ATMIN_HUMAN
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 03-AUG-2022, entry version 174.
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; 12.
DR IntAct; O43313; 5.
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; O43313; -.
DR PeptideAtlas; O43313; -.
DR PRIDE; O43313; -.
DR ProteomicsDB; 48890; -. [O43313-1]
DR ProteomicsDB; 48891; -. [O43313-2]
DR Antibodypedia; 30434; 141 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 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 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; 583153at2759; -.
DR PhylomeDB; O43313; -.
DR TreeFam; TF331171; -.
DR PathwayCommons; O43313; -.
DR SignaLink; O43313; -.
DR BioGRID-ORCS; 23300; 137 hits in 1090 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 207 other tissues.
DR ExpressionAtlas; O43313; baseline and differential.
DR Genevisible; O43313; HS.
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:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0044458; P:motile cilium assembly; IEA:Ensembl.
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:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR DisProt; DP01288; -.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
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
