BPM1_ARATH
ID BPM1_ARATH Reviewed; 407 AA.
AC Q8L765;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=BTB/POZ and MATH domain-containing protein 1;
DE AltName: Full=Protein BTB-POZ AND MATH DOMAIN 1;
DE Short=AtBPM1;
GN Name=BPM1; OrderedLocusNames=At5g19000; ORFNames=T16G12.40;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY.
RX PubMed=14693377; DOI=10.1016/j.gene.2003.09.022;
RA Huang C.-J., Chen C.-Y., Chen H.-H., Tsai S.-F., Choo K.-B.;
RT "TDPOZ, a family of bipartite animal and plant proteins that contain the
RT TRAF (TD) and POZ/BTB domains.";
RL Gene 324:117-127(2004).
RN [5]
RP INTERACTION WITH CUL3A AND CUL3B.
RX PubMed=15749712; DOI=10.1074/jbc.m413247200;
RA Gingerich D.J., Gagne J.M., Salter D.W., Hellmann H., Estelle M., Ma L.,
RA Vierstra R.D.;
RT "Cullins 3a and 3b assemble with members of the broad
RT complex/tramtrack/bric-a-brac (BTB) protein family to form essential
RT ubiquitin-protein ligases (E3s) in Arabidopsis.";
RL J. Biol. Chem. 280:18810-18821(2005).
RN [6]
RP INTERACTION WITH CUL3A.
RX PubMed=15772280; DOI=10.1105/tpc.105.031989;
RA Figueroa P., Gusmaroli G., Serino G., Habashi J., Ma L., Shen Y., Feng S.,
RA Bostick M., Callis J., Hellmann H., Deng X.W.;
RT "Arabidopsis has two redundant Cullin3 proteins that are essential for
RT embryo development and that interact with RBX1 and BTB proteins to form
RT multisubunit E3 ubiquitin ligase complexes in vivo.";
RL Plant Cell 17:1180-1195(2005).
RN [7]
RP GENE FAMILY, NOMENCLATURE, FUNCTION, IDENTIFICATION IN THE CUL3-RBX1-BTB
RP UBIQUITIN-PROTEIN LIGASE COMPLEX, INTERACTION WITH CUL3A AND CUL3B,
RP SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=15618422; DOI=10.1104/pp.104.052654;
RA Weber H., Bernhardt A., Dieterle M., Hano P., Mutlu A., Estelle M.,
RA Genschik P., Hellmann H.;
RT "Arabidopsis AtCUL3a and AtCUL3b form complexes with members of the
RT BTB/POZ-MATH protein family.";
RL Plant Physiol. 137:83-93(2005).
RN [8]
RP INTERACTION WITH RAP2-4 AND RAP2-13, TISSUE SPECIFICITY, INDUCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19843165; DOI=10.1111/j.1742-4658.2009.07373.x;
RA Weber H., Hellmann H.;
RT "Arabidopsis thaliana BTB/ POZ-MATH proteins interact with members of the
RT ERF/AP2 transcription factor family.";
RL FEBS J. 276:6624-6635(2009).
RN [9]
RP INTERACTION WITH MYB56.
RC STRAIN=cv. Columbia;
RX PubMed=25343985; DOI=10.1093/mp/ssu120;
RA Chen L., Bernhardt A., Lee J., Hellmann H.;
RT "Identification of Arabidopsis MYB56 as a novel substrate for CRL3BPM E3
RT ligases.";
RL Mol. Plant 0:0-0(2014).
CC -!- FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex (CUL3-RBX1-BTB) which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. {ECO:0000269|PubMed:15618422}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer or heterodimer with BPM3, BPM5 and BPM6. Interacts
CC with CUL3A and CUL3B. Interacts with RAP2-4 and RAP2-13. Binds to MYB56
CC at the promoter of FLOWERING LOCUS T (FT) (PubMed:25343985).
CC {ECO:0000269|PubMed:15618422, ECO:0000269|PubMed:15749712,
CC ECO:0000269|PubMed:15772280, ECO:0000269|PubMed:19843165,
CC ECO:0000269|PubMed:25343985}.
CC -!- INTERACTION:
CC Q8L765; F4JUM1: At4g14160; NbExp=3; IntAct=EBI-540891, EBI-25510940;
CC Q8L765; Q8L765: BPM1; NbExp=2; IntAct=EBI-540891, EBI-540891;
CC Q8L765; Q9SGS4: CDSP32; NbExp=3; IntAct=EBI-540891, EBI-25517863;
CC Q8L765; Q9ZVH4: CUL3A; NbExp=5; IntAct=EBI-540891, EBI-531362;
CC Q8L765; Q9C9L0: CUL3B; NbExp=3; IntAct=EBI-540891, EBI-541687;
CC Q8L765; O65665: ERF060; NbExp=4; IntAct=EBI-540891, EBI-7529041;
CC Q8L765; Q9MAI5: ERF8; NbExp=3; IntAct=EBI-540891, EBI-2000137;
CC Q8L765; Q9FY93: NAC083; NbExp=3; IntAct=EBI-540891, EBI-4453280;
CC Q8L765; Q9LM15: RAP2-13; NbExp=2; IntAct=EBI-540891, EBI-7528397;
CC Q8L765; Q8H1E4: RAP2-4; NbExp=5; IntAct=EBI-540891, EBI-7528315;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19843165}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8L765-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8L765-2; Sequence=VSP_040654;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15618422,
CC ECO:0000269|PubMed:19843165}.
CC -!- INDUCTION: By drought. {ECO:0000269|PubMed:19843165}.
CC -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC of ubiquitin ligase complexes.
CC -!- SIMILARITY: Belongs to the Tdpoz family. {ECO:0000305}.
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DR EMBL; AC068809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92637.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92638.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68871.1; -; Genomic_DNA.
DR EMBL; AY136451; AAM97116.1; -; mRNA.
DR EMBL; BT002593; AAO00953.1; -; mRNA.
DR RefSeq; NP_001190334.1; NM_001203405.1. [Q8L765-2]
DR RefSeq; NP_001330589.1; NM_001343580.1. [Q8L765-1]
DR RefSeq; NP_197401.2; NM_121905.3. [Q8L765-1]
DR AlphaFoldDB; Q8L765; -.
DR SMR; Q8L765; -.
DR BioGRID; 17294; 20.
DR IntAct; Q8L765; 13.
DR MINT; Q8L765; -.
DR STRING; 3702.AT5G19000.2; -.
DR PRIDE; Q8L765; -.
DR ProteomicsDB; 240478; -. [Q8L765-1]
DR EnsemblPlants; AT5G19000.1; AT5G19000.1; AT5G19000. [Q8L765-1]
DR EnsemblPlants; AT5G19000.2; AT5G19000.2; AT5G19000. [Q8L765-2]
DR EnsemblPlants; AT5G19000.3; AT5G19000.3; AT5G19000. [Q8L765-1]
DR GeneID; 832018; -.
DR Gramene; AT5G19000.1; AT5G19000.1; AT5G19000. [Q8L765-1]
DR Gramene; AT5G19000.2; AT5G19000.2; AT5G19000. [Q8L765-2]
DR Gramene; AT5G19000.3; AT5G19000.3; AT5G19000. [Q8L765-1]
DR KEGG; ath:AT5G19000; -.
DR Araport; AT5G19000; -.
DR TAIR; locus:2179599; AT5G19000.
DR eggNOG; KOG1987; Eukaryota.
DR HOGENOM; CLU_004253_2_0_1; -.
DR InParanoid; Q8L765; -.
DR OMA; IKFNYMW; -.
DR PhylomeDB; Q8L765; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8L765; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L765; baseline and differential.
DR Genevisible; Q8L765; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0071472; P:cellular response to salt stress; IEP:TAIR.
DR GO; GO:0042631; P:cellular response to water deprivation; IEP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006970; P:response to osmotic stress; IEP:TAIR.
DR CDD; cd14736; BACK_AtBPM-like; 1.
DR CDD; cd00121; MATH; 1.
DR Gene3D; 2.60.210.10; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR045005; BPM1-6.
DR InterPro; IPR034090; BPM_C.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR008974; TRAF-like.
DR PANTHER; PTHR26379; PTHR26379; 1.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS50144; MATH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..407
FT /note="BTB/POZ and MATH domain-containing protein 1"
FT /id="PRO_0000405265"
FT DOMAIN 33..167
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 203..270
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT VAR_SEQ 254
FT /note="F -> FKVLPLTLLLIVYSRMYHPGSSPGALLLFSSLLTRD (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040654"
SQ SEQUENCE 407 AA; 44729 MW; 863D1AFF7068CD66 CRC64;
MGTTRVCSEV SSGSSKSLSQ SLTVSTSTTE TVNGFHEFKI CGYSLAKGVG VGKYVASDTF
MVGGYSWAIY FYPDGKSPED NSSYVSLFIA LASEGADVRA LFELTLVDQS GNGKHKVHSH
FGRALDSGPY TLKYRGSMWG YKRFFRRSSL ESSDYLKENS LLVRCRVGVV KSVTEGPRYY
NIPVPVSNLG QQLGNLLESG KGCDVVFQVD GETFNAHKLV LATRSPVFNA QLFGPLGDRN
TKCITIEDME APIFKVLLHF IYWDELPDMQ ELIGTDSTLA STLVAQHLLA AADRYALERL
KAICESKLCE GVAINTVATT LALAEQHHCL QLKAVCLKFV ALPENLKAVM QTDGFDYLKE
SCPSLLTELL QYVARLSEHS VIVSGHRKEI FADGCDASGR RVKPRLH
