Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9JKK8

- ATR_MOUSE

UniProt

Q9JKK8 - ATR_MOUSE

Protein

Serine/threonine-protein kinase ATR

Gene

Atr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (29 Mar 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates BRCA1, CHEK1, MCM2, RAD17, RPA2, SMC1 and p53/TP53, which collectively inhibit DNA replication and mitosis and promote DNA repair, recombination and apoptosis. Phosphorylates Ser-139 of histone variant H2AX/H2AFX at sites of DNA damage, thereby regulating DNA damage response mechanism. Required for FANCD2 ubiquitination. Critical for maintenance of fragile site stability and efficient regulation of centrosome duplication By similarity. Essential for preventing the occurrence of DNA damage during early embryogenesis.By similarity4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Manganese.By similarity

    Enzyme regulationi

    Activated by DNA, and slightly by ATRIP. Inhibited by caffeine, wortmannin and LY294002 By similarity.By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. protein kinase activity Source: MGI
    5. protein serine/threonine kinase activity Source: Reactome

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: MGI
    2. DNA damage checkpoint Source: MGI
    3. DNA repair Source: MGI
    4. protein phosphorylation Source: MGI
    5. regulation of protein binding Source: MGI

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    ATP-binding, DNA-binding, Manganese, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198626. Meiotic synapsis.
    REACT_75800. Meiotic Synapsis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase ATR (EC:2.7.11.1)
    Alternative name(s):
    Ataxia telangiectasia and Rad3-related protein
    Gene namesi
    Name:Atr
    Synonyms:Kiaa4069
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:108028. Atr.

    Subcellular locationi

    Nucleus By similarity. Chromosome 3 Publications
    Note: Recruited to chromatin during S-phase. Redistributes to discrete nuclear foci upon DNA damage, hypoxia or replication fork stalling By similarity.By similarity

    GO - Cellular componenti

    1. chromosome Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: MGI
    4. PML body Source: UniProtKB
    5. XY body Source: MGI

    Keywords - Cellular componenti

    Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 26352635Serine/threonine-protein kinase ATRPRO_0000088845Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei431 – 4311PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9JKK8.
    PaxDbiQ9JKK8.
    PRIDEiQ9JKK8.

    PTM databases

    PhosphoSiteiQ9JKK8.

    Expressioni

    Tissue specificityi

    Ubiquitous. Expression is highest in testis, where it is restricted to primary spermatocytes. Expression decreases as spermiogenesis proceeds (at protein level).1 Publication

    Gene expression databases

    CleanExiMM_ATR.
    GenevestigatoriQ9JKK8.

    Interactioni

    Subunit structurei

    Forms a heterodimer with ATRIP. Binds to DNA, and to UV-damaged DNA with higher affinity. Interacts with RAD17, MSH2 and HDAC2. Present in a complex containing ATRIP and RPA-coated single-stranded DNA. Present in a complex containing CHD4 and HDAC2. Interacts with EEF1E1. This interaction is enhanced by UV irradiation. Interacts with CLSPN and CEP164 By similarity. Interacts with TELO2 AND TTI1 By similarity. Interacts with ATRIP.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AtripQ8BMG12EBI-1202426,EBI-5235246

    Protein-protein interaction databases

    IntActiQ9JKK8. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JKK8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati799 – 83537HEAT 1Add
    BLAST
    Repeati1329 – 136537HEAT 2Add
    BLAST
    Domaini1634 – 2179546FATPROSITE-ProRule annotationAdd
    BLAST
    Domaini2313 – 2558246PI3K/PI4KPROSITE-ProRule annotationAdd
    BLAST
    Domaini2603 – 263533FATCPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PI3/PI4-kinase family. ATM subfamily.Curated
    Contains 1 FAT domain.PROSITE-ProRule annotation
    Contains 1 FATC domain.PROSITE-ProRule annotation
    Contains 2 HEAT repeats.PROSITE-ProRule annotation
    Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5032.
    HOVERGENiHBG050619.
    InParanoidiQ3TBS8.
    PhylomeDBiQ9JKK8.

    Family and domain databases

    Gene3Di1.10.1070.11. 2 hits.
    1.25.10.10. 4 hits.
    1.25.40.10. 2 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR003152. FATC.
    IPR021133. HEAT_type_2.
    IPR011009. Kinase-like_dom.
    IPR000403. PI3/4_kinase_cat_dom.
    IPR018936. PI3/4_kinase_CS.
    IPR003151. PIK-rel_kinase_FAT.
    IPR014009. PIK_FAT.
    IPR011990. TPR-like_helical.
    IPR012993. UME.
    [Graphical view]
    PfamiPF02259. FAT. 1 hit.
    PF02260. FATC. 1 hit.
    PF00454. PI3_PI4_kinase. 1 hit.
    PF08064. UME. 1 hit.
    [Graphical view]
    SMARTiSM00146. PI3Kc. 1 hit.
    SM00802. UME. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 5 hits.
    SSF56112. SSF56112. 2 hits.
    PROSITEiPS51189. FAT. 1 hit.
    PS51190. FATC. 1 hit.
    PS50077. HEAT_REPEAT. 1 hit.
    PS00916. PI3_4_KINASE_2. 1 hit.
    PS50290. PI3_4_KINASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9JKK8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDHGLELAS MIPALRELGS ATPEEYNTVV QKPRQILCQF IDRILTDVNV     50
    VALELVKKTD AQPTSVMLLD FIQHIMKSSP LMFVNVNGSQ GQNEAKDSCI 100
    EFSHWIITRL LRIAATPSCH MLHKKICEVI CSLLFLFKSK NPAIFGVLTR 150
    ELLYLFEDLI YLHKRNAVGE VMEWPVVVSR FLSRLDEHMG CLQPAPLQFM 200
    NVQNVEFIEV TLLMVLIHIV PTVFFRRQEL LLWQIGCALL EHGSPKIRSL 250
    AISLLTELFE LGGLPAQPAS TFFSLFLELL QHLVGMDADQ LKLYEEPLSK 300
    LLKTLFPFEA EAYRNIEPVY LNVLLEKLSV MFEDRVLMRL KSDLLKAALC 350
    HLLQYFLTFV PAGYESALQV RKVYVTNICR ALVDALGVQK HVGYLLGPFY 400
    AALKMESKEI IERIQCQAQQ ENLSGNNDEV SPKRRKLSSS LSSYKKPSRQ 450
    PEEIIHVDMD KKSILWNVLK QKAESLQISL ECGTLKNSVA EALEGITVVL 500
    QLTALCTVHC SHQDMDGHNV KDHQHKYKKK PPVVVTWMSL DFYTKVLKSC 550
    RSLLESVQKL ELELVIDSMV RICDALMYMQ VKSSFKDHVL EELCGMLSLP 600
    WIYSYSDDNS LKMTTFATNL LPLSQRVWDS YSPQAQSKCV FLLTLFPRRI 650
    FLEWRTAVYN WALKSSHEVI RASCVKGFFI LLHQQNSCNQ IPKMLVDRVK 700
    DDSDMVKKEF ASVLGQLVCT LHGMFYLSSS VEPCFEHMDL FSKNLKATSQ 750
    HECSSSQVKA STCKPFLFLL TKNTPSPVKL AFIDNLHHLC KHLDFQEDER 800
    EVKAVLGTLL NLMEDPDKDV RIAFSGNIKY ILESLNSEDG FVKELFVLRM 850
    KEAYTHAQIA RNNELKDTLI LTTGDIGRAA KGDLIPFALL HLLHCLLSKS 900
    ASVSGAAYTE IRALVAAKSV KLQNFFSQYK KPICQFLVES LHSSQMTALP 950
    SAPCQSSEIR KQDVAHHREM ALNTLSEIAN VFDFPDLNRF LTRTLQVLLP 1000
    DLAAKASPAA SALIRTLGKQ LNVSRREILI NNFKYIFSHL VCSCSKDELE 1050
    RALHYLKNET EIELGSLLRQ DFQGLHNELL LRIGEHYQQV FNGLSILASF 1100
    ASSDDPYQGP RDITSPELMA DYLQPKLLGI LAFFNMQLLS SSVGIEDKKM 1150
    ALTSLMSLMK LMGPKHVSSV RVKMMTTLRT GLRFKDDFPE LCCRAWDCFV 1200
    RCLDHAYLGP LLSHVIVALL PLIHMQPKET AAIFHYLIIE NRDAVQDFLH 1250
    EIYFLPDHPE LEKIKAVLQE YRKETSETTD LQTTLQLSMK AIQHENVDVR 1300
    IHALTSLKET LYKNQEKLIK YATDSETVEP VISQLVTVIL KGCQDANSQA 1350
    RLLCGECLGE LGAIDPGRLD FSTTETQGKD FTFVTGVEDL SFAYGLLMEL 1400
    TRAYLAYADN SRAQDSAAYA IQELLSIYDC REMQSNGPGY QLWKRFPEHV 1450
    REILEPHLNT RYKSSQKSTD WSGVTKPIYL SKLGNNFAEW SSSWAGYLIT 1500
    KVRDNLASKI FTCCSIMMKH DFKVTIYLLP HILVYVLLGC NQEDQQEVYA 1550
    EIMAVLKHDE QHAISTQDSA SDLCQLSTQT VFSVLDHLTQ WARHKFQALN 1600
    AEKLAQNKPK GVSNVNFEDY QSVTRFLDLI PQDTLAVASF RSKAYTRAVM 1650
    HFESFITEKK QNIQKHLGFL QKLYAAMHEP DGVAGVSAIR KAEPSLKEQI 1700
    LEHESIGLLR DATACYDRAI QLEPDQIIHY HGVVKSMLGL GQLSTVITQV 1750
    NGVHANRSEW TDELNTYRVE AAWKLSQWDL VENYLAADGK STTWSVRLGQ 1800
    LLLSAKKRDT TTFYDTLKLV RAEQIVPLSA ASFERGSYQR GYEFIVRLHM 1850
    LCELEHSLKP LFRKSPGDSC NEDSLNWGAR LEMTQNSYRA KEPILALRRA 1900
    LLSLNKRPDY NEMVGECWLQ SARVARKAGH HQTAYNALLN AGESRLAELY 1950
    VERAKWLWSK GDVHQALIVL QKGVELCFPE NKSPSESKHM LIHGRATLLV 2000
    GRFMEETANF ESNAVMKKYK DVTLFLPEWE DGHFYLAKYY DKLMPMVTDN 2050
    KMEKQGDLIR YIVLHFGRSL QYGNQFIYQS MPRMLSLWLD FGAKAYEWEK 2100
    GGRSDRLQMR NDLAKINSVL TEHTNRLAPY QFLTAFSQLI SRICHSHDEV 2150
    FVVLMEIIAK VFLAYPQQAM WMMTAVSKSS YPMRVNRCKE ILTKAIHMKK 2200
    SLEKFVGDAT RLTDKLLELC NKSVDGSNST LSMSTHFKML KRLVEDPTFS 2250
    EILIPLQSVM IPTLPSVLGA HANHDPFPGH WAYLAGFDDV VEILSSLQKP 2300
    KKISLKGSDG KFYIMMCKPK DDLRKDCRLM EFNSLINKSL RKDAESRRRE 2350
    LHIRTYAVIP LNDECGIIEW VNNTAGLRPI LTKIYKEKGV YMTGKELRQC 2400
    MLPKSAALSE KLKVFQELLL PRHPPVFHEW FLRTFPDPTS WYSSRSAYCR 2450
    STAVMSMVGY ILGLGDRHGE NILFDSFTGE CVHVDFNCLF NKGETFEVPE 2500
    IVPFRLTHNM VNGMGPMGTE GLFRRACEVT LRLMRDQREP LMSVLKTFLH 2550
    DPLVEGSKPV KGHSKAPLNE TGEVVNEKAK THVLDIEQRL QGVIKTRNRV 2600
    TGLPLSIEGH VHYLIQEATD ENLLCQMYLG WTPYM 2635
    Length:2,635
    Mass (Da):300,224
    Last modified:March 29, 2005 - v2
    Checksum:iC126413D15ACB8DC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 191G → A in BAE24154. (PubMed:16141072)Curated
    Sequence conflicti19 – 191G → A in BAE34182. (PubMed:16141072)Curated
    Sequence conflicti19 – 191G → A in BAE42229. (PubMed:16141072)Curated
    Sequence conflicti2208 – 22081D → E in BAE37964. (PubMed:16141072)Curated
    Sequence conflicti2347 – 23471R → C in BAE37964. (PubMed:16141072)Curated
    Sequence conflicti2556 – 25561G → W in BAE21043. (PubMed:16141072)Curated
    Sequence conflicti2556 – 25561G → W in BAD90361. (PubMed:15449545)Curated
    Sequence conflicti2563 – 25631H → R in BAE21043. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC091531 Genomic DNA. No translation available.
    AC121499 Genomic DNA. No translation available.
    AK132223 mRNA. Translation: BAE21043.1.
    AK139834 mRNA. Translation: BAE24154.1.
    AK157754 mRNA. Translation: BAE34182.1.
    AK164916 mRNA. Translation: BAE37964.1.
    AK171072 mRNA. Translation: BAE42229.1.
    AK220176 mRNA. Translation: BAD90361.1.
    AF236887 mRNA. Translation: AAF61728.1.
    UniGeneiMm.212462.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC091531 Genomic DNA. No translation available.
    AC121499 Genomic DNA. No translation available.
    AK132223 mRNA. Translation: BAE21043.1 .
    AK139834 mRNA. Translation: BAE24154.1 .
    AK157754 mRNA. Translation: BAE34182.1 .
    AK164916 mRNA. Translation: BAE37964.1 .
    AK171072 mRNA. Translation: BAE42229.1 .
    AK220176 mRNA. Translation: BAD90361.1 .
    AF236887 mRNA. Translation: AAF61728.1 .
    UniGenei Mm.212462.

    3D structure databases

    ProteinModelPortali Q9JKK8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9JKK8. 2 interactions.

    PTM databases

    PhosphoSitei Q9JKK8.

    Proteomic databases

    MaxQBi Q9JKK8.
    PaxDbi Q9JKK8.
    PRIDEi Q9JKK8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:108028. Atr.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG5032.
    HOVERGENi HBG050619.
    InParanoidi Q3TBS8.
    PhylomeDBi Q9JKK8.

    Enzyme and pathway databases

    Reactomei REACT_198626. Meiotic synapsis.
    REACT_75800. Meiotic Synapsis.

    Miscellaneous databases

    ChiTaRSi ATR. mouse.
    PROi Q9JKK8.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_ATR.
    Genevestigatori Q9JKK8.

    Family and domain databases

    Gene3Di 1.10.1070.11. 2 hits.
    1.25.10.10. 4 hits.
    1.25.40.10. 2 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR003152. FATC.
    IPR021133. HEAT_type_2.
    IPR011009. Kinase-like_dom.
    IPR000403. PI3/4_kinase_cat_dom.
    IPR018936. PI3/4_kinase_CS.
    IPR003151. PIK-rel_kinase_FAT.
    IPR014009. PIK_FAT.
    IPR011990. TPR-like_helical.
    IPR012993. UME.
    [Graphical view ]
    Pfami PF02259. FAT. 1 hit.
    PF02260. FATC. 1 hit.
    PF00454. PI3_PI4_kinase. 1 hit.
    PF08064. UME. 1 hit.
    [Graphical view ]
    SMARTi SM00146. PI3Kc. 1 hit.
    SM00802. UME. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 5 hits.
    SSF56112. SSF56112. 2 hits.
    PROSITEi PS51189. FAT. 1 hit.
    PS51190. FATC. 1 hit.
    PS50077. HEAT_REPEAT. 1 hit.
    PS00916. PI3_4_KINASE_2. 1 hit.
    PS50290. PI3_4_KINASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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 1-1134 AND 1578-2635.
      Strain: C57BL/6J and NOD.
      Tissue: Brain, Dendritic cell, Egg, Embryo and Lung.
    3. "Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
      DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1684-2635.
      Tissue: Embryonic intestine.
    4. "Targeted disruption of the cell-cycle checkpoint gene ATR leads to early embryonic lethality in mice."
      de Klein A., Muijtjens M., van Os R., Verhoeven Y., Smit B., Carr A.M., Lehmann A.R., Hoeijmakers J.H.J.
      Curr. Biol. 10:479-482(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2362-2635, FUNCTION.
    5. "The Atr and Atm protein kinases associate with different sites along meiotically pairing chromosomes."
      Keegan K.S., Holtzman D.A., Plug A.W., Christenson E.R., Brainerd E.E., Flaggs G., Bentley N.J., Taylor E.M., Meyn M.S., Moss S.B., Carr A.M., Ashley T., Hoekstra M.F.
      Genes Dev. 10:2423-2437(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "ATR disruption leads to chromosomal fragmentation and early embryonic lethality."
      Brown E.J., Baltimore D.
      Genes Dev. 14:397-402(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Essential and dispensable roles of ATR in cell cycle arrest and genome maintenance."
      Brown E.J., Baltimore D.
      Genes Dev. 17:615-628(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes."
      Takai H., Xie Y., de Lange T., Pavletich N.P.
      Genes Dev. 24:2019-2030(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATRIP.
    9. "HORMAD2 is essential for synapsis surveillance during meiotic prophase via the recruitment of ATR activity."
      Kogo H., Tsutsumi M., Inagaki H., Ohye T., Kiyonari H., Kurahashi H.
      Genes Cells 17:897-912(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. "Meiotic DNA double-strand breaks and chromosome asynapsis in mice are monitored by distinct HORMAD2-independent and -dependent mechanisms."
      Wojtasz L., Cloutier J.M., Baumann M., Daniel K., Varga J., Fu J., Anastassiadis K., Stewart A.F., Remenyi A., Turner J.M., Toth A.
      Genes Dev. 26:958-973(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiATR_MOUSE
    AccessioniPrimary (citable) accession number: Q9JKK8
    Secondary accession number(s): Q3TBS8
    , Q3TNX3, Q3TZM6, Q3UT26, Q3V1V6, Q571L3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3