ZN263_MOUSE
ID ZN263_MOUSE Reviewed; 680 AA.
AC Q8CF60; E9PXW0; Q7TMI6; Q8K439;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Zinc finger protein 263 {ECO:0000312|MGI:MGI:1921370};
DE AltName: Full=Zinc finger protein FPM315 {ECO:0000250|UniProtKB:O14978};
DE AltName: Full=Zinc finger protein with KRAB and SCAN domains 12 {ECO:0000250|UniProtKB:O14978};
GN Name=Znf263 {ECO:0000312|MGI:MGI:1921370};
GN Synonyms=FPM315 {ECO:0000250|UniProtKB:O14978}, Zfp263 {ECO:0000305},
GN ZKSCAN12 {ECO:0000250|UniProtKB:O14978};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:AAM93158.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=12024037; DOI=10.1128/mcb.22.12.4256-4267.2002;
RA Tanaka K., Tsumaki N., Kozak C.A., Matsumoto Y., Nakatani F., Iwamoto Y.,
RA Yamada Y.;
RT "A Kruppel-associated box-zinc finger protein, NT2, represses cell-type-
RT specific promoter activity of the alpha 2(XI) collagen gene.";
RL Mol. Cell. Biol. 22:4256-4267(2002).
RN [2] {ECO:0000312|EMBL:AAH56222.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129/Sv X 129SvCp {ECO:0000312|EMBL:AAH56222.1};
RC TISSUE=Embryonic stem cell {ECO:0000312|EMBL:AAH56222.1};
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC25096.1};
RC TISSUE=Lung {ECO:0000312|EMBL:BAC25096.1};
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 [4] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26089202; DOI=10.1093/hmg/ddv231;
RA Ning Z., McLellan A.S., Ball M., Wynne F., O'Neill C., Mills W.,
RA Quinn J.P., Kleinjan D.A., Anney R.J., Carmody R.J., O'Keeffe G., Moore T.;
RT "Regulation of SPRY3 by X chromosome and PAR2-linked promoters in an autism
RT susceptibility region.";
RL Hum. Mol. Genet. 24:5126-5141(2015).
CC -!- FUNCTION: Transcription factor that binds to the consensus sequence 5'-
CC TCCTCCC-3' and acts as a transcriptional repressor (By similarity).
CC Binds to the promoter region of SIX3 and recruits other proteins
CC involved in chromatin modification and transcriptional corepression,
CC resulting in methylation of the promoter and transcriptional repression
CC (By similarity). Acts as transcriptional repressor of HS3ST1 and
CC HS3ST3A1 via binding to gene promoter regions (By similarity).
CC {ECO:0000250|UniProtKB:O14978}.
CC -!- SUBUNIT: Interacts with a number of proteins involved in chromatin
CC modification and transcriptional corepression including DNMT1, DNMT3A,
CC HDAC2, PHF8, TRIM28/KAP1, SETDB1, EZH2, UHRF1, CBX3/HP1-gamma, and
CC CBX5/HP1-alpha; recruits these proteins to the SIX3 promoter region,
CC leading to SIX3 transcriptional repression (By similarity). Interacts
CC with MAPK3/ERK1 and MAPK1/ERK2 (By similarity).
CC {ECO:0000250|UniProtKB:O14978}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26089202}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CF60-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CF60-2; Sequence=VSP_060908;
CC -!- TISSUE SPECIFICITY: Expressed in Purkinje cells in the brain (at
CC protein level). {ECO:0000269|PubMed:26089202}.
CC -!- PTM: Ubiquitinated, leading to proteasomal degradation.
CC {ECO:0000250|UniProtKB:O14978}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF499776; AAM93158.1; -; mRNA.
DR EMBL; BC056222; AAH56222.1; -; mRNA.
DR EMBL; AK004765; BAC25096.1; -; mRNA.
DR EMBL; AK159455; BAE35098.1; -; mRNA.
DR EMBL; AC139347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS27909.1; -. [Q8CF60-1]
DR RefSeq; NP_683726.2; NM_148924.3. [Q8CF60-1]
DR AlphaFoldDB; Q8CF60; -.
DR SMR; Q8CF60; -.
DR IntAct; Q8CF60; 4.
DR STRING; 10090.ENSMUSP00000023176; -.
DR iPTMnet; Q7TMI6; -.
DR PhosphoSitePlus; Q8CF60; -.
DR EPD; Q8CF60; -.
DR jPOST; Q8CF60; -.
DR MaxQB; Q8CF60; -.
DR PaxDb; Q8CF60; -.
DR PRIDE; Q8CF60; -.
DR ProteomicsDB; 332519; -. [Q8CF60-1]
DR ProteomicsDB; 348829; -.
DR Antibodypedia; 24089; 233 antibodies from 23 providers.
DR DNASU; 74120; -.
DR Ensembl; ENSMUST00000023176; ENSMUSP00000023176; ENSMUSG00000022529. [Q8CF60-1]
DR Ensembl; ENSMUST00000162207; ENSMUSP00000124433; ENSMUSG00000022529. [Q8CF60-2]
DR GeneID; 74120; -.
DR KEGG; mmu:74120; -.
DR UCSC; uc007xyn.2; mouse. [Q8CF60-1]
DR UCSC; uc007xyq.2; mouse.
DR CTD; 74120; -.
DR MGI; MGI:1921370; Zfp263.
DR VEuPathDB; HostDB:ENSMUSG00000022529; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159965; -.
DR HOGENOM; CLU_002678_2_1_1; -.
DR InParanoid; Q8CF60; -.
DR OMA; NVEDKEM; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q8CF60; -.
DR TreeFam; TF350829; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 74120; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Zfp263; mouse.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8CF60; protein.
DR Bgee; ENSMUSG00000022529; Expressed in rostral migratory stream and 227 other tissues.
DR ExpressionAtlas; Q8CF60; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR030752; ZNF263.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23226:SF224; PTHR23226:SF224; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 9.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..680
FT /note="Zinc finger protein 263"
FT /id="PRO_0000452087"
FT DOMAIN 43..125
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 378..400
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 434..456
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 462..484
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 490..512
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 518..540
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 572..594
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 600..622
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 628..650
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 656..678
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 147..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14978"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14978"
FT CROSSLNK 19
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14978"
FT CROSSLNK 159
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14978"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14978"
FT CROSSLNK 300
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14978"
FT CROSSLNK 376
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14978"
FT CROSSLNK 570
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14978"
FT CROSSLNK 579
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O14978"
FT VAR_SEQ 1..288
FT /note="Missing (in isoform 2)"
FT /id="VSP_060908"
FT CONFLICT 116
FT /note="T -> I (in Ref. 1; AAM93158)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="V -> F (in Ref. 1; AAM93158)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="T -> I (in Ref. 1; AAM93158)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="F -> S (in Ref. 2; AAH56222)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 680 AA; 77527 MW; A84E79E3A8EC467A CRC64;
MTMAAGPSSQ EPEGLLIVKL EEDCAWSHEV PPPEPEPSPE ASHLRFRRFR FQDAPGPREA
LSRLQELCRG WLRPEMRTKE QILELLVLEQ FLTILPQEIQ SRVQELRPES GEEAVTLVER
MQKELGKLRQ QVTNQGRGAE VLLEEPLPLE TAGESPSFKL EPMETERSPG PRLQELLDPS
PQRDSQAVKE RALSAPWLSL FPPEGNVEDK DMTGTQLPES LEDMAMYISQ EWDHQDPSKR
ALSRYMVQDS YENSGTLESS IPSQEVSSTH VEQGEKLWDS SVQTCKEGMN PRNPVPGVEK
FENQERNVES VSPESTHPPV LLPGQARREV PWSPEQGRLD DREGHWECPP EDKIEESLVG
TPSCKGLVQA KEQPKKLHLC ALCGKNFSNN SNLIRHQRIH AAEKLCMDVE CGEVFGGHPH
FLSLHRTHIG EEAHKCLECG KCFSQNTHLT RHQRTHTGEK PFQCNACGKS FSCNSNLNRH
QRTHTGEKPY KCPECGEIFA HSSNLLRHQR IHTGERPYRC SECGKSFSRS SHLVIHERTH
EKERLDPFPE CGQGMNDSAP FLTNHRVEKK LFECSTCGKS FRQGMHLTRH QRTHTGEKPY
KCILCGENFS HRSNLIRHQR IHTGEKPYTC HECGDSFSHS SNRIRHLRTH TGERPYKCSE
CGESFSRSSR LTSHQRTHTG
