ID CMTA2_HUMAN Reviewed; 1202 AA.
AC O94983; B9EGL0; D3DTL5; E7EWU5; Q7Z6M8; Q8N3V0; Q8NDG4; Q96G17;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 3.
DT 27-MAR-2024, entry version 188.
DE RecName: Full=Calmodulin-binding transcription activator 2;
GN Name=CAMTA2; Synonyms=KIAA0909;
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 1), AND VARIANTS PRO-267
RP AND PRO-903.
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANTS
RP PRO-267 AND PRO-903.
RC TISSUE=Amygdala, and Brain;
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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-267.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5 AND 6), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 485-1202 (ISOFORM 2).
RC TISSUE=Eye, and Placenta;
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 FUNCTION, TISSUE SPECIFICITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11925432; DOI=10.1074/jbc.m200268200;
RA Bouche N., Scharlat A., Snedden W., Bouchez D., Fromm H.;
RT "A novel family of calmodulin-binding transcription activators in
RT multicellular organisms.";
RL J. Biol. Chem. 277:21851-21861(2002).
RN [7]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=15138581;
RA Nakatani K., Nishioka J., Itakura T., Nakanishi Y., Horinouchi J., Abe Y.,
RA Wada H., Nobori T.;
RT "Cell cycle-dependent transcriptional regulation of calmodulin-binding
RT transcription activator 1 in neuroblastoma cells.";
RL Int. J. Oncol. 24:1407-1412(2004).
CC -!- FUNCTION: Transcription activator. May act as tumor suppressor.
CC {ECO:0000269|PubMed:11925432}.
CC -!- SUBUNIT: May interact with calmodulin. {ECO:0000305}.
CC -!- INTERACTION:
CC O94983; P42582: Nkx2-5; Xeno; NbExp=2; IntAct=EBI-936534, EBI-297021;
CC O94983-5; B4DJ51: CALM1; NbExp=5; IntAct=EBI-10176008, EBI-10171450;
CC O94983-5; P27797: CALR; NbExp=3; IntAct=EBI-10176008, EBI-1049597;
CC O94983-5; P12830: CDH1; NbExp=3; IntAct=EBI-10176008, EBI-727477;
CC O94983-5; Q15078: CDK5R1; NbExp=3; IntAct=EBI-10176008, EBI-746189;
CC O94983-5; P36957: DLST; NbExp=3; IntAct=EBI-10176008, EBI-351007;
CC O94983-5; P43360: MAGEA6; NbExp=3; IntAct=EBI-10176008, EBI-1045155;
CC O94983-5; Q9Y316: MEMO1; NbExp=3; IntAct=EBI-10176008, EBI-1104564;
CC O94983-5; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-10176008, EBI-1055945;
CC O94983-5; Q6P088: ZNF483; NbExp=3; IntAct=EBI-10176008, EBI-10196963;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:11925432}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=O94983-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94983-2; Sequence=VSP_018493;
CC Name=3;
CC IsoId=O94983-3; Sequence=VSP_018490, VSP_018493;
CC Name=4;
CC IsoId=O94983-4; Sequence=VSP_018491, VSP_018492;
CC Name=5;
CC IsoId=O94983-5; Sequence=VSP_018489;
CC Name=6;
CC IsoId=O94983-6; Sequence=VSP_018491, VSP_046059;
CC -!- TISSUE SPECIFICITY: Detected in brain. Expressed at constant levels
CC throughout the cell cycle in neuroblastoma cell lines.
CC {ECO:0000269|PubMed:11925432, ECO:0000269|PubMed:15138581}.
CC -!- SIMILARITY: Belongs to the CAMTA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16163.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA74932.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB020716; BAA74932.1; ALT_INIT; mRNA.
DR EMBL; AL833974; CAD38818.2; -; mRNA.
DR EMBL; AL831849; CAD38553.1; -; mRNA.
DR EMBL; AC004771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90372.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90373.1; -; Genomic_DNA.
DR EMBL; BC010050; AAH10050.2; -; mRNA.
DR EMBL; BC016163; AAH16163.1; ALT_FRAME; mRNA.
DR EMBL; BC136534; AAI36535.1; -; mRNA.
DR EMBL; BC142606; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS11063.1; -. [O94983-1]
DR CCDS; CCDS54071.1; -. [O94983-4]
DR CCDS; CCDS54072.1; -. [O94983-6]
DR CCDS; CCDS54073.1; -. [O94983-3]
DR RefSeq; NP_001164637.1; NM_001171166.1. [O94983-3]
DR RefSeq; NP_001164638.1; NM_001171167.1. [O94983-6]
DR RefSeq; NP_001164639.1; NM_001171168.1. [O94983-4]
DR RefSeq; NP_055914.2; NM_015099.3. [O94983-1]
DR AlphaFoldDB; O94983; -.
DR SMR; O94983; -.
DR BioGRID; 116744; 18.
DR IntAct; O94983; 18.
DR MINT; O94983; -.
DR STRING; 9606.ENSP00000412886; -.
DR iPTMnet; O94983; -.
DR PhosphoSitePlus; O94983; -.
DR BioMuta; CAMTA2; -.
DR jPOST; O94983; -.
DR MassIVE; O94983; -.
DR PaxDb; 9606-ENSP00000412886; -.
DR PeptideAtlas; O94983; -.
DR ProteomicsDB; 18913; -.
DR ProteomicsDB; 50603; -. [O94983-1]
DR ProteomicsDB; 50604; -. [O94983-2]
DR ProteomicsDB; 50605; -. [O94983-3]
DR ProteomicsDB; 50606; -. [O94983-4]
DR ProteomicsDB; 50607; -. [O94983-5]
DR Antibodypedia; 53152; 30 antibodies from 19 providers.
DR DNASU; 23125; -.
DR Ensembl; ENST00000348066.8; ENSP00000321813.7; ENSG00000108509.21. [O94983-1]
DR Ensembl; ENST00000361571.9; ENSP00000354828.5; ENSG00000108509.21. [O94983-4]
DR Ensembl; ENST00000381311.9; ENSP00000370712.5; ENSG00000108509.21. [O94983-3]
DR Ensembl; ENST00000414043.7; ENSP00000412886.3; ENSG00000108509.21. [O94983-6]
DR GeneID; 23125; -.
DR KEGG; hsa:23125; -.
DR MANE-Select; ENST00000348066.8; ENSP00000321813.7; NM_015099.4; NP_055914.2.
DR UCSC; uc002gag.3; human. [O94983-1]
DR AGR; HGNC:18807; -.
DR CTD; 23125; -.
DR DisGeNET; 23125; -.
DR GeneCards; CAMTA2; -.
DR HGNC; HGNC:18807; CAMTA2.
DR HPA; ENSG00000108509; Tissue enhanced (brain).
DR MIM; 611508; gene.
DR neXtProt; NX_O94983; -.
DR OpenTargets; ENSG00000108509; -.
DR PharmGKB; PA38689; -.
DR VEuPathDB; HostDB:ENSG00000108509; -.
DR eggNOG; KOG0520; Eukaryota.
DR GeneTree; ENSGT00940000160105; -.
DR HOGENOM; CLU_003170_2_0_1; -.
DR InParanoid; O94983; -.
DR OMA; VQLYSNP; -.
DR OrthoDB; 470813at2759; -.
DR PhylomeDB; O94983; -.
DR TreeFam; TF323452; -.
DR PathwayCommons; O94983; -.
DR SignaLink; O94983; -.
DR BioGRID-ORCS; 23125; 13 hits in 1180 CRISPR screens.
DR ChiTaRS; CAMTA2; human.
DR GenomeRNAi; 23125; -.
DR Pharos; O94983; Tbio.
DR PRO; PR:O94983; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O94983; Protein.
DR Bgee; ENSG00000108509; Expressed in right hemisphere of cerebellum and 158 other cell types or tissues.
DR ExpressionAtlas; O94983; baseline and differential.
DR Genevisible; O94983; HS.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:ARUK-UCL.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR Gene3D; 1.20.5.190; -; 2.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005559; CG-1_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR PANTHER; PTHR23335:SF9; CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR 2; 1.
DR PANTHER; PTHR23335; CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR CAMTA; 1.
DR Pfam; PF03859; CG-1; 1.
DR Pfam; PF01833; TIG; 1.
DR SMART; SM01076; CG-1; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS51437; CG_1; 1.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; ANK repeat; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1202
FT /note="Calmodulin-binding transcription activator 2"
FT /id="PRO_0000235821"
FT DOMAIN 537..615
FT /note="IPT/TIG"
FT REPEAT 712..745
FT /note="ANK 1"
FT REPEAT 757..787
FT /note="ANK 2"
FT REPEAT 791..821
FT /note="ANK 3"
FT DOMAIN 1049..1078
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1102..1131
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DNA_BIND 30..155
FT /note="CG-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00767"
FT REGION 263..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 79..86
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00767"
FT COMPBIAS 266..285
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..477
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..873
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018489"
FT VAR_SEQ 1..10
FT /note="MNTKDTTEVA -> MAAAAVTRGTPG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_018490"
FT VAR_SEQ 1
FT /note="M -> MGTDSPSPRPLRPGVTLPPGALTM (in isoform 4 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_018491"
FT VAR_SEQ 114..137
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_018492"
FT VAR_SEQ 1088..1094
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_018493"
FT VAR_SEQ 1158..1202
FT /note="GSFLTKKQDQAARKIMRFLRRCRHRMRELKQNQELEGLPQPGLAT -> LLS
FT HQEAGPGSPEDHEIPAALPTQDEGTEAEPGAGRASPAGTGHMTWPPPFSPPWGRLVQS
FT (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046059"
FT VARIANT 267
FT /note="A -> P (in dbSNP:rs238234)"
FT /evidence="ECO:0000269|PubMed:10048485,
FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.4"
FT /id="VAR_026417"
FT VARIANT 903
FT /note="S -> P (in dbSNP:rs16942615)"
FT /evidence="ECO:0000269|PubMed:10048485,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_026418"
FT CONFLICT 140
FT /note="D -> G (in Ref. 2; CAD38818)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="A -> V (in Ref. 2; CAD38818)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="V -> L (in Ref. 2; CAD38818)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="S -> P (in Ref. 2; CAD38818)"
FT /evidence="ECO:0000305"
FT CONFLICT 1175
FT /note="F -> S (in Ref. 2; CAD38818)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1202 AA; 131530 MW; 09E17E4E240F4A58 CRC64;
MNTKDTTEVA ENSHHLKIFL PKKLLECLPR CPLLPPERLR WNTNEEIASY LITFEKHDEW
LSCAPKTRPQ NGSIILYNRK KVKYRKDGYL WKKRKDGKTT REDHMKLKVQ GMECLYGCYV
HSSIVPTFHR RCYWLLQNPD IVLVHYLNVP ALEDCGKGCS PIFCSISSDR REWLKWSREE
LLGQLKPMFH GIKWSCGNGT EEFSVEHLVQ QILDTHPTKP APRTHACLCS GGLGSGSLTH
KCSSTKHRII SPKVEPRALT LTSIPHAHPP EPPPLIAPLP PELPKAHTSP SSSSSSSSSG
FAEPLEIRPS PPTSRGGSSR GGTAILLLTG LEQRAGGLTP TRHLAPQADP RPSMSLAVVV
GTEPSAPPAP PSPAFDPDRF LNSPQRGQTY GGGQGVSPDF PEAEAAHTPC SALEPAAALE
PQAAARGPPP QSVAGGRRGN CFFIQDDDSG EELKGHGAAP PIPSPPPSPP PSPAPLEPSS
RVGRGEALFG GPVGASELEP FSLSSFPDLM GELISDEAPS IPAPTPQLSP ALSTITDFSP
EWSYPEGGVK VLITGPWTEA AEHYSCVFDH IAVPASLVQP GVLRCYCPAH EVGLVSLQVA
GREGPLSASV LFEYRARRFL SLPSTQLDWL SLDDNQFRMS ILERLEQMEK RMAEIAAAGQ
VPCQGPDAPP VQDEGQGPGF EARVVVLVES MIPRSTWKGP ERLAHGSPFR GMSLLHLAAA
QGYARLIETL SQWRSVETGS LDLEQEVDPL NVDHFSCTPL MWACALGHLE AAVLLFRWNR
QALSIPDSLG RLPLSVAHSR GHVRLARCLE ELQRQEPSVE PPFALSPPSS SPDTGLSSVS
SPSELSDGTF SVTSAYSSAP DGSPPPAPLP ASEMTMEDMA PGQLSSGVPE APLLLMDYEA
TNSKGPLSSL PALPPASDDG AAPEDADSPQ AVDVIPVDMI SLAKQIIEAT PERIKREDFV
GLPEAGASMR ERTGAVGLSE TMSWLASYLE NVDHFPSSTP PSELPFERGR LAVPSAPSWA
EFLSASTSGK MESDFALLTL SDHEQRELYE AARVIQTAFR KYKGRRLKEQ QEVAAAVIQR
CYRKYKQLTW IALKFALYKK MTQAAILIQS KFRSYYEQKR FQQSRRAAVL IQQHYRSYRR
RPGPPHRTSA TLPARNKGSF LTKKQDQAAR KIMRFLRRCR HRMRELKQNQ ELEGLPQPGL
AT
//
