ID   JADE1_XENLA             Reviewed;         827 AA.
AC   Q6GQJ2;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Protein Jade-1;
DE   AltName: Full=Jade family PHD finger protein 1;
DE   AltName: Full=PHD finger protein 17;
GN   Name=jade1; Synonyms=phf17;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Scaffold subunit of some HBO1 complexes, which have a histone
CC       H4 acetyltransferase activity. Plays a key role in HBO1 complex by
CC       directing KAT7/HBO1 specificity towards histone H4 acetylation (H4K5ac,
CC       H4K8ac and H4K12ac), regulating DNA replication initiation, regulating
CC       DNA replication initiation. {ECO:0000250|UniProtKB:Q6IE81}.
CC   -!- SUBUNIT: Component of the HBO1 complex composed.
CC       {ECO:0000250|UniProtKB:Q6IE81}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6IE81}.
CC       Chromosome {ECO:0000250|UniProtKB:Q6IE81}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q6IE81}. Cytoplasm, cytoskeleton, cilium basal
CC       body {ECO:0000250|UniProtKB:Q6IE81}. Note=Localizes to the ciliary
CC       transition zone. {ECO:0000250|UniProtKB:Q6IE81}.
CC   -!- DOMAIN: The 2 PHD-type zinc fingers are required for transcriptional
CC       activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the JADE family. {ECO:0000305}.
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DR   EMBL; BC072750; AAH72750.1; -; mRNA.
DR   RefSeq; NP_001085440.1; NM_001091971.1.
DR   AlphaFoldDB; Q6GQJ2; -.
DR   SMR; Q6GQJ2; -.
DR   DNASU; 443866; -.
DR   GeneID; 443866; -.
DR   KEGG; xla:443866; -.
DR   CTD; 443866; -.
DR   Xenbase; XB-GENE-949218; jade1.S.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 443866; Expressed in pancreas and 18 other tissues.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   CDD; cd15679; PHD_JADE1; 1.
DR   Gene3D; 3.30.40.10; -; 2.
DR   InterPro; IPR019542; Enhancer_polycomb-like_N.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR039546; Jade-1_PHD.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF10513; EPL1; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   2: Evidence at transcript level;
KW   Activator; Apoptosis; Cell projection; Chromosome; Cytoplasm; Cytoskeleton;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..827
FT                   /note="Protein Jade-1"
FT                   /id="PRO_0000253532"
FT   ZN_FING         200..250
FT                   /note="PHD-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         252..286
FT                   /note="C2HC pre-PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT   ZN_FING         310..366
FT                   /note="PHD-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          769..810
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..683
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   827 AA;  94392 MW;  58B2B67ECF2EA830 CRC64;
     MKRVCLPSSS EDSDDNGSLS TSWSQHSRSL PSFRHEDRKP SEVFRTDLIT AMKLHDSNQL
     NPEDYYVLAD PWRQEWEKGV QVPVNPEFIP ETIARVIAEK DKVVTFTRPR KYIHSSGSEP
     PEVGYVDIQT LADAVCRYDL NEMDVAWLQL INEEFKEMGM QQLDEYTMEQ VLEEFEKKCY
     DKMNHAIETE EGLGIEYDED VVCDVCQSPD GEDGNEMVFC DKCNICVHQA CYGILKVPEG
     SWLCRTCALG VQPKCLLCPK KGGAMKPTRS GTKWVHVSCA LWIPEVSIGS PEKMEPITKV
     SHIPSNRWAL LCSLCNEKVG ACIQCSIKNC RTAFHVTCAF DHGLEMKTIL TQEDEVKFKS
     YCPKHGSTKK PEDSHFCRSA SDGKDTCEAS PTFLGGLRVL EASQQNVKHG SQRKLKLQQL
     EDDFYSFVDV HDISQALKIP LDVTEYIYQY WKLRRKANFN EPLITPKKDE EDNLAKKEQD
     VLIRRLQLFT HLRQDLERVR NLTYMVTRRE KMKRSVCRVQ EQIFNLYTKI SEQEKDLGFP
     LENGLLFNTQ PSNPDAPKIE DLKWHSAFFR KRLGSSLRCS MKDSHKKSRE RIIGKSLDTE
     ILLTDRKKEG QTSDVSFPLE KTVAKIKPVQ QKNGGSFPEH RKRRDSRTQG DTKFDSKEKP
     LRQQHRPAKH TEPPERPAEK KRALSQCGGK SATASSNKKQ CSSSLPRYSG SLIKIHCNRP
     SVKVPTSPIK NWGGFRIPKK GEKVQPGSME TCQPNLNCQF LGQVSKKGRT KEKVKLDNDN
     DGYTPDAEMS DSESEPTDKC RLQRLTSSSS LSRGYETDFI RRSILAS