AEBP2_DANRE
ID AEBP2_DANRE Reviewed; 415 AA.
AC Q7SXV2; Q1LUY9; Q1LUZ0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Zinc finger protein AEBP2;
DE AltName: Full=Adipocyte enhancer-binding protein 2 homolog;
DE Short=AE-binding protein 2 homolog;
GN Name=aebp2; ORFNames=si:dkey-158p11.2, zgc:63755;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 94-415 (ISOFORM 1).
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-binding transcriptional repressor. May interact with and
CC stimulate the activity of histone methyltransferase complexes.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7SXV2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7SXV2-2; Sequence=VSP_034364;
CC -!- SIMILARITY: Belongs to the AEBP2/jing C2H2-type zinc-finger family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH55234.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX914207; CAK05191.1; -; Genomic_DNA.
DR EMBL; BX914207; CAK05192.1; -; Genomic_DNA.
DR EMBL; BC055234; AAH55234.1; ALT_INIT; mRNA.
DR RefSeq; NP_998659.2; NM_213494.2. [Q7SXV2-1]
DR AlphaFoldDB; Q7SXV2; -.
DR SMR; Q7SXV2; -.
DR STRING; 7955.ENSDARP00000022060; -.
DR PaxDb; Q7SXV2; -.
DR PRIDE; Q7SXV2; -.
DR Ensembl; ENSDART00000019518; ENSDARP00000022060; ENSDARG00000006038. [Q7SXV2-1]
DR Ensembl; ENSDART00000128934; ENSDARP00000106888; ENSDARG00000006038. [Q7SXV2-2]
DR GeneID; 406815; -.
DR KEGG; dre:406815; -.
DR CTD; 121536; -.
DR ZFIN; ZDB-GENE-040426-2885; aebp2.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00510000048519; -.
DR HOGENOM; CLU_029789_1_1_1; -.
DR InParanoid; Q7SXV2; -.
DR OMA; LPCKVPG; -.
DR OrthoDB; 959457at2759; -.
DR PhylomeDB; Q7SXV2; -.
DR Reactome; R-DRE-212300; PRC2 methylates histones and DNA.
DR Reactome; R-DRE-3214841; PKMTs methylate histone lysines.
DR PRO; PR:Q7SXV2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000006038; Expressed in early embryo and 26 other tissues.
DR GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chromatin regulator; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..415
FT /note="Zinc finger protein AEBP2"
FT /id="PRO_0000341592"
FT ZN_FING 179..204
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 218..240
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 246..270
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 413..415
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034364"
FT CONFLICT 103
FT /note="L -> S (in Ref. 2; AAH55234)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 45388 MW; 9C21A485B804EF8B CRC64;
MASTTSDASE QESANPSEKN GDGSESGLRA ADPEPAVKMD EADTDEKPGG HEPTEQSPEE
ATRDGGNDED GETEKEQQKS PGSADGTAER MKREQREEES VSLPAEKNSG GGGTGMKRRA
SLEMMSSSSD GEPLSRMDSE DSINSTLMDT ESIPSSGRST PAMMNGLGGA SSSTKGSSYP
CCWDQCHMLF NTSPDLAEHI RGVHVDGQRG GVFVCLWKGC KVYNTPSTSQ SWLQRHMLSH
SGDKPFKCVV GGCNATFASQ GGLARHVPTH FSSQNSSKLS SQTKVKEESP SKAGMNKRRK
LKYKRRRSLP RPHDFFDAQT MDAIRHRAIC LNLATHIESQ GKGHSVVFHS TVIARRKEDS
GKVKVLLHWT PEDILPDSWV SESDRPQLKT KVVHLSQLPQ DTAFLLDPNI YRMFF
