ATRIP_HUMAN
ID ATRIP_HUMAN Reviewed; 791 AA.
AC Q8WXE1; A8K6A3; A8K714; B2RCE7; B4DU92; B5MEB7; Q69YK9; Q8NHQ2; Q8WUG7;
AC Q96CL3; Q9HA30;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=ATR-interacting protein;
DE AltName: Full=ATM and Rad3-related-interacting protein;
GN Name=ATRIP; Synonyms=AGS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 147-160 AND
RP 722-733, IDENTIFICATION BY MASS SPECTROMETRY, ALTERNATIVE SPLICING,
RP PHOSPHORYLATION, INTERACTION WITH ATR, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11721054; DOI=10.1126/science.1065521;
RA Cortez D., Guntuku S., Qin J., Elledge S.J.;
RT "ATR and ATRIP: partners in checkpoint signaling.";
RL Science 294:1713-1716(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Endothelial cell, Fetal brain, Placenta, and Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Colon, Lymph, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 134-791 (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH THE RPA COMPLEX.
RX PubMed=12791985; DOI=10.1126/science.1083430;
RA Zou L., Elledge S.J.;
RT "Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes.";
RL Science 300:1542-1548(2003).
RN [8]
RP DOMAIN, AND MUTAGENESIS OF 769-GLU-GLU-770 AND 774-ASP-ASP-775.
RX PubMed=15758953; DOI=10.1038/nature03442;
RA Falck J., Coates J., Jackson S.P.;
RT "Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA
RT damage.";
RL Nature 434:605-611(2005).
RN [9]
RP INTERACTION WITH CEP164, AND SUBCELLULAR LOCATION.
RX PubMed=18283122; DOI=10.1101/gad.1627708;
RA Sivasubramaniam S., Sun X., Pan Y.R., Wang S., Lee E.Y.;
RT "Cep164 is a mediator protein required for the maintenance of genomic
RT stability through modulation of MDC1, RPA, and CHK1.";
RL Genes Dev. 22:587-600(2008).
RN [10]
RP INTERACTION WITH CINP.
RX PubMed=19889979; DOI=10.1073/pnas.0909345106;
RA Lovejoy C.A., Xu X., Bansbach C.E., Glick G.G., Zhao R., Ye F., Sirbu B.M.,
RA Titus L.C., Shyr Y., Cortez D.;
RT "Functional genomic screens identify CINP as a genome maintenance
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19304-19309(2009).
CC -!- FUNCTION: Required for checkpoint signaling after DNA damage. Required
CC for ATR expression, possibly by stabilizing the protein.
CC {ECO:0000269|PubMed:12791985}.
CC -!- SUBUNIT: Interacts with ATR (By similarity). Heterodimer with ATR. The
CC heterodimer binds the RPA complex and is then recruited to single-
CC stranded DNA. Interacts with CEP164 (via N-terminus). Interacts with
CC CINP. {ECO:0000250, ECO:0000269|PubMed:11721054,
CC ECO:0000269|PubMed:12791985, ECO:0000269|PubMed:18283122,
CC ECO:0000269|PubMed:19889979}.
CC -!- INTERACTION:
CC Q8WXE1; Q13535: ATR; NbExp=4; IntAct=EBI-747353, EBI-968983;
CC Q8WXE1; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-747353, EBI-946029;
CC Q8WXE1; Q9BUN5: CCDC28B; NbExp=3; IntAct=EBI-747353, EBI-10299032;
CC Q8WXE1; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-747353, EBI-396137;
CC Q8WXE1; P50750: CDK9; NbExp=3; IntAct=EBI-747353, EBI-1383449;
CC Q8WXE1; Q9BW66: CINP; NbExp=9; IntAct=EBI-747353, EBI-739784;
CC Q8WXE1; Q8NDB6: FAM156A; NbExp=3; IntAct=EBI-747353, EBI-749727;
CC Q8WXE1; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-747353, EBI-739832;
CC Q8WXE1; Q8WXB1: METTL21A; NbExp=3; IntAct=EBI-747353, EBI-8652459;
CC Q8WXE1; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-747353, EBI-10172526;
CC Q8WXE1; P00540: MOS; NbExp=3; IntAct=EBI-747353, EBI-1757866;
CC Q8WXE1; P20592: MX2; NbExp=3; IntAct=EBI-747353, EBI-10200618;
CC Q8WXE1; Q9BRL4: PCTK1; NbExp=3; IntAct=EBI-747353, EBI-10296950;
CC Q8WXE1; O15160: POLR1C; NbExp=3; IntAct=EBI-747353, EBI-1055079;
CC Q8WXE1; P13521: SCG2; NbExp=3; IntAct=EBI-747353, EBI-947132;
CC Q8WXE1; O43597: SPRY2; NbExp=3; IntAct=EBI-747353, EBI-742487;
CC Q8WXE1; Q5VWN6-2: TASOR2; NbExp=3; IntAct=EBI-747353, EBI-10172380;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11721054,
CC ECO:0000269|PubMed:18283122}. Note=Redistributes to discrete nuclear
CC foci upon DNA damage.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8WXE1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WXE1-2; Sequence=VSP_010504;
CC Name=3;
CC IsoId=Q8WXE1-3; Sequence=VSP_010501;
CC Name=4;
CC IsoId=Q8WXE1-5; Sequence=VSP_047011;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11721054}.
CC -!- DOMAIN: The EEXXXDDL motif is required for the interaction with
CC catalytic subunit PRKDC and its recruitment to sites of DNA damage.
CC {ECO:0000269|PubMed:15758953}.
CC -!- PTM: Phosphorylated by ATR. {ECO:0000269|PubMed:11721054}.
CC -!- SIMILARITY: Belongs to the ATRIP family. {ECO:0000305}.
CC -!- CAUTION: The gene for this protein is either identical to or adjacent
CC to that of TREX1. Some of the mRNAs that encode ATRIP also encode TREX1
CC in another reading frame. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14029.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14029.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAF84257.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF451323; AAL38042.1; -; mRNA.
DR EMBL; AK022405; BAB14029.1; ALT_SEQ; mRNA.
DR EMBL; AK291568; BAF84257.1; ALT_INIT; mRNA.
DR EMBL; AK291829; BAF84518.1; -; mRNA.
DR EMBL; AK315075; BAG37544.1; -; mRNA.
DR EMBL; AK300548; BAG62254.1; -; mRNA.
DR EMBL; AC104448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64876.1; -; Genomic_DNA.
DR EMBL; CH471055; EAW64878.1; -; Genomic_DNA.
DR EMBL; BC014153; AAH14153.2; -; mRNA.
DR EMBL; BC020563; AAH20563.1; -; mRNA.
DR EMBL; BC030597; AAH30597.1; -; mRNA.
DR EMBL; AL832917; CAH10621.1; -; mRNA.
DR CCDS; CCDS2767.1; -. [Q8WXE1-2]
DR CCDS; CCDS2768.1; -. [Q8WXE1-1]
DR CCDS; CCDS59449.1; -. [Q8WXE1-3]
DR CCDS; CCDS59450.1; -. [Q8WXE1-5]
DR RefSeq; NP_001257951.1; NM_001271022.1. [Q8WXE1-5]
DR RefSeq; NP_001257952.1; NM_001271023.1. [Q8WXE1-3]
DR RefSeq; NP_115542.2; NM_032166.3. [Q8WXE1-2]
DR RefSeq; NP_569055.1; NM_130384.2. [Q8WXE1-1]
DR PDB; 4IGK; X-ray; 1.75 A; C/D=237-243.
DR PDB; 4NB3; X-ray; 1.35 A; C/D=54-67.
DR PDB; 5YZ0; EM; 4.70 A; C/D=1-791.
DR PDBsum; 4IGK; -.
DR PDBsum; 4NB3; -.
DR PDBsum; 5YZ0; -.
DR AlphaFoldDB; Q8WXE1; -.
DR SMR; Q8WXE1; -.
DR BioGRID; 313463; 91.
DR ComplexPortal; CPX-3622; ATR-ATRIP DNA damage-sensing kinase complex.
DR CORUM; Q8WXE1; -.
DR DIP; DIP-46495N; -.
DR ELM; Q8WXE1; -.
DR IntAct; Q8WXE1; 42.
DR MINT; Q8WXE1; -.
DR STRING; 9606.ENSP00000323099; -.
DR BindingDB; Q8WXE1; -.
DR ChEMBL; CHEMBL4106138; -.
DR GlyGen; Q8WXE1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WXE1; -.
DR PhosphoSitePlus; Q8WXE1; -.
DR BioMuta; ATRIP; -.
DR DMDM; 48428109; -.
DR CPTAC; CPTAC-3216; -.
DR CPTAC; CPTAC-3217; -.
DR CPTAC; CPTAC-914; -.
DR CPTAC; CPTAC-915; -.
DR EPD; Q8WXE1; -.
DR jPOST; Q8WXE1; -.
DR MassIVE; Q8WXE1; -.
DR MaxQB; Q8WXE1; -.
DR PaxDb; Q8WXE1; -.
DR PeptideAtlas; Q8WXE1; -.
DR PRIDE; Q8WXE1; -.
DR ProteomicsDB; 6227; -.
DR ProteomicsDB; 75018; -. [Q8WXE1-1]
DR ProteomicsDB; 75019; -. [Q8WXE1-2]
DR ProteomicsDB; 75020; -. [Q8WXE1-3]
DR Antibodypedia; 30090; 597 antibodies from 37 providers.
DR CPTC; Q8WXE1; 1 antibody.
DR DNASU; 84126; -.
DR Ensembl; ENST00000320211.10; ENSP00000323099.3; ENSG00000164053.22. [Q8WXE1-1]
DR Ensembl; ENST00000346691.9; ENSP00000302338.5; ENSG00000164053.22. [Q8WXE1-2]
DR Ensembl; ENST00000412052.4; ENSP00000400930.1; ENSG00000164053.22. [Q8WXE1-3]
DR GeneID; 84126; -.
DR KEGG; hsa:84126; -.
DR MANE-Select; ENST00000320211.10; ENSP00000323099.3; NM_130384.3; NP_569055.1.
DR UCSC; uc003ctf.3; human. [Q8WXE1-1]
DR CTD; 84126; -.
DR DisGeNET; 84126; -.
DR GeneCards; ATRIP; -.
DR HGNC; HGNC:33499; ATRIP.
DR HPA; ENSG00000164053; Tissue enhanced (testis).
DR MalaCards; ATRIP; -.
DR MIM; 606605; gene.
DR neXtProt; NX_Q8WXE1; -.
DR OpenTargets; ENSG00000164053; -.
DR Orphanet; 808; Seckel syndrome.
DR PharmGKB; PA162377290; -.
DR VEuPathDB; HostDB:ENSG00000164053; -.
DR eggNOG; ENOG502QQF4; Eukaryota.
DR GeneTree; ENSGT00390000012850; -.
DR HOGENOM; CLU_024109_0_0_1; -.
DR InParanoid; Q8WXE1; -.
DR OMA; CQCNLEV; -.
DR PhylomeDB; Q8WXE1; -.
DR TreeFam; TF324417; -.
DR PathwayCommons; Q8WXE1; -.
DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51.
DR SignaLink; Q8WXE1; -.
DR SIGNOR; Q8WXE1; -.
DR BioGRID-ORCS; 84126; 523 hits in 1084 CRISPR screens.
DR ChiTaRS; ATRIP; human.
DR GenomeRNAi; 84126; -.
DR Pharos; Q8WXE1; Tbio.
DR PRO; PR:Q8WXE1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8WXE1; protein.
DR Bgee; ENSG00000164053; Expressed in left testis and 106 other tissues.
DR ExpressionAtlas; Q8WXE1; baseline and differential.
DR Genevisible; Q8WXE1; HS.
DR GO; GO:0070310; C:ATR-ATRIP complex; IPI:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; TAS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IC:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR InterPro; IPR033349; ATRIP.
DR PANTHER; PTHR28594; PTHR28594; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Direct protein sequencing;
KW DNA damage; DNA repair; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..791
FT /note="ATR-interacting protein"
FT /id="PRO_0000064740"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..156
FT /note="Interaction with CINP"
FT /evidence="ECO:0000269|PubMed:19889979"
FT COILED 108..217
FT /evidence="ECO:0000255"
FT MOTIF 769..776
FT /note="EEXXXDL motif"
FT COMPBIAS 13..29
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..127
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047011"
FT VAR_SEQ 1..93
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010501"
FT VAR_SEQ 661..687
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_010504"
FT VARIANT 125
FT /note="K -> Q (in dbSNP:rs11925638)"
FT /id="VAR_050683"
FT VARIANT 240
FT /note="P -> L (in dbSNP:rs35240314)"
FT /id="VAR_050684"
FT MUTAGEN 769..770
FT /note="EE->AA: Abolishes interaction with ATR and its
FT recruitment to sites of DNA damage."
FT /evidence="ECO:0000269|PubMed:15758953"
FT MUTAGEN 774..775
FT /note="DD->AA: Abolishes interaction with ATR and its
FT recruitment to sites of DNA damage."
FT /evidence="ECO:0000269|PubMed:15758953"
FT CONFLICT 280
FT /note="P -> L (in Ref. 5; AAH14153)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="T -> A (in Ref. 2; BAF84257)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="V -> I (in Ref. 2; BAF84257)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="A -> T (in Ref. 2; BAG62254)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="N -> D (in Ref. 2; BAF84257)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="V -> I (in Ref. 5; AAH30597)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="Q -> K (in Ref. 2; BAF84257)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="C -> G (in Ref. 2; BAF84257)"
FT /evidence="ECO:0000305"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:4NB3"
SQ SEQUENCE 791 AA; 85838 MW; 58981602F7961756 CRC64;
MAGTSAPGSK RRSEPPAPRP GPPPGTGHPP SKRARGFSAA AAPDPDDPFG AHGDFTADDL
EELDTLASQA LSQCPAAARD VSSDHKVHRL LDGMSKNPSG KNRETVPIKD NFELEVLQAQ
YKELKEKMKV MEEEVLIKNG EIKILRDSLH QTESVLEEQR RSHFLLEQEK TQALSDKEKE
FSKKLQSLQS ELQFKDAEMN ELRTKLQTSE RANKLAAPSV SHVSPRKNPS VVIKPEACSP
QFGKTSFPTK ESFSANMSLP HPCQTESGYK PLVGREDSKP HSLRGDSIKQ EEAQKSFVDS
WRQRSNTQGS ILINLLLKQP LIPGSSLSLC HLLSSSSESP AGTPLQPPGF GSTLAGMSGL
RTTGSYDGSF SLSALREAQN LAFTGLNLVA RNECSRDGDP AEGGRRAFPL CQLPGAVHFL
PLVQFFIGLH CQALQDLAAA KRSGAPGDSP THSSCVSSGV ETNPEDSVCI LEGFSVTALS
ILQHLVCHSG AVVSLLLSGV GADSAAGEGN RSLVHRLSDG DMTSALRGVA DDQGQHPLLK
MLLHLLAFSS AATGHLQASV LTQCLKVLVK LAENTSCDFL PRFQCVFQVL PKCLSPETPL
PSVLLAVELL SLLADHDQLA PQLCSHSEGC LLLLLYMYIT SRPDRVALET QWLQLEQEVV
WLLAKLGVQS PLPPVTGSNC QCNVEVVRAL TVMLHRQWLT VRRAGGPPRT DQQRRTVRCL
RDTVLLLHGL SQKDKLFMMH CVEVLHQFDQ VMPGVSMLIR GLPDVTDCEE AALDDLCAAE
TDVEDPEVEC G
