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Q9QWZ1

- RAD1_MOUSE

UniProt

Q9QWZ1 - RAD1_MOUSE

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Protein

Cell cycle checkpoint protein RAD1

Gene
Rad1, Rec1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

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. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase. Isoform 1 possesses 3'->5' double stranded DNA exonuclease activity By similarity.

Catalytic activityi

Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.

GO - Molecular functioni

  1. 3'-5' exonuclease activity Source: UniProtKB
  2. exodeoxyribonuclease III activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular response to ionizing radiation Source: Ensembl
  2. DNA damage checkpoint Source: Ensembl
  3. DNA repair Source: UniProtKB-KW
  4. nucleic acid phosphodiester bond hydrolysis Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair

Names & Taxonomyi

Protein namesi
Recommended name:
Cell cycle checkpoint protein RAD1 (EC:3.1.11.2)
Short name:
mRAD1
Alternative name(s):
DNA repair exonuclease rad1 homolog
Rad1-like DNA damage checkpoint protein
Gene namesi
Name:Rad1
Synonyms:Rec1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1316678. Rad1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 280280Cell cycle checkpoint protein RAD1PRO_0000225006Add
BLAST

Proteomic databases

PRIDEiQ9QWZ1.

PTM databases

PhosphoSiteiQ9QWZ1.

Expressioni

Tissue specificityi

Expressed in testis, uterus, bladder, spleen, ovaries, lung, brain and muscle (at protein level). Expressed in brain, testis, kidney, heart, liver and lung.3 Publications

Gene expression databases

ArrayExpressiQ9QWZ1.
BgeeiQ9QWZ1.
CleanExiMM_RAD1.
GenevestigatoriQ9QWZ1.

Interactioni

Subunit structurei

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. Interacts with DNAJC7 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ9QWZ1.
SMRiQ9QWZ1. Positions 15-275.

Family & Domainsi

Sequence similaritiesi

Belongs to the rad1 family.

Phylogenomic databases

eggNOGiNOG324428.
GeneTreeiENSGT00500000044913.
HOGENOMiHOG000008015.
HOVERGENiHBG053058.
InParanoidiQ9QWZ1.
KOiK02830.
OMAiCKVSVRT.
OrthoDBiEOG7N0C4P.
PhylomeDBiQ9QWZ1.
TreeFamiTF101211.

Family and domain databases

InterProiIPR003011. Cell_cycle_checkpoint_Rad1.
IPR003021. Rad1_Rec1_Rad17.
[Graphical view]
PANTHERiPTHR10870. PTHR10870. 1 hit.
PfamiPF02144. Rad1. 1 hit.
[Graphical view]
PRINTSiPR01245. RAD1REC1.
PR01246. RAD1REPAIR.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9QWZ1-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MPLLTQYNEE EYEQYCLVAS LDNVRNLSTV LKAIHFREHA TCFATKNGIK    50
VTVENAKCVQ ANAFIQADVF QEFVIQEESV TFRINLTILL DCLSIFGSSP 100
TPGTLTALRM CYQGYGHPLM LFLEEGGVVT VCKITTQEPE ETLDFDFCST 150
NVMNKIILQS EGLREAFSEL DMTGDVLQIT VSPDKPYFRL STFGNAGNSH 200
LDYPKDSDLV EAFHCDKTQV NRYKLSLLKP STKALALSCK VSIRTDNRGF 250
LSLQYMIRNE DGQICFVEYY CCPDEEVPES 280
Length:280
Mass (Da):31,610
Last modified:May 1, 2000 - v1
Checksum:iF9D6ED292C5D4361
GO
Isoform 2 (identifier: Q9QWZ1-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:272
Mass (Da):30,565
Checksum:i36207A21BA05BCF8
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei223 – 28058YKLSL…EVPES → ISDVKYSCKTWLQLPEGVGY DPLSGLEWTLSERDGEQEVA QWVNVVPVQA in isoform 2. VSP_017337Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281S → F1 Publication
Sequence conflicti28 – 281S → F1 Publication
Sequence conflicti28 – 281S → F1 Publication
Sequence conflicti28 – 281S → F1 Publication
Sequence conflicti71 – 711Q → E in BAE28343. 1 Publication
Sequence conflicti118 – 1181P → T in BAE40457. 1 Publication
Sequence conflicti198 – 1981N → S in AAC95465. 1 Publication
Sequence conflicti216 – 2161D → N in AAC27248. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS27379.1. [Q9QWZ1-1]
CCDS70618.1. [Q9QWZ1-2]
RefSeqiNP_001276376.1. NM_001289447.1. [Q9QWZ1-1]
NP_001276377.1. NM_001289448.1. [Q9QWZ1-2]
NP_035362.2. NM_011232.3. [Q9QWZ1-1]
XP_006520102.1. XM_006520039.1. [Q9QWZ1-1]
UniGeneiMm.38376.

Genome annotation databases

EnsembliENSMUST00000022856; ENSMUSP00000022856; ENSMUSG00000022248. [Q9QWZ1-1]
ENSMUST00000100775; ENSMUSP00000098338; ENSMUSG00000022248. [Q9QWZ1-2]
GeneIDi19355.
KEGGimmu:19355.
UCSCiuc007vgh.1. mouse. [Q9QWZ1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS27379.1. [Q9QWZ1-1 ]
CCDS70618.1. [Q9QWZ1-2 ]
RefSeqi NP_001276376.1. NM_001289447.1. [Q9QWZ1-1 ]
NP_001276377.1. NM_001289448.1. [Q9QWZ1-2 ]
NP_035362.2. NM_011232.3. [Q9QWZ1-1 ]
XP_006520102.1. XM_006520039.1. [Q9QWZ1-1 ]
UniGenei Mm.38376.

3D structure databases

ProteinModelPortali Q9QWZ1.
SMRi Q9QWZ1. Positions 15-275.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9QWZ1.

Proteomic databases

PRIDEi Q9QWZ1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022856 ; ENSMUSP00000022856 ; ENSMUSG00000022248 . [Q9QWZ1-1 ]
ENSMUST00000100775 ; ENSMUSP00000098338 ; ENSMUSG00000022248 . [Q9QWZ1-2 ]
GeneIDi 19355.
KEGGi mmu:19355.
UCSCi uc007vgh.1. mouse. [Q9QWZ1-1 ]

Organism-specific databases

CTDi 5810.
MGIi MGI:1316678. Rad1.

Phylogenomic databases

eggNOGi NOG324428.
GeneTreei ENSGT00500000044913.
HOGENOMi HOG000008015.
HOVERGENi HBG053058.
InParanoidi Q9QWZ1.
KOi K02830.
OMAi CKVSVRT.
OrthoDBi EOG7N0C4P.
PhylomeDBi Q9QWZ1.
TreeFami TF101211.

Miscellaneous databases

NextBioi 296395.
PROi Q9QWZ1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9QWZ1.
Bgeei Q9QWZ1.
CleanExi MM_RAD1.
Genevestigatori Q9QWZ1.

Family and domain databases

InterProi IPR003011. Cell_cycle_checkpoint_Rad1.
IPR003021. Rad1_Rec1_Rad17.
[Graphical view ]
PANTHERi PTHR10870. PTHR10870. 1 hit.
Pfami PF02144. Rad1. 1 hit.
[Graphical view ]
PRINTSi PR01245. RAD1REC1.
PR01246. RAD1REPAIR.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Limb.

Entry informationi

Entry nameiRAD1_MOUSE
AccessioniPrimary (citable) accession number: Q9QWZ1
Secondary accession number(s): O70452
, O88391, Q3TGU1, Q3UG66, Q9QWZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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