNVRNLSTV LKAIHFREHA TCFATKNGIK VTVENAKCVQ 70 80 90 100 110 120 ANAFIQADVF QEFVIQEESV TFRINLTILL DCLSIFGSSP TPGTLTALRM CYQGYGHPLM 130 140 150 160 170 180 LFLEEGGVVT VCKITTQEPE ETLDFDFCST NVMNKIILQS EGLREAFSEL DMTGDVLQIT 190 200 210 220 230 240 VSPDKPYFRL STFGNAGNSH LDYPKDSDLV EAFHCDKTQV NRISDVKYSC KTWLQLPEGV 250 260 270 GYDPLSGLEW TLSERDGEQE VAQWVNVVPV QA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human and mouse homologs of Schizosaccharomyces pombe rad1(+) and Saccharomyces cerevisiae RAD17: linkage to checkpoint control and mammalian meiosis." Freire R., Murguia J.R., Tarsounas M., Lowndes N.F., Moens P.B., Jackson S.P. Genes Dev. 12:2560-2573(1998) [PubMed: 9716408] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]	"A human and mouse homolog of the Schizosaccharomyces pombe rad1+ cell cycle checkpoint control gene." Bluyssen H.A.R., van Os R.I., Naus N.C., Jaspers I., Hoeijmakers J.H.J., de Klein A. Genomics 54:331-337(1998) [PubMed: 9828137] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[3]	"cDNA cloning and gene mapping of human homologs for Schizosaccharomyces pombe rad17, rad1, and hus1 and cloning of homologs from mouse, Caenorhabditis elegans, and Drosophila melanogaster." Dean F.B., Lian L., O'Donnell M. Genomics 54:424-436(1998) [PubMed: 9878245] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"A human homologue of the Schizosaccharomyces pombe rad1+ checkpoint gene encodes an exonuclease." Parker A.E., Van de Weyer I., Laus M.C., Oostveen I., Yon J., Verhasselt P., Luyten W.H.M.L. J. Biol. Chem. 273:18332-18339(1998) [PubMed: 9660799] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[5]	"HRAD1 and MRad1 encode mammalian homologues of the fission yeast rad1+ cell cycle checkpoint control gene." Udell C.M., Lee S.K., Davey S. Nucleic Acids Res. 26:3971-3976(1998) [PubMed: 9705507] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]	"Identification and cloning of Hrad1, a human homolog of the SchizosaCCharomyces pombe checkpoint protein." Hao L., Chang M., Liu J., Chen L.B. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[7]	"Mammalian REC1, encoding a 3'-5' exonuclease, is differentially expressed during meiosis." Shannon M.E., Naureckiene S., Stubbs L., Holloman W.K., Thelen M.P. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[8]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J. Tissue: Bone marrow, Fetal kidney and Heart.
[9]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Limb.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF074718 mRNA. Translation: AAC98094.1. AF073523 mRNA. Translation: AAC95465.1. AF076842 mRNA. Translation: AAC95524.1. AJ004976 mRNA. Translation: CAA06250.1. AF038841 mRNA. Translation: AAC27248.1. AF058394 mRNA. Translation: AAC14139.1. AF084514 mRNA. Translation: AAC35551.1. AK146533 mRNA. Translation: BAE27240.1. AK148098 mRNA. Translation: BAE28343.1. AK150466 mRNA. Translation: BAE29583.1. AK168588 mRNA. Translation: BAE40457.1. BC048693 mRNA. Translation: AAH48693.1.
IPI	IPI00316229. IPI00742429.
RefSeq	NP_035362.2.
UniGene	Mm.38376
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9QWZ1.
Proteomic databases
PRIDE	Q9QWZ1.
Genome annotation databases
Ensembl	ENSMUST00000022856; ENSMUSP00000022856; ENSMUSG00000022248; Mus musculus. [Genome view] ENSMUST00000100775; ENSMUSP00000098338; ENSMUSG00000022248; Mus musculus. [Genome view]
GeneID	19355.
KEGG	mmu:19355.
UCSC	uc007vgh.1. mouse.
Organism-specific databases
CTD	19355.
MGI	MGI:1316678. Rad1.
Phylogenomic databases
HOGENOM	Q9QWZ1.
HOVERGEN	Q9QWZ1.
OMA	YYANTDL.
Enzyme and pathway databases
BRENDA	3.1.11.2. 244.
Gene expression databases
ArrayExpress	Q9QWZ1.
Bgee	Q9QWZ1.
CleanEx	MM_RAD1.
Genevestigator	Q9QWZ1.
GermOnline	ENSMUSG00000022248. Mus musculus.
Family and domain databases
InterPro	IPR003021. Rad1_Rec1. IPR003011. Rad1_repair. [Graphical view]
PANTHER	PTHR10870. Rad1_Rec1. 1 hit.
Pfam	PF02144. Rad1. 1 hit. [Graphical view]
PRINTS	PR01245. RAD1REC1. PR01246. RAD1REPAIR.
ProtoNet	Search...
Other Resources
NextBio	296395.
SOURCE	Search...

Entry information

Entry name

RAD1_MOUSE

Accession

Primary (citable) accession number: Q9QWZ1
Secondary accession number(s): O70452 , O88391, Q3TGU1, Q3UG66, Q9QWZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)