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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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. DR Genevisible; O94983; HS. 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 //