CREST_MOUSE
ID CREST_MOUSE Reviewed; 402 AA.
AC Q8BW22; Q6A014; Q7TQF3; Q8BYQ7;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Calcium-responsive transactivator;
DE AltName: Full=SS18-like protein 1;
GN Name=Ss18l1; Synonyms=Crest, Kiaa0693;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Olfactory bulb;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14716005; DOI=10.1126/science.1089845;
RA Aizawa H., Hu S.-C., Bobb K., Balakrishnan K., Ince G., Gurevich I.,
RA Cowan M., Ghosh A.;
RT "Dendrite development regulated by CREST, a calcium-regulated
RT transcriptional activator.";
RL Science 303:197-202(2004).
RN [6]
RP INTERACTION WITH THE NBAF COMPLEX.
RX PubMed=17920018; DOI=10.1016/j.neuron.2007.08.021;
RA Wu J.I., Lessard J., Olave I.A., Qiu Z., Ghosh A., Graef I.A.,
RA Crabtree G.R.;
RT "Regulation of dendritic development by neuron-specific chromatin
RT remodeling complexes.";
RL Neuron 56:94-108(2007).
RN [7]
RP FUNCTION.
RX PubMed=19081374; DOI=10.1016/j.neuron.2008.09.040;
RA Qiu Z., Ghosh A.;
RT "A calcium-dependent switch in a CREST-BRG1 complex regulates activity-
RT dependent gene expression.";
RL Neuron 60:775-787(2008).
CC -!- FUNCTION: Transcriptional activator which is required for calcium-
CC dependent dendritic growth and branching in cortical neurons. Recruits
CC CREB-binding protein (CREBBP) to nuclear bodies. Component of the
CC CREST-BRG1 complex, a multiprotein complex that regulates promoter
CC activation by orchestrating a calcium-dependent release of a repressor
CC complex and a recruitment of an activator complex. In resting neurons,
CC transcription of the c-FOS promoter is inhibited by BRG1-dependent
CC recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium
CC influx, RB1 is dephosphorylated by calcineurin, which leads to release
CC of the repressor complex. At the same time, there is increased
CC recruitment of CREBBP to the promoter by a CREST-dependent mechanism,
CC which leads to transcriptional activation. The CREST-BRG1 complex also
CC binds to the NR2B promoter, and activity-dependent induction of NR2B
CC expression involves a release of HDAC1 and recruitment of CREBBP.
CC {ECO:0000269|PubMed:14716005, ECO:0000269|PubMed:19081374}.
CC -!- SUBUNIT: Homodimer. Dimerization may be necessary for its function in
CC neuronal dendritic development. Interacts (via C-terminus) with CREBBP
CC (via N-terminus), EP300 and SMARCA4/BRG1. Interacts with the nBAF
CC complex. Association with CREBBP facilitates transcription while the
CC association with SMARCA4/BRG1 suppresses CREST-mediated transcription
CC in resting neurons (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere,
CC kinetochore {ECO:0000250}. Note=Localizes to nuclear bodies.
CC Colocalizes with SGO1 at kinetochore (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The MFD (multi-functional domain) domain is involved in
CC transcription transactivation, nuclear body targeting and dimerization.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice are smaller than littermates and show
CC coordination defects. There is increased mortality in beginning at
CC about P14, and about 80% die by P28. Less than 20% survive to
CC adulthood, and they are infertile. {ECO:0000269|PubMed:14716005}.
CC -!- SIMILARITY: Belongs to the SS18 family. {ECO:0000305}.
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DR EMBL; AK173004; BAD32282.1; -; mRNA.
DR EMBL; AK038669; BAC30089.1; -; mRNA.
DR EMBL; AK054560; BAC35824.1; -; mRNA.
DR EMBL; AK133944; BAE21942.1; -; mRNA.
DR EMBL; AL663067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053087; AAH53087.1; -; mRNA.
DR EMBL; BC054730; AAH54730.1; -; mRNA.
DR CCDS; CCDS17167.1; -.
DR RefSeq; NP_848865.4; NM_178750.5.
DR AlphaFoldDB; Q8BW22; -.
DR SMR; Q8BW22; -.
DR BioGRID; 234646; 2.
DR CORUM; Q8BW22; -.
DR STRING; 10090.ENSMUSP00000041288; -.
DR iPTMnet; Q8BW22; -.
DR PhosphoSitePlus; Q8BW22; -.
DR MaxQB; Q8BW22; -.
DR PaxDb; Q8BW22; -.
DR PeptideAtlas; Q8BW22; -.
DR PRIDE; Q8BW22; -.
DR ProteomicsDB; 284135; -.
DR Antibodypedia; 44341; 156 antibodies from 23 providers.
DR DNASU; 269397; -.
DR Ensembl; ENSMUST00000041126; ENSMUSP00000041288; ENSMUSG00000039086.
DR GeneID; 269397; -.
DR KEGG; mmu:269397; -.
DR UCSC; uc008oic.2; mouse.
DR CTD; 26039; -.
DR MGI; MGI:2444061; Ss18l1.
DR VEuPathDB; HostDB:ENSMUSG00000039086; -.
DR eggNOG; KOG3227; Eukaryota.
DR GeneTree; ENSGT00940000159853; -.
DR HOGENOM; CLU_054580_1_0_1; -.
DR InParanoid; Q8BW22; -.
DR OMA; SAQQYMG; -.
DR OrthoDB; 1442230at2759; -.
DR PhylomeDB; Q8BW22; -.
DR TreeFam; TF330999; -.
DR BioGRID-ORCS; 269397; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q8BW22; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BW22; protein.
DR Bgee; ENSMUSG00000039086; Expressed in CA1 field of hippocampus and 207 other tissues.
DR Genevisible; Q8BW22; MM.
DR GO; GO:0000775; C:chromosome, centromeric region; ISS:MGI.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0071565; C:nBAF complex; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0050773; P:regulation of dendrite development; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR InterPro; IPR044779; SS18.
DR InterPro; IPR007726; SS18_N.
DR PANTHER; PTHR23107; PTHR23107; 1.
DR Pfam; PF05030; SSXT; 1.
PE 1: Evidence at protein level;
KW Activator; Calcium; Centromere; Chromatin regulator; Chromosome;
KW Kinetochore; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..402
FT /note="Calcium-responsive transactivator"
FT /id="PRO_0000391346"
FT REGION 1..148
FT /note="N-terminal auto-inhibitory domain; necessary for
FT interaction with SMARCA4/BRG1"
FT /evidence="ECO:0000250"
FT REGION 72..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..238
FT /note="Methionine-rich intra-molecular domain"
FT /evidence="ECO:0000250"
FT REGION 221..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..323
FT /note="MFD domain"
FT /evidence="ECO:0000250"
FT REGION 340..402
FT /note="Necessary for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 393..402
FT /note="Necessary for interaction with CREBBP and for the
FT recruitment of CREBBP to the nuclear bodies"
FT /evidence="ECO:0000250"
FT MOTIF 50..53
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 359..362
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 377..385
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 397..400
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 241..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 130
FT /note="V -> L (in Ref. 2; BAC30089)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="S -> I (in Ref. 4; AAH54730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 43729 MW; 9C309B9E7446CCAA CRC64;
MSVAFASARP RGKGEVTQQT IQKMLDENHH LIQCILDYQS KGKTAECTQY QQILHRNLVY
LATIADSNQN MQSLLPAPPT QNMNLGPGAL SQSGSSQGLH PQGSLSDTVS TGLPPASLMQ
GQIGNGPNHV SMQQTAQSTL PTTSMSLSGS GHGTGPGYSH SGPTSQSVPM QGQGAISNYV
SRTNINMQSN PVSMMHQQAA TSHYNSAQGG SQHYQGQAPI AMMGQGGQGG SMMGQRPMAP
YRPSQQGSSQ QYLGQEEYYS EQYSHSQGSA EPMSQQYYPD GHGDYAYQQS SYTEQSYDRS
FEDPTQHYYE GGNSQYSQQQ AGYQQGTAQQ QTYSQQQYPN QQSYPGQQQG YGPAQGAPSQ
YSSYQQGQGQ QYGSYRTSQT GPSAQQQRPY GYEQGQYGNY QQ
