ID G3SJ72_GORGO Unreviewed; 630 AA.
AC G3SJ72;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=Mbt domain containing 1 {ECO:0000313|Ensembl:ENSGGOP00000028162.2};
GN Name=MBTD1 {ECO:0000313|Ensembl:ENSGGOP00000028162.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000028162.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000028162.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000028162.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000028162.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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 EMBL; CABD030037192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030037193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_018883391.1; XM_019027846.1.
DR AlphaFoldDB; G3SJ72; -.
DR STRING; 9593.ENSGGOP00000028162; -.
DR Ensembl; ENSGGOT00000025817.2; ENSGGOP00000028162.2; ENSGGOG00000003708.3.
DR KEGG; ggo:101153709; -.
DR eggNOG; KOG3766; Eukaryota.
DR GeneTree; ENSGT00940000153840; -.
DR InParanoid; G3SJ72; -.
DR OMA; NTDCNLP; -.
DR OrthoDB; 5405166at2759; -.
DR TreeFam; TF316498; -.
DR Proteomes; UP000001519; Chromosome 5.
DR Bgee; ENSGGOG00000003708; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:Ensembl.
DR GO; GO:0000786; C:nucleosome; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR GO; GO:0062060; F:NuA4 histone acetyltransferase complex binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR CDD; cd20120; MBT_MBTD1_rpt1; 1.
DR CDD; cd20123; MBT_MBTD1_rpt2; 1.
DR CDD; cd20126; MBT_MBTD1_rpt3; 1.
DR CDD; cd20129; MBT_MBTD1_rpt4; 1.
DR Gene3D; 2.30.30.140; -; 4.
DR Gene3D; 3.30.60.160; -; 1.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR012313; Znf_FCS.
DR InterPro; IPR038603; Znf_FCS_sf.
DR PANTHER; PTHR12247:SF79; MBT DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR12247; POLYCOMB GROUP PROTEIN; 1.
DR Pfam; PF02820; MBT; 4.
DR Pfam; PF21319; zf-FCS_1; 1.
DR SMART; SM00561; MBT; 4.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 4.
DR PROSITE; PS51079; MBT; 4.
DR PROSITE; PS51024; ZF_FCS; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00367}.
FT DOMAIN 45..80
FT /note="FCS-type"
FT /evidence="ECO:0000259|PROSITE:PS51024"
FT REPEAT 143..247
FT /note="MBT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT REPEAT 255..351
FT /note="MBT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT REPEAT 353..458
FT /note="MBT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT REPEAT 466..562
FT /note="MBT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 70748 MW; E3B63F491214A654 CRC64;
MFDGYDSCSE DTSSSSSSEE SEEEVAPLPS NLPIIKNNGQ VYTYPDGKSG MATCEMCGMV
GVRDAFYSKT KRFCSVSCSR SYSSNSKKAS ILARLQVTGK PPTKKAKVLQ KQPLVAKLAA
YAQYQATLQN QAKTKAAVSM EGFSWGNYIN SNSFIAAPVT CFKHAPMGTC WGDISENVRV
EVPNTDCSLP TKVFWIAGIV KLAGYNALLR YEGFENDSGL DFWCNICGSD IHPVGWCAAS
GKPLVPPRTI QHKYTNWKAF LVKRLTGAKT LPPDFSQKVS ESMQYPFKPC MRVEVVDKRH
LCRTRVAVVE SVIGGRLRLV YEESEDRTDD FWCHMHSPLI HHIGWSRSIG HRFKRSDITK
KQDGHFDTPP HLFAKVKEVD QSGEWFKEGM KLEAIDPLNL STICVATIRK VLADGFLMIG
IDGSEAADGS DWFCYHATSP SIFPVGFCEI NMIELTPPRG YTKLPFKWFD YLRETGSIAA
PVKLFNKDVP NHGFRVGMKL EAVDLMEPRL ICVATVTRII HRLLRIHFDG WEEEYDQWVD
CESPDLYPVG WCQLTGYQLQ PPASQSSREN QSASSKQKKK AKSQQYKGHK KMTTLQLKEE
LLDGEDYNFL QGASDQESNG SANFYIKQEP
//