ZHX3_MOUSE
ID ZHX3_MOUSE Reviewed; 951 AA.
AC Q8C0Q2; Q80U14;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Zinc fingers and homeoboxes protein 3;
DE AltName: Full=Triple homeobox protein 1;
DE AltName: Full=Zinc finger and homeodomain protein 3;
GN Name=Zhx3; Synonyms=Kiaa0395, Tix1 {ECO:0000312|MGI:MGI:2444772};
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:BAC26763.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=129 {ECO:0000269|PubMed:14659886};
RX PubMed=14659886; DOI=10.1016/j.gene.2003.09.013;
RA Kawata H., Yamada K., Shou Z., Mizutani T., Miyamoto K.;
RT "The mouse zinc-fingers and homeoboxes (ZHX) family: ZHX2 forms a
RT heterodimer with ZHX3.";
RL Gene 323:133-140(2003).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26763.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAC26763.1};
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 [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH58111.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH58111.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 754-951.
RC TISSUE=Brain {ECO:0000312|EMBL:BAC65553.1};
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
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. Involved in the early
CC stages of mesenchymal stem cell (MSC) osteogenic differentiation. Is a
CC regulator of podocyte gene expression during primary glomerula disease.
CC Binds to promoter DNA.
CC -!- SUBUNIT: Homodimer (via homeobox domain 1). Heterodimer with ZHX1 (via
CC homeobox domain 1). Heterodimer with ZHX2 (via homeobox domain 1).
CC Heterodimerization with ZHX1 is a prerequisite for repressor activity.
CC Interacts with NFYA. {ECO:0000250|UniProtKB:Q9H4I2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H4I2,
CC ECO:0000255|PROSITE-ProRule:PRU00108}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:14659886}.
CC -!- SIMILARITY: Belongs to the ZHX family. {ECO:0000255}.
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DR EMBL; AB099527; BAC87711.2; -; mRNA.
DR EMBL; AB099703; BAC87741.2; -; Genomic_DNA.
DR EMBL; AK030057; BAC26763.1; -; mRNA.
DR EMBL; BC058111; AAH58111.1; -; mRNA.
DR EMBL; AK122271; BAC65553.1; -; mRNA.
DR CCDS; CCDS16997.1; -.
DR RefSeq; NP_796237.2; NM_177263.3.
DR AlphaFoldDB; Q8C0Q2; -.
DR SMR; Q8C0Q2; -.
DR STRING; 10090.ENSMUSP00000099400; -.
DR iPTMnet; Q8C0Q2; -.
DR PhosphoSitePlus; Q8C0Q2; -.
DR MaxQB; Q8C0Q2; -.
DR PaxDb; Q8C0Q2; -.
DR PRIDE; Q8C0Q2; -.
DR ProteomicsDB; 275370; -.
DR Antibodypedia; 1834; 150 antibodies from 21 providers.
DR DNASU; 320799; -.
DR Ensembl; ENSMUST00000103111; ENSMUSP00000099400; ENSMUSG00000035877.
DR Ensembl; ENSMUST00000103112; ENSMUSP00000099401; ENSMUSG00000035877.
DR Ensembl; ENSMUST00000109460; ENSMUSP00000105086; ENSMUSG00000035877.
DR GeneID; 320799; -.
DR KEGG; mmu:320799; -.
DR UCSC; uc008nre.1; mouse.
DR CTD; 23051; -.
DR MGI; MGI:2444772; Zhx3.
DR VEuPathDB; HostDB:ENSMUSG00000035877; -.
DR eggNOG; ENOG502RC6G; Eukaryota.
DR GeneTree; ENSGT00950000182893; -.
DR HOGENOM; CLU_009147_1_0_1; -.
DR InParanoid; Q8C0Q2; -.
DR OMA; ACEPEDD; -.
DR OrthoDB; 518562at2759; -.
DR PhylomeDB; Q8C0Q2; -.
DR TreeFam; TF333363; -.
DR BioGRID-ORCS; 320799; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Zhx3; mouse.
DR PRO; PR:Q8C0Q2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8C0Q2; protein.
DR Bgee; ENSMUSG00000035877; Expressed in otolith organ and 218 other tissues.
DR ExpressionAtlas; Q8C0Q2; baseline and differential.
DR Genevisible; Q8C0Q2; MM.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; 2.
DR Pfam; PF11569; Homez; 1.
DR Pfam; PF18387; zf_C2H2_ZHX; 1.
DR SMART; SM00389; HOX; 4.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF46689; SSF46689; 5.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 4.
PE 1: Evidence at protein level;
KW Differentiation; DNA-binding; Homeobox; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..951
FT /note="Zinc fingers and homeoboxes protein 3"
FT /id="PRO_0000049396"
FT ZN_FING 77..100
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255"
FT ZN_FING 109..132
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255"
FT DNA_BIND 300..359
FT /note="Homeobox 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 489..548
FT /note="Homeobox 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 607..666
FT /note="Homeobox 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 759..818
FT /note="Homeobox 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 830..889
FT /note="Homeobox 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..107
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..483
FT /note="Required for homodimerization and interaction with
FT NFYA"
FT /evidence="ECO:0000250"
FT REGION 299..497
FT /note="Required for repressor activity"
FT /evidence="ECO:0000250"
FT REGION 492..550
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 662..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4I2"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4I2"
FT MOD_RES 922
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4I2"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4I2"
FT CONFLICT 763
FT /note="S -> N (in Ref. 2; BAC26763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 951 AA; 104343 MW; C6625D6FB139E3DE CRC64;
MASKRKSTTP CMIPVKTVVL PGASTEPQPV ESLPEGPQQD LPSEAPDASS EAAPNPSSTD
GSALANGHRS TLDGYVYCCK ECEFRSQDVT HFIGHMNSEH TDFNKDPTFV CTGCSFLAKN
PEGLSLHNAK CHSGEASFLW NVTKPDNHVV VEQSVPDSAS SSVLAGESTT EGTEIIITKT
PIMKIMKGKA EAKKIHMLKE NAPNQPGSEA LPKPLAGERE VKEGDHTFIN GAAPGSQASA
KSTKPPPAAN GPLIGTVPVL PAGIAQFLSL QQQPPVHAQH HTHQPLPTSK TLPKVMIPLS
SIPTYNAAMD SNSFLKNSFH KFPYPTKAEL CYLTVVTKYP EEQLKIWFTA QRLKQGISWS
PEEIEDARKK MFNTVIQSVP QPTITVLNTP LVASAGNVQH LIQATLPGHA VGQPEGTAGG
LLVTQPLMAN GLQASSSSLP LTTASVPKPT VAPINTVCSN SASAVKVVNA AQSLLTACPS
ITSQAFLDAN IYKNKKSHEQ LSALKGSFCR NQFPGQSEVE HLTKVTGLST REVRKWFSDR
RYHCRNLKGS RAMMPGEHGS VLIDSVPEVP FPLASKVPEV TCIPTATSLV SHPATKRQSW
HQTPDFTPTK YKERAPEQLR VLENSFAQNP LPPEEELDRL RSETKMTRRE IDGWFSERRK
KVNTEETKKA DGHMPKEEEE GAEQEGRDEE LANELRVPGE NGSPEMFLSH ALAERKVSPI
KINLKNLRVT EASGKSEFPG MGVCEPEEDG LNKLVEQPPS KVSYKKTAQQ RHLLRQLFVQ
TQWPSNQDYD SIMAQTGLPR PEVVRWFGDS RYALKNGQLK WYEDYKRGNF PPGLLVIAPG
NRELLQDYYM THKMLCEEDL QTLCDKTQMS AQQVKQWFAE KMGEETRAVA DISSEDQGPR
NGEPVAVHKV LGDAYSELSE NSESWEPSAP EASSEPFDTS SPQSGRQLEA D
