ID Z518B_MOUSE Reviewed; 1077 AA. AC B2RRE4; Q69ZC1; DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 14-DEC-2022, entry version 92. DE RecName: Full=Zinc finger protein 518B; GN Name=Znf518b; Synonyms=Kiaa1729, Zfp518b; 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; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 102-1077. RC TISSUE=Embryonic tail; RX PubMed=15368895; DOI=10.1093/dnares/11.3.205; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., RA Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 11:205-218(2004). RN [3] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=25680957; DOI=10.1074/mcp.m114.044586; RA Maier V.K., Feeney C.M., Taylor J.E., Creech A.L., Qiao J.W., Szanto A., RA Das P.P., Chevrier N., Cifuentes-Rojas C., Orkin S.H., Carr S.A., RA Jaffe J.D., Mertins P., Lee J.T.; RT "Functional Proteomic Analysis of Repressive Histone Methyltransferase RT Complexes Reveals ZNF518B as a G9A Regulator."; RL Mol. Cell. Proteomics 14:1435-1446(2015). CC -!- FUNCTION: Through its association with the EHMT1-EHMT2/G9A and CC PRC2/EED-EZH2 histone methyltransferase complexes may function in gene CC silencing, regulating repressive post-translational methylation of CC histone tails at promoters of target genes. CC {ECO:0000269|PubMed:25680957}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25680957}. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. 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; BC138368; AAI38369.1; -; mRNA. DR EMBL; BC138369; AAI38370.1; -; mRNA. DR EMBL; AK173245; BAD32523.1; -; mRNA. DR AlphaFoldDB; B2RRE4; -. DR STRING; 10090.ENSMUSP00000061753; -. DR iPTMnet; B2RRE4; -. DR PhosphoSitePlus; B2RRE4; -. DR MaxQB; B2RRE4; -. DR PaxDb; B2RRE4; -. DR PeptideAtlas; B2RRE4; -. DR ProteomicsDB; 302101; -. DR AGR; MGI:2140750; -. DR MGI; MGI:2140750; Zfp518b. DR eggNOG; KOG1721; Eukaryota. DR InParanoid; B2RRE4; -. DR PhylomeDB; B2RRE4; -. DR PRO; PR:B2RRE4; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; B2RRE4; protein. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR SMART; SM00355; ZnF_C2H2; 4. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2. PE 2: Evidence at transcript level; KW Chromatin regulator; DNA-binding; Isopeptide bond; Metal-binding; Nucleus; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..1077 FT /note="Zinc finger protein 518B" FT /id="PRO_0000353095" FT ZN_FING 160..182 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 188..211 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 1039..1061 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 9..35 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 372..397 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 561..585 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 599..622 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 675..739 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 825..852 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 895..914 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 373..391 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 600..622 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 675..695 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 701..715 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CROSSLNK 479 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9C0D4" FT CROSSLNK 847 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9C0D4" FT CROSSLNK 861 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9C0D4" SQ SEQUENCE 1077 AA; 118997 MW; 49508EF4638A6670 CRC64; MKDIGEQLYT TQVNGGPSSL TMSPKQPNRA TRTERQEAQT LLYQGSEAEA ATMTIATCVQ CKSVHKIPTQ DLRKGPGQSQ DTYVCFKCSL RAVPTQLHFV NNNAGAAHVR NETETISSPV NKFKVRNFKP GKYYCDKCRF STKDPLQYRK HTLQHEEIRF ICSHCSYISY TKGEFQRHLV KHTGIFPYRC EYCDYGAIRN DYIVKHRRRV HERAGAKRPF KTVAKLEPKR TSIPKQSMEL SKGPSPRAAF QNKLSDQLSR FSLHANKDKT HNLMLLPELK KYQKDVVCIP NKVTLSEPRE VSLLGNKNVE VEVLSPSKEP VHPGMPLTVM APSELVVPTN CLAQLMDVKV VNGAQQLVLK LFPLEENARL ETSRGDGGTS ECLSTEKGSG GQKKMLSPEA SRSLAVEGNA GDFVGLDRLH SLVQKQLKNV KWVKSCNFFM PNSGVHSQQE SFLGSDTIKE LQKSHSLCPP RALPSAAIKS HSPASVQNSV PYGPGATVSH FLSKAAVAFA DDRRGARSNS QQLLPLASLP SKVPFSGEKG LLPIGESDLE ARNRISRPET LVSSDRKLED KQMESKAVGN TGQVSSVQNK EYLHINITGE DKPRSQQPGD QPGQPKTSET AGATFEGPII SSVFSLSSGS ENVPEAIKWN SSTTKIKSIE LLRRKIAQLI ESCGKPSSLS ANSAQRRSIG QAPKLTSKAT PKAIQEMSVS LTGPGPTPGP SVGPLQKPPN EDSITGSRQL VPQQVCPQFI SANDGKMENR VTRKTPVATP VLIPKGAVLR VLNSSEDAHI IEATCDTPVS IPCSEAQLAG TLPFCPMKQT GSGSQPLTCR SGPADMSPGL ETSLRPKSRK EDTICSATAK KMVPVYSTAP GSSDSIRQGR PVSRNLTVSK NKTKQVNSTK KKNKMQANPG RYFKDPPSFF QVARQLRLIA AKPDQLIKCP RRNQPVIVLN HPDVDSPEVT NVMKVINKYK GNVLKVVLSE RTRCQLGVRR YHMRLTYQNV AETNHMKRQM MLKMKLKKVH KNNYQVVGSM PDDPAQCVFK CWFCGRLYED QEEWMSHGQR HLIEATRDWD VLSSKGK //