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ZBED2_HUMAN
ID   ZBED2_HUMAN             Reviewed;         218 AA.
AC   Q9BTP6; D3DN62;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Zinc finger BED domain-containing protein 2;
GN   Name=ZBED2;
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=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary, and Uterus;
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   [4]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=31552090; DOI=10.3389/fgene.2019.00775;
RA   Finnegan A., Cho R.J., Luu A., Harirchian P., Lee J., Cheng J.B.,
RA   Song J.S.;
RT   "Single-Cell Transcriptomics Reveals Spatial and Temporal Turnover of
RT   Keratinocyte Differentiation Regulators.";
RL   Front. Genet. 10:775-775(2019).
RN   [5]
RP   FUNCTION, AND INDUCTION BY TGF-BETA.
RX   PubMed=32385160; DOI=10.1073/pnas.1921484117;
RA   Somerville T.D.D., Xu Y., Wu X.S., Maia-Silva D., Hur S.K.,
RA   de Almeida L.M.N., Preall J.B., Koo P.K., Vakoc C.R.;
RT   "ZBED2 is an antagonist of interferon regulatory factor 1 and modifies cell
RT   identity in pancreatic cancer.";
RL   Proc. Natl. Acad. Sci. U.S.A. 117:11471-11482(2020).
RN   [6]
RP   STRUCTURE BY NMR OF 55-117.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structures of the C2H2 type zinc finger domain of human zinc
RT   finger BED domain containing protein 2.";
RL   Submitted (OCT-2006) to the PDB data bank.
RN   [7]
RP   VARIANT MET-2 DEL.
RX   PubMed=32383616; DOI=10.34172/aim.2020.21;
RA   Mehrjoo Z., Kahrizi K., Mohseni M., Akbari M., Arzhangi S., Jalalvand K.,
RA   Najmabadi H., Farhadi M., Mohseni M., Asghari A., Mohebbi S., Daneshi A.;
RT   "Limbic System Associated Membrane Protein Mutation in an Iranian Family
RT   Diagnosed with Meniere's Disease.";
RL   Arch. Iran. Med. 23:319-325(2020).
CC   -!- FUNCTION: Transcriptional regulator which has intrinsic repressor
CC       activity and which competes with the transcriptional activator IRF1 for
CC       binding to the 5'-[CA]GAA[AC]C[CT]-3' consensus sequence in gene
CC       promoters (PubMed:32385160). May thereby play a role in keratinocyte
CC       differentiation (PubMed:31552090). {ECO:0000269|PubMed:31552090,
CC       ECO:0000269|PubMed:32385160}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:32385160}.
CC   -!- TISSUE SPECIFICITY: Expressed in keratinocytes.
CC       {ECO:0000269|PubMed:31552090}.
CC   -!- INDUCTION: Induced by TGF-beta. {ECO:0000269|PubMed:32385160}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH03536.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH71956.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AC055748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471052; EAW79699.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW79700.1; -; Genomic_DNA.
DR   EMBL; BC003536; AAH03536.1; ALT_INIT; mRNA.
DR   EMBL; BC071956; AAH71956.1; ALT_INIT; mRNA.
DR   CCDS; CCDS2960.2; -.
DR   RefSeq; NP_078784.2; NM_024508.4.
DR   PDB; 2DJR; NMR; -; A=55-117.
DR   PDBsum; 2DJR; -.
DR   AlphaFoldDB; Q9BTP6; -.
DR   SMR; Q9BTP6; -.
DR   BioGRID; 122663; 4.
DR   IntAct; Q9BTP6; 2.
DR   STRING; 9606.ENSP00000321370; -.
DR   iPTMnet; Q9BTP6; -.
DR   PhosphoSitePlus; Q9BTP6; -.
DR   BioMuta; ZBED2; -.
DR   DMDM; 251757414; -.
DR   EPD; Q9BTP6; -.
DR   MassIVE; Q9BTP6; -.
DR   PaxDb; Q9BTP6; -.
DR   PeptideAtlas; Q9BTP6; -.
DR   PRIDE; Q9BTP6; -.
DR   ProteomicsDB; 79003; -.
DR   Antibodypedia; 32442; 62 antibodies from 21 providers.
DR   DNASU; 79413; -.
DR   Ensembl; ENST00000317012.5; ENSP00000321370.4; ENSG00000177494.6.
DR   GeneID; 79413; -.
DR   KEGG; hsa:79413; -.
DR   MANE-Select; ENST00000317012.5; ENSP00000321370.4; NM_024508.5; NP_078784.2.
DR   UCSC; uc003dxy.4; human.
DR   CTD; 79413; -.
DR   GeneCards; ZBED2; -.
DR   HGNC; HGNC:20710; ZBED2.
DR   HPA; ENSG00000177494; Tissue enhanced (lymphoid tissue, thyroid gland).
DR   MalaCards; ZBED2; -.
DR   MIM; 615246; gene.
DR   neXtProt; NX_Q9BTP6; -.
DR   OpenTargets; ENSG00000177494; -.
DR   PharmGKB; PA134879520; -.
DR   VEuPathDB; HostDB:ENSG00000177494; -.
DR   eggNOG; ENOG502SQ4N; Eukaryota.
DR   GeneTree; ENSGT00940000163343; -.
DR   HOGENOM; CLU_112726_0_0_1; -.
DR   InParanoid; Q9BTP6; -.
DR   OMA; TPMPHNK; -.
DR   OrthoDB; 1464780at2759; -.
DR   PhylomeDB; Q9BTP6; -.
DR   TreeFam; TF338048; -.
DR   PathwayCommons; Q9BTP6; -.
DR   SignaLink; Q9BTP6; -.
DR   BioGRID-ORCS; 79413; 30 hits in 1090 CRISPR screens.
DR   EvolutionaryTrace; Q9BTP6; -.
DR   GenomeRNAi; 79413; -.
DR   Pharos; Q9BTP6; Tdark.
DR   PRO; PR:Q9BTP6; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9BTP6; protein.
DR   Bgee; ENSG00000177494; Expressed in tongue squamous epithelium and 92 other tissues.
DR   Genevisible; Q9BTP6; HS.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:HGNC.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR043471; ZBED2/3.
DR   InterPro; IPR003656; Znf_BED.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   PANTHER; PTHR35827; PTHR35827; 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   3D-structure; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..218
FT                   /note="Zinc finger BED domain-containing protein 2"
FT                   /id="PRO_0000066561"
FT   ZN_FING         52..113
FT                   /note="BED-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT   VARIANT         2
FT                   /note="Missing"
FT                   /evidence="ECO:0000269|PubMed:32383616"
FT                   /id="VAR_083712"
FT   HELIX           55..60
FT                   /evidence="ECO:0007829|PDB:2DJR"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:2DJR"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:2DJR"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:2DJR"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:2DJR"
FT   HELIX           97..104
FT                   /evidence="ECO:0007829|PDB:2DJR"
FT   HELIX           107..112
FT                   /evidence="ECO:0007829|PDB:2DJR"
SQ   SEQUENCE   218 AA;  25122 MW;  2E2602FA7FC3BEE2 CRC64;
     MMRREDEEEE GTMMKAKGDL EMKEEEEISE TGELVGPFVS AMPTPMPHNK GTRFSEAWEY
     FHLAPARAGH HPNQYATCRL CGRQVSRGPG VNVGTTALWK HLKSMHREEL EKSGHGQAGQ
     RQDPRPHGPQ LPTGIEGNWG RLLEQVGTMA LWASQREKEV LRRERAVEWR ERAVEKRERA
     LEEVERAILE MKWKVRAEKE ACQREKELPA AVHPFHFV
 
 
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