CECR2_MOUSE
ID CECR2_MOUSE Reviewed; 1453 AA.
AC E9Q2Z1; E9QA25; F6VR46; F7B218; Q6PAQ2; Q6ZPI9;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Chromatin remodeling regulator CECR2 {ECO:0000305};
DE AltName: Full=Cat eye syndrome critical region protein 2 homolog;
GN Name=Cecr2 {ECO:0000312|MGI:MGI:1923799};
GN Synonyms=Kiaa1740 {ECO:0000303|PubMed:14621295};
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-1425 (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1188-1453.
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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=15640247; DOI=10.1093/hmg/ddi048;
RA Banting G.S., Barak O., Ames T.M., Burnham A.C., Kardel M.D., Cooch N.S.,
RA Davidson C.E., Godbout R., McDermid H.E., Shiekhattar R.;
RT "CECR2, a protein involved in neurulation, forms a novel chromatin
RT remodeling complex with SNF2L.";
RL Hum. Mol. Genet. 14:513-524(2005).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20589882; DOI=10.1002/bdra.20695;
RA Fairbridge N.A., Dawe C.E., Niri F.H., Kooistra M.K., King-Jones K.,
RA McDermid H.E.;
RT "Cecr2 mutations causing exencephaly trigger misregulation of
RT mesenchymal/ectodermal transcription factors.";
RL Birth Defects Res. A Clin. Mol. Teratol. 88:619-625(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=21246654; DOI=10.1002/dvdy.22547;
RA Dawe C.E., Kooistra M.K., Fairbridge N.A., Pisio A.C., McDermid H.E.;
RT "Role of chromatin remodeling gene Cecr2 in neurulation and inner ear
RT development.";
RL Dev. Dyn. 240:372-383(2011).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22154806; DOI=10.1016/j.jmb.2011.11.041;
RA Thompson P.J., Norton K.A., Niri F.H., Dawe C.E., McDermid H.E.;
RT "CECR2 is involved in spermatogenesis and forms a complex with SNF2H in the
RT testis.";
RL J. Mol. Biol. 415:793-806(2012).
RN [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1166 AND ARG-1172, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Regulatory subunit of the ATP-dependent CERF-1 and CERF-5
CC ISWI chromatin remodeling complexes, which form ordered nucleosome
CC arrays on chromatin and facilitate access to DNA during DNA-templated
CC processes such as DNA replication, transcription, and repair (By
CC similarity). The complexes do not have the ability to slide
CC mononucleosomes to the center of a DNA template (By similarity). The
CC CERF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis
CC rate than the CERF-5 ISWI chromatin remodeling complex (By similarity).
CC Plays a role in various processes during development: required during
CC embryogenesis for neural tube closure and inner ear development
CC (PubMed:15640247, PubMed:20589882, PubMed:21246654). In adults,
CC required for spermatogenesis, via the formation of ISWI-type chromatin
CC complexes (PubMed:22154806). In histone-modifying complexes, CECR2
CC recognizes and binds acylated histones: binds histones that are
CC acetylated and/or butyrylated (By similarity). May also be involved
CC through its interaction with LRPPRC in the integration of cytoskeletal
CC network with vesicular trafficking, nucleocytosolic shuttling,
CC transcription, chromosome remodeling and cytokinesis (By similarity).
CC {ECO:0000250|UniProtKB:Q9BXF3, ECO:0000269|PubMed:15640247,
CC ECO:0000269|PubMed:20589882, ECO:0000269|PubMed:21246654,
CC ECO:0000269|PubMed:22154806}.
CC -!- SUBUNIT: Component of the CERF-1 ISWI chromatin remodeling complex
CC (also called the CECR2-containing remodeling factor (CERF) complex) at
CC least composed of CECR2 and SMARCA1 (By similarity). Component of the
CC CERF-5 ISWI chromatin remodeling complex at least composed of
CC SMARCA5/SNF2H and CECR2 (By similarity). Within the CERF-1 and CERF-5
CC ISWI chromatin remodeling complexes interacts with SMARCA1 and
CC SMARCA5/SNF2H, respectively (By similarity). Interacts with acetylated
CC lysine residues on histone H2A and H3 (in vitro) (By similarity).
CC Interacts with LRPPRC (By similarity). {ECO:0000250|UniProtKB:Q9BXF3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=E9Q2Z1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E9Q2Z1-2; Sequence=VSP_059110;
CC -!- DEVELOPMENTAL STAGE: In embryos, predominantly expressed in neural
CC tissues (PubMed:15640247). Expressed throughout inner ear development:
CC expressed in the neuroepithelium, head mesenchyme and the cochlear
CC floor (PubMed:21246654). {ECO:0000269|PubMed:15640247,
CC ECO:0000269|PubMed:21246654}.
CC -!- DOMAIN: The Bromo domain recognizes and binds acetylated histones. Also
CC recognizes and binds histones that are butyrylated.
CC {ECO:0000250|UniProtKB:Q9BXF3}.
CC -!- DISRUPTION PHENOTYPE: Perinatal death with high penetrance due to
CC cranial neural tube defects (PubMed:15640247, PubMed:20589882).
CC Exencephaly is frequently associated by open eyelids (PubMed:20589882).
CC Defects may be due to misregulation of mesenchymal/ectodermal
CC transcription factors (PubMed:20589882). Fetuses also show specific
CC inner ear defects, such as smaller cochleae as well as rotational
CC defects of sensory cells and extra cell rows in the inner ear
CC reminiscent of planar cell polarity (PCP) mutants (PubMed:21246654).
CC Mutant males non-penetrant for neural tube defects produce smaller
CC litters: mutants have normal seminiferous epithelium morphology, sperm
CC count, motility and morphology, but the mutant spermatozoa are
CC compromised in their ability to fertilize oocytes (PubMed:22154806).
CC {ECO:0000269|PubMed:15640247, ECO:0000269|PubMed:20589882,
CC ECO:0000269|PubMed:21246654, ECO:0000269|PubMed:22154806}.
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DR EMBL; AC084273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK129435; BAC98245.1; -; mRNA.
DR EMBL; BC060152; AAH60152.1; -; mRNA.
DR CCDS; CCDS51890.1; -. [E9Q2Z1-2]
DR CCDS; CCDS90117.1; -. [E9Q2Z1-1]
DR RefSeq; NP_001121623.1; NM_001128151.1. [E9Q2Z1-2]
DR RefSeq; XP_006506383.1; XM_006506320.1.
DR AlphaFoldDB; E9Q2Z1; -.
DR SMR; E9Q2Z1; -.
DR ComplexPortal; CPX-454; CERF chromatin remodelling complex.
DR STRING; 10090.ENSMUSP00000108306; -.
DR iPTMnet; E9Q2Z1; -.
DR PhosphoSitePlus; E9Q2Z1; -.
DR MaxQB; E9Q2Z1; -.
DR PeptideAtlas; E9Q2Z1; -.
DR PRIDE; E9Q2Z1; -.
DR ProteomicsDB; 280056; -. [E9Q2Z1-1]
DR ProteomicsDB; 280057; -. [E9Q2Z1-2]
DR Antibodypedia; 283; 66 antibodies from 22 providers.
DR Ensembl; ENSMUST00000100993; ENSMUSP00000098556; ENSMUSG00000071226. [E9Q2Z1-1]
DR Ensembl; ENSMUST00000112686; ENSMUSP00000108306; ENSMUSG00000071226. [E9Q2Z1-2]
DR GeneID; 330409; -.
DR KEGG; mmu:330409; -.
DR CTD; 27443; -.
DR MGI; MGI:1923799; Cecr2.
DR VEuPathDB; HostDB:ENSMUSG00000071226; -.
DR eggNOG; KOG1472; Eukaryota.
DR GeneTree; ENSGT00940000160360; -.
DR InParanoid; E9Q2Z1; -.
DR OMA; HQGMRYP; -.
DR OrthoDB; 103411at2759; -.
DR PhylomeDB; E9Q2Z1; -.
DR TreeFam; TF324727; -.
DR BioGRID-ORCS; 330409; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Cecr2; mouse.
DR PRO; PR:E9Q2Z1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; E9Q2Z1; protein.
DR Bgee; ENSMUSG00000071226; Expressed in animal zygote and 132 other tissues.
DR ExpressionAtlas; E9Q2Z1; baseline and differential.
DR Genevisible; E9QA25; MM.
DR GO; GO:0090537; C:CERF complex; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; IDA:MGI.
DR GO; GO:0031010; C:ISWI-type complex; IPI:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0090102; P:cochlea development; IMP:MGI.
DR GO; GO:0097194; P:execution phase of apoptosis; ISO:MGI.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IMP:MGI.
DR GO; GO:0001842; P:neural fold formation; IMP:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0021915; P:neural tube development; IMP:MGI.
DR GO; GO:0007338; P:single fertilization; IMP:MGI.
DR Gene3D; 1.20.920.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR029614; CECR2.
DR PANTHER; PTHR47092; PTHR47092; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Bromodomain; Chromatin regulator; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1453
FT /note="Chromatin remodeling regulator CECR2"
FT /id="PRO_0000441775"
FT DOMAIN 431..501
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 170..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..851
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..905
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..948
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1368
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXF3"
FT MOD_RES 526
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXF3"
FT MOD_RES 983
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXF3"
FT MOD_RES 1166
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1172
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXF3"
FT VAR_SEQ 601..628
FT /note="Missing (in isoform 2)"
FT /id="VSP_059110"
SQ SEQUENCE 1453 AA; 161530 MW; BCD9BA085DC40814 CRC64;
MCPEEGGAAG LGELRSWWEV PAIAHFCSLF RTAFRLPDFE IEELEAALHR DDVEFISDLI
ACLLQGCYQR RDITPQTFHS YLEDIINYRW ELEEGKPNPL REASFQDLPL RTRVEILHRL
CDYRLDADDV FDLLKGLDAD SLRVEPLGED NSGALYWYFY GTRMYKEDPV QGRSNGELSL
CRESERQKNV SNVPGKTGKR RGRPPKRKKL QEEIISSEKQ EENSLTSDLQ TRNGSRGPGQ
GTWWLLCQTE EEWRQVTESF RERTSLRERQ LYKLLSEDFL PEICNMIAQK GKRPQRTKPE
LQHRFMSDHL SIKSIKLEET PMLTKIEKQK RREEEEERQL LLAVQKKEQE QMLKEERKRE
MEEKVKAVED RAKRRKLREE RAWLLAQGKE LPPELSHLDL NSPMREGKKT KDLFELDDDF
TAMYKVLDVV KAHKDSWPFL EPVDESYAPN YYQIIKIPMD ISSMEKKLNG GLYCNKEEFV
NDMKTMFRNC RKYNGDSSEY TKMSDNLERC FHRAMTKHFP GEDGDTDEEF WIKEDEKREK
RRSRSGRSSG SHVWTRSRDT EGSSRKQPPV ENGGKSLPPA RRAASSGDDQ SRSSIQLPPE
VGTSHGQGFS RPLHCGRVPS HAPPLNQMRP AAPGTFGSLQ GSDPTNLHGS SRIPEAPPGE
PLQHPPFAIQ APVGISNHRG SLLSAPDLSN MGSHVPSLQL GQMNCPSQDG NMYPPAPFQA
GFIPSRHGGT PARPPDFPES SEIPPGHIYH SYKYLNRAHP AVWNGNHGTT NPGRLGPDEK
PHLGPGPSHH PHTLGHMMDG RVMRQPIPPN QWTKQSSFLP HGVPSSGYMQ PPCKSAGHRL
QPPPTPAPSP RFRGPSQALR GAQGGESMMD SPEMIAMQQL SSRVCPPGVP YHPRQPTPPQ
LPGPFPQVAH SASVCVSAPK PALDNPGSTQ EMTETHEPEE DPAEPLPGHE EKAASICSSE
GVYLKQLPHP APPLQASCTR QSSPQERETE DSQLKSDASD SADTYKTSKN KNTWPLDNSY
SSPAVQGCLR DLSIVAETGN LPENGVVGEA SPCRSEGKGL DGSGSEKPLC PRGKTLQEAV
PCTGPNATTP PCTDPSLMAA TVNQFSPLYM PGIEYSNSAT QYPMSPSLQG LASMMGGKSS
GSQPQSFPPR GFQANGPHPG LFPRYRPQQG MRYSYQPPSQ PSYHPYQRTP YYTCPQGFSD
WQRSLPSQRS PSGPPGSHPP RSLFSEKNVL SSLQGCETLN TALTSPTQMD VVTAKVVPPD
GHNSGPEEEK MDESVERPES PKEFLDLDNH NAATKRQNSL STSDYLYGTP PPSLSSGMTF
GSSAFPPHSV MLQTGSPYTP QRSASHFQPR AYPSPVPAHP PPHPVATQPN GLSPEDSLYC
CQEEGLGHFQ ASMMEQTGTG SGLRGSFQEV HRPPGLQMHP VQSQSLFPKT PAPAASPEQL
PPHKTPTLPL DQS
