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 27-MAR-2024, entry version 98.
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}.
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DR EMBL; BC138368; AAI38369.1; -; mRNA.
DR EMBL; BC138369; AAI38370.1; -; mRNA.
DR EMBL; AK173245; BAD32523.1; -; mRNA.
DR AlphaFoldDB; B2RRE4; -.
DR STRING; 10090.ENSMUSP00000137381; -.
DR iPTMnet; B2RRE4; -.
DR PhosphoSitePlus; B2RRE4; -.
DR MaxQB; B2RRE4; -.
DR PaxDb; 10090-ENSMUSP00000061753; -.
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; IEA:UniProtKB-SubCell.
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 Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24392; ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR24392:SF41; ZINC FINGER PROTEIN 518B; 1.
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
//
