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Protein

ATR-interacting protein

Gene

Atrip

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

Functioni

Required for checkpoint signaling after DNA damage. Required for ATR expression, possibly by stabilizing the protein (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiR-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-6783310. Fanconi Anemia Pathway.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-69473. G2/M DNA damage checkpoint.

Names & Taxonomyi

Protein namesi
Recommended name:
ATR-interacting protein
Alternative name(s):
ATM and Rad3-related-interacting protein
Gene namesi
Name:Atrip
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1925349. Atrip.

Subcellular locationi

  • Nucleus By similarity

  • Note: Redistributes to discrete nuclear foci upon DNA damage. Interacts with CEP164 (via N-terminus) (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 785785ATR-interacting proteinPRO_0000064742Add
BLAST

Post-translational modificationi

Phosphorylated by ATR.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BMG1.
MaxQBiQ8BMG1.
PaxDbiQ8BMG1.
PRIDEiQ8BMG1.

PTM databases

iPTMnetiQ8BMG1.
PhosphoSiteiQ8BMG1.

Expressioni

Gene expression databases

BgeeiQ8BMG1.
CleanExiMM_6620401K05RIK.
ExpressionAtlasiQ8BMG1. baseline and differential.
GenevisibleiQ8BMG1. MM.

Interactioni

Subunit structurei

Heterodimer with ATR. The heterodimer binds the RPA complex and is then recruited to single-stranded DNA. Interacts with CINP (By similarity). Interacts with ATR.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AtrQ9JKK82EBI-5235246,EBI-1202426

GO - Molecular functioni

Protein-protein interaction databases

BioGridi231691. 1 interaction.
IntActiQ8BMG1. 2 interactions.
STRINGi10090.ENSMUSP00000044831.

Structurei

3D structure databases

ProteinModelPortaliQ8BMG1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni118 – 15639Interaction with CINPBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili108 – 209102Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi763 – 7708EEXXXDL motif

Domaini

The EEXXXDDL motif is required for the interaction with catalytic subunit PRKDC and its recruitment to sites of DNA damage.By similarity

Sequence similaritiesi

Belongs to the ATRIP family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IHIV. Eukaryota.
ENOG41107QS. LUCA.
GeneTreeiENSGT00390000012850.
HOGENOMiHOG000273897.
HOVERGENiHBG050618.
InParanoidiQ8BMG1.
KOiK10905.
OMAiGSNCQCN.
TreeFamiTF324417.

Family and domain databases

InterProiIPR033349. ATRIP.
[Graphical view]
PANTHERiPTHR28594. PTHR28594. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8BMG1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGTPAPNSH RKQSGGLEPF PGLSRSIENP PSKRARSFSE TTVPDPEDPF
60 70 80 90 100
GEHAEFTADD LEELDILASQ ALSQCPVAPR NLSSAHKVRR LDGLPNSPIR
110 120 130 140 150
KSREDIPVKD NFELEVLQIQ YKELKEKLKA MEEEILIKNG EIKILRDSLR
160 170 180 190 200
QTESVLEEQK RSHFLLEQEK TQALSEKEKE FSRKLQSLQS ELQFKDAEMN
210 220 230 240 250
ELRTKSQSNG RTNKPAAPSV SHVSPRKGSS VVLKSEACSP HVGKTTFPTK
260 270 280 290 300
ESFSANTPLF HPCQTEAGHR FLVGQEVSDN KNHSLGGSLM KQDVQQRILA
310 320 330 340 350
DGWMQRKDAQ GSILINLLLK QPLVPGSSLG LCHLLSSCPE VPTGTLLQPP
360 370 380 390 400
GLSTLPGTSG LRTISSSDGP FSPSALREAQ NLAFTGLNLV ARTESSHDGD
410 420 430 440 450
MAGRRVFPLH QLPGAVHLLP LVQFFVGLHC QALQDLAPAK KSGVPGDSAT
460 470 480 490 500
HTSCMSSGVE ASPEDSIHGL ESFSVASLSV LQNLVCHSGA VVCLLLSGMG
510 520 530 540 550
TEAAAREGNL VQTCADTTSA SREDAHDQDQ HPLLKMLLQL MASSSAASGH
560 570 580 590 600
FQASVLGLCL KVLVKLAENA SSDLLPRFSC VFPVLPQCLG SALPLPCVLL
610 620 630 640 650
AVELLSVLLD HDSLAWQLCS HPEGCLLLRL YMYITSRPDR TASETQWLQL
660 670 680 690 700
EQEVVWLLAK LSVQSPAPAG IGSDCHCNVE AVRALTVMLH RQWLTVRRAG
710 720 730 740 750
GPRTHQQKQT IRCLRDTVLL LHSLSQKDKL FTVHCVEVLH QYDQVMPGVS
760 770 780
MLIRALPDVT DCEEAALDDL CAAETDLEDS EMDCN
Length:785
Mass (Da):85,548
Last modified:July 27, 2011 - v2
Checksum:i59D782B5CB3D1F7B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti408 – 4081P → A in BAC27324 (PubMed:16141072).Curated
Sequence conflicti462 – 4621S → R in BAC27324 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031257 mRNA. Translation: BAC27324.1.
AC174646 Genomic DNA. No translation available.
CCDSiCCDS23545.1.
RefSeqiNP_766362.2. NM_172774.3.
UniGeneiMm.100622.

Genome annotation databases

EnsembliENSMUST00000045011; ENSMUSP00000044831; ENSMUSG00000025646.
GeneIDi235610.
KEGGimmu:235610.
UCSCiuc009rru.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031257 mRNA. Translation: BAC27324.1.
AC174646 Genomic DNA. No translation available.
CCDSiCCDS23545.1.
RefSeqiNP_766362.2. NM_172774.3.
UniGeneiMm.100622.

3D structure databases

ProteinModelPortaliQ8BMG1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231691. 1 interaction.
IntActiQ8BMG1. 2 interactions.
STRINGi10090.ENSMUSP00000044831.

PTM databases

iPTMnetiQ8BMG1.
PhosphoSiteiQ8BMG1.

Proteomic databases

EPDiQ8BMG1.
MaxQBiQ8BMG1.
PaxDbiQ8BMG1.
PRIDEiQ8BMG1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045011; ENSMUSP00000044831; ENSMUSG00000025646.
GeneIDi235610.
KEGGimmu:235610.
UCSCiuc009rru.2. mouse.

Organism-specific databases

CTDi84126.
MGIiMGI:1925349. Atrip.

Phylogenomic databases

eggNOGiENOG410IHIV. Eukaryota.
ENOG41107QS. LUCA.
GeneTreeiENSGT00390000012850.
HOGENOMiHOG000273897.
HOVERGENiHBG050618.
InParanoidiQ8BMG1.
KOiK10905.
OMAiGSNCQCN.
TreeFamiTF324417.

Enzyme and pathway databases

ReactomeiR-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-6783310. Fanconi Anemia Pathway.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-69473. G2/M DNA damage checkpoint.

Miscellaneous databases

PROiQ8BMG1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BMG1.
CleanExiMM_6620401K05RIK.
ExpressionAtlasiQ8BMG1. baseline and differential.
GenevisibleiQ8BMG1. MM.

Family and domain databases

InterProiIPR033349. ATRIP.
[Graphical view]
PANTHERiPTHR28594. PTHR28594. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: C57BL/6J.
    Tissue: Forelimb.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.
  4. "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 ATR.

Entry informationi

Entry nameiATRIP_MOUSE
AccessioniPrimary (citable) accession number: Q8BMG1
Secondary accession number(s): E9QLS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 98 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.