ID A0A2K5P4H5_CERAT Unreviewed; 1202 AA.
AC A0A2K5P4H5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Zinc finger MYND-type containing 8 {ECO:0000313|Ensembl:ENSCATP00000044611.1};
GN Name=ZMYND8 {ECO:0000313|Ensembl:ENSCATP00000044611.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000044611.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000044611.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A2K5P4H5; -.
DR Ensembl; ENSCATT00000069053.1; ENSCATP00000044611.1; ENSCATG00000044267.1.
DR GeneTree; ENSGT00940000154897; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000044267; Expressed in bone marrow and 12 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd05508; Bromo_RACK7; 1.
DR CDD; cd15538; PHD_PRKCBP1; 1.
DR CDD; cd20160; PWWP_PRKCBP1; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
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; IPR044075; PRKCBP1_PHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR021931; ZMYND8.
DR InterPro; IPR037967; ZMYND8_Bromo_dom.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR002893; Znf_MYND.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46453; PROTEIN KINASE C-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR46453:SF3; PROTEIN KINASE C-BINDING PROTEIN 1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF12064; DUF3544; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 104..149
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 181..251
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 293..343
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1044..1078
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 991..1040
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1202 AA; 133422 MW; 3969063102AA33D7 CRC64;
ILAEEEIKTE QEVVEGMDIS TRSKDPGSAE RTAQKRKFPS PPHSSNGHSP QDTSTSPIKK
KKKPGLLNSN NKEQSELRHG PFYYMKQPLT TDPVDVVPQD GRNDFYCWVC HREGQVLCCE
LCPRVYHAKC LRLTSEPEGD WFCPECEKIT VAECIETQSK AMTMLTIEQL SYLLKFAIQK
MKQPGTDAFQ KPVPLEQHPD YAEYIFHPMD LCTLEKNAKK KMYGCTEAFL ADAKWILHNC
IIYNGGNHKL TQIAKVVIKI CEHEMNEIEV CPECYLAACQ KRDNWFCEPC SNPHPLVWAK
LKGFPFWPAK ALRDKDGQVD ARFFGQHDRA WVPINNCYLM SKEIPFSVKK TKSIFNSAMQ
EMEVYVENIR RKFGVFNYSP FRTPYTPNSQ YQMLLDPTNP SAGTAKIDKQ EKVKLNFDMT
ASPKILMSKP VLSGGTGRRI SLSDMPRSPM STNSSVHTGS DVEQDAEKKA TSSHFSASEE
SMDFLDKSTA SPASTKTGQA GSLSGSPKPF SPQLSTPITT KTDKTSTTGS ILNLNLDRSK
AEMDLKELSE SVQQQSTPVP LISPKRQIRS RFQLNLDKTI ESCKAQLGIN EISEDVYTAV
EHSDSEDSEK SDSSDSEYIS DDEQKSKNEP EDTEDKEGCR MDKEPSAVKK KPKPTNPVEI
KEELKSTSPA SEKTDPGAVK DKASPEPEKD FSEKAKPSPH PTKDKLKGKD ETDSPTVHLG
LDSDSESELV IDLGEDHSGR EGRKNKKEPK EPSPKQDVVG KAPPSTTAGS QSPPETPVLT
RSSAQTPAAG ATATTSTSST VTVTAPAPAA TGSPVKKQRP LLPKETAPAV QRVVWNSSSK
FQTSSQKWHM QKMQRQQQQQ QQQNQQQQPQ SSQGTRYQTR QAVKAVQQKE ITQSPSTSTI
TLVTSTQSSP LVTSSGSTST LVSSVNADLP IATASADVAA DIAKYTSKMM DAIKGTMTEI
YNDLSKNTTG STIAEIRRLR IEIEKLQWLH QQELSEMKHN LELTMAEMRQ SLEQERDRLI
AEVKKQLELE KQQAVDETKK KQWCANCKKE AIFYCCWNTS YCDYPCQQAH WPEHMKSCTQ
SATAPQQEAD AEVNTETLNK SSQGSSSSTQ SAPSETASAS KEKETSTEKS KDSGSTLDLS
GSRETPSSIL LGSNQGSDHS RSSKSSWSSS DEKRGSARAE HNSSTSTKSL LPKESRLDTF
WD
//
