ID   ATMIN_HUMAN             Reviewed;         823 AA.
AC   O43313; A8K4H8; Q68DC9;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   24-JAN-2024, entry version 182.
DE   RecName: Full=ATM interactor;
DE   AltName: Full=ATM/ATR-substrate CHK2-interacting zinc finger protein;
DE            Short=ASCIZ;
DE   AltName: Full=Zinc finger protein 822;
GN   Name=ATMIN; Synonyms=KIAA0431, ZNF822;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA   Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT   new cDNA clones from brain which code for large proteins in vitro.";
RL   DNA Res. 4:307-313(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Liver;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-823 (ISOFORM 1).
RC   TISSUE=Uterus;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-823 (ISOFORM 1).
RC   TISSUE=Teratocarcinoma;
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   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND REGION.
RX   PubMed=15933716; DOI=10.1038/sj.emboj.7600704;
RA   McNees C.J., Conlan L.A., Tenis N., Heierhorst J.;
RT   "ASCIZ regulates lesion-specific Rad51 focus formation and apoptosis after
RT   methylating DNA damage.";
RL   EMBO J. 24:2447-2457(2005).
RN   [7]
RP   FUNCTION, INTERACTION WITH ATM, AND SUBCELLULAR LOCATION.
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   [8]
RP   FUNCTION, AND INTERACTION WITH DYNLL1.
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. Binds to the DYNLL1
CC       promoter and activates its transcription. {ECO:0000269|PubMed:15933716,
CC       ECO:0000269|PubMed:17525732, ECO:0000269|PubMed:22167198}.
CC   -!- SUBUNIT: Interacts via its C-terminus with ATM. Interacts with DYNLL1;
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. {ECO:0000269|PubMed:17525732,
CC       ECO:0000269|PubMed:22167198}.
CC   -!- INTERACTION:
CC       O43313; Q13315: ATM; NbExp=5; IntAct=EBI-7422202, EBI-495465;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15933716,
CC       ECO:0000269|PubMed:17525732}. Note=Nuclear, in discrete foci during G1
CC       phase.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O43313-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O43313-2; Sequence=VSP_035820;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in normal tissues and cancer
CC       cell lines with highest levels in placenta and skeletal muscle.
CC       {ECO:0000269|PubMed:15933716}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA24861.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAF83632.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB007891; BAA24861.2; ALT_INIT; mRNA.
DR   EMBL; CR749457; CAH18291.1; -; mRNA.
DR   EMBL; AC092718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002701; AAH02701.2; -; mRNA.
DR   EMBL; AK290943; BAF83632.1; ALT_INIT; mRNA.
DR   CCDS; CCDS32494.1; -. [O43313-1]
DR   CCDS; CCDS73917.1; -. [O43313-2]
DR   PIR; T00061; T00061.
DR   RefSeq; NP_001287657.1; NM_001300728.1. [O43313-2]
DR   RefSeq; NP_056066.2; NM_015251.2. [O43313-1]
DR   AlphaFoldDB; O43313; -.
DR   BioGRID; 116892; 13.
DR   IntAct; O43313; 4.
DR   MINT; O43313; -.
DR   STRING; 9606.ENSP00000299575; -.
DR   iPTMnet; O43313; -.
DR   PhosphoSitePlus; O43313; -.
DR   BioMuta; ATMIN; -.
DR   EPD; O43313; -.
DR   jPOST; O43313; -.
DR   MassIVE; O43313; -.
DR   MaxQB; O43313; -.
DR   PaxDb; 9606-ENSP00000299575; -.
DR   PeptideAtlas; O43313; -.
DR   ProteomicsDB; 48890; -. [O43313-1]
DR   ProteomicsDB; 48891; -. [O43313-2]
DR   Antibodypedia; 30434; 158 antibodies from 25 providers.
DR   DNASU; 23300; -.
DR   Ensembl; ENST00000299575.5; ENSP00000299575.3; ENSG00000166454.10. [O43313-1]
DR   Ensembl; ENST00000564241.5; ENSP00000463478.1; ENSG00000166454.10. [O43313-2]
DR   Ensembl; ENST00000566488.1; ENSP00000455497.1; ENSG00000166454.10. [O43313-2]
DR   Ensembl; ENST00000709336.1; ENSP00000517627.1; ENSG00000291953.1. [O43313-1]
DR   Ensembl; ENST00000709339.1; ENSP00000517628.1; ENSG00000291953.1. [O43313-2]
DR   Ensembl; ENST00000709341.1; ENSP00000517630.1; ENSG00000291953.1. [O43313-2]
DR   GeneID; 23300; -.
DR   KEGG; hsa:23300; -.
DR   MANE-Select; ENST00000299575.5; ENSP00000299575.3; NM_015251.3; NP_056066.2.
DR   UCSC; uc002ffz.2; human. [O43313-1]
DR   AGR; HGNC:29034; -.
DR   CTD; 23300; -.
DR   DisGeNET; 23300; -.
DR   GeneCards; ATMIN; -.
DR   HGNC; HGNC:29034; ATMIN.
DR   HPA; ENSG00000166454; Low tissue specificity.
DR   MIM; 614693; gene.
DR   neXtProt; NX_O43313; -.
DR   OpenTargets; ENSG00000166454; -.
DR   PharmGKB; PA162377191; -.
DR   VEuPathDB; HostDB:ENSG00000166454; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00390000013091; -.
DR   HOGENOM; CLU_023902_0_0_1; -.
DR   InParanoid; O43313; -.
DR   OMA; LCALFQH; -.
DR   OrthoDB; 5363046at2759; -.
DR   PhylomeDB; O43313; -.
DR   TreeFam; TF331171; -.
DR   PathwayCommons; O43313; -.
DR   SignaLink; O43313; -.
DR   BioGRID-ORCS; 23300; 141 hits in 1168 CRISPR screens.
DR   ChiTaRS; ATMIN; human.
DR   GenomeRNAi; 23300; -.
DR   Pharos; O43313; Tbio.
DR   PRO; PR:O43313; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; O43313; Protein.
DR   Bgee; ENSG00000166454; Expressed in sperm and 209 other cell types or tissues.
DR   ExpressionAtlas; O43313; baseline and differential.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS: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; IPI:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR   GO; GO:0044458; P:motile cilium assembly; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:ARUK-UCL.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   DisProt; DP01288; -.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR46664; ATM INTERACTOR; 1.
DR   PANTHER; PTHR46664:SF2; ATM INTERACTOR; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   Genevisible; O43313; HS.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; DNA damage; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..823
FT                   /note="ATM interactor"
FT                   /id="PRO_0000050756"
FT   ZN_FING         84..109
FT                   /note="C2H2-type 1"
FT   ZN_FING         165..184
FT                   /note="C2H2-type 2; degenerate"
FT   REGION          28..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..442
FT                   /note="Required for formation of RAD51 foci"
FT   REGION          268..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..156
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005,
FT                   ECO:0000303|PubMed:9455477"
FT                   /id="VSP_035820"
FT   VARIANT         240
FT                   /note="S -> P (in dbSNP:rs2278022)"
FT                   /id="VAR_050681"
FT   VARIANT         305
FT                   /note="K -> E (in dbSNP:rs2278023)"
FT                   /id="VAR_050682"
FT   CONFLICT        174
FT                   /note="Y -> C (in Ref. 2; CAH18291)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        309
FT                   /note="M -> V (in Ref. 5; BAF83632)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        338
FT                   /note="T -> A (in Ref. 2; CAH18291)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        433
FT                   /note="A -> T (in Ref. 2; CAH18291)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        474
FT                   /note="A -> P (in Ref. 2; CAH18291)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        525
FT                   /note="Y -> H (in Ref. 2; CAH18291)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        703
FT                   /note="Q -> R (in Ref. 5; BAF83632)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        814
FT                   /note="S -> P (in Ref. 2; CAH18291)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   823 AA;  88348 MW;  59CDBD56381539E9 CRC64;
     MAASEAAAAA GSAALAAGAR AVPAATTGAA AAASGPWVPP GPRLRGSRPR PAGATQQPAV
     PAPPAGELIQ PSVSELSRAV RTNILCTVRG CGKILPNSPA LNMHLVKSHR LQDGIVNPTI
     RKDLKTGPKF YCCPIEGCPR GPERPFSQFS LVKQHFMKMH AEKKHKCSKC SNSYGTEWDL
     KRHAEDCGKT FRCTCGCPYA SRTALQSHIY RTGHEIPAEH RDPPSKKRKM ENCAQNQKLS
     NKTIESLNNQ PIPRPDTQEL EASEIKLEPS FEDSCGSNTD KQTLTTPPRY PQKLLLPKPK
     VALVKLPVMQ FSVMPVFVPT ADSSAQPVVL GVDQGSATGA VHLMPLSVGT LILGLDSEAC
     SLKESLPLFK IANPIAGEPI STGVQVNFGK SPSNPLQELG NTCQKNSISS INVQTDLSYA
     SQNFIPSAQW ATADSSVSSC SQTDLSFDSQ VSLPISVHTQ TFLPSSKVTS SIAAQTDAFM
     DTCFQSGGVS RETQTSGIES PTDDHVQMDQ AGMCGDIFES VHSSYNVATG NIISNSLVAE
     TVTHSLLPQN EPKTLNQDIE KSAPIINFSA QNSMLPSQNM TDNQTQTIDL LSDLENILSS
     NLPAQTLDHR SLLSDTNPGP DTQLPSGPAQ NPGIDFDIEE FFSASNIQTQ TEESELSTMT
     TEPVLESLDI ETQTDFLLAD TSAQSYGCRG NSNFLGLEMF DTQTQTDLNF FLDSSPHLPL
     GSILKHSSFS VSTDSSDTET QTEGVSTAKN IPALESKVQL NSTETQTMSS GFETLGSLFF
     TSNETQTAMD DFLLADLAWN TMESQFSSVE TQTSAEPHTV SNF
//