ZHX1_RAT
ID ZHX1_RAT Reviewed; 873 AA.
AC Q8R515;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Zinc fingers and homeoboxes protein 1;
GN Name=Zhx1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:BAB85763.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], HOMODIMERIZATION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC TISSUE=Ovary {ECO:0000312|EMBL:BAB85763.1};
RX PubMed=12062805; DOI=10.1016/s0378-1119(02)00553-x;
RA Hirano S., Yamada K., Kawata H., Shou Z., Mizutani T., Yazawa T.,
RA Kajitani T., Sekiguchi T., Yoshino M., Shigematsu Y., Mayumi M.,
RA Miyamoto K.;
RT "Rat zinc-fingers and homeoboxes 1 (ZHX1), a nuclear factor-YA-interacting
RT nuclear protein, forms a homodimer.";
RL Gene 290:107-114(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-48, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:12062805}. Note=Colocalized in the nucleus with
CC DNMT3B. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12062805}.
CC -!- INDUCTION: Not induced by gonadotropins. {ECO:0000269|PubMed:12062805}.
CC -!- SIMILARITY: Belongs to the ZHX family. {ECO:0000305}.
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DR EMBL; AB072439; BAB85763.1; -; mRNA.
DR RefSeq; NP_598304.1; NM_133620.1.
DR AlphaFoldDB; Q8R515; -.
DR SMR; Q8R515; -.
DR BioGRID; 251160; 2.
DR IntAct; Q8R515; 1.
DR MINT; Q8R515; -.
DR STRING; 10116.ENSRNOP00000008454; -.
DR iPTMnet; Q8R515; -.
DR PhosphoSitePlus; Q8R515; -.
DR PaxDb; Q8R515; -.
DR PRIDE; Q8R515; -.
DR GeneID; 171159; -.
DR KEGG; rno:171159; -.
DR UCSC; RGD:620010; rat.
DR CTD; 11244; -.
DR RGD; 620010; Zhx1.
DR eggNOG; ENOG502QT3D; Eukaryota.
DR InParanoid; Q8R515; -.
DR PhylomeDB; Q8R515; -.
DR PRO; PR:Q8R515; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
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; IDA:RGD.
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_0000049390"
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..631
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 1..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 430..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..664
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..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..247
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:0000250|UniProtKB:Q9UKY1"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKY1"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKY1"
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"
SQ SEQUENCE 873 AA; 97570 MW; DE4F77FC20CC73AD CRC64;
MASRRKSTTP CMVLASEQDP DLELISDLEE GPPVLTPVEN ARAESVSSDE EVHESVDSDN
QQNKKVEGGY ECKYCTFQTP DLNMFTFHVD SEHPNVVLNS SYVCVECNFL TKRYDALSEH
NLKYHPGEEN FKLTMVKRNN QTIFEQTIND LTFDGSFVKE ENTEQGESID VSSSGISISK
TPIMKMMKNK VENKRITVHH NSAEGTSEEK ENGVKASREE NAENTSSSAS ESNTSTSTVN
QVHPSPAGTV VTPTAVLPGL AQVITAVSAQ QNSNLVPKVL IPVNSIPTYN AALDNNPLLL
NTYNKFPYPT MSEITVLSAQ AKYTEEQIKI WFSAQRLKHG VSWTPEEVEE ARRKQFNGTV
HTVPQTITVI PTHISTGSNG LPSILQTCQI VGQPGLVLTQ VAGANTLPVT APIALTVAGV
PNQTNVQKSQ VPAAQPAAET KPATAAVPSS PSVRPEAALV NPDSFGIRAK KTKEQLAELK
VSYLKNQFPH DSEIIRLMKI TGLTKGEIKK WFSDTRYNQR NSKSNQCLHL NNDSSATIII
DSSDETPEPP AAAASQPKQS WNPFPDFAPQ KFKEKTAEQL RVLQASFLNS SVLTDEELNR
LRAQTKLTRR EIDAWFTEKN KTKALKDEKV EVDESNVGSS KEEPGENSPG DEAVAPKSAG
TGKICKKTPE QLHMLKSAFV RTQWPSPEEY DKLAEESGLA RTDIVSWFGD TRYAWKNGNL
KWYYYYQSSN SSSLNGLSSL RKRGRGRPKG RGRGRPRGRP RGGKRMNTWD RVPSLIKFKT
GTAILKDYYL KHKFLNEQDL DELVNRSHMG YEQVREWFAE RQRRSELGIE LFEENEEEDE
VIDDQEEDEE ETDDSDTWEP PRHVKRKLSK SDD
