Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9JKK8

- ATR_MOUSE

UniProt

Q9JKK8 - ATR_MOUSE

(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)

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

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

Mn2+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 kinase activity Source: MGI
  4. 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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiQ9JKK8.
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_dom.
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

        10         20         30         40         50
MGDHGLELAS MIPALRELGS ATPEEYNTVV QKPRQILCQF IDRILTDVNV
60 70 80 90 100
VALELVKKTD AQPTSVMLLD FIQHIMKSSP LMFVNVNGSQ GQNEAKDSCI
110 120 130 140 150
EFSHWIITRL LRIAATPSCH MLHKKICEVI CSLLFLFKSK NPAIFGVLTR
160 170 180 190 200
ELLYLFEDLI YLHKRNAVGE VMEWPVVVSR FLSRLDEHMG CLQPAPLQFM
210 220 230 240 250
NVQNVEFIEV TLLMVLIHIV PTVFFRRQEL LLWQIGCALL EHGSPKIRSL
260 270 280 290 300
AISLLTELFE LGGLPAQPAS TFFSLFLELL QHLVGMDADQ LKLYEEPLSK
310 320 330 340 350
LLKTLFPFEA EAYRNIEPVY LNVLLEKLSV MFEDRVLMRL KSDLLKAALC
360 370 380 390 400
HLLQYFLTFV PAGYESALQV RKVYVTNICR ALVDALGVQK HVGYLLGPFY
410 420 430 440 450
AALKMESKEI IERIQCQAQQ ENLSGNNDEV SPKRRKLSSS LSSYKKPSRQ
460 470 480 490 500
PEEIIHVDMD KKSILWNVLK QKAESLQISL ECGTLKNSVA EALEGITVVL
510 520 530 540 550
QLTALCTVHC SHQDMDGHNV KDHQHKYKKK PPVVVTWMSL DFYTKVLKSC
560 570 580 590 600
RSLLESVQKL ELELVIDSMV RICDALMYMQ VKSSFKDHVL EELCGMLSLP
610 620 630 640 650
WIYSYSDDNS LKMTTFATNL LPLSQRVWDS YSPQAQSKCV FLLTLFPRRI
660 670 680 690 700
FLEWRTAVYN WALKSSHEVI RASCVKGFFI LLHQQNSCNQ IPKMLVDRVK
710 720 730 740 750
DDSDMVKKEF ASVLGQLVCT LHGMFYLSSS VEPCFEHMDL FSKNLKATSQ
760 770 780 790 800
HECSSSQVKA STCKPFLFLL TKNTPSPVKL AFIDNLHHLC KHLDFQEDER
810 820 830 840 850
EVKAVLGTLL NLMEDPDKDV RIAFSGNIKY ILESLNSEDG FVKELFVLRM
860 870 880 890 900
KEAYTHAQIA RNNELKDTLI LTTGDIGRAA KGDLIPFALL HLLHCLLSKS
910 920 930 940 950
ASVSGAAYTE IRALVAAKSV KLQNFFSQYK KPICQFLVES LHSSQMTALP
960 970 980 990 1000
SAPCQSSEIR KQDVAHHREM ALNTLSEIAN VFDFPDLNRF LTRTLQVLLP
1010 1020 1030 1040 1050
DLAAKASPAA SALIRTLGKQ LNVSRREILI NNFKYIFSHL VCSCSKDELE
1060 1070 1080 1090 1100
RALHYLKNET EIELGSLLRQ DFQGLHNELL LRIGEHYQQV FNGLSILASF
1110 1120 1130 1140 1150
ASSDDPYQGP RDITSPELMA DYLQPKLLGI LAFFNMQLLS SSVGIEDKKM
1160 1170 1180 1190 1200
ALTSLMSLMK LMGPKHVSSV RVKMMTTLRT GLRFKDDFPE LCCRAWDCFV
1210 1220 1230 1240 1250
RCLDHAYLGP LLSHVIVALL PLIHMQPKET AAIFHYLIIE NRDAVQDFLH
1260 1270 1280 1290 1300
EIYFLPDHPE LEKIKAVLQE YRKETSETTD LQTTLQLSMK AIQHENVDVR
1310 1320 1330 1340 1350
IHALTSLKET LYKNQEKLIK YATDSETVEP VISQLVTVIL KGCQDANSQA
1360 1370 1380 1390 1400
RLLCGECLGE LGAIDPGRLD FSTTETQGKD FTFVTGVEDL SFAYGLLMEL
1410 1420 1430 1440 1450
TRAYLAYADN SRAQDSAAYA IQELLSIYDC REMQSNGPGY QLWKRFPEHV
1460 1470 1480 1490 1500
REILEPHLNT RYKSSQKSTD WSGVTKPIYL SKLGNNFAEW SSSWAGYLIT
1510 1520 1530 1540 1550
KVRDNLASKI FTCCSIMMKH DFKVTIYLLP HILVYVLLGC NQEDQQEVYA
1560 1570 1580 1590 1600
EIMAVLKHDE QHAISTQDSA SDLCQLSTQT VFSVLDHLTQ WARHKFQALN
1610 1620 1630 1640 1650
AEKLAQNKPK GVSNVNFEDY QSVTRFLDLI PQDTLAVASF RSKAYTRAVM
1660 1670 1680 1690 1700
HFESFITEKK QNIQKHLGFL QKLYAAMHEP DGVAGVSAIR KAEPSLKEQI
1710 1720 1730 1740 1750
LEHESIGLLR DATACYDRAI QLEPDQIIHY HGVVKSMLGL GQLSTVITQV
1760 1770 1780 1790 1800
NGVHANRSEW TDELNTYRVE AAWKLSQWDL VENYLAADGK STTWSVRLGQ
1810 1820 1830 1840 1850
LLLSAKKRDT TTFYDTLKLV RAEQIVPLSA ASFERGSYQR GYEFIVRLHM
1860 1870 1880 1890 1900
LCELEHSLKP LFRKSPGDSC NEDSLNWGAR LEMTQNSYRA KEPILALRRA
1910 1920 1930 1940 1950
LLSLNKRPDY NEMVGECWLQ SARVARKAGH HQTAYNALLN AGESRLAELY
1960 1970 1980 1990 2000
VERAKWLWSK GDVHQALIVL QKGVELCFPE NKSPSESKHM LIHGRATLLV
2010 2020 2030 2040 2050
GRFMEETANF ESNAVMKKYK DVTLFLPEWE DGHFYLAKYY DKLMPMVTDN
2060 2070 2080 2090 2100
KMEKQGDLIR YIVLHFGRSL QYGNQFIYQS MPRMLSLWLD FGAKAYEWEK
2110 2120 2130 2140 2150
GGRSDRLQMR NDLAKINSVL TEHTNRLAPY QFLTAFSQLI SRICHSHDEV
2160 2170 2180 2190 2200
FVVLMEIIAK VFLAYPQQAM WMMTAVSKSS YPMRVNRCKE ILTKAIHMKK
2210 2220 2230 2240 2250
SLEKFVGDAT RLTDKLLELC NKSVDGSNST LSMSTHFKML KRLVEDPTFS
2260 2270 2280 2290 2300
EILIPLQSVM IPTLPSVLGA HANHDPFPGH WAYLAGFDDV VEILSSLQKP
2310 2320 2330 2340 2350
KKISLKGSDG KFYIMMCKPK DDLRKDCRLM EFNSLINKSL RKDAESRRRE
2360 2370 2380 2390 2400
LHIRTYAVIP LNDECGIIEW VNNTAGLRPI LTKIYKEKGV YMTGKELRQC
2410 2420 2430 2440 2450
MLPKSAALSE KLKVFQELLL PRHPPVFHEW FLRTFPDPTS WYSSRSAYCR
2460 2470 2480 2490 2500
STAVMSMVGY ILGLGDRHGE NILFDSFTGE CVHVDFNCLF NKGETFEVPE
2510 2520 2530 2540 2550
IVPFRLTHNM VNGMGPMGTE GLFRRACEVT LRLMRDQREP LMSVLKTFLH
2560 2570 2580 2590 2600
DPLVEGSKPV KGHSKAPLNE TGEVVNEKAK THVLDIEQRL QGVIKTRNRV
2610 2620 2630
TGLPLSIEGH VHYLIQEATD ENLLCQMYLG WTPYM
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 Q9JKK8.
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_dom.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 112 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