ZBED3_HUMAN
ID ZBED3_HUMAN Reviewed; 234 AA.
AC Q96IU2;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Zinc finger BED domain-containing protein 3;
DE AltName: Full=Axin-interacting protein;
GN Name=ZBED3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY HYPERGLYCEMIA
RP AND HYPERINSULINEMIA.
RX PubMed=24283382; DOI=10.1111/joim.12170;
RA Jia Y., Yuan L., Hu W., Luo Y., Suo L., Yang M., Chen S., Wang Y., Liu H.,
RA Yang G., Li L.;
RT "Zinc-finger BED domain-containing 3 (Zbed3) is a novel secreted protein
RT associated with insulin resistance in humans.";
RL J. Intern. Med. 275:522-533(2014).
CC -!- FUNCTION: Acts as a positive regulator in the activation of the
CC canonical Wnt/beta-catenin signaling pathway by stabilizing cytoplasmic
CC beta-catenin (By similarity). Involved in transcription activation of
CC Wnt target gene expression (By similarity). Plays a role in symmetric
CC division of blastomeres in the early stages of embryogenesis via
CC regulation of mitotic spindle central positioning and organization of
CC the F-actin filament network (By similarity). Plays a role in
CC regulating the distribution of cellular organelles, via modulation of
CC cytoskeletal dynamics and cytoplasmic lattice formation (By
CC similarity). {ECO:0000250|UniProtKB:Q9D0L1}.
CC -!- SUBUNIT: Associates with the subcortical maternal complex (SCMC)
CC composed of at least NLRP5, KHDC3L, OOEP, and TLE6 via interaction with
CC NLRP5 and TLE6 (By similarity). Interacts with AXIN1; the interaction
CC is direct, enhanced by protein kinase GSK3B and casein kinase CSNK1E
CC activities and decreases GSK3B-induced beta-catenin serine and
CC threonine phosphorylations (By similarity).
CC {ECO:0000250|UniProtKB:Q9D0L1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9D0L1}.
CC Membrane {ECO:0000250|UniProtKB:Q9D0L1}. Secreted
CC {ECO:0000269|PubMed:24283382}.
CC -!- TISSUE SPECIFICITY: Secreted in blood plasma, and expressed in skeletal
CC muscle and adipose tissue (at protein level).
CC {ECO:0000269|PubMed:24283382}.
CC -!- INDUCTION: Induced in blood plasma by hyperglycemia (PubMed:24283382).
CC Decreased in blood plasma by hyperinsulinemia (PubMed:24283382).
CC {ECO:0000269|PubMed:24283382}.
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DR EMBL; AC008581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007239; AAH07239.1; -; mRNA.
DR CCDS; CCDS4036.1; -.
DR RefSeq; NP_001316493.1; NM_001329564.1.
DR RefSeq; NP_115743.1; NM_032367.3.
DR AlphaFoldDB; Q96IU2; -.
DR SMR; Q96IU2; -.
DR BioGRID; 124051; 7.
DR IntAct; Q96IU2; 2.
DR STRING; 9606.ENSP00000255198; -.
DR iPTMnet; Q96IU2; -.
DR PhosphoSitePlus; Q96IU2; -.
DR BioMuta; ZBED3; -.
DR DMDM; 34925646; -.
DR jPOST; Q96IU2; -.
DR MassIVE; Q96IU2; -.
DR MaxQB; Q96IU2; -.
DR PaxDb; Q96IU2; -.
DR PeptideAtlas; Q96IU2; -.
DR PRIDE; Q96IU2; -.
DR ProteomicsDB; 76853; -.
DR Antibodypedia; 24479; 88 antibodies from 24 providers.
DR DNASU; 84327; -.
DR Ensembl; ENST00000255198.3; ENSP00000255198.2; ENSG00000132846.6.
DR GeneID; 84327; -.
DR KEGG; hsa:84327; -.
DR MANE-Select; ENST00000255198.3; ENSP00000255198.2; NM_032367.4; NP_115743.1.
DR UCSC; uc003kev.2; human.
DR CTD; 84327; -.
DR DisGeNET; 84327; -.
DR GeneCards; ZBED3; -.
DR HGNC; HGNC:20711; ZBED3.
DR HPA; ENSG00000132846; Low tissue specificity.
DR MIM; 615250; gene.
DR neXtProt; NX_Q96IU2; -.
DR OpenTargets; ENSG00000132846; -.
DR PharmGKB; PA134974972; -.
DR VEuPathDB; HostDB:ENSG00000132846; -.
DR eggNOG; ENOG502SQ4N; Eukaryota.
DR GeneTree; ENSGT00940000164103; -.
DR HOGENOM; CLU_112726_0_0_1; -.
DR InParanoid; Q96IU2; -.
DR OMA; RDSCVIT; -.
DR OrthoDB; 1464780at2759; -.
DR PhylomeDB; Q96IU2; -.
DR TreeFam; TF338048; -.
DR PathwayCommons; Q96IU2; -.
DR SignaLink; Q96IU2; -.
DR BioGRID-ORCS; 84327; 14 hits in 1085 CRISPR screens.
DR ChiTaRS; ZBED3; human.
DR GenomeRNAi; 84327; -.
DR Pharos; Q96IU2; Tbio.
DR PRO; PR:Q96IU2; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96IU2; protein.
DR Bgee; ENSG00000132846; Expressed in kidney epithelium and 157 other tissues.
DR ExpressionAtlas; Q96IU2; baseline and differential.
DR Genevisible; Q96IU2; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0051643; P:endoplasmic reticulum localization; ISS:UniProtKB.
DR GO; GO:0051293; P:establishment of spindle localization; ISS:UniProtKB.
DR GO; GO:0051646; P:mitochondrion localization; ISS:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0040019; P:positive regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009749; P:response to glucose; IDA:UniProtKB.
DR GO; GO:0032868; P:response to insulin; IDA:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR043471; ZBED2/3.
DR InterPro; IPR033546; ZBED3.
DR InterPro; IPR003656; Znf_BED.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR35827; PTHR35827; 1.
DR PANTHER; PTHR35827:SF2; PTHR35827:SF2; 1.
DR Pfam; PF02892; zf-BED; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50808; ZF_BED; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Metal-binding; Reference proteome; Secreted;
KW Wnt signaling pathway; Zinc; Zinc-finger.
FT CHAIN 1..234
FT /note="Zinc finger BED domain-containing protein 3"
FT /id="PRO_0000066562"
FT ZN_FING 43..104
FT /note="BED-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT REGION 19..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
SQ SEQUENCE 234 AA; 25132 MW; 3E615F16B68EE3B2 CRC64;
MRSGEPACTM DQARGLDDAA ARGGQCPGLG PAPTPTPPGR LGAPYSEAWG YFHLAPGRPG
HPSGHWATCR LCGEQVGRGP GFHAGTSALW RHLRSAHRRE LESSGAGSSP PAAPCPPPPG
PAAAPEGDWA RLLEQMGALA VRGSRREREL ERRELAVEQG ERALERRRRA LQEEERAAAQ
ARRELQAERE ALQARLRDVS RREGALGWAP AAPPPLKDDP EGDRDGCVIT KVLL
