Z518A_MOUSE
ID Z518A_MOUSE Reviewed; 1478 AA.
AC B2RRF6; Q9CSF6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Zinc finger protein 518A;
GN Name=Znf518a; Synonyms=Kiaa0335, Zfp518, Zfp518a, Znf518;
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 1-370.
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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:0000305|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; BC138382; AAI38383.1; -; mRNA.
DR EMBL; BC138383; AAI38384.1; -; mRNA.
DR EMBL; AK012959; BAB28569.3; -; mRNA.
DR CCDS; CCDS37982.1; -.
DR RefSeq; NP_082595.1; NM_028319.1.
DR RefSeq; XP_006527431.1; XM_006527368.2.
DR RefSeq; XP_011245661.1; XM_011247359.2.
DR RefSeq; XP_011245662.1; XM_011247360.1.
DR RefSeq; XP_011245663.1; XM_011247361.1.
DR RefSeq; XP_011245665.1; XM_011247363.1.
DR RefSeq; XP_011245666.1; XM_011247364.1.
DR AlphaFoldDB; B2RRF6; -.
DR BioGRID; 215508; 5.
DR STRING; 10090.ENSMUSP00000055956; -.
DR iPTMnet; B2RRF6; -.
DR PhosphoSitePlus; B2RRF6; -.
DR EPD; B2RRF6; -.
DR jPOST; B2RRF6; -.
DR MaxQB; B2RRF6; -.
DR PaxDb; B2RRF6; -.
DR PeptideAtlas; B2RRF6; -.
DR PRIDE; B2RRF6; -.
DR ProteomicsDB; 302100; -.
DR Antibodypedia; 30696; 24 antibodies from 10 providers.
DR Ensembl; ENSMUST00000050092; ENSMUSP00000055956; ENSMUSG00000049164.
DR Ensembl; ENSMUST00000235207; ENSMUSP00000158039; ENSMUSG00000049164.
DR GeneID; 72672; -.
DR KEGG; mmu:72672; -.
DR UCSC; uc008hlk.1; mouse.
DR CTD; 72672; -.
DR MGI; MGI:1919922; Zfp518a.
DR VEuPathDB; HostDB:ENSMUSG00000049164; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162006; -.
DR HOGENOM; CLU_005711_0_0_1; -.
DR InParanoid; B2RRF6; -.
DR OMA; LVTCELC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; B2RRF6; -.
DR TreeFam; TF332842; -.
DR BioGRID-ORCS; 72672; 0 hits in 69 CRISPR screens.
DR ChiTaRS; Zfp518a; mouse.
DR PRO; PR:B2RRF6; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; B2RRF6; protein.
DR Bgee; ENSMUSG00000049164; Expressed in animal zygote and 225 other tissues.
DR Genevisible; B2RRF6; MM.
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; IPR027760; ZNF518A.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24403:SF81; PTHR24403:SF81; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1478
FT /note="Zinc finger protein 518A"
FT /id="PRO_0000349265"
FT ZN_FING 152..174
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 209..231
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 236..258
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 264..287
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1444..1466
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 356..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 359
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 391
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 430
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 521
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 709
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 794
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 884
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 897
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 989
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 1010
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 1043
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 1057
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 1078
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 1116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 1180
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 1441
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CONFLICT 350
FT /note="F -> L (in Ref. 2; BAB28569)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1478 AA; 165604 MW; 3C993056631ADB00 CRC64;
MPFEQTQLFC DEKPTILKKL DTRNEIADTI RSVSTSKISE TSFQYVLKDV NICLPKINIP
NEILMKHEVE KYRLLFQSKP QTARKSISVK TVSCAEECVL LCKSERAEDE TVNMSAKILN
FSCSKCQDST QYSPNDLQKH FEMWHHGELP SFPCEMCSFS ASDFQIFKQH RKTHRNTFVK
CDICNSERSY TLLDLTKHFT SKHCVNGNFQ CEECRFFTQD VGTFVQHIHR HKEVHYKCGK
CHHLCFTKGE LQKHLRVHSG TLPFTCHYCS YGAIHKDQLI RHVITLHKEH LYAKEKLERD
QYDKRVAKTT TTGLKLILKR YKIGPTKTFW KRKTITSGND ESIGKNAQAF NIVSKTQTKS
EDQSQEQVNG EKGEKQHCEN GDKPVESESE KATVLSTGQY NKADEGASTT SSSVLSAVQG
PTVLLVRNNK ITIPANYSAK FMGFKMVDGR QHIVIKLLPA NKQILPSPVL QSNTEKNSTA
NLSPQAVANT GFATGLTTKV NDTDFVKAAP PACSSPVLAR KVISEKEAAF ISEKNNTLQM
VDDSKSLSSL PTTSTTSVRV TTKVEARDNV DLWENDSPQS HPDASDTSIS SPDKVSLTPK
PNAYSSGDMH NYCINYVNSE LPAESSNSFE FSNQGSLPFH NYSKVNNKRR RFSRATLCEN
LQKESPNKTV TQQSTSDSDT ASPLLRKESS NSDNLFASIN PLNGTLKIKT EIEEPYNLEE
TQNFNEQSLF TNENQNLLNV TEEPKWNDIP SAGSPMMPRI TSVFSLQSEQ ASEFLTPEVN
QLLQDTLKPK SDIKEDSNNI PSKNLPFDCD QTLKKSEEVV IKSSKDFQMQ DDIPVPSASV
GVNVPANDLN SKCNGQEKQG LSVLQDVRDS EVTTKIPNII TLLKTQSDAI ITQQLVKDKL
RTTTQNSGPV YVQNPFLTSE QKNPVFVQTP KGFIIPLHVA NKPGLHVFSG RPVPLVNTRS
VPATLLVNKK PGMLLATNNG KPESVPTVKT ENVHSYGTVT KEPCKTPFLK AEHNNSCLTP
GLCSSIGNCV NMKTCSENTL PLKGSYIIKT SVNSSVKAVP NILPEQQGPK MNILDTVKQQ
NENLPKASLY TLMPDGKQAV FFKCVMPNNT KLLKPKLVQS STYQHIQPKR PAGAPQKILV
KIFNPVLSMS AFNNLSASNS ASSFQKEIVP SKPTVHGEQK EPETSRNALP VLVHGLMPAN
ETVHSSTTAC PGSSEEPVYI SERSETRVLR GKANCAVERN FNKRKTCKNK FAKIKTRIDQ
DSETAFVSRN RSCKRKYIDN YQEPPRKKST LNRKGKERAS AEDVQEAFGF SRPRLPKDSS
RTLRLFPFSS KQLVKCPRRN QPVVVLNHPD ADTPEVERVM KTIAKFNGHV LKVSLSQTTI
NALLKPVSNT SETTYNDFSK RQKMLKPVNS VKERFVLKLT LKKTSKNNYQ IVKTTSEDVL
KSQFNCWFCG RVFDNQDVWA GHGQRHLVEA TRDWNMLE
