ID H9ER70_MACMU Unreviewed; 1135 AA.
AC H9ER70;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Protein kinase C-binding protein 1 isoform c {ECO:0000313|EMBL:AFE64879.1};
GN Name=ZMYND8 {ECO:0000313|EMBL:AFE64879.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE64879.1};
RN [1] {ECO:0000313|EMBL:AFE64879.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate {ECO:0000313|EMBL:AFE64879.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
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DR EMBL; JU321123; AFE64879.1; -; mRNA.
DR RefSeq; XP_015004374.1; XM_015148888.1.
DR AlphaFoldDB; H9ER70; -.
DR GeneID; 716058; -.
DR CTD; 23613; -.
DR OrthoDB; 764287at2759; -.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; 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 2: Evidence at transcript level;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFE64879.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000313|EMBL:AFE64879.1};
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 977..1011
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..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 924..973
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..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1135 AA; 125446 MW; 41AEDE4B14FF8422 CRC64;
MHPQSLAEEE IKTEQEVVEG 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 QMLLDPTNPS AGTAKIDKQE KVKLNFDMTA SPKILMSKPV LSGGTGRRIS
LSDMPRSPMS TNSSVHTGSD VEQDAEKKAT SSHFSASEES MDFLDKSTAS PASTKTGQAG
SLSGSPKPFS PQLSTPITTK TDKTSTTGSI LNLNLDRSKA EMDLKELSES VQQQSTPVPL
ISPKRQIRSR FQLNLDKTIE SCKAQLGINE ISEDVYTAVE HSDSEDSEKS DSSDSEYISD
DEQKSKNEPE DTEDKEGCRM DKEPSAVKKK PKPTNPVEIK EELKSTSPAS EKTDPGAVKD
KASPEPEKDF SEKAKPSPHP TKDKLKGKDE TDSPTVHLGL DSDSESELVI DLGEDHSGRE
GRKNKKEPKE PSPKQDVVGK APPSTTAGSQ SPPETPVLTR SSAQTPAAGA TATTSTSSTV
TVTAPAPATT GSPVKKQRPL LPKETAPAVQ RVVWNSSTVQ QKEITQSPST ATITLVTSTQ
SSPLVTSSGS TSTLVSSVNA DLPIATASAD VAADIAKYTS KMMDAIKGTM TEIYNDLSKN
TTGSTIAEIR RLRIEIEKLQ WLHQQELSEM KHNLELTMAE MRQSLEQERD RLIAEVKKQL
ELEKQQAVDE TKKKQWCANC KKEAIFYCCW NTSYCDYPCQ QAHWPEHMKS CTQSATAPQQ
EADAEVNTET LNKSSQGSSS STQSAPSETA SASKEKETST EKSKDSGSTL DLSGSRETPS
SILLGSNQGS DHSRSSKSSW SSSDEKRGST RAEHNSSTST KSLLPKESRL DTFWD
//
