ID F6V252_CALJA Unreviewed; 1138 AA.
AC F6V252;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Zinc finger MYND-type containing 8 {ECO:0000313|Ensembl:ENSCJAP00000030986.2};
GN Name=ZMYND8 {ECO:0000313|Ensembl:ENSCJAP00000030986.2};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000030986.2, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000030986.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000030986.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; F6V252; -.
DR Ensembl; ENSCJAT00000032744.4; ENSCJAP00000030986.2; ENSCJAG00000016698.5.
DR GeneTree; ENSGT00940000154897; -.
DR Proteomes; UP000008225; Chromosome 5.
DR Bgee; ENSCJAG00000016698; Expressed in cerebellum and 6 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:UP000008225};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 83..128
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 160..230
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 272..322
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 952..986
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 877..948
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1138 AA; 125604 MW; 5349D849178D04A4 CRC64;
MHPQSLAEEE VKAEQEVVEG MDISTRSKDP GSAERTAQKR KFPSPPHSSN GHSPQDTSTS
PIKKKKKPGL LNSNNKEQDG RNDFYCWVCH REGQVLCCEL CPRVYHAKCL RLTSEPEGDW
FCPECEKITV AECIETQSKA MTMLTIEQLS YLLKFAIQKM KQPGTDAFQK PVPLEQHPDY
AEYIFHPMDL CTLEKNAKKK MYGCTEAFLA DAKWILHNCI IYNGGNHKLT QIAKVVIKIC
EHEMNEIEVC PECYLAACQK RDNWFCEPCS NPHPLVWAKL KGFPFWPAKA LRDKDGQVDA
RFFGQHDRAW VPINNCYLMS KEIPFSVKKT KSIFNSAMQE MEVYVENIRR KFGVFNYSPF
RTPYTPNSQY QMLLDPSNPS AGTAKIDKQE KVKLNFDMTA SPKILMSKPV LSGGTGRRIS
LSDMPRSPMS TNSSVHTGSD VEQDAEKKAT SSHFSASEES MDFLDKSTAS PASTKAGQAG
SLSGSPKPFS PQLSTPVTTK MDKTSTTGSI LNLNLDRSKA EMDLKELSES VQQQSTPVPL
ISPKRQIRSR FQLNLDKTIE SCKAQLGINE ISEDVYTAVE HSDSEDSEKS DSSDSEYISD
DEQKAKNEPE DAEDKEGCQL DKEPSAVKKK PKPTNPVEIK EELKSTSPAS EKADPAAVTV
KDKASPEPEK DFSEKAKPSP HPTKDKLKGK DETDSPTVHL GLDSDSESEL VIDLGEDHSG
REGRKNKKEP KAPSPKQDVV GKAPPSTTAG SQSPPETPVL TRSSAQTPAA GATATTSAPS
SVTVTAPAPA AAGSPVKKQR PLLPKETAPA VQRVVWNSST VQQKEITQSP STSTITLVTS
TQSSPLVTSS GSMNTLVSSV NADLPIATAS ADVAADIAKY TSKIRRLRIE IEKLQWLHQQ
ELSEMKHNLE LTMAEMRQSL EQERDRLIAE VKKQLELEKQ QAVDETKKKQ WCANCKKEAI
FYCCWNTSYC DYPCQQAHWP EHMKSCTQSA TAPQQEADAE VNTETLNKSS QGSSSSTQSA
PSETASASKE KETSAEKSKD SGSTLDLSGS RETPSSVLLG SNPGSVSKRC DKQPAYAPTT
TDHQPHPNYP AQKYHSRSSK SSWSSSDEKR GSARSEHNTS TSTKSLLPKE SRLDTFWD
//
