ZN568_MOUSE
ID ZN568_MOUSE Reviewed; 671 AA.
AC E9PYI1; Q0VGV0; Q3UPK4;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Zinc finger protein 568 {ECO:0000312|MGI:MGI:2142347};
GN Name=Znf568 {ECO:0000250|UniProtKB:Q3ZCX4};
GN Synonyms=chato {ECO:0000303|PubMed:18701545, ECO:0000312|MGI:MGI:2142347},
GN Zfp568 {ECO:0000312|MGI:MGI:2142347};
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:BAE25391.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE25391.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAE25391.1};
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 [2] {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 [3] {ECO:0000312|EMBL:AAH82606.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH82606.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAH82606.1};
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 [4] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF LEU-64.
RX PubMed=18701545; DOI=10.1242/dev.022897;
RA Garcia-Garcia M.J., Shibata M., Anderson K.V.;
RT "Chato, a KRAB zinc-finger protein, regulates convergent extension in the
RT mouse embryo.";
RL Development 135:3053-3062(2008).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH TRIM28, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LEU-64.
RX PubMed=22110054; DOI=10.1242/dev.072546;
RA Shibata M., Blauvelt K.E., Liem K.F. Jr., Garcia-Garcia M.J.;
RT "TRIM28 is required by the mouse KRAB domain protein ZFP568 to control
RT convergent extension and morphogenesis of extra-embryonic tissues.";
RL Development 138:5333-5343(2011).
RN [6] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF LEU-64.
RX PubMed=21094155; DOI=10.1016/j.ydbio.2010.11.015;
RA Shibata M., Garcia-Garcia M.J.;
RT "The mouse KRAB zinc-finger protein CHATO is required in embryonic-derived
RT tissues to control yolk sac and placenta morphogenesis.";
RL Dev. Biol. 349:331-341(2011).
RN [7] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=23071813; DOI=10.1371/journal.pone.0047481;
RA Chien H.C., Wang H.Y., Su Y.N., Lai K.Y., Lu L.C., Chen P.C., Tsai S.F.,
RA Wu C.I., Hsieh W.S., Shen C.K.;
RT "Targeted disruption in mice of a neural stem cell-maintaining, KRAB-Zn
RT finger-encoding gene that has rapidly evolved in the human lineage.";
RL PLoS ONE 7:E47481-E47481(2012).
RN [8]
RP FUNCTION, INTERACTION WITH TRIM28, MUTAGENESIS OF LYS-37; GLN-45; GLN-55;
RP ASP-61; LEU-64; GLU-65; LEU-154 AND ASP-155, AND DOMAIN.
RX PubMed=27658112; DOI=10.1371/journal.pone.0163555;
RA Murphy K.E., Shylo N.A., Alexander K.A., Churchill A.J., Copperman C.,
RA Garcia-Garcia M.J.;
RT "The Transcriptional Repressive Activity of KRAB Zinc Finger Proteins Does
RT Not Correlate with Their Ability to Recruit TRIM28.";
RL PLoS ONE 11:E0163555-E0163555(2016).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DNA-BINDING.
RX PubMed=28522536; DOI=10.1126/science.aah6895;
RA Yang P., Wang Y., Hoang D., Tinkham M., Patel A., Sun M.A., Wolf G.,
RA Baker M., Chien H.C., Lai K.N., Cheng X., Shen C.J., Macfarlan T.S.;
RT "A placental growth factor is silenced in mouse embryos by the zinc finger
RT protein ZFP568.";
RL Science 356:757-759(2017).
CC -!- FUNCTION: Has transcriptional repression activity, partially through
CC the recruitment of the corepressor TRIM28 but has also repression
CC activity independently of this interaction (PubMed:22110054,
CC PubMed:27658112). Essential during embryonic development, where it acts
CC as direct repressor of IGF2-P0, placental-specific transcript of IGF2,
CC in early development and regulates convergent extension movements
CC required for axis elongation and tissue morphogenesis in all germ
CC layers (PubMed:18701545, PubMed:22110054, PubMed:28522536). Also
CC important for normal morphogenesis of extraembryonic tissues including
CC the yolk sac, extraembryonic mesoderm and placenta (PubMed:18701545,
CC PubMed:21094155). May enhance proliferation or maintenance of neural
CC stem cells (PubMed:23071813). {ECO:0000269|PubMed:18701545,
CC ECO:0000269|PubMed:21094155, ECO:0000269|PubMed:22110054,
CC ECO:0000269|PubMed:23071813, ECO:0000269|PubMed:27658112}.
CC -!- SUBUNIT: Interacts with TRIM28. {ECO:0000269|PubMed:22110054,
CC ECO:0000269|PubMed:27658112, ECO:0000269|PubMed:28522536}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22110054,
CC ECO:0000269|PubMed:23071813}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=E9PYI1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E9PYI1-2; Sequence=VSP_058610;
CC -!- TISSUE SPECIFICITY: Little or no expression detected in most adult
CC tissues (brain, liver, kidney, spleen, testis, ovary). In the
CC hippocampus, detected in neural stem cells within the subventricular
CC zone and subgranular zone. {ECO:0000269|PubMed:23071813}.
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously at 7.5 dpc and 8.5 dpc,
CC with especially high levels in the extraembryonic ectoderm
CC (PubMed:18701545). Expressed strongly in head from stages 10.5 dpc to
CC 12.5 dpc (PubMed:23071813). In fetal brain, shows highest expression
CC levels at stage 13.5 dpc with low levels thereafter (PubMed:23071813).
CC Detected in neural stem cells of the neocortex at stage 12.5 dpc
CC (PubMed:23071813). {ECO:0000269|PubMed:18701545,
CC ECO:0000269|PubMed:23071813}.
CC -!- DOMAIN: KRAB domain 1, but not KRAB domain 2, is required for
CC transcriptional repression. Both contribute to interaction with TRIM28.
CC Differences in repressive activity between KRAB domain 1 and 2 are
CC likely due to amino acid differences at multiple residues.
CC {ECO:0000269|PubMed:27658112}.
CC -!- DISRUPTION PHENOTYPE: Mutant embryos arrest at 9 dpc, they fail to
CC complete gastrulation, have convergent-extension failure and a yolk sac
CC membrane-ruffling phenotype (PubMed:28522536). Conditional knockdown in
CC neural stem cells results in reduced brain weight at birth, however
CC adult brain weights are normal and no other defects in brain
CC development or morphology are apparent (PubMed:23071813). Double
CC knockout for ZNF568 and IGF2 embryos and fetuses are found at near
CC Mendelian ratios and indistiguishable of wild type littermates at 12.5
CC dpc to 18.5 dpc. However, after birth few dead pups are recovered
CC (PubMed:28522536). {ECO:0000269|PubMed:23071813,
CC ECO:0000269|PubMed:28522536}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK143471; BAE25391.1; -; mRNA.
DR EMBL; AC149283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC082606; AAH82606.1; -; mRNA.
DR CCDS; CCDS21077.1; -. [E9PYI1-1]
DR CCDS; CCDS52176.1; -. [E9PYI1-2]
DR RefSeq; NP_001028527.2; NM_001033355.3. [E9PYI1-1]
DR RefSeq; NP_001161344.1; NM_001167872.1. [E9PYI1-1]
DR RefSeq; NP_001161345.1; NM_001167873.1. [E9PYI1-2]
DR RefSeq; XP_011248871.1; XM_011250569.2. [E9PYI1-1]
DR PDB; 5V3J; X-ray; 2.06 A; E/F=362-640.
DR PDB; 5V3M; X-ray; 2.09 A; C=362-669.
DR PDB; 5WJQ; X-ray; 2.79 A; D=388-668.
DR PDBsum; 5V3J; -.
DR PDBsum; 5V3M; -.
DR PDBsum; 5WJQ; -.
DR AlphaFoldDB; E9PYI1; -.
DR SMR; E9PYI1; -.
DR STRING; 10090.ENSMUSP00000118387; -.
DR iPTMnet; E9PYI1; -.
DR PhosphoSitePlus; E9PYI1; -.
DR MaxQB; E9PYI1; -.
DR PaxDb; E9PYI1; -.
DR PeptideAtlas; E9PYI1; -.
DR PRIDE; E9PYI1; -.
DR ProteomicsDB; 302088; -. [E9PYI1-1]
DR ProteomicsDB; 302089; -. [E9PYI1-2]
DR Ensembl; ENSMUST00000074322; ENSMUSP00000073930; ENSMUSG00000074221. [E9PYI1-1]
DR Ensembl; ENSMUST00000146074; ENSMUSP00000118823; ENSMUSG00000074221. [E9PYI1-2]
DR Ensembl; ENSMUST00000148442; ENSMUSP00000118387; ENSMUSG00000074221. [E9PYI1-1]
DR Ensembl; ENSMUST00000177931; ENSMUSP00000137438; ENSMUSG00000074221. [E9PYI1-2]
DR GeneID; 243905; -.
DR KEGG; mmu:243905; -.
DR UCSC; uc009gct.2; mouse. [E9PYI1-1]
DR UCSC; uc009gcu.2; mouse.
DR CTD; 243905; -.
DR MGI; MGI:2142347; Zfp568.
DR VEuPathDB; HostDB:ENSMUSG00000074221; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164032; -.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; E9PYI1; -.
DR OMA; NREIKCH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; E9PYI1; -.
DR TreeFam; TF341817; -.
DR BioGRID-ORCS; 243905; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Zfp568; mouse.
DR PRO; PR:E9PYI1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; E9PYI1; protein.
DR Bgee; ENSMUSG00000074221; Expressed in placenta labyrinth and 214 other tissues.
DR ExpressionAtlas; E9PYI1; baseline and differential.
DR Genevisible; Q3UPK4; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:UniProtKB.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB.
DR GO; GO:0060028; P:convergent extension involved in axis elongation; IMP:MGI.
DR GO; GO:0022007; P:convergent extension involved in neural plate elongation; IMP:MGI.
DR GO; GO:0060669; P:embryonic placenta morphogenesis; IMP:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010646; P:regulation of cell communication; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 2.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 2.
DR Pfam; PF00096; zf-C2H2; 10.
DR SMART; SM00349; KRAB; 2.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF109640; SSF109640; 2.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS50805; KRAB; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Developmental protein; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..671
FT /note="Zinc finger protein 568"
FT /id="PRO_0000438106"
FT DOMAIN 34..105
FT /note="KRAB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT DOMAIN 124..195
FT /note="KRAB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 363..385
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 391..413
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 419..441
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 447..469
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 475..497
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 503..525
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 531..553
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 559..581
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 587..609
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 615..637
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 643..665
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 106
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_058610"
FT MUTAGEN 37
FT /note="K->E: No effect on transcriptional repression."
FT /evidence="ECO:0000269|PubMed:27658112"
FT MUTAGEN 38..39
FT /note="DV->AA: Strongly decreases transcriptional
FT repression. No effect on interaction with THRIM28. No
FT effect on interaction with THRIM28."
FT /evidence="ECO:0000269|PubMed:27658112"
FT MUTAGEN 45
FT /note="Q->L: No effect on transcriptional repression."
FT /evidence="ECO:0000269|PubMed:27658112"
FT MUTAGEN 55
FT /note="Q->H: Decreases transcriptional repression."
FT /evidence="ECO:0000269|PubMed:27658112"
FT MUTAGEN 61
FT /note="D->A: Decreases transcriptional repression."
FT /evidence="ECO:0000269|PubMed:27658112"
FT MUTAGEN 64
FT /note="L->P: In chato; probable null mutation. Almost
FT abolishes transcriptional repression. No effect on
FT interaction with THRIM28. Embryonic development arrests at
FT stage 9 dpc. Widespread morphogenetic defects are found in
FT all germ layers, associated with defective convergent
FT extension movements. The anterior-posterior axis is
FT abnormally shortened, somites are mediolaterally expanded,
FT and the neural tube fails to close normally. Morphogenesis
FT of most mesodermal tissues is also defective. The
FT definitive endoderm fails to narrow and elongate leading to
FT an open gut tube. Extraembryonic tissues are also abnormal
FT with bubble-like protrusions in the yolk sac, aberrant
FT migration of extraembryonic mesoderm, and incomplete
FT placental development. Abolishes interaction with TRIM28;
FT when associated with P-154."
FT /evidence="ECO:0000269|PubMed:18701545,
FT ECO:0000269|PubMed:21094155, ECO:0000269|PubMed:22110054,
FT ECO:0000269|PubMed:27658112"
FT MUTAGEN 65
FT /note="E->D: Decreases transcriptional repression."
FT /evidence="ECO:0000269|PubMed:27658112"
FT MUTAGEN 128..129
FT /note="DV->AA: No effect on transcriptional repression. No
FT effect on interaction with THRIM28."
FT /evidence="ECO:0000269|PubMed:27658112"
FT MUTAGEN 154
FT /note="L->P: No effect on transcriptional repression.
FT Abolishes interaction with TRIM28; when associated with P-
FT 64."
FT /evidence="ECO:0000269|PubMed:27658112"
FT MUTAGEN 155
FT /note="D->E: Increases transcriptional repression. No
FT effect on interaction with THRIM28."
FT /evidence="ECO:0000269|PubMed:27658112"
FT CONFLICT 569
FT /note="T -> S (in Ref. 1; BAE25391)"
FT /evidence="ECO:0000305"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:5V3J"
FT HELIX 375..387
FT /evidence="ECO:0007829|PDB:5V3J"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:5V3J"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:5V3J"
FT HELIX 403..410
FT /evidence="ECO:0007829|PDB:5V3J"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:5V3J"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:5V3J"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:5V3J"
FT STRAND 427..430
FT /evidence="ECO:0007829|PDB:5V3J"
FT HELIX 431..442
FT /evidence="ECO:0007829|PDB:5V3J"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:5V3J"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:5V3J"
FT HELIX 459..466
FT /evidence="ECO:0007829|PDB:5V3J"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:5WJQ"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:5V3J"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:5V3J"
FT HELIX 487..498
FT /evidence="ECO:0007829|PDB:5V3J"
FT TURN 506..508
FT /evidence="ECO:0007829|PDB:5V3J"
FT STRAND 511..514
FT /evidence="ECO:0007829|PDB:5V3J"
FT HELIX 515..521
FT /evidence="ECO:0007829|PDB:5V3J"
FT HELIX 523..526
FT /evidence="ECO:0007829|PDB:5V3J"
FT TURN 534..536
FT /evidence="ECO:0007829|PDB:5V3J"
FT STRAND 539..542
FT /evidence="ECO:0007829|PDB:5V3J"
FT HELIX 543..554
FT /evidence="ECO:0007829|PDB:5V3J"
FT TURN 562..564
FT /evidence="ECO:0007829|PDB:5V3J"
FT STRAND 567..570
FT /evidence="ECO:0007829|PDB:5V3J"
FT HELIX 571..582
FT /evidence="ECO:0007829|PDB:5V3J"
FT TURN 590..592
FT /evidence="ECO:0007829|PDB:5V3J"
FT STRAND 595..598
FT /evidence="ECO:0007829|PDB:5V3J"
FT HELIX 599..610
FT /evidence="ECO:0007829|PDB:5V3J"
FT TURN 618..620
FT /evidence="ECO:0007829|PDB:5V3J"
FT STRAND 623..626
FT /evidence="ECO:0007829|PDB:5V3J"
FT HELIX 627..637
FT /evidence="ECO:0007829|PDB:5V3J"
FT TURN 646..648
FT /evidence="ECO:0007829|PDB:5WJQ"
FT HELIX 655..662
FT /evidence="ECO:0007829|PDB:5WJQ"
FT TURN 663..665
FT /evidence="ECO:0007829|PDB:5WJQ"
SQ SEQUENCE 671 AA; 77116 MW; 7131EA8702CE490E CRC64;
MERLSQMAGR RAWCAEDSVP RQEEEDRTRP SKTVTFKDVA VDLTQEEWQQ MKPAQRALYR
DVMLETYSNL VTVGCQVTKP DVIFKLEQAE EPWVLEEEMF WRRSPEAARG RMKSFAFKDM
AKDLRFEDVV IYFSLEEWEC LRHSHRNLYR AVMLDNYSNL LSLSLADTKP RVVSLLEQGK
EPWMVMRNET KIWHPDWVSR TEAKDSSKIK TLQEKMAKKH TCPTLEDSKT RGDREVTREL
EGQQVHQEGH LRQAAVTSVE RPDSVQCTAH REAHPGGKPC SSEKSQKTSL CQPPPIEREQ
LHSKAKASEH AQHGKVFNSC TSDTAVHPRP QESRKDSERK KSALAGGPDT SKPQSAQGSE
RPHKCKECGK AFHTPSQLSH HQKLHVGEKP YKCQECGKAF PSNAQLSLHH RVHTDEKCFE
CKECGKAFMR PSHLLRHQRI HTGEKPHKCK ECGKAFRYDT QLSLHLLTHA GARRFECKDC
DKVYSCASQL ALHQMSHTGE KPHKCKECGK GFISDSHLLR HQSVHTGETP YKCKECGKGF
RRGSELARHQ RAHSGDKPYK CKECGKSFTC TTELFRHQKV HTGDRPHKCK ECGKAFIRRS
ELTHHERSHS GEKPYECKEC GKTFGRGSEL SRHQKIHTGE KPYKCQQCGK AFIRGSHLTQ
HQRIHTGRRS E
