CSR2B_MOUSE
ID CSR2B_MOUSE Reviewed; 779 AA.
AC Q8CID0; A2ANA8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Cysteine-rich protein 2-binding protein;
DE Short=CSRP2-binding protein;
DE AltName: Full=ADA2A-containing complex subunit 2;
DE Short=ATAC2;
DE AltName: Full=CRP2-binding partner;
DE Short=CRP2BP;
DE AltName: Full=Lysine acetyltransferase 14 {ECO:0000250|UniProtKB:Q9H8E8};
GN Name=Kat14 {ECO:0000250|UniProtKB:Q9H8E8}; Synonyms=Csrp2bp;
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].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=19103755; DOI=10.1128/mcb.01599-08;
RA Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J.,
RA Lill J.R., Zha J.;
RT "The double-histone-acetyltransferase complex ATAC is essential for
RT mammalian development.";
RL Mol. Cell. Biol. 29:1176-1188(2009).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-230 AND LYS-291, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Component of the ATAC complex, a complex with histone
CC acetyltransferase activity on histones H3 and H4. May function as a
CC scaffold for the ATAC complex to promote ATAC complex stability. Has
CC also weak histone acetyltransferase activity toward histone H4.
CC Required for the normal progression through G1 and G2/M phases of the
CC cell cycle (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the LIM 1 domain of CSRP2. Component of the
CC ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L,
CC TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. In the complex, it
CC probably interacts directly with KAT2A, MBIP and WDR5. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Mainly nuclear. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Early embryonic lethality. Severe growth
CC retardation, increased apoptosis, and alterations in the cell cycle.
CC {ECO:0000269|PubMed:19103755}.
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DR EMBL; AL808123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031563; AAH31563.1; -; mRNA.
DR CCDS; CCDS16819.1; -.
DR RefSeq; NP_852082.2; NM_181417.3.
DR AlphaFoldDB; Q8CID0; -.
DR SMR; Q8CID0; -.
DR BioGRID; 230756; 10.
DR ComplexPortal; CPX-1025; GCN5-containing ATAC complex.
DR ComplexPortal; CPX-1029; PCAF-containing ATAC complex.
DR IntAct; Q8CID0; 2.
DR MINT; Q8CID0; -.
DR STRING; 10090.ENSMUSP00000028911; -.
DR iPTMnet; Q8CID0; -.
DR PhosphoSitePlus; Q8CID0; -.
DR EPD; Q8CID0; -.
DR MaxQB; Q8CID0; -.
DR PaxDb; Q8CID0; -.
DR PRIDE; Q8CID0; -.
DR ProteomicsDB; 285211; -.
DR Antibodypedia; 24530; 161 antibodies from 23 providers.
DR DNASU; 228714; -.
DR Ensembl; ENSMUST00000028911; ENSMUSP00000028911; ENSMUSG00000027425.
DR GeneID; 228714; -.
DR KEGG; mmu:228714; -.
DR UCSC; uc008mqy.2; mouse.
DR CTD; 57325; -.
DR MGI; MGI:1917264; Kat14.
DR VEuPathDB; HostDB:ENSMUSG00000027425; -.
DR eggNOG; KOG3138; Eukaryota.
DR GeneTree; ENSGT00390000001146; -.
DR HOGENOM; CLU_022855_0_0_1; -.
DR InParanoid; Q8CID0; -.
DR OMA; RNWPWLQ; -.
DR OrthoDB; 1404086at2759; -.
DR PhylomeDB; Q8CID0; -.
DR TreeFam; TF324809; -.
DR BioGRID-ORCS; 228714; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Kat14; mouse.
DR PRO; PR:Q8CID0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8CID0; protein.
DR Bgee; ENSMUSG00000027425; Expressed in primary oocyte and 218 other tissues.
DR ExpressionAtlas; Q8CID0; baseline and differential.
DR Genevisible; Q8CID0; MM.
DR GO; GO:0140672; C:ATAC complex; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISO:MGI.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:0016573; P:histone acetylation; IMP:MGI.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0051302; P:regulation of cell division; IDA:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IDA:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; ISO:MGI.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR037829; KAT14.
DR PANTHER; PTHR20916:SF0; PTHR20916:SF0; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..779
FT /note="Cysteine-rich protein 2-binding protein"
FT /id="PRO_0000304937"
FT DOMAIN 635..779
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8E8"
FT MOD_RES 230
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8E8"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8E8"
FT CONFLICT 144
FT /note="G -> V (in Ref. 2; AAH31563)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="A -> L (in Ref. 2; AAH31563)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 779 AA; 88217 MW; 6750A26E6DF1B749 CRC64;
MDSSIHLSGL LSRHDDDATR TSTSEGLEEG EVEGETLLIV ESEDQASVDL SHDQSGDSLN
SDEGDVSWME EQLSYFCDKC QKWIPASQLR EQLSYLKGDN FFRFTCCDCS ADGKEQYERL
KLTWQQVVML AMYNLSLEGS GRQGYFRWKE DICAFIEKHW TFLLGNRKKT STWWSTVAGC
LSVGSPVYFR SGAQEFGEPG WWKLVHNRPP TMRPEGEKLA ASTLKVKASK PTLDPIITVE
GLRKRASRNP VESAMELKEK RSRTQEAKDI RRAQKEAAGL LDRSTSSTPV KFISRGRRPD
LILEKGEVID FSSLSSSDRT PLTSPSPSPS LDFSAPGTPA SHSATPSLLS EADLIPDVMP
PQALFHDDDE LEGDGVIDPG MEYIPPPAGS ASGLLGSRKK VRAPEQIKQE VDSEEEKPDR
MDGDSEDTDS NISLHTRARE KRKPPLEKDM KPKGPRYTPV SIYEEKLLLK RLEACPGAVA
MTPEARRLKR KLIVRQAKRD RGLPLFDLDE VVNAALLLVD GIYGAKDGGA SRLAAGQATY
RTTCQDFRIL DRYQTALPAR KGFRHQTTRF LYRLVGSEDL AVDQSIISPY TSRILKPYIR
RDYETKPPKL QLLSQIRSHL HRSDPHWTPG PDAPLDYCYV RPNHIPTINS MCQEFFWPGI
DLSECLQYPD FSVVVLYKKV IVAFGFMVPD VKYNEAYISF LLVHPEWRRA GIATFMIYHL
IQTCMGKDVT LHVSASNPAM LLYQKFGFKT EEYVLDFYDK YYPLESTECK HAFFLRLRR
