ZHX1_PANPA
ID ZHX1_PANPA Reviewed; 873 AA.
AC A1YG99;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Zinc fingers and homeoboxes protein 1;
GN Name=ZHX1;
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nickel G.C., Tefft D.L., Trevarthen K., Funt J., Adams M.D.;
RT "Positive selection in transcription factor genes on the human lineage.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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. Note=Colocalized in the nucleus with
CC DNMT3B. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ZHX family. {ECO:0000305}.
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DR EMBL; DQ977244; ABM54324.1; -; Genomic_DNA.
DR RefSeq; XP_003820532.1; XM_003820484.2.
DR RefSeq; XP_003820533.1; XM_003820485.2.
DR AlphaFoldDB; A1YG99; -.
DR SMR; A1YG99; -.
DR STRING; 9597.XP_003820532.1; -.
DR GeneID; 100984802; -.
DR KEGG; pps:100984802; -.
DR CTD; 11244; -.
DR eggNOG; ENOG502QT3D; Eukaryota.
DR OrthoDB; 518562at2759; -.
DR Proteomes; UP000240080; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 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 3: Inferred from homology;
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_0000285461"
FT ZN_FING 70..93
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 102..125
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 284..346
FT /note="Homeobox 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 464..526
FT /note="Homeobox 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 569..630
FT /note="Homeobox 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 660..722
FT /note="Homeobox 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 777..832
FT /note="Homeobox 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 24..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..236
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 626..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..769
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 200..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..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:0000250|UniProtKB:Q9UKY1"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKY1"
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 454
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; 98098 MW; E04EA2F9C36BEF6A CRC64;
MASRRKSTTP CMVLASEQDP DLELISDLDE GPPVLTPVEN TRAESISSDE EVHESVDSDN
QQNKKVEGGY ECKYCTFQTP DLNMFTFHVD SEHPNVVLNS SYVCVECNFL TKRYDALSEH
NLKYHPGEEN FKLTMVKRNN QTIFEQTIND LTFDGSFIKE ENAEQAESTE VSSSGISISK
TPIMKMMKNK VENKRIAVHH NSVEDVPEEK ENEIKPDREE IVENPSSSAS ESNTSTSIVN
RIHPSTASTV VTPAAVLPGL AQVITAVSAQ QNSNLIPKVL IPVNSIPTYN AALDNNPLLL
NTYNKFPYPT MSEITVLSAQ AKYTEEQIKI WFSAQRLKHG VSWTPEEVEE ARRKQFNGTV
HTVPQTITVI PTHISTGSNG LPSILQTCQI VGQPGLVLTQ VAGTNTLPVT APIALTVAGV
PSQNNIQKSQ VPAAQPTAET KPATAAVPTS QSVKHETALV NPDSFGIRAK KTKEQLAELK
VSYLKNQFPH DSEIIRLMKI TGLTKGEIKK WFSDTRYNQR NSKSNQCLHL NNDSSTTIII
DSSDETTESP TVGTAQPKQS WNPFPDFTPQ KFKEKTAEQL RVLQASFLNS SVLTDEELNR
LRAQTKLTRR EIDAWFTEKK KSKALKEEKM EIDESNAGSS KEEAGETSPG DESGAPKSGS
TGKICKKTPE QLHMLKSAFV RTQWPSPEEY DKLAKESGLA RTDIVSWFGD TRYAWKNGNL
KWYYYYQSAN SSSMNGLSSL RKRGRGRPKG RGRGRPRGRP RGSKRINNWD RGPSLIKFKT
GTAILKDYYL KHKFLNEQDL DELVNKSHMG YEQVREWFAE RQRRSELGIE LFEENEEEDE
VIDDQEEDEE ETDDSDTWEP PRHVKRKLSK SDD
