ZEB2_MOUSE
ID ZEB2_MOUSE Reviewed; 1215 AA.
AC Q9R0G7; Q6P9M5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Zinc finger E-box-binding homeobox 2;
DE AltName: Full=Smad-interacting protein 1 {ECO:0000303|PubMed:10400677};
DE AltName: Full=Zinc finger homeobox protein 1b;
GN Name=Zeb2; Synonyms=Sip1 {ECO:0000303|PubMed:10400677}, Zfhx1b, Zfx1b;
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 [MRNA].
RX PubMed=10400677; DOI=10.1074/jbc.274.29.20489;
RA Verschueren K., Remacle J.E., Collart C., Kraft H., Baker B.S.,
RA Tylzanowski P., Nelles L., Wuytens G., Su M.-T., Bodmer R., Smith J.C.,
RA Huylebroeck D.;
RT "SIP1, a novel zinc finger/homeodomain repressor, interacts with Smad
RT proteins and binds to 5'-CACCT sequences in candidate target genes.";
RL J. Biol. Chem. 274:20489-20498(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-360; SER-364;
RP SER-731; SER-780; SER-784; SER-1124 AND SER-1203, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transcriptional inhibitor that binds to DNA sequence 5'-
CC CACCT-3' in different promoters. Represses transcription of E-cadherin.
CC Represses expression of MEOX2. {ECO:0000250|UniProtKB:O60315}.
CC -!- SUBUNIT: Interacts with CBX4 and CTBP1 (By similarity). Binds activated
CC SMAD1, activated SMAD2 and activated SMAD3; binding with SMAD4 is not
CC detected (By similarity). {ECO:0000250|UniProtKB:O60315}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O60315}.
CC Chromosome {ECO:0000250|UniProtKB:O60315}.
CC -!- PTM: Sumoylation on Lys-391 and Lys-866 is promoted by the E3 SUMO-
CC protein ligase CBX4, and impairs interaction with CTBP1 and
CC transcription repression activity. {ECO:0000250|UniProtKB:O60315}.
CC -!- SIMILARITY: Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger
CC family. {ECO:0000305}.
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DR EMBL; AF033116; AAD56590.1; -; mRNA.
DR EMBL; AL929120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL935127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060699; AAH60699.1; -; mRNA.
DR CCDS; CCDS16020.1; -.
DR RefSeq; NP_001276450.1; NM_001289521.1.
DR RefSeq; NP_056568.2; NM_015753.4.
DR RefSeq; XP_011237404.1; XM_011239102.2.
DR RefSeq; XP_017173550.1; XM_017318061.1.
DR RefSeq; XP_017173552.1; XM_017318063.1.
DR RefSeq; XP_017173554.1; XM_017318065.1.
DR AlphaFoldDB; Q9R0G7; -.
DR BMRB; Q9R0G7; -.
DR SMR; Q9R0G7; -.
DR BioGRID; 204915; 15.
DR IntAct; Q9R0G7; 2.
DR MINT; Q9R0G7; -.
DR STRING; 10090.ENSMUSP00000069685; -.
DR iPTMnet; Q9R0G7; -.
DR PhosphoSitePlus; Q9R0G7; -.
DR SwissPalm; Q9R0G7; -.
DR jPOST; Q9R0G7; -.
DR MaxQB; Q9R0G7; -.
DR PaxDb; Q9R0G7; -.
DR PRIDE; Q9R0G7; -.
DR ProteomicsDB; 302125; -.
DR Antibodypedia; 18810; 673 antibodies from 41 providers.
DR DNASU; 24136; -.
DR Ensembl; ENSMUST00000068415; ENSMUSP00000069685; ENSMUSG00000026872.
DR Ensembl; ENSMUST00000176438; ENSMUSP00000134849; ENSMUSG00000026872.
DR Ensembl; ENSMUST00000177302; ENSMUSP00000134747; ENSMUSG00000026872.
DR GeneID; 24136; -.
DR KEGG; mmu:24136; -.
DR UCSC; uc008jpc.2; mouse.
DR CTD; 9839; -.
DR MGI; MGI:1344407; Zeb2.
DR VEuPathDB; HostDB:ENSMUSG00000026872; -.
DR eggNOG; KOG3623; Eukaryota.
DR GeneTree; ENSGT00950000183208; -.
DR InParanoid; Q9R0G7; -.
DR OMA; IATPFSC; -.
DR OrthoDB; 890458at2759; -.
DR PhylomeDB; Q9R0G7; -.
DR TreeFam; TF331759; -.
DR BioGRID-ORCS; 24136; 14 hits in 78 CRISPR screens.
DR ChiTaRS; Zeb2; mouse.
DR PRO; PR:Q9R0G7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9R0G7; protein.
DR Bgee; ENSMUSG00000026872; Expressed in rostral migratory stream and 292 other tissues.
DR ExpressionAtlas; Q9R0G7; baseline and differential.
DR Genevisible; Q9R0G7; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:MGI.
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:0070412; F:R-SMAD binding; IDA:MGI.
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:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0021846; P:cell proliferation in forebrain; IMP:MGI.
DR GO; GO:0007417; P:central nervous system development; IGI:MGI.
DR GO; GO:0048668; P:collateral sprouting; IMP:MGI.
DR GO; GO:0021540; P:corpus callosum morphogenesis; IMP:MGI.
DR GO; GO:0021957; P:corticospinal tract morphogenesis; IMP:MGI.
DR GO; GO:0048066; P:developmental pigmentation; IMP:BHF-UCL.
DR GO; GO:0048598; P:embryonic morphogenesis; IGI:MGI.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:0061373; P:mammillary axonal complex development; IMP:MGI.
DR GO; GO:0097324; P:melanocyte migration; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0001755; P:neural crest cell migration; IMP:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IMP:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:MGI.
DR GO; GO:1902748; P:positive regulation of lens fiber cell differentiation; IMP:UniProtKB.
DR GO; GO:0048023; P:positive regulation of melanin biosynthetic process; IC:BHF-UCL.
DR GO; GO:0045636; P:positive regulation of melanocyte differentiation; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:MGI.
DR GO; GO:1903056; P:regulation of melanosome organization; IMP:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR008598; Di19_Zn-bd.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR Pfam; PF05605; zf-Di19; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; DNA-binding; Homeobox; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1215
FT /note="Zinc finger E-box-binding homeobox 2"
FT /id="PRO_0000047237"
FT ZN_FING 211..234
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 241..263
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 282..304
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 310..334
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 581..605
FT /note="C2H2-type 5; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 644..703
FT /note="Homeobox; atypical"
FT ZN_FING 999..1021
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1027..1049
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1055..1076
FT /note="C2H2-type 8; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..487
FT /note="SMAD-MH2 binding domain"
FT REGION 702..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60315"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 377
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60315"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60315"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 782
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60315"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60315"
FT MOD_RES 1124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 391
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 391
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O60315"
FT CROSSLNK 479
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60315"
FT CROSSLNK 555
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60315"
FT CROSSLNK 611
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60315"
FT CROSSLNK 632
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60315"
FT CROSSLNK 713
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60315"
FT CROSSLNK 866
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 866
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O60315"
FT CONFLICT 1102
FT /note="E -> G (in Ref. 1; AAD56590)"
FT /evidence="ECO:0000305"
FT CONFLICT 1215
FT /note="E -> G (in Ref. 1; AAD56590)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1215 AA; 136615 MW; 1DA4236E43A96BE7 CRC64;
MKQPIMADGP RCKRRKQANP RRKNVVNYDN VVDAGSETDE EDKLHIAEDD SLANPLDQDT
SPASMPNHES SPHMSQGLLP REEEEEELRE SVVEHSWHSG EILQASVAGP EEMKEDYDAM
GPEATIQTTI NNGTVKNANC TSDFEEYFAK RKLEERDGHA VSIEEYLQRS DTAIIYPEAP
EELSRLGTPE ANGQEENDLP PGTPDAFAQL LTCPYCDRGY KRLTSLKEHI KYRHEKNEEN
FSCPLCSYTF AYRTQLERHM VTHKPGTDQH QMLTQGAGNR KFKCTECGKA FKYKHHLKEH
LRIHSGEKPY ECPNCKKRFS HSGSYSSHIS SKKCIGLISV NGRMRNNIKT GSSPNSVSSS
PTNSAITQLR NKLENGKPLS MSEQTGLLKI KTEPLDFNDY KVLMATHGFS GSSPFMNGGL
GATSPLGVHP SAQSPMQHLG VGMEAPLLGF PTMNSNLSEV QKVLQIVDNT VSRQKMDCKT
EDISKLKGYH MKDPCSQPEE QGVTSPNIPP VGLPVVSHNG ATKSIIDYTL EKVNEAKACL
QSLTTDSRRQ ISNIKKEKLR TLIDLVTDDK MIENHSISTP FSCQFCKESF PGPIPLHQHE
RYLCKMNEEI KAVLQPHENI VPNKAGVFVD NKALLLSSVL SEKGLTSPIN PYKDHMSVLK
AYYAMNMEPN SDELLKISIA VGLPQEFVKE WFEQRKVYQY SNSRSPSLER TSKPLAPNSN
PTTKDSLLPR SPVKPMDSIT SPSIAELHNS VTSCDPPLRL TKSSHFTNIK AVDKLDHSRS
NTPSPLNLSS TSSKNSHSSS YTPNSFSSEE LQAEPLDLSL PKQMREPKGI IATKNKTKAT
SINLDHNSVS SSSENSDEPL NLTFIKKEFS NSNNLDNKSN NPVFGMNPFS AKPLYTPLPP
QSAFPPATFM PPVQTSIPGL RPYPGLDQMS FLPHMAYTYP TGAATFADMQ QRRKYQRKQG
FQGDLLDGAQ DYMSGLDDMT DSDSCLSRKK IKKTESGMYA CDLCDKTFQK SSSLLRHKYE
HTGKRPHQCQ ICKKAFKHKH HLIEHSRLHS GEKPYQCDKC GKRFSHSGSY SQHMNHRYSY
CKREAEEREA AEREAREKGH LEPTELLMNR AYLQSITPQG YSDSEERESM PRDGESEKEH
EKEGEEGYGK LRRRDGDEEE EEEEEESENK SMDTDPETIR DEEETGDHSM DDSSEDGKME
TKSDHEEDNM EDGME
