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   27-MAR-2024, entry version 136.
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; 3.
DR   MINT; Q8CID0; -.
DR   STRING; 10090.ENSMUSP00000028911; -.
DR   iPTMnet; Q8CID0; -.
DR   PhosphoSitePlus; Q8CID0; -.
DR   EPD; Q8CID0; -.
DR   MaxQB; Q8CID0; -.
DR   PaxDb; 10090-ENSMUSP00000028911; -.
DR   ProteomicsDB; 285211; -.
DR   Antibodypedia; 24530; 187 antibodies from 23 providers.
DR   DNASU; 228714; -.
DR   Ensembl; ENSMUST00000028911.15; ENSMUSP00000028911.9; ENSMUSG00000027425.19.
DR   GeneID; 228714; -.
DR   KEGG; mmu:228714; -.
DR   UCSC; uc008mqy.2; mouse.
DR   AGR; MGI:1917264; -.
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; PRRNWPW; -.
DR   OrthoDB; 26652at2759; -.
DR   PhylomeDB; Q8CID0; -.
DR   TreeFam; TF324809; -.
DR   Reactome; R-MMU-9772755; Formation of WDR5-containing histone-modifying complexes.
DR   BioGRID-ORCS; 228714; 7 hits in 77 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 221 other cell types or tissues.
DR   ExpressionAtlas; Q8CID0; baseline and differential.
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; NAS: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:0000122; P:negative regulation of transcription by RNA polymerase II; 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:0006355; P:regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0045995; P:regulation of embryonic development; IDA:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0090043; P:regulation of tubulin deacetylation; ISO:MGI.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.90.980.20; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   PANTHER; PTHR20916; CYSTEINE AND GLYCINE-RICH PROTEIN 2 BINDING PROTEIN; 1.
DR   PANTHER; PTHR20916:SF26; CYSTEINE-RICH PROTEIN 2-BINDING PROTEIN; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51186; GNAT; 1.
DR   Genevisible; Q8CID0; MM.
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
//