ID E9Q8D1_MOUSE Unreviewed; 1199 AA.
AC E9Q8D1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 2.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Zinc finger, MYND-type containing 8 {ECO:0000313|Ensembl:ENSMUSP00000104889.5};
GN Name=Zmynd8 {ECO:0000313|Ensembl:ENSMUSP00000104889.5,
GN ECO:0000313|MGI:MGI:1918025};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000104889.5, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:17242355}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [2] {ECO:0007829|PubMed:19144319}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000104889.5, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000104889.5,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5] {ECO:0007829|PubMed:23806337}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6] {ECO:0000313|Ensembl:ENSMUSP00000104889.5}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000104889.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; NP_001239514.1; NM_001252585.1.
DR AlphaFoldDB; E9Q8D1; -.
DR SMR; E9Q8D1; -.
DR jPOST; E9Q8D1; -.
DR MaxQB; E9Q8D1; -.
DR ProteomicsDB; 345337; -.
DR Antibodypedia; 13294; 225 antibodies from 30 providers.
DR DNASU; 228880; -.
DR Ensembl; ENSMUST00000109266.11; ENSMUSP00000104889.5; ENSMUSG00000039671.19.
DR GeneID; 228880; -.
DR UCSC; uc008nya.2; mouse.
DR AGR; MGI:1918025; -.
DR CTD; 23613; -.
DR MGI; MGI:1918025; Zmynd8.
DR VEuPathDB; HostDB:ENSMUSG00000039671; -.
DR GeneTree; ENSGT00940000154897; -.
DR OrthoDB; 764287at2759; -.
DR BioGRID-ORCS; 228880; 15 hits in 85 CRISPR screens.
DR ChiTaRS; Zmynd8; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000039671; Expressed in metanephric loop of Henle and 252 other cell types or tissues.
DR ExpressionAtlas; E9Q8D1; baseline and differential.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0090734; C:site of DNA damage; ISO:MGI.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISO:MGI.
DR GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0098815; P:modulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI.
DR GO; GO:1902952; P:positive regulation of dendritic spine maintenance; ISO:MGI.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISO:MGI.
DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; ISO:MGI.
DR GO; GO:0071168; P:protein localization to chromatin; ISO:MGI.
DR GO; GO:1902897; P:regulation of postsynaptic density protein 95 clustering; ISO:MGI.
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 1: Evidence at protein level;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|EPD:E9Q8D1,
KW ECO:0007829|MaxQB:E9Q8D1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 108..153
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 185..255
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 297..347
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1008..1042
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 940..1004
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1199 AA; 131911 MW; 074431EC348C63CE CRC64;
MSAAGSLLLS SFGTEEPGSL SGQAASMADP VSTEKTAPKR RFPSPPHSSN GHSPQDSSTS
PIKKKKKPGL LNSSNKEQSE 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 HDRAWVPVNN CYLMSKEIPF SVKKTKSIFN
SAMQEMEVYV ENIRRKFGVF NYSPFRTPYT PNNQYQMLLD PSNPSAGTAK TDKQEKVKLN
FDMTASPKIL LSKPLLSGGA GRRISLSDMP RSPTSTNSSV HTGSDVEQDP EKKAPSSHFS
ASEESMDFLD KSTASPASTK TGQAGSLSGS PKPFSPQAPT PIMTKPDKTS TSTTGSILNL
NLDRSKAEMD LKELSESVQQ QSAPVPLISP KRQIRSRFQL NLDKTIESCK AQLGINEISE
DVYTAVEHSD SEDSEKSESS DSEYVSDEEQ KPKNEPEDPE DKEGSRVDKE APAIKRKPKP
TNQVEVKEEA KSNSPVSEKP DPTPAKDKAS PEPEKDFVEK AKPSPHPTKD KLKGKDETDS
PTVHLGLDSD SESELVIDLG EDPSGREGRK NKKDPKVPSP KQDAIGKPPP SSTSAGNQSP
PETPVLTRSA TQAPAAGVTV AAATTSTMST VTVTAPATAV TGSPVKKQRP LLPKETVPAV
QRVVWNASTV QQKEVTQSPS TSTITLVTST QPAALVSSSG SASTLASAIN ADLPIATASA
DVAADIAKYT SKMMDAIKGT MTEIYNDLSK NTTGSTIAEI RRLRIEIEKL QWLHQQELAE
MKHNLELTMA EMRQSLEQER DRLIAEVKKQ LELEKQQAVD ETKKKQWCAN CKKEAIFYCC
WNTSYCDYPC QQAHWPEHMK SCTQSATAPQ QEADAEASTE TGNKSSQGNS SNTQSAPSEP
ASAPKEKEAP AEKSKDSSNS TLDLSGSRET PSSMLLGSNQ SSVSKRCDKQ PAYTPTTTDH
QPHPNYPAQK YHSRSSKAGL WSSSEEKRAS SRSEHSGGTS TKNLMPKESR ESRLDAFWD
//
