ZBT7B_MOUSE
ID ZBT7B_MOUSE Reviewed; 544 AA.
AC Q64321; Q80VV5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Zinc finger and BTB domain-containing protein 7B {ECO:0000305};
DE AltName: Full=Krueppel-related zinc finger protein cKrox;
DE Short=c-Krox;
DE AltName: Full=T-helper-inducing POZ/Krueppel-like factor;
DE AltName: Full=Zinc finger protein 67;
DE Short=Zfp-67;
DE AltName: Full=Zinc finger protein Th-POK {ECO:0000303|PubMed:24880459};
GN Name=Zbtb7b {ECO:0000312|MGI:MGI:102755};
GN Synonyms=Thpok {ECO:0000303|PubMed:24880459}, Zfp67;
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 STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [MRNA] OF 85-544, FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=7937772; DOI=10.1073/pnas.91.20.9372;
RA Galera P., Musso M., Ducy P., Karsenty G.;
RT "c-Krox, a transcriptional regulator of type I collagen gene expression, is
RT preferentially expressed in skin.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9372-9376(1994).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND VARIANT HD GLY-389.
RX PubMed=15729333; DOI=10.1038/nature03338;
RA He X., He X., Dave V.P., Zhang Y., Hua X., Nicolas E., Xu W., Roe B.A.,
RA Kappes D.J.;
RT "The zinc finger transcription factor Th-POK regulates CD4 versus CD8 T-
RT cell lineage commitment.";
RL Nature 433:826-833(2005).
RN [4]
RP FUNCTION.
RX PubMed=18258917; DOI=10.1126/science.1151844;
RA Setoguchi R., Tachibana M., Naoe Y., Muroi S., Akiyama K., Tezuka C.,
RA Okuda T., Taniuchi I.;
RT "Repression of the transcription factor Th-POK by Runx complexes in
RT cytotoxic T cell development.";
RL Science 319:822-825(2008).
RN [5]
RP ACETYLATION AT LYS-210; LYS-216 AND LYS-339, MUTAGENESIS OF LYS-207;
RP LYS-210; LYS-216; LYS-339 AND LYS-343, AND UBIQUITINATION AT LYS-210;
RP LYS-216 AND LYS-339.
RX PubMed=20810990; DOI=10.4049/jimmunol.1001462;
RA Zhang M., Zhang J., Rui J., Liu X.;
RT "p300-mediated acetylation stabilizes the Th-inducing POK factor.";
RL J. Immunol. 185:3960-3969(2010).
RN [6]
RP FUNCTION, MUTAGENESIS OF LEU-21 AND 27-GLN-ARG-28, VARIANT HD GLY-389,
RP CHARACTERIZATION OF VARIANT HD GLY-389, HOMODIMERIZATION, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH HDAC4 AND HDAC5.
RX PubMed=22730529; DOI=10.4049/jimmunol.1201077;
RA Rui J., Liu H., Zhu X., Cui Y., Liu X.;
RT "Epigenetic silencing of CD8 genes by ThPOK-mediated deacetylation during
RT CD4 T cell differentiation.";
RL J. Immunol. 189:1380-1390(2012).
RN [7]
RP FUNCTION, VARIANT HELPLESS ARG-102, AND CHARACTERIZATION OF VARIANT
RP ARG-102.
RX PubMed=23105140; DOI=10.4049/jimmunol.1201486;
RA Enders A., Stankovic S., Teh C., Uldrich A.P., Yabas M., Juelich T.,
RA Altin J.A., Frankenreiter S., Bergmann H., Roots C.M., Kyparissoudis K.,
RA Goodnow C.C., Godfrey D.I.;
RT "ZBTB7B (Th-POK) regulates the development of IL-17-producing CD1d-
RT restricted mouse NKT cells.";
RL J. Immunol. 189:5240-5249(2012).
RN [8]
RP FUNCTION.
RX PubMed=23481257; DOI=10.1038/emboj.2013.47;
RA Tanaka H., Naito T., Muroi S., Seo W., Chihara R., Miyamoto C.,
RA Kominami R., Taniuchi I.;
RT "Epigenetic Thpok silencing limits the time window to choose CD4(+) helper-
RT lineage fate in the thymus.";
RL EMBO J. 32:1183-1194(2013).
RN [9]
RP FUNCTION, AND VARIANT HD GLY-389.
RX PubMed=24880459; DOI=10.1038/ni.2917;
RA Luckey M.A., Kimura M.Y., Waickman A.T., Feigenbaum L., Singer A.,
RA Park J.H.;
RT "The transcription factor ThPOK suppresses Runx3 and imposes CD4(+) lineage
RT fate by inducing the SOCS suppressors of cytokine signaling.";
RL Nat. Immunol. 15:638-645(2014).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INTERACTION WITH HNRNPU; NCL; NEDD4 AND YBX1.
RX PubMed=28784777; DOI=10.1073/pnas.1703494114;
RA Li S., Mi L., Yu L., Yu Q., Liu T., Wang G.X., Zhao X.Y., Wu J., Lin J.D.;
RT "Zbtb7b engages the long noncoding RNA Blnc1 to drive brown and beige fat
RT development and thermogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E7111-E7120(2017).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY INSULIN,
RP AND SUBCELLULAR LOCATION.
RX PubMed=29420538; DOI=10.1371/journal.pgen.1007211;
RA Zhang R., Ma H., Gao Y., Wu Y., Qiao Y., Geng A., Cai C., Han Y.,
RA Zeng Y.A., Liu X., Ge G.;
RT "Th-POK regulates mammary gland lactation through mTOR-SREBP pathway.";
RL PLoS Genet. 14:E1007211-E1007211(2018).
CC -!- FUNCTION: Transcription regulator that acts as a key regulator of
CC lineage commitment of immature T-cell precursors. Exerts distinct
CC biological functions in the mammary epithelial cells and T cells in a
CC tissue-specific manner (PubMed:15729333, PubMed:29420538). Necessary
CC and sufficient for commitment of CD4 lineage, while its absence causes
CC CD8 commitment. Development of immature T-cell precursors (thymocytes)
CC to either the CD4 helper or CD8 killer T-cell lineages correlates
CC precisely with their T-cell receptor specificity for major
CC histocompatibility complex class II or class I molecules, respectively.
CC Cross-antagonism between ZBTB7B and CBF complexes are determinative to
CC CD4 versus CD8 cell fate decision (PubMed:15729333, PubMed:24880459,
CC PubMed:18258917, PubMed:23481257). Suppresses RUNX3 expression and
CC imposes CD4+ lineage fate by inducing the SOCS suppressors of cytokine
CC signaling. induces, as a transcriptional activator, SOCS genes
CC expression which represses RUNX3 expression and promotes the CD4+
CC lineage fate (PubMed:24880459). During CD4 lineage commitment,
CC associates with multiple sites at the CD8 locus, acting as a negative
CC regulator of the CD8 promoter and enhancers by epigenetic silencing
CC through the recruitment of class II histone deacetylases, such as HDAC4
CC and HDAC5, to these loci (PubMed:22730529). Regulates the development
CC of IL17-producing CD1d-restricted naural killer (NK) T cells
CC (PubMed:23105140). Also functions as an important metabolic regulator
CC in the lactating mammary glands. Critical feed-forward regulator of
CC insulin signaling in mammary gland lactation, directly regulates
CC expression of insulin receptor substrate-1 (IRS-1) and insulin-induced
CC Akt-mTOR-SREBP signaling (PubMed:29420538). Transcriptional repressor
CC of the collagen COL1A1 and COL1A2 genes. May also function as a
CC repressor of fibronectin and possibly other extracellular matrix genes
CC (PubMed:7937772). Potent driver of brown fat development, thermogenesis
CC and cold-induced beige fat formation (PubMed:28784777). Recruits the
CC brown fat lncRNA 1 (Blnc1):HNRNPU ribonucleoprotein complex to activate
CC thermogenic gene expression in brown and beige adipocytes
CC (PubMed:28784777). {ECO:0000269|PubMed:15729333,
CC ECO:0000269|PubMed:18258917, ECO:0000269|PubMed:22730529,
CC ECO:0000269|PubMed:23105140, ECO:0000269|PubMed:23481257,
CC ECO:0000269|PubMed:24880459, ECO:0000269|PubMed:28784777,
CC ECO:0000269|PubMed:29420538, ECO:0000269|PubMed:7937772}.
CC -!- SUBUNIT: Homodimerizes (PubMed:22730529). Interacts with NCL, NEDD4 and
CC YBX1 (PubMed:28784777). Interacts with HNRNPU (via RNA-binding RGG-box
CC region); the interaction facilitates the recruitment of long non-coding
CC RNA Blnc1 by ZBTB7B (PubMed:28784777). Interacts with HDAC4 and HDAC5;
CC the interaction allows the recruitment of HDAC4 and HDAC5 on CD8 loci
CC for deacetylation and possible inhibition of CD8 genes expression
CC (PubMed:22730529). {ECO:0000269|PubMed:22730529,
CC ECO:0000269|PubMed:28784777}.
CC -!- INTERACTION:
CC Q64321; Q8CIH5: Plcg2; NbExp=3; IntAct=EBI-642868, EBI-617954;
CC Q64321; Q61029: Tmpo; NbExp=2; IntAct=EBI-642868, EBI-6172136;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22730529,
CC ECO:0000269|PubMed:29420538}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with a higher level in skin.
CC Expressed in thymus. Restricted to CD4 cells (mature single positive
CC CD4(+) and intermediate CD4(+)CD8(+) cells). Expressed in the luminal
CC epithelial cells in the mammary glands where is up-regulated at late
CC pregnancy and lactation (PubMed:29420538). Expression is enriched in
CC brown fat (PubMed:28784777). {ECO:0000269|PubMed:15729333,
CC ECO:0000269|PubMed:28784777, ECO:0000269|PubMed:29420538,
CC ECO:0000269|PubMed:7937772}.
CC -!- DEVELOPMENTAL STAGE: Expressed, beginning at 9.5 days of gestation and
CC at 10.5 days in regions destined to become skin. In adult animals,
CC expression is predominantly in skin (PubMed:7937772). Expression is
CC significantly increased during brown adipocyte differentiation
CC (PubMed:28784777). {ECO:0000269|PubMed:28784777,
CC ECO:0000269|PubMed:7937772}.
CC -!- INDUCTION: Expression in mammary glands is induced by insulin.
CC {ECO:0000269|PubMed:29420538}.
CC -!- PTM: Acetylated directly and specifically by EP300. EP300-mediated
CC acetylation of Lys-210, Lys-216 and Lys-339 stabilizes the protein by
CC antagonizing ubiquitin conjugation. {ECO:0000269|PubMed:20810990}.
CC -!- PTM: Ubiquitinated, leading to proteasomal degradation. Competes with
CC acetylation on Lys-210, Lys-216 and Lys-339.
CC {ECO:0000269|PubMed:20810990}.
CC -!- DISEASE: Note=Defects in Zbtb7b are the cause of helper deficient
CC disease (HD) or helpless disease. HD and helpless mice are
CC distinguished by the virtual absence of peripheral T-cells of the
CC CD4(+)CD8(-) major histocompatibility complex (MHC) class II-restricted
CC T-helper subset due to a specific block in thymic development. The
CC developmental defect is selective for CD4(+)CD8(-) cells; the
CC maturation of CD4(-)CD8(+) and gamma delta T-cells is normal indicating
CC that lineage commitment is specifically perturbed without affecting
CC positive selection. In helpless disease, NKT cells are
CC hyperproliferative, most lack CD4 and instead express CD8. The majority
CC of NKT cells in the thymus produce IL17 with high frequency while very
CC few produce IFNG or other cytokines (PubMed:23105140).
CC {ECO:0000269|PubMed:15729333, ECO:0000269|PubMed:22730529,
CC ECO:0000269|PubMed:23105140, ECO:0000269|PubMed:24880459}.
CC -!- DISRUPTION PHENOTYPE: Mutant females are unable to efficiently secrete
CC milk lipid and to nurse the offspring. They show normal mammary gland
CC morphogenesis in puberty and alveologenesis in pregnancy, but are
CC defective in triggering the onset of lactation upon parturition with
CC large cellular lipid droplets retained within alveolar epithelial cells
CC (PubMed:29420538). Mice are more sensitive to cold temperature, with
CC impaired cold-induced transcriptional remodeling in brown fat and
CC diminished browning of inguinal white fat (PubMed:28784777).
CC {ECO:0000269|PubMed:28784777, ECO:0000269|PubMed:29420538}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA61956.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA61956.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
CC Sequence=CAA85307.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA85307.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR EMBL; BC046533; AAH46533.1; -; mRNA.
DR EMBL; L35307; AAA61956.1; ALT_SEQ; mRNA.
DR EMBL; Z36549; CAA85307.1; ALT_SEQ; mRNA.
DR CCDS; CCDS17504.1; -.
DR PIR; I49603; I49603.
DR RefSeq; NP_033591.2; NM_009565.4.
DR RefSeq; XP_006501376.1; XM_006501313.2.
DR RefSeq; XP_006501377.1; XM_006501314.2.
DR RefSeq; XP_006501379.1; XM_006501316.2.
DR RefSeq; XP_006501380.1; XM_006501317.3.
DR RefSeq; XP_006501381.1; XM_006501318.3.
DR RefSeq; XP_006501382.1; XM_006501319.3.
DR AlphaFoldDB; Q64321; -.
DR SMR; Q64321; -.
DR BioGRID; 204677; 324.
DR IntAct; Q64321; 4.
DR MINT; Q64321; -.
DR STRING; 10090.ENSMUSP00000029677; -.
DR iPTMnet; Q64321; -.
DR PhosphoSitePlus; Q64321; -.
DR MaxQB; Q64321; -.
DR PaxDb; Q64321; -.
DR PRIDE; Q64321; -.
DR ProteomicsDB; 275339; -.
DR Antibodypedia; 20407; 293 antibodies from 38 providers.
DR Ensembl; ENSMUST00000029677; ENSMUSP00000029677; ENSMUSG00000028042.
DR Ensembl; ENSMUST00000107432; ENSMUSP00000103055; ENSMUSG00000028042.
DR Ensembl; ENSMUST00000107433; ENSMUSP00000103056; ENSMUSG00000028042.
DR Ensembl; ENSMUST00000107435; ENSMUSP00000103058; ENSMUSG00000028042.
DR GeneID; 22724; -.
DR KEGG; mmu:22724; -.
DR UCSC; uc008pza.1; mouse.
DR CTD; 51043; -.
DR MGI; MGI:102755; Zbtb7b.
DR VEuPathDB; HostDB:ENSMUSG00000028042; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160219; -.
DR HOGENOM; CLU_025627_0_0_1; -.
DR InParanoid; Q64321; -.
DR OMA; NGHREEM; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q64321; -.
DR TreeFam; TF331824; -.
DR BioGRID-ORCS; 22724; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Zbtb7b; mouse.
DR PRO; PR:Q64321; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q64321; protein.
DR Bgee; ENSMUSG00000028042; Expressed in granulocyte and 183 other tissues.
DR ExpressionAtlas; Q64321; baseline and differential.
DR Genevisible; Q64321; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:1990845; P:adaptive thermogenesis; IMP:UniProtKB.
DR GO; GO:0007595; P:lactation; IMP:UniProtKB.
DR GO; GO:0043377; P:negative regulation of CD8-positive, alpha-beta T cell differentiation; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:MGI.
DR GO; GO:0051141; P:negative regulation of NK T cell proliferation; IMP:UniProtKB.
DR GO; GO:2000320; P:negative regulation of T-helper 17 cell differentiation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:GO_Central.
DR GO; GO:0001865; P:NK T cell differentiation; IMP:UniProtKB.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0043372; P:positive regulation of CD4-positive, alpha-beta T cell differentiation; IMP:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IMP:UniProtKB.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IMP:UniProtKB.
DR GO; GO:2000640; P:positive regulation of SREBP signaling pathway; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0043376; P:regulation of CD8-positive, alpha-beta T cell differentiation; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0045622; P:regulation of T-helper cell differentiation; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032868; P:response to insulin; IMP:UniProtKB.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; Developmental protein; Differentiation; Disease variant;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..544
FT /note="Zinc finger and BTB domain-containing protein 7B"
FT /id="PRO_0000047720"
FT DOMAIN 34..115
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 350..372
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 378..400
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 406..428
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 434..458
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 171..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..404
FT /note="Required for interaction with and acetylation by
FT EP300"
FT /evidence="ECO:0000269|PubMed:20810990"
FT REGION 465..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..201
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15156"
FT MOD_RES 210
FT /note="N6-acetyllysine; by EP300; alternate"
FT /evidence="ECO:0000269|PubMed:20810990"
FT MOD_RES 216
FT /note="N6-acetyllysine; by EP300; alternate"
FT /evidence="ECO:0000269|PubMed:20810990"
FT MOD_RES 339
FT /note="N6-acetyllysine; by EP300; alternate"
FT /evidence="ECO:0000269|PubMed:20810990"
FT MOD_RES 373
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15156"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:20810990"
FT CROSSLNK 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:20810990"
FT CROSSLNK 339
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:20810990"
FT VARIANT 102
FT /note="L -> R (in helpless)"
FT /evidence="ECO:0000269|PubMed:23105140"
FT VARIANT 389
FT /note="R -> G (in HD; disrupts sequence-specific DNA-
FT binding; no effect on homodimerization or interaction with
FT HDAC4 and HDAC5)"
FT /evidence="ECO:0000269|PubMed:15729333,
FT ECO:0000269|PubMed:22730529, ECO:0000269|PubMed:24880459"
FT MUTAGEN 21
FT /note="L->S: Fails to repress CD8 expression. Abolishes
FT interaction with HDAC4 and HDAC5. No effect on
FT homodimerization and DNA binding."
FT /evidence="ECO:0000269|PubMed:22730529"
FT MUTAGEN 27..28
FT /note="QR->AL: Fails to repress CD8 expression. Abolishes
FT interaction with HDAC4 and HDAC5. No effect on
FT homodimerization and DNA binding."
FT /evidence="ECO:0000269|PubMed:22730529"
FT MUTAGEN 207
FT /note="K->R: No effect on acetylation levels. Slightly
FT decreases acetylation levels; when associated with R-210.
FT Slightly decreases acetylation levels; when associated with
FT R-216."
FT /evidence="ECO:0000269|PubMed:20810990"
FT MUTAGEN 210
FT /note="K->R: Slightly decreases acetylation levels. No
FT effect on protein stability. Slightly decreases acetylation
FT levels; when associated with R-207. Slightly decreases
FT acetylation levels and increases protein stability; when
FT associated with R-216. Increases protein stability; when
FT associated with R-339. Decreases acetylation levels; when
FT associated with R-216 and R-343. Abolishes acetylation
FT levels and ubiquitination and highly increases protein
FT stability; when associated with R-216 and R-339."
FT /evidence="ECO:0000269|PubMed:20810990"
FT MUTAGEN 216
FT /note="K->R: Slightly decreases acetylation levels. No
FT effect on protein stability. Slightly decreases acetylation
FT levels; when associated with R-207. Slightly decreases
FT acetylation levels and increases protein stability; when
FT associated with R-210. Increases protein stability; when
FT associated with R-339. Decreases acetylation levels; when
FT associated with R-210 and R-343. Abolishes acetylation
FT levels and ubiquitination and highly increases protein
FT stability; when associated with R-210 and R-339."
FT /evidence="ECO:0000269|PubMed:20810990"
FT MUTAGEN 339
FT /note="K->R: Slightly decreases acetylation levels.
FT Slightly increases protein stability. Slightly decreases
FT acetylation levels; when associated with R-343. Increases
FT protein stability; when associated with R-210 or R-216.
FT Abolishes acetylation levels and ubiquitination and highly
FT increases protein stability; when associated with R-210 and
FT R-216."
FT /evidence="ECO:0000269|PubMed:20810990"
FT MUTAGEN 343
FT /note="K->R: No effect on acetylation levels. Slightly
FT decreases acetylation levels; when associated with R-339.
FT Decreases acetylation levels; when associated with R-210
FT and R-216."
FT /evidence="ECO:0000269|PubMed:20810990"
FT CONFLICT 268
FT /note="A -> T (in Ref. 2; AAA61956/CAA85307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 58918 MW; 5A43F10AE2970709 CRC64;
MGSPEDDLIG IPFPDHSSEL LSCLNEQRQL GHLCDLTIRT QGLEYRTHRA VLAACSHYFK
KLFTEGGGGT VMGTGGGGTA SGGAGAGVCE LDFVGPEALG ALLEFAYTAT LTTSSANMPA
VLQAARLLEI PCVIAACMEI LQGSGLEAPS PDEDDCERAR QYLEAFATAT TTASTSGMPN
GEDSPPQVPL LPPPPPPPRP VARRSRKPRK AFLQTKGARA NHLVPEAPTV LTHPLTYEEE
EMVGRLGNSG GSGLGDSYSP PTGAASPAEG PLNYEVFEGE EEEEEMAYPP GYGLAQSNEP
SLSPEELGSD EDPIDPDLMA YLSSLHQDAL TPGLDGQDKL VRKRRSQMPQ ECPVCHKIIH
GAGKLPRHMR THTGEKPFAC EVCGVRFTRN DKLKIHMRKH TGERPYSCPH CPARFLHSYD
LKNHMHLHTG DRPYECHLCH KAFAKEDHLQ RHLKGQNCLE VRTRRRRKDD VAAPHYPPPS
TTTSSPAGLD LSNGHLDTFH LSLARFWEQS ATTGPPVTTQ GPPEEEEEEG TPTTPQAEGA
MESS
