JADE1_BOVIN
ID JADE1_BOVIN Reviewed; 509 AA.
AC Q5E9T7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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. May also promote acetylation of nucleosomal
CC histone H4 by KAT5. Promotes apoptosis. May act as a renal tumor
CC suppressor. Negatively regulates canonical Wnt signaling; at least in
CC part, cooperates with NPHP4 in this function.
CC {ECO:0000250|UniProtKB:Q6IE81}.
CC -!- SUBUNIT: Component of the HBO1 complex composed at least of ING4 or
CC ING5, KAT7/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3. Interacts
CC with NPHP4. {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; BT020833; AAX08850.1; -; mRNA.
DR RefSeq; NP_001015559.1; NM_001015559.1.
DR AlphaFoldDB; Q5E9T7; -.
DR SMR; Q5E9T7; -.
DR STRING; 9913.ENSBTAP00000032057; -.
DR PaxDb; Q5E9T7; -.
DR PRIDE; Q5E9T7; -.
DR GeneID; 509264; -.
DR KEGG; bta:509264; -.
DR CTD; 79960; -.
DR eggNOG; KOG0954; Eukaryota.
DR InParanoid; Q5E9T7; -.
DR OrthoDB; 1235709at2759; -.
DR Proteomes; UP000009136; 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; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
DR GO; GO:0043983; P:histone H4-K12 acetylation; ISS:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
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 Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..509
FT /note="Protein Jade-1"
FT /id="PRO_0000253528"
FT ZN_FING 203..253
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 255..289
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 313..369
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..80
FT /note="Interaction with KAT7/HBO1 and histones"
FT /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT REGION 80..188
FT /note="Interaction with histones"
FT /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT REGION 373..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT CROSSLNK 114
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6IE81"
SQ SEQUENCE 509 AA; 58312 MW; A624A7008000BB88 CRC64;
MKRGRLPSSS EDSDDNGSLS TTWSQNSRSQ HRRSSCSRPE DRKPSEVFRT DLITAMKLHD
SYQLNPDEYY VLADPWRQEW EKGVQVPVSP GTIPQPVARV VSEEKSLMFI RPKKYIVSSG
SEPPELGYVD IRTLADSVCR YDLNDMDAAW LELTNEEFKE MGMPELDEYT MERVLEEFEQ
RCYDNMNHAI ETEEGLGIEY DEYVVCDVCQ SPDGEDGNEM VFCDKCNICV HQACYGILKV
PEGSWLCRTC ALGVQPKCLL CPKKGGAMKP TRSGTKWVHV SCALWIPEVS IGSPEKMEPI
TKVSHIPSSR WALVCSLCNE KFGASIQCSV KNCRTAFHVT CAFDRGLEMK TILAENDEVK
FKSYCPKHSS HRKAEEGLGE GTAQENGAPE CSPRDPLEPF AGLEQNREEA HRVSVRKQKL
QQLEDEFYTF VNLLDVARAL RLPEEVVDFL YQYWKLKRKV NFNKPLITPK KDEEDNLAKR
EQDVLFRRLQ LFTHLRQDLE RVMTDTDTL
