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BBX19_ARATH
ID   BBX19_ARATH             Reviewed;         183 AA.
AC   C0SVM5; Q6NML9; Q9SVJ7;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=B-box zinc finger protein 19 {ECO:0000303|PubMed:19920209};
DE   AltName: Full=Protein DOUBLE B-BOX 1B;
DE   AltName: Full=Protein SALT TOLERANCE HOMOLOG 5;
GN   Name=BBX19 {ECO:0000303|PubMed:19920209};
GN   Synonyms=DBB1B {ECO:0000303|PubMed:18540109}, STH5;
GN   OrderedLocusNames=At4g38960 {ECO:0000312|Araport:AT4G38960};
GN   ORFNames=F19H22.60 {ECO:0000312|EMBL:CAB38816.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000312|EMBL:BAH30566.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA   Takagi M.;
RT   "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION.
RX   PubMed=18540109; DOI=10.1271/bbb.80041;
RA   Kumagai T., Ito S., Nakamichi N., Niwa Y., Murakami M., Yamashino T.,
RA   Mizuno T.;
RT   "The common function of a novel subfamily of B-Box zinc finger proteins
RT   with reference to circadian-associated events in Arabidopsis thaliana.";
RL   Biosci. Biotechnol. Biochem. 72:1539-1549(2008).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19920209; DOI=10.1105/tpc.109.069088;
RA   Khanna R., Kronmiller B., Maszle D.R., Coupland G., Holm M., Mizuno T.,
RA   Wu S.H.;
RT   "The Arabidopsis B-box zinc finger family.";
RL   Plant Cell 21:3416-3420(2009).
CC   -!- FUNCTION: Acts as negative regulator of seedling photomorphogenesis.
CC       {ECO:0000269|PubMed:18540109}.
CC   -!- INTERACTION:
CC       C0SVM5; Q9LVG4: APRR3; NbExp=4; IntAct=EBI-4430993, EBI-1606968;
CC       C0SVM5; Q8L500: APRR9; NbExp=3; IntAct=EBI-4430993, EBI-7920168;
CC       C0SVM5; C0SV91: At2g46670; NbExp=3; IntAct=EBI-4430993, EBI-15192193;
CC       C0SVM5; O82617: BBX23; NbExp=3; IntAct=EBI-4430993, EBI-15191793;
CC       C0SVM5; O50055: COL1; NbExp=3; IntAct=EBI-4430993, EBI-1112154;
CC       C0SVM5; O22800-2: COL14; NbExp=3; IntAct=EBI-4430993, EBI-15192033;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9SJU5}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=C0SVM5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=C0SVM5-2; Sequence=VSP_056808;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB38816.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80559.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL035679; CAB38816.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161594; CAB80559.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86999.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE87000.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66091.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66093.1; -; Genomic_DNA.
DR   EMBL; BT010927; AAR24705.1; -; mRNA.
DR   EMBL; BT011638; AAS47644.1; -; mRNA.
DR   EMBL; AB493728; BAH30566.1; -; mRNA.
DR   PIR; T06056; T06056.
DR   RefSeq; NP_001031811.1; NM_001036734.2. [C0SVM5-2]
DR   RefSeq; NP_001320162.1; NM_001342518.1. [C0SVM5-1]
DR   RefSeq; NP_001320163.1; NM_001342519.1. [C0SVM5-2]
DR   RefSeq; NP_195607.2; NM_120056.6. [C0SVM5-1]
DR   AlphaFoldDB; C0SVM5; -.
DR   BioGRID; 15331; 28.
DR   IntAct; C0SVM5; 21.
DR   PRIDE; C0SVM5; -.
DR   ProteomicsDB; 240651; -. [C0SVM5-1]
DR   EnsemblPlants; AT4G38960.1; AT4G38960.1; AT4G38960. [C0SVM5-1]
DR   EnsemblPlants; AT4G38960.2; AT4G38960.2; AT4G38960. [C0SVM5-2]
DR   EnsemblPlants; AT4G38960.5; AT4G38960.5; AT4G38960. [C0SVM5-2]
DR   EnsemblPlants; AT4G38960.6; AT4G38960.6; AT4G38960. [C0SVM5-1]
DR   GeneID; 830051; -.
DR   Gramene; AT4G38960.1; AT4G38960.1; AT4G38960. [C0SVM5-1]
DR   Gramene; AT4G38960.2; AT4G38960.2; AT4G38960. [C0SVM5-2]
DR   Gramene; AT4G38960.5; AT4G38960.5; AT4G38960. [C0SVM5-2]
DR   Gramene; AT4G38960.6; AT4G38960.6; AT4G38960. [C0SVM5-1]
DR   KEGG; ath:AT4G38960; -.
DR   Araport; AT4G38960; -.
DR   PhylomeDB; C0SVM5; -.
DR   PRO; PR:C0SVM5; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; C0SVM5; baseline and differential.
DR   Genevisible; C0SVM5; AT.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0010100; P:negative regulation of photomorphogenesis; IDA:UniProtKB.
DR   GO; GO:0009640; P:photomorphogenesis; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   InterPro; IPR000315; Znf_B-box.
DR   Pfam; PF00643; zf-B_box; 2.
DR   SMART; SM00336; BBOX; 2.
DR   PROSITE; PS50119; ZF_BBOX; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..183
FT                   /note="B-box zinc finger protein 19"
FT                   /id="PRO_0000430586"
FT   ZN_FING         5..47
FT                   /note="B box-type 1; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   ZN_FING         56..96
FT                   /note="B box-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   REGION          105..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         5
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         8
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         28
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         33
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   VAR_SEQ         1..33
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_056808"
SQ   SEQUENCE   183 AA;  20147 MW;  72180B3358CB5177 CRC64;
     MRILCDACEN AAAIIFCAAD EAALCRPCDE KVHMCNKLAS RHVRVGLAEP SNAPCCDICE
     NAPAFFYCEI DGSSLCLQCD MVVHVGGKRT HGRFLLLRQR IEFPGDKPKE NNTRDNLQNQ
     RVSTNGNGEA NGKIDDEMID LNANPQRVHE PSSNNNGIDV NNENNHEPAG LVPVGPFKRE
     SEK
 
 
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