ID A0A2K5ICK1_COLAP Unreviewed; 2372 AA.
AC A0A2K5ICK1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000014374.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000014374.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSCANT00000037299.1; ENSCANP00000014374.1; ENSCANG00000030426.1.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:UniProt.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:UniProt.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd05495; Bromo_cbp_like; 1.
DR CDD; cd20910; NCBD_CREBBP-p300_like; 1.
DR CDD; cd15802; RING_CBP-p300; 1.
DR CDD; cd02337; ZZ_CBP; 1.
DR Gene3D; 2.10.110.40; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.10.246.20; Coactivator CBP, KIX domain; 1.
DR Gene3D; 1.10.1630.10; Nuclear receptor coactivator, CREB-bp-like, interlocking domain; 1.
DR Gene3D; 1.20.1020.10; TAZ domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR003101; KIX_dom.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
DR InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_sf.
DR InterPro; IPR010303; RING_CBP-p300.
DR InterPro; IPR038547; RING_CBP-p300_sf.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR PANTHER; PTHR13808:SF29; HISTONE ACETYLTRANSFERASE P300; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF09030; Creb_binding; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF02172; KIX; 1.
DR Pfam; PF06001; RING_CBP-p300; 1.
DR Pfam; PF02135; zf-TAZ; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF47040; Kix domain of CBP (creb binding protein); 1.
DR SUPFAM; SSF69125; Nuclear receptor coactivator interlocking domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF57933; TAZ domain; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS50952; KIX; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00203}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00203};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 294..380
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 529..608
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 1030..1102
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1244..1620
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1622..1670
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1685..1766
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 294..380
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1685..1766
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 445..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1477..1535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1790..1881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1945..1967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2051..2120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2143..2197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2224..2343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..812
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..859
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..992
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1522
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1808..1843
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1866..1881
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1947..1967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2057..2071
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2072..2120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2163..2197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2224..2268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2269..2300
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2320..2343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2372 AA; 260200 MW; E38F72A2E9082697 CRC64;
DFGSLFDLEH DLPDELINST ELGLTNGGDI NQLQTSLGIV QDAASKHKQL SELLRSGSSP
NLNMGVGGPG QVMASQAQQN SPGLGLINSM VKSLTSPNMG MGTSGPNQGP TQSTGMMNSP
VNQPAMGMNT GMNAGMNPGM LAAGNGQGIM PNQVMNGSIG AGRGRQNMQY PNPGMGSAGN
LLTEPLQQGS PQMGGQTGLR GPQPLKMGMM NNPNPYGSPY TQNPGQQIGA SGLGLQIQTK
TVLSNNLSPF AMDKKTVPGG GMPNMGQQPA PQVQQPGLVT PVAQGMGSGA HTADPEKRKL
IQQQLVLLLH AHKCQRREQA NGEVRQCNLP HCRTMKNVLN HMTHCQSGKS CQVAHCASSR
QIISHWKNCT RHDCPVCLPL KNAGDKRNQQ PILTGAPVGL GNPSSLGVGQ QSTPNLSTVS
QIDPSSIERA YAALGLPYQV NQMPTQPQVQ AKNQQNQQPG QSPQGMRPMS NMSASPMGVN
GGVGVQTPSL LSDSMLHSAI NSQNPMMSEN ASVPSLGPMP TAAQPSTTGI RKQWHEDITQ
DLRNHLVHKL VQAIFPTPDP AALKDRRMEN LVAYARKVEG DMYESANNRA EYYHLLAEKI
YKIQKELEEK RRTRLQKQNM LPNAAGMVPV SMNPGPNMGQ PQPGMTSNGP LPDPTMIRGS
VPNQMMPRIT PQSGLNQFGQ MSMAQPPIVP RQTAPLQHHG QLAQPGTLNP PMGYGPRMQQ
PSNQSQFLPQ TQFPSQGMNV TNMPLAPSSG QAPVSQAQMS SSSCPVNSPI MPPGSQGSHI
HCPQLPQPAL HQNSPSPVPS RTPTPHHTPP SIGAQQPPAT TIPAPVPTPP AMPPGPQSQA
LHPPPRQTPT PPPTQLPQQV QPSLPAAPSA DQPQQQPRSQ QSTAASVPTP TAPLLAPQPA
TPLSQPAISI EGQVSNPPST SSTEVNSQAI PEKQPSQEVK MEAKMEVDQP EPADTQPEDI
SESKVEDCKI EPTETEERST ELKTEIKEEE DQPSTSATQS SPAPGQSKKK IFKPEELRQA
LMPTLEALYR QDPESLPFRQ PVDPQLLGIP DYFDIVKSPM DLSTIKRKLD TGQYQEPWQY
VDDIWLMFNN AWLYNRKTSR VYKYCSKLSE VFEQEIDPVM QSLGYCCGRK LEFSPQTLCC
YGKQLCTIPR DATYYSYQNR YHFCEKCFNE IQGESVSLGD DPSQPQTTIN KEQFSKRKND
TLDPELFVEC IECGRKMHQI CVLHHEMIWP FFIVCNDCII SSKSLSLNWL PSTRLGTFLE
NRVNDFLRRQ NHPESGEVTV RVVHASDKTV EVKPGMKARF VDSGEMAESF PYRTKALFAF
EEIDGVDLCF FGMHVQEYGS DCPPPNQRRV YISYLDSVHF FRPKCLRTAV YHEILIGYLE
YVKKLGYTTG HIWACPPSEG DDYIFHCHPP DQKIPKPKRL QEWYKKMLDK AVSERIVHDY
KDIFKQATED RLTSAKELPY FEGDFWPNVL EESIKELEQE EEERKREENT SNESTDVTKG
DSKNAKKKNN KKTSKNKSSL SRGNKKKPGM PNVSNDLSQK LYATMEKHKE VFFVIRLIAG
PTANSLPPIV DPDPLIPCDL MDGRDAFLTL ARDKHLEFSS LRRAQWSTMC MLVELHTQSQ
DRFVYTCNEC KHHVETRWHC TVCEDYDLCI TCYNTKNHDH KMEKLGLGLD DESNNQQAAA
TQSPGDSRRL SIQRCIQSLV HACQCRNANC SLPSCQKMKR VVQHTKGCKR KTNGGCPICK
QLIALCCYHA KHCQENKCPV PFCLNIKQKL RQQQLQHRLQ QAQMLRRRMA SMQRTGVVGQ
QQGLPSPTPA TPTTPTGQQP TTPQTPQPTS QPQPTPPNSM PPYLPRTQAA GPVSQGKAAG
QVTPPTPPQT AQPPLPGPPP AAVEMAMQIQ RAAETQRQMA HVQIFQRPIQ HQMPPMTPMA
PMGMNPPPMT RGPSGHLEPG MGPTGMQQQP PWGQGGLPQP QQLQSGMPRP AMMSVAQHGQ
PLNMAPQPGL GQVGVSPLKP GTVSQQALQN LLRTLRSPSS PLQQQQVLSI LHANPQLLAA
FIKQRAAKYA NSNPQPIPGQ PGMPQGQPGL QPPTMPGQQG VHSNPAMQNM NPMQAGVQRA
GLPQQQPQQQ LQPPMGGMSP QAQQMNMNHN TMPSQFRDIL RRQQMMQQQQ QQGAGPGIGP
GMANHNQFQQ PQGVGYPPQQ QQQRMQHHMQ QMQQGNMGQM GQLPQALGAE AGASLQAYQQ
RLLQQQMGSP AQPNPMSPQQ HMLPNQAQSP HLQGQQIPNS LSNQVRSPQP VPSPRPQSQP
PHSSPSPRMQ PQPSPHHVSP QTSSPHPGLV AAQANPMEQG HFASPDQNSM LSQLASNPGM
ANLHGASATD LGLSTDNSDL NSNLSQSTLD IH
//
