ID A0A075B6H4_HUMAN Unreviewed; 781 AA.
AC A0A075B6H4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Cysteine-rich protein 2-binding protein {ECO:0000313|Ensembl:ENSP00000366909};
DE SubName: Full=Lysine acetyltransferase 14 {ECO:0000313|Ensembl:ENSP00000504748.1};
GN Name=KAT14 {ECO:0000313|Ensembl:ENSP00000366909};
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 {ECO:0000313|Ensembl:ENSP00000366909, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000366909, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [2] {ECO:0007829|PubMed:18669648}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [3] {ECO:0007829|PubMed:19608861}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [4] {ECO:0007829|PubMed:23186163}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23186163;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [5] {ECO:0000313|Ensembl:ENSP00000366909}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2014) to UniProtKB.
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DR EMBL; AL050321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF459584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Antibodypedia; 24530; 187 antibodies from 23 providers.
DR Ensembl; ENST00000377681; ENSP00000366909; ENSG00000149474.
DR Ensembl; ENST00000677610.1; ENSP00000504748.1; ENSG00000149474.15.
DR Ensembl; ENST00000688188.1; ENSP00000508684.1; ENSG00000149474.15.
DR MANE-Select; ENST00000688188.1; ENSP00000508684.1; NM_001392073.1; NP_001379002.1.
DR UCSC; uc010zru.3; human.
DR HGNC; HGNC:15904; KAT14.
DR OpenTargets; ENSG00000149474; -.
DR VEuPathDB; HostDB:ENSG00000149474; -.
DR GeneTree; ENSGT00390000001146; -.
DR ChiTaRS; KAT14; human.
DR Proteomes; UP000005640; Chromosome 20.
DR Bgee; ENSG00000149474; Expressed in deltoid and 184 other cell types or tissues.
DR GO; GO:0140672; C:ATAC complex; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0051302; P:regulation of cell division; IEA:Ensembl.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
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.
PE 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|EPD:A0A075B6H4,
KW ECO:0007829|MaxQB:A0A075B6H4};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT DOMAIN 637..781
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 13..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..281
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 399..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..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 403..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 88773 MW; E994CCA6CE3F89CA CRC64;
MDSSIHLSSL ISRHDDEATR TSTSEGLEEG EVEGETLLIV ESEDQASVDL SHDQSGDSLN
SDEGDVSWME EQLSYFCDKC QKWIPASQLR EQLSYLKGDN FFRFTCSDCS ADGKEQYERL
KLTWQQVVML AMYNLSLEGS GRQGYFRWKE DICAFIEKHW TFLLGNRKKT STWWSTVAGC
LSVGSPMYFR SGAQEFGEPG WWKLVHNKPP TMKPEGEKLS ASTLKIKASK PTLDPIITVE
GLRKRASRNP VESAMELKEK RSRTQEAKDI RRAQKEAAGF LDRSTSSTPV KFISRGRRPD
VILEKGEVID FSSLSSSDRT PLTSPSPSPS LDFSAPGTPA SHSATPSLLS EADLIPDVMP
PQALFHDDDE MEGDGVIDPG MEYVPPPAGS VASGPVVGVR KKVRGPEQIK QEVESEEEKP
DRMDIDSEDT DSNTSLQTRA REKRKPQLEK DTKPKEPRYT PVSIYEEKLL LKRLEACPGA
VAMTPEARRL KRKLIVRQAK RDRGLPLFDL DQVVNAALLL VDGIYGAKEG GISRLPAGQA
TYRTTCQDFR ILDRYQTSLP SRKGFRHQTT KFLYRLVGSE DMAVDQSIVS PYTSRILKPY
IRRDYETKPP KLQLLSQIRS HLHRSDPHWT PEPDAPLDYC YVRPNHIPTI NSMCQEFFWP
GIDLSECLQY PDFSVVVLYK KVIIAFGFMV PDVKYNEAYI SFLFVHPEWR RAGIATFMIY
HLIQTCMGKD VTLHVSASNP AMLLYQKFGF KTEEYVLDFY DKYYPLESTE CKHAFFLRLR
R
//
