ID A0A2K6CEE2_MACNE Unreviewed; 1186 AA.
AC A0A2K6CEE2;
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:ENSMNEP00000022033.1};
GN Name=ZMYND8 {ECO:0000313|Ensembl:ENSMNEP00000022033.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000022033.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000022033.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A2K6CEE2; -.
DR Ensembl; ENSMNET00000046285.1; ENSMNEP00000022033.1; ENSMNEG00000033850.1.
DR GeneTree; ENSGT00940000154897; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000033850; Expressed in pituitary gland 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:UP000233120};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 88..133
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 165..235
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 277..327
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1028..1062
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 18..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 975..1024
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 18..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1186 AA; 131640 MW; 02818005A4830460 CRC64;
MFSSLQKSFD LAEEEIKTEQ EVVEGMDIST RSKDPGSAER TAQKRKFPSP PHSSNGHSPQ
DTSTSPIKKK KKPGLLNSNN KEQDGRNDFY CWVCHREGQV LCCELCPRVY HAKCLRLTSE
PEGDWFCPEC EKITVAECIE TQSKAMTMLT IEQLSYLLKF AIQKMKQPGT DAFQKPVPLE
QHPDYAEYIF HPMDLCTLEK NAKKKMYGCT EAFLADAKWI LHNCIIYNGG NHKLTQIAKV
VIKICEHEMN EIEVCPECYL AACQKRDNWF CEPCSNPHPL VWAKLKGFPF WPAKALRDKD
GQVDARFFGQ HDRAWVPINN CYLMSKEIPF SVKKTKSIFN SAMQEMEVYV ENIRRKFGVF
NYSPFRTPYT PNSQYQMLLD PTNPSAGTAK IDKQEKVKLN FDMTASPKIL MSKPVLSGGT
GRRISLSDMP RSPMSTNSSV HTGSDVEQDA EKKATSSHFS ASEESMDFLD KSTASPASTK
TGQAGSLSGS PKPFSPQLST PITTKTDKTS TTGSILNLNL DRSKAEMDLK ELSESVQQQS
TPVPLISPKR QIRSRFQLNL DKTIESCKAQ LGINEISEDV YTAVEHSDSE DSEKSDSSDS
EYISDDEQKS KNEPEDTEDK EGCRMDKEPS AVKKKPKPTN PVEIKEELKS TSPASEKTDP
GAVKDKASPE PEKDFSEKAK PSPHPTKDKL KGKDETDSPT VHLGLDSDSE SELVIDLGED
HSGREGRKNK KEPKEPSPKQ DVVGKAPPST TAGSQSPPET PVLTRSSAQT PAAGATATTS
TSSTVTVTAP APATTGSPVK KQRPLLPKET APAVQRVVWN SSSKFQTSSQ KWHMQKMQRQ
QQQQQQQNQQ QQPQSSQGTR YQTRQAVKAV QQKEITQSPS TSTITLVTST QSSPLVTSSG
STSTLVSSVN ADLPIATASA DVAADIAKYT SKMMDAIKGT MTEIYNDLSK NTTGSTIAEI
RRLRIEIEKL QWLHQQELSE MKHNLELTMA EMRQSLEQER DRLIAEVKKQ LELEKQQAVD
ETKKKQWCAN CKKEAIFYCC WNTSYCDYPC QQAHWPEHMK SCTQSATAPQ QEADAEVNTE
TLNKSSQGSS SSTQSAPSET ASASKEKETS TEKSKDSGST LDLSGSRETP SSILLGSNQG
SDHSRSSKSS WSSSDEKRGS TRAEHNSSTS TKSLLPKESR LDTFWD
//
