Z518A_RAT
ID Z518A_RAT Reviewed; 1478 AA.
AC Q499R0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Zinc finger protein 518A;
GN Name=Znf518a; Synonyms=Zfp518, Zfp518a, Znf518;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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).
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:B2RRF6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:B2RRF6}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; BC099801; AAH99801.1; -; mRNA.
DR RefSeq; NP_001025209.1; NM_001030038.1.
DR RefSeq; XP_006231459.1; XM_006231397.3.
DR RefSeq; XP_006231460.1; XM_006231398.3.
DR RefSeq; XP_008758662.1; XM_008760440.2.
DR RefSeq; XP_017444785.1; XM_017589296.1.
DR AlphaFoldDB; Q499R0; -.
DR STRING; 10116.ENSRNOP00000051600; -.
DR CarbonylDB; Q499R0; -.
DR iPTMnet; Q499R0; -.
DR PhosphoSitePlus; Q499R0; -.
DR PaxDb; Q499R0; -.
DR PRIDE; Q499R0; -.
DR Ensembl; ENSRNOT00000054717; ENSRNOP00000051600; ENSRNOG00000036592.
DR Ensembl; ENSRNOT00000097947; ENSRNOP00000092189; ENSRNOG00000036592.
DR Ensembl; ENSRNOT00000098938; ENSRNOP00000096129; ENSRNOG00000036592.
DR Ensembl; ENSRNOT00000105629; ENSRNOP00000095709; ENSRNOG00000036592.
DR Ensembl; ENSRNOT00000111652; ENSRNOP00000080397; ENSRNOG00000036592.
DR GeneID; 309478; -.
DR KEGG; rno:309478; -.
DR UCSC; RGD:1305314; rat.
DR CTD; 72672; -.
DR RGD; 1305314; Zfp518a.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162006; -.
DR HOGENOM; CLU_005711_0_0_1; -.
DR InParanoid; Q499R0; -.
DR OMA; LVTCELC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q499R0; -.
DR TreeFam; TF332842; -.
DR PRO; PR:Q499R0; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000036592; Expressed in thymus and 19 other tissues.
DR Genevisible; Q499R0; RN.
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_0000349266"
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 355..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 358
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 390
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 428
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 518
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 707
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 792
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 882
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 895
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 987
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 1008
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 1041
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6AHZ1"
FT CROSSLNK 1055
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 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"
SQ SEQUENCE 1478 AA; 165539 MW; 7D5A04C646980C6F CRC64;
MPFEQTQLFC DEKQTILKKI DTRNEIPDTI KSIPIPKISE AGFHYEPKNV NICLPKINIP
NEILMKHEVE KYRKLFQSKP QTARKSVSVR TVSCAKGCAQ RCESERAEDE AGKMCAKILN
FTCSKCQDRT QYSPNDLQKH FEMWHHGELP SFPCEMCSFS ASDFQIFKQH RKTHRNTFVK
CDICNSERSY TLLDLTKHFT SKHCVNGNFQ CEECRFFTQD VGTFVQHIHR HKEVHYKCGK
CHHLCFTKGE LQKHLRVHSG TLPFTCHYCS YGAIHKDQLV RHVITLHKEH LYAKEKLERD
QYDKRVAKTT TGLKLILKRY KIGPTKTFWK RKTIASGNDE SIGKNAQAFN IVSKTQTKSE
DQSQEQLNEE KGGRQHCEDG DKPIESGSEK ATVLSTGQCN KADEGASAPS SVLSAVQGPT
VLLVRNNKIT IPANYSAKFM GFKMVDGRQH IVIKLLPANK QILPSPALQP NTEKESTANL
PPQAMDNTGF ATGLTAMNDT DFVKAAPLSC SSPELPRKVI SEKETAFISE KNNMLQMVDD
SKSVTSLPTP SESVTSVRLT TKVEARDNVD LWENPSTQSH PDLIGTSINS PDKVNLTIRP
NAYSCGDMHN YCINYVNSEL PAESSNCFEF SNQGSLPFHN YSKVNNKRRR FSRGAVCENL
QRESSNKTVT QQSTSDSDTT SPLRKESSNS DSLLASISPL SGTLKIKTEI EEPCDLEETQ
NFNEQSLFTN ENQNLLNMTE EPKWDDIPCA GSPMMPRITS VFSLQSEQAS EFLPPEVNQL
LQDTLKPRSD IKEDSNNIPS KNLPLDCDQT LKKSKEEVIK SSKDFQMQDI ISVPSASVGV
NVPANDLNLK CNGQEKQALS VLQDVRDPGV TTKIPSIITL LKTQSDAIIT QQLVKDKLRT
TTQHSGPVYV QNPLLTSEQK NPVFVQTPKG FIIPLHVANK PGLHVFSGRP VPLVNTQSVP
AALLVNKKPG VVLTVNNGKP EGVPTVKTEN VHSYGTVTKE PCRTPFLKAE HNRYCLTPGL
CSSIGSCVNM KTCSENTLPL KGSYIIKTSV SSSVKAVPFA NVLPEQQGPN VNVLDAVKQQ
NESLPKASLY TLMPDGKQAV FFKCMMPNNT KLLKPRLVQN STYQRIQPKR PAGAPQKILL
KIFNPVLSMS AVNNLSVGNS ASSFQKEIVP SKPTVHGEQK VPQSSRDALP VSVQDLMPAN
EAVLSSTAAC PGSSEEPVHI SERSETRVSR SKANCTIERN FNKRKTCKNK FAKIKTRISQ
DSETAFVSRN RSCKRKYIDN YQEPPRKKSA THRKCKERAN AEDVQETFGF SRPRLPKDSG
RTLRLFPFNS EQLVKCPRRN QPVVVLNHPD ADAPEVERVM KTITKFNGRV LKVSLSKATI
NALLKPVSIT SETTYSDFSK RHKMLKPVNS VKERFVLKLT LKKTSKNNYQ IVKTTSEDVL
KSKFNCWFCG RVFDNQDVWA GHGQRHLVEA TKDWNMLE
