JADE1_DANRE
ID JADE1_DANRE Reviewed; 829 AA.
AC Q803A0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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; ORFNames=zgc:55323;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION.
RX PubMed=14612400; DOI=10.1128/mcb.23.23.8553-8562.2003;
RA Tzouanacou E., Tweedie S., Wilson V.;
RT "Identification of Jade1, a gene encoding a PHD zinc finger protein, in a
RT gene trap mutagenesis screen for genes involved in anteroposterior axis
RT development.";
RL Mol. Cell. Biol. 23:8553-8562(2003).
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; BC046874; AAH46874.1; -; mRNA.
DR EMBL; BN000276; CAE30491.1; -; mRNA.
DR RefSeq; NP_956099.1; NM_199805.1.
DR AlphaFoldDB; Q803A0; -.
DR SMR; Q803A0; -.
DR BioGRID; 84576; 1.
DR STRING; 7955.ENSDARP00000042059; -.
DR PaxDb; Q803A0; -.
DR PRIDE; Q803A0; -.
DR GeneID; 327437; -.
DR KEGG; dre:327437; -.
DR CTD; 79960; -.
DR ZFIN; ZDB-GENE-030131-5648; jade1.
DR eggNOG; KOG0954; Eukaryota.
DR InParanoid; Q803A0; -.
DR OrthoDB; 1235709at2759; -.
DR PhylomeDB; Q803A0; -.
DR Reactome; R-DRE-3214847; HATs acetylate histones.
DR PRO; PR:Q803A0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IGI:ZFIN.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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..829
FT /note="Protein Jade-1"
FT /id="PRO_0000253531"
FT ZN_FING 196..246
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 248..282
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 306..362
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 829 AA; 94548 MW; 4AF7760FC43DB54C CRC64;
MKRSRVPSTS EDSDNGSNST SWSQHSNSKH RKQSGKRPSE VFRTDLITAM KLHDSHQLNP
EDYYELADPW RQEWEKGVQV PVSPESIPQC AVRTVAEKST APLFIKPKKL IRSSESSMLG
YVGIQTLADG MCRYDLNEED VAWLQITNEE FSKMGMQPLD ELTMERVMEE FERRCYDNMS
HAMETEEGLG IEYDEDVVCD VCQSPDGEDG NEMVFCDKCN ICVHQACYGI LKVPEGSWLC
RTCALGIFPK CHLCPKKGGA MKPTRSGTKW VHVSCALWIP EVSIGNPEKM EPITNVSHIP
SNRWALICCL CKEKTGACIQ CSAKSCRVAF HVTCGLHCGL KMNTILTEAD EVKFKSFCPK
HSGLDWNEEE GDDDRPVKVP TREDRSRNRG IDFSASSQTR LSQNPEETRL SERKLRVQQL
EDEFYRFVAA DEVAEHLQLP LEMVDILFQY WKLKRKVNFN QPLIMPKKEE EDSLARREQE
VLLRRLRLFT HLRQDLERVR NLTYMVSRRE RIKRTLCRVQ EQIFHHHVRL LEQGRVTGVS
STRRLEEAMF YFRTTPPVPA SPQPLKGHCG QNSTLSSSEK GSNSYRSSKH IEADKPAKML
MDGVPSSGDS VRSETVMSAS SRRSEGRTRS GESHRKEEES ERPLEDRRRK SKLWDQVSIK
DKLRHAKSME DTLSSETELD TMDDRLLLSH TNANSVATAP NMYSGSPRKT NASHQGKLVP
NGTSGRHLKN WGSFRIPKRS ERTSAGRQTE RQEADNTADQ NSSLKTFSTS PSSPQIRTRL
RTGSENRRHL EESDLGQSEQ GKRCHTQRLP SPMTRRYGSD VIQRGVLAS
