ZHX1_MOUSE
ID ZHX1_MOUSE Reviewed; 873 AA.
AC P70121; Q8BQ68; Q8C6T4; Q8CJG3;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Zinc fingers and homeoboxes protein 1;
GN Name=Zhx1;
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|EMBL:CAA90905.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow stroma {ECO:0000269|PubMed:8713137};
RX PubMed=8713137; DOI=10.1006/bbrc.1996.1114;
RA Barthelemy I., Carramolino L., Gutierrez J., Barbero J.L., Marquez G.,
RA Zaballos A.;
RT "zhx-1: a novel mouse homeodomain protein containing two zinc-fingers and
RT five homeodomains.";
RL Biochem. Biophys. Res. Commun. 224:870-876(1996).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ {ECO:0000312|EMBL:BAC22110.1};
RX PubMed=12527199; DOI=10.1016/s0378-1119(02)01093-4;
RA Shou Z., Yamada K., Inazu T., Kawata H., Hirano S., Mizutani T., Yazawa T.,
RA Sekiguchi T., Yoshino M., Kajitani T., Okada K., Miyamoto K.;
RT "Genomic structure and analysis of transcriptional regulation of the mouse
RT zinc-fingers and homeoboxes 1 (ZHX1) gene.";
RL Gene 302:83-94(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung, and Spinal ganglion;
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:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH54543.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH54543.1};
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 [5] {ECO:0000305}
RP INDUCTION.
RX PubMed=14741719; DOI=10.1016/j.bbrc.2003.12.162;
RA Shou Z., Yamada K., Kawata H., Yokoyama O., Miyamoto K.;
RT "A mechanism of induction of the mouse zinc-fingers and homeoboxes 1 (ZHX1)
RT gene expression by interleukin-2.";
RL Biochem. Biophys. Res. Commun. 314:885-890(2004).
RN [6]
RP SUBCELLULAR LOCATION.
RC TISSUE=Kidney;
RX PubMed=17056598; DOI=10.1074/jbc.m606664200;
RA Liu G., Clement L.C., Kanwar Y.S., Avila-Casado C., Chugh S.S.;
RT "ZHX proteins regulate podocyte gene expression during the development of
RT nephrotic syndrome.";
RL J. Biol. Chem. 281:39681-39692(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-47 AND SER-48, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-48 AND SER-648, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Acts as a transcriptional repressor. Increases DNMT3B-
CC mediated repressive transcriptional activity when DNMT3B is tethered to
CC DNA. May link molecule between DNMT3B and other co-repressor proteins
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms homodimers. Heterodimer (via HD1 domain) with ZHX2 (via
CC HD1 domain). Also forms a heterodimer with ZHX3 which is a prerequisite
CC for repressor activity. Interacts with ATF7IP and NFYA. Interacts (via
CC homeobox domains) with DNMT3B (via PWWP domain) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000269|PubMed:17056598}. Note=Colocalized in the nucleus with
CC DNMT3B. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain.
CC {ECO:0000269|PubMed:8713137}.
CC -!- INDUCTION: By interleukin-2. {ECO:0000269|PubMed:14741719}.
CC -!- SIMILARITY: Belongs to the ZHX family. {ECO:0000305}.
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DR EMBL; Z54200; CAA90905.1; -; mRNA.
DR EMBL; AB078421; BAC22110.1; -; Genomic_DNA.
DR EMBL; AK051410; BAC34629.1; -; mRNA.
DR EMBL; AK053191; BAC35306.1; -; mRNA.
DR EMBL; BC054543; AAH54543.1; -; mRNA.
DR CCDS; CCDS27488.1; -.
DR PIR; JC4863; JC4863.
DR RefSeq; NP_001035903.1; NM_001042438.2.
DR RefSeq; NP_033598.2; NM_009572.4.
DR AlphaFoldDB; P70121; -.
DR SMR; P70121; -.
DR BioGRID; 204693; 1.
DR IntAct; P70121; 1.
DR MINT; P70121; -.
DR STRING; 10090.ENSMUSP00000066201; -.
DR iPTMnet; P70121; -.
DR PhosphoSitePlus; P70121; -.
DR EPD; P70121; -.
DR jPOST; P70121; -.
DR MaxQB; P70121; -.
DR PaxDb; P70121; -.
DR PeptideAtlas; P70121; -.
DR PRIDE; P70121; -.
DR ProteomicsDB; 302059; -.
DR Antibodypedia; 26954; 169 antibodies from 24 providers.
DR DNASU; 22770; -.
DR Ensembl; ENSMUST00000070143; ENSMUSP00000066201; ENSMUSG00000022361.
DR Ensembl; ENSMUST00000110168; ENSMUSP00000105797; ENSMUSG00000022361.
DR Ensembl; ENSMUST00000175805; ENSMUSP00000134844; ENSMUSG00000022361.
DR GeneID; 22770; -.
DR KEGG; mmu:22770; -.
DR UCSC; uc007vtd.2; mouse.
DR CTD; 11244; -.
DR MGI; MGI:109271; Zhx1.
DR VEuPathDB; HostDB:ENSMUSG00000022361; -.
DR eggNOG; ENOG502QT3D; Eukaryota.
DR GeneTree; ENSGT00950000182893; -.
DR InParanoid; P70121; -.
DR OMA; HSVVCSA; -.
DR OrthoDB; 518562at2759; -.
DR PhylomeDB; P70121; -.
DR TreeFam; TF333363; -.
DR BioGRID-ORCS; 22770; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Zhx1; mouse.
DR PRO; PR:P70121; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P70121; protein.
DR Bgee; ENSMUSG00000022361; Expressed in undifferentiated genital tubercle and 75 other tissues.
DR ExpressionAtlas; P70121; baseline and differential.
DR Genevisible; P70121; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:GO_Central.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO: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:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR CDD; cd00086; homeodomain; 5.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR024578; Homez_homeobox_dom.
DR InterPro; IPR041057; ZHX_Znf_C2H2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00046; Homeodomain; 4.
DR Pfam; PF11569; Homez; 1.
DR Pfam; PF18387; zf_C2H2_ZHX; 1.
DR SMART; SM00389; HOX; 5.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF46689; SSF46689; 5.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS50071; HOMEOBOX_2; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Homeobox; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..873
FT /note="Zinc fingers and homeoboxes protein 1"
FT /id="PRO_0000049389"
FT ZN_FING 70..93
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT ECO:0000305"
FT ZN_FING 102..125
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042,
FT ECO:0000305"
FT DNA_BIND 284..346
FT /note="Homeobox 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108,
FT ECO:0000305"
FT DNA_BIND 464..526
FT /note="Homeobox 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108,
FT ECO:0000305"
FT DNA_BIND 569..630
FT /note="Homeobox 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108,
FT ECO:0000305"
FT DNA_BIND 660..722
FT /note="Homeobox 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108,
FT ECO:0000305"
FT DNA_BIND 777..832
FT /note="Homeobox 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108,
FT ECO:0000305"
FT REGION 41..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..564
FT /note="Required for interaction with NFYA"
FT /evidence="ECO:0000250"
FT REGION 272..432
FT /note="Required for dimerization"
FT /evidence="ECO:0000250"
FT REGION 429..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..768
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 829..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..873
FT /note="Required for repressor activity"
FT /evidence="ECO:0000250"
FT COMPBIAS 44..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..762
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..855
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..873
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKY1"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKY1"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKY1"
FT CROSSLNK 159
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKY1"
FT CROSSLNK 441
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKY1"
FT CROSSLNK 485
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKY1"
FT CROSSLNK 629
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKY1"
FT CONFLICT 375
FT /note="S -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="C -> Y (in Ref. 3; BAC34629)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="A -> R (in Ref. 1; CAA90905)"
FT /evidence="ECO:0000305"
FT CONFLICT 867..868
FT /note="KL -> NV (in Ref. 1; CAA90905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 873 AA; 97551 MW; 98C5D5714D479364 CRC64;
MASRRKSTTP CMVLASEQDP DLELISDLDE GPPILTPVEN AKAESVSSDE EVHGSVDSDN
QQNKKVEGGY ECKYCTFQTP DLNMFTFHVD SEHPNVVLNS SYVCVECNFL TKRYDALSEH
NLKYHPGEEN FKLTMVKRNN QTIFEQTIND LTFDGSFVKE ENTEQGESID VSSSGISISK
TPIMKMMKNK VENKRITVHH NSAEGTSEEK ENGVKASQEE NAESVSSSAL ESNTSTSTIN
RVHPSPASTV VTPTAVLPGL AQVITAVSAQ QNSNLLPKVL IPVNSIPTYN AALDNNPLLL
NTYNKFPYPT MSEITVLSAQ AKYTEEQIKI WFSAQRLKHG VSWTPEEVEE ARRKQFNGTV
HTVPQTITVI PTHISTGSNG LPSILQTCQI VGQPGLVLTQ VAGTNTLPVT APIALTVAGV
PNQTNVQKSQ VPAAQPATDT KPATAAVPSS PSVRPEAALV NPDSFGIRAK KTKEQLAELK
VSYLKNQFPH DSEIIRLMKI TGLTKGEIKK WFSDTRYNQR NSKSNQCLHL NNDSSATIII
DSSDETPEPP AAAASQQKQS WNPFPDFAPQ KFKEKTAEQL RALQASFLNS SVLTDEEVNR
LRAQTKLTRR EIDAWFTEKN KTKALKDEKI EVDESNVGSS KEEPGESSPG DETVAPKSGG
TGKICKKTPE QLHMLKSAFV RTQWPSAEEY DKLAEESGLA RTDIVSWFGD TRYAWKNGNL
KWYYYYQSSN SSSLNGLSSL RRRGRGRPKG RGRGRPRGRP RGGKRMNTWD RVPSLIKFKT
GTAILKDYYL KHKFLNEQDL DELVNRSHMG YEQVREWFAE RQRRSELGIE LFEENEEEDE
VVDDQEEDEE ETDDSDTWEP PRHVKRKLSK SDD
