ID A0A455CA75_PHYMC Unreviewed; 1216 AA.
AC A0A455CA75;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=MYND-type zinc finger-containing chromatin reader ZMYND8 isoform X1 {ECO:0000313|RefSeq:XP_028354191.1};
GN Name=ZMYND8 {ECO:0000313|RefSeq:XP_028354191.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028354191.1};
RN [1] {ECO:0000313|RefSeq:XP_028354191.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028354191.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_028354191.1; XM_028498390.2.
DR AlphaFoldDB; A0A455CA75; -.
DR STRING; 9755.ENSPCTP00005012916; -.
DR Ensembl; ENSPCTT00005014292; ENSPCTP00005012916; ENSPCTG00005007132.
DR KEGG; pcad:102986818; -.
DR InParanoid; A0A455CA75; -.
DR OrthoDB; 764287at2759; -.
DR Proteomes; UP000248484; Chromosome 14.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0090734; C:site of DNA damage; IEA:Ensembl.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IEA:Ensembl.
DR GO; GO:0035064; F:methylated histone binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0071168; P:protein localization to chromatin; IEA:Ensembl.
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
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 1030..1064
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 977..1026
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..38
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..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1216 AA; 134979 MW; 4BDE77891E65F971 CRC64;
MWSCVSLSDP GSTERTAQKR KFPSPPHSSN GHSPQDTSTS PIKKKKKPGL LNNNNKEQSE
LRHGPFYYMK QPLTTDPVDV VPQDGRNDFY 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 PSNPSAGAAK IDKQEKVKLN FDMTASPKIL MSKPMLSGGT
GRRISLSDMP RSPMSTNSSV HTGSDVEQDA EKKATSSHFS ASEESMDFLD KSTASPASTK
TGQAGSLSGS PKPFSPQVST PITTKTDKTS TTGSILNLNL DRSKAEMDLK ELSESVQQQS
APVPLISPKR QIRSRFQLNL DKTIESCKAQ LGINEISEDV YTAVEHSDSE DSEKSDSSGS
DSISDEEQRS KNEPEDAEDK EDARMDKEPS AVKKKPKLSN PMETKEELKV STSPASEKAD
PGLVKEKTSP QPEKDFSDKA KPLPHPTKDK LKGKDETDSP TVHLGLDSDS ESELVIDLGE
DHSGREGRKN KKEPKEPSPK QEVVGKAPPS TTAGSQSPPE TPVLTRSSAQ TPTAGVTATT
STTSTVTAPA AAATGSPVKK QRPLLPKETA PAVQRVVWNS SSKFQTSSQK WHMQKMQRQQ
QQQNQQQNQQ QNQQPQSSQG TRYQTRQAVK AVQQKEITQS PSTSTITLVT STQSSPLVTS
SGSTSTLASS VSADLPIATA SADVAADIAK YTSKMMDAIK GTMTEIYNDL SKNTTGSTIA
EIRRLRIEIE KLQWLHQQEL SEMKHNLELT MAEMRQSLEQ ERDRLIAEVK KQLELEKQQA
VDETKKKQWC ANCKKEAIFY CCWNTSYCDY PCQQAHWPEH MKSCTQSATA PQQEADAEVN
TETLNKSNQG TSSNTQAAPP ETSSSKEKET PAEKSKDSGS TLDLSGSRET PSSILLGSNQ
GSVSNRCDKQ PASVPTSTDH QPHPSYPAQK YHSRSSKSSC WSGSDEKRGS ARSEHTASTS
SKSLIPKESR LDTFWD
//
