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Database: UniProt
Entry: A2A481_MOUSE
LinkDB: A2A481_MOUSE
Original site: A2A481_MOUSE 
ID   A2A481_MOUSE            Unreviewed;       472 AA.
AC   A2A481;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 126.
DE   SubName: Full=Zinc finger, MYND-type containing 8 {ECO:0000313|Ensembl:ENSMUSP00000104885.2};
GN   Name=Zmynd8 {ECO:0000313|Ensembl:ENSMUSP00000104885.2,
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:ENSMUSP00000104885.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000104885.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000104885.2,
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   [2] {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   [3] {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   [4] {ECO:0000313|Ensembl:ENSMUSP00000104885.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000104885.2};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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DR   AlphaFoldDB; A2A481; -.
DR   SMR; A2A481; -.
DR   IntAct; A2A481; 1.
DR   MINT; A2A481; -.
DR   jPOST; A2A481; -.
DR   MaxQB; A2A481; -.
DR   PeptideAtlas; A2A481; -.
DR   ProteomicsDB; 354886; -.
DR   Antibodypedia; 13294; 225 antibodies from 30 providers.
DR   Ensembl; ENSMUST00000109262.8; ENSMUSP00000104885.2; ENSMUSG00000039671.19.
DR   AGR; MGI:1918025; -.
DR   MGI; MGI:1918025; Zmynd8.
DR   VEuPathDB; HostDB:ENSMUSG00000039671; -.
DR   GeneTree; ENSGT00940000154897; -.
DR   HOGENOM; CLU_045990_0_0_1; -.
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; A2A481; 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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; 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; 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   PRINTS; PR00503; BROMODOMAIN.
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; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50812; PWWP; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Proteomics identification {ECO:0007829|EPD:A2A481,
KW   ECO:0007829|MaxQB:A2A481};
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:PRU00146}.
FT   DOMAIN          63..108
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          140..210
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          252..302
FT                   /note="PWWP"
FT                   /evidence="ECO:0000259|PROSITE:PS50812"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   472 AA;  53594 MW;  92D32963EDC37F60 CRC64;
     MDISTRSKDP VSTEKTAPKR RFPSPPHSSN GHSPQDSSTS PIKKKKKPGL LNSSNKEQDG
     RNDFYCWVCH REGQVLCCEL CPRVYHAKCL RLTSEPEGDW FCPECEKITV AECIETQSKA
     MTMLTIEQLS YLLKFAIQKM KQPGTDAFQK PVPLEQHPDY AEYIFHPMDL CTLEKNAKKK
     MYGCTEAFLA DAKWILHNCI IYNGGNHKLT QIAKVVIKIC EHEMNEIEVC PECYLAACQK
     RDNWFCEPCS NPHPLVWAKL KGFPFWPAKA LRDKDGQVDA RFFGQHDRAW VPVNNCYLMS
     KEIPFSVKKT KSIFNSAMQE MEVYVENIRR KFGVFNYSPF RTPYTPNNQY QMLLDPSNPS
     AGTAKTDKQE KVKLNFDMTA SPKILLSKPL LSGGAGRRIS LSDMPRSPTS TNSSVHTGSD
     VEQDPEKKAP SSHFSASEES MDFLDKSTGQ PQLGELGRRP LGAFWRPWMP PS
//
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