Z518B_HUMAN
ID Z518B_HUMAN Reviewed; 1074 AA.
AC Q9C0D4; Q96LN8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Zinc finger protein 518B;
GN Name=ZNF518B; Synonyms=KIAA1729;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-1074, AND VARIANTS PRO-105 AND
RP ASN-523.
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 442-1074, AND VARIANT ASN-523.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP FUNCTION.
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).
RN [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-482; LYS-491; LYS-558; LYS-594;
RP LYS-809; LYS-846 AND LYS-860, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
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:0000250|UniProtKB:B2RRE4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:B2RRE4}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AC110768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB051516; BAB21820.1; -; mRNA.
DR EMBL; AK058072; BAB71650.2; -; mRNA.
DR CCDS; CCDS33960.1; -.
DR RefSeq; NP_444270.2; NM_053042.2.
DR RefSeq; XP_005248250.1; XM_005248193.2.
DR RefSeq; XP_016864273.1; XM_017008784.1.
DR RefSeq; XP_016864274.1; XM_017008785.1.
DR RefSeq; XP_016864275.1; XM_017008786.1.
DR AlphaFoldDB; Q9C0D4; -.
DR BioGRID; 124544; 8.
DR IntAct; Q9C0D4; 10.
DR STRING; 9606.ENSP00000317614; -.
DR iPTMnet; Q9C0D4; -.
DR PhosphoSitePlus; Q9C0D4; -.
DR BioMuta; ZNF518B; -.
DR DMDM; 166979949; -.
DR EPD; Q9C0D4; -.
DR MassIVE; Q9C0D4; -.
DR MaxQB; Q9C0D4; -.
DR PaxDb; Q9C0D4; -.
DR PeptideAtlas; Q9C0D4; -.
DR PRIDE; Q9C0D4; -.
DR ProteomicsDB; 80013; -.
DR Antibodypedia; 22893; 16 antibodies from 7 providers.
DR DNASU; 85460; -.
DR Ensembl; ENST00000326756.4; ENSP00000317614.3; ENSG00000178163.8.
DR GeneID; 85460; -.
DR KEGG; hsa:85460; -.
DR MANE-Select; ENST00000326756.4; ENSP00000317614.3; NM_053042.3; NP_444270.2.
DR UCSC; uc003gmn.4; human.
DR CTD; 85460; -.
DR DisGeNET; 85460; -.
DR GeneCards; ZNF518B; -.
DR HGNC; HGNC:29365; ZNF518B.
DR HPA; ENSG00000178163; Low tissue specificity.
DR MIM; 617734; gene.
DR neXtProt; NX_Q9C0D4; -.
DR OpenTargets; ENSG00000178163; -.
DR PharmGKB; PA162410199; -.
DR VEuPathDB; HostDB:ENSG00000178163; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160595; -.
DR HOGENOM; CLU_015341_0_0_1; -.
DR InParanoid; Q9C0D4; -.
DR OMA; PEGIKWN; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9C0D4; -.
DR TreeFam; TF332842; -.
DR PathwayCommons; Q9C0D4; -.
DR SignaLink; Q9C0D4; -.
DR BioGRID-ORCS; 85460; 10 hits in 1082 CRISPR screens.
DR ChiTaRS; ZNF518B; human.
DR GenomeRNAi; 85460; -.
DR Pharos; Q9C0D4; Tdark.
DR PRO; PR:Q9C0D4; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9C0D4; protein.
DR Bgee; ENSG00000178163; Expressed in cardiac muscle of right atrium and 172 other tissues.
DR ExpressionAtlas; Q9C0D4; baseline and differential.
DR Genevisible; Q9C0D4; HS.
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; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein 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..1074
FT /note="Zinc finger protein 518B"
FT /id="PRO_0000317255"
FT ZN_FING 162..184
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 190..213
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1036..1058
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 12..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 482
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 491
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 558
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 594
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 809
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 846
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 860
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 92
FT /note="G -> S (in dbSNP:rs10007352)"
FT /id="VAR_061955"
FT VARIANT 105
FT /note="S -> P (in dbSNP:rs10016702)"
FT /evidence="ECO:0000269|PubMed:11214970"
FT /id="VAR_038491"
FT VARIANT 523
FT /note="S -> N (in dbSNP:rs9291410)"
FT /evidence="ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_038492"
FT CONFLICT 452
FT /note="K -> E (in Ref. 3; BAB71650)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1074 AA; 119531 MW; C61B56FE1A3EB7CB CRC64;
MKDIGQQLYT THLNGGHNSL TMSPKQPDAN GAPRPNRQEA QTLLYQGSEA EAAMMTIATC
AKCKSVHKIS LQDLQKGTGK DGMYVCFQCS LGAAPPNFHF VSNNSSATHV GNKTENFSSS
VNSKFKVRNF KPGKYYCDKC RFSTKDPLQY KKHTLQHEEI KFICSHCSYI SYTKGEFQRH
LVKHTGIFPY QCEYCDYGAI RNDYIVKHTK RVHERAGAKR PVKAVAKLEP KRTGTSKQNP
ELLKASNPRT TFQNKWSDQL SGFSLHANKD KMHNIMLLPE PKEYQKDVVC IPNKMTLSEP
NEVNLFENKN VEVEVLSPAK EPVQPGMPLT VVAPAELVVP ANCLAQLIDV KVVNGTQQLV
LKLFPLEENN CLEAGRDNGG NSERMVKEKG SNEQEKVLSA EKTKSLTVDG NVGKLVGIDS
FQPSVQKQLK NVKWVRSYDF IMPNSSVHNN GKSFINSETI EDFQKKNNLY PHRTAFPSVA
LKGHSLASVF KNSVLRSLGA ASNPFPYKAA VCFAESGRNL HSSSQQLLPF AASPATCSFS
GEKGLLPVSE NDLESTSKVN IPVKVVSSNR KQEDNQTEEH KAVSTVGQIS SQHKSEYLHI
NITGEDRSQQ PGDKPLELKN SERTNNTNDG PVISSVFSLS SGSENVPEGI KWNSSTSKIK
SIELLRRKIA QLIESCGKPS SLASNSAHRR SVGQASKGTS KATSEGIQEI NVSLTGLGHS
TGTLQKPPND GGITGNRQLT HQQIYPHFAD GSNRKTKSRV ARKAHVATPV LIPKGAVLRV
LNSSENAHII EATCEAPVSI PCSERQLIKP VPFCPVRQAD SDLQPLRSER GPIDMSPNIE
TPLRPKLRKE SAVCSTIHRK TGLLYGQQGS SELNKQGRLL SRSLSISRNK TKQVHLSRKK
NKIQAEPSRC LKDPSIFQVA RQLRLIAAKP DQLIKCPRRN QPVIVLNHPD VDSPEVTNVM
KVINKYKGNV LKVVLSERTR CQLGIRRHHV RLTYQNAEEA SQIKRQMMLK MKLKKVHKNN
YQVVDSLPDD SSQCVFKCWF CGRLYEDQEE WMSHGQRHLI EATRDWDVLS SKGK
