ATMIN_MOUSE
ID ATMIN_MOUSE Reviewed; 818 AA.
AC Q6P9S1; Q05CB1; Q80U05; Q8C311;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=ATM interactor {ECO:0000312|EMBL:AAH60631.1};
DE AltName: Full=ATM/ATR-substrate CHK2-interacting zinc finger protein {ECO:0000250|UniProtKB:O43313};
DE Short=ASCIZ {ECO:0000250|UniProtKB:O43313};
GN Name=Atmin {ECO:0000312|MGI:MGI:2682328};
GN Synonyms=Kiaa0431 {ECO:0000312|EMBL:BAC65563.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain {ECO:0000269|PubMed:17525732};
RX PubMed=17525732; DOI=10.1038/sj.emboj.7601733;
RA Kanu N., Behrens A.;
RT "ATMIN defines an NBS1-independent pathway of ATM signalling.";
RL EMBO J. 26:2933-2941(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH60631.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH60631.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH60631.1}, and
RC Mammary tumor {ECO:0000312|EMBL:AAH27752.1};
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 [4] {ECO:0000305, ECO:0000312|EMBL:BAC65563.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-818.
RC TISSUE=Brain {ECO:0000312|EMBL:BAC65563.1};
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5] {ECO:0000305, ECO:0000312|EMBL:BAC39849.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 220-818.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC39849.1};
RC TISSUE=Lung {ECO:0000312|EMBL:BAC39849.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP FUNCTION.
RX PubMed=22167198; DOI=10.1074/jbc.m111.306019;
RA Jurado S., Conlan L.A., Baker E.K., Ng J.L., Tenis N., Hoch N.C.,
RA Gleeson K., Smeets M., Izon D., Heierhorst J.;
RT "ATM substrate Chk2-interacting Zn2+ finger (ASCIZ) Is a bi-functional
RT transcriptional activator and feedback sensor in the regulation of dynein
RT light chain (DYNLL1) expression.";
RL J. Biol. Chem. 287:3156-3164(2012).
CC -!- FUNCTION: Transcription factor. Plays a crucial role in cell survival
CC and RAD51 foci formation in response to methylating DNA damage.
CC Involved in regulating the activity of ATM in the absence of DNA
CC damage. May play a role in stabilizing ATM (By similarity). Binds to
CC the DYNLL1 promoter and activates its transcription. {ECO:0000250,
CC ECO:0000269|PubMed:22167198}.
CC -!- SUBUNIT: Interacts via its C-terminus with ATM. Interacts with DYNLL;
CC this interaction inhibits ATMIN transcriptional activity and hence may
CC play a role in a feedback loop whereby DYNLL1 inhibits transactivation
CC of its own promoter by ATMIN. ATMIN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43313}.
CC Note=Nuclear, in discrete foci during G1 phase.
CC {ECO:0000250|UniProtKB:O43313}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27752.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH60631.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC39849.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC162858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027752; AAH27752.1; ALT_SEQ; mRNA.
DR EMBL; BC060631; AAH60631.1; ALT_INIT; mRNA.
DR EMBL; AK122281; BAC65563.1; -; mRNA.
DR EMBL; AK087334; BAC39849.1; ALT_FRAME; mRNA.
DR CCDS; CCDS22694.2; -.
DR RefSeq; NP_808368.3; NM_177700.4.
DR AlphaFoldDB; Q6P9S1; -.
DR STRING; 10090.ENSMUSP00000104727; -.
DR iPTMnet; Q6P9S1; -.
DR PhosphoSitePlus; Q6P9S1; -.
DR EPD; Q6P9S1; -.
DR PaxDb; Q6P9S1; -.
DR PRIDE; Q6P9S1; -.
DR ProteomicsDB; 277070; -.
DR Antibodypedia; 30434; 141 antibodies from 25 providers.
DR DNASU; 234776; -.
DR Ensembl; ENSMUST00000109099; ENSMUSP00000104727; ENSMUSG00000047388.
DR GeneID; 234776; -.
DR KEGG; mmu:234776; -.
DR UCSC; uc009nop.2; mouse.
DR CTD; 23300; -.
DR MGI; MGI:2682328; Atmin.
DR VEuPathDB; HostDB:ENSMUSG00000047388; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00390000013091; -.
DR HOGENOM; CLU_023902_0_0_1; -.
DR InParanoid; Q6P9S1; -.
DR OMA; LCALFQH; -.
DR OrthoDB; 583153at2759; -.
DR PhylomeDB; Q6P9S1; -.
DR TreeFam; TF331171; -.
DR BioGRID-ORCS; 234776; 10 hits in 72 CRISPR screens.
DR ChiTaRS; Atmin; mouse.
DR PRO; PR:Q6P9S1; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q6P9S1; protein.
DR Bgee; ENSMUSG00000047388; Expressed in animal zygote and 244 other tissues.
DR Genevisible; Q6P9S1; MM.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0070840; F:dynein complex binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0044458; P:motile cilium assembly; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 2: Evidence at transcript level;
KW Activator; DNA damage; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..818
FT /note="ATM interactor"
FT /id="PRO_0000355036"
FT ZN_FING 80..105
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255"
FT ZN_FING 161..181
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..437
FT /note="Required for formation of RAD51 foci"
FT /evidence="ECO:0000250"
FT REGION 603..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1..3
FT /note="MAA -> MGP (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1
FT /note="M -> TRP (in Ref. 3; AAH27752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 818 AA; 87424 MW; F083B47FE0621B35 CRC64;
MAATEAAAAD SAGPAPGVPA TPASTRGAAA ASSPWRPPES RLQGSRPRPA RARAAAPVPP
ARELIQPTVS ELSRAVRTNI LCTVRGCGKI LPNSPALNMH LVKSHRLQDG IVNPTIRKDL
TTAPKFYCCP IKGCPRGPDR PFSQFSLVKQ HFMKMHAEKK HKCSKCSNSY GTEWDLKRHE
EDCGKTFQCT CGCPYASRTA LQSHIYRTGH EIPAEHRDPP SKKRKMESYL QNQKLSSKTT
EPLSDQAAPR QDAAEPDAPE VKPAASLEDS CSAHTKKQSV ATPPRCPQKL LLPKPKVALV
KLPVMQFSPV PVFVPTAESS AQPVVLGVDH SSAAGTVHLV PLSVGALILS LDSEACSLKE
SLPLSKIISP VVEPMNTGVQ VNLGKSLCSP LQEVGSVCQR TSISSSNVQT DLTYASANLI
PSAQWLGPDS SVSSCSQTDL SFDSQVSLPV SVHTQTLVPS SKVTSSIAAQ TDAFIDACFQ
PGGVSRETQT SRMQNRTNDS VPVGHTGLCG DIFESVHASY SVPTDTIMSS SLVAETGTHG
LPPQSDPKIL GQVMEKSAPV LNFSTQNGLL PAHTMTDNQT QTIDLLSDLE NILSSNLPGQ
TLDNRSLLSD TNPGPDAQLP AGSAQNSGID FDIEEFLSAS NIQTQTEESE LSSMSTEPVL
ESLDIETQTD VLLSDPSTQP YGFRAGSGFL GLEMFDTQTQ TDLNFFLDSS PHLPLGSILK
HSSFSMSTDS SDTETQTEGA CPARHLPALE SKVQLSSTET QTMSSGFEPL GNLFLTSNET
QTAMDDFLLA DLAWNTMESQ FSSVETQTCA ELHAVSSF
