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 26-FEB-2020, entry version 86. 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). CC -!- FUNCTION: May be involved in transcriptional regulation. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. 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 SMR; B2RRE4; -. DR STRING; 10090.ENSMUSP00000061753; -. DR iPTMnet; B2RRE4; -. DR PhosphoSitePlus; B2RRE4; -. DR jPOST; B2RRE4; -. DR MaxQB; B2RRE4; -. DR PaxDb; B2RRE4; -. DR PeptideAtlas; B2RRE4; -. DR PRIDE; B2RRE4; -. DR MGI; MGI:2140750; Zfp518b. DR eggNOG; KOG1721; Eukaryota. DR eggNOG; COG5048; LUCA. 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:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR SMART; SM00355; ZnF_C2H2; 4. DR SUPFAM; SSF57667; SSF57667; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2. PE 2: Evidence at transcript level; KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome; KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc; KW 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 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 //