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POB1_ARATH
ID   POB1_ARATH              Reviewed;         561 AA.
AC   Q9FPW6; Q9M309;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 2.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=BTB/POZ domain-containing protein POB1;
DE   AltName: Full=POZ/BTB CONTAINING-PROTEIN 1;
DE            Short=AtPOB1;
GN   Name=POB1; OrderedLocusNames=At3g61600; ORFNames=F15G16.4, F2A19.200;
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 [MRNA] (ISOFORM 2).
RX   PubMed=12008900; DOI=10.1023/a:1014440531842;
RA   Thelander M., Fredriksson D., Schouten J., Hoge J.H.C., Ronne H.;
RT   "Cloning by pathway activation in yeast: identification of an Arabidopsis
RT   thaliana F-box protein that can turn on glucose repression.";
RL   Plant Mol. Biol. 49:69-79(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   DOMAIN BTB.
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).
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:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- INTERACTION:
CC       Q9FPW6; Q9M126: NAC69; NbExp=3; IntAct=EBI-15194725, EBI-15191931;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9FPW6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FPW6-2; Sequence=VSP_040845;
CC   -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC       of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AF337913; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAB71090.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF292397; AAG44951.1; -; mRNA.
DR   EMBL; AL132959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL132962; CAB71090.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002686; AEE80229.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE80230.1; -; Genomic_DNA.
DR   EMBL; AF337913; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BT030347; ABO38760.1; -; mRNA.
DR   PIR; T47952; T47952.
DR   RefSeq; NP_567115.1; NM_116025.4. [Q9FPW6-2]
DR   RefSeq; NP_850733.1; NM_180402.2. [Q9FPW6-1]
DR   AlphaFoldDB; Q9FPW6; -.
DR   SMR; Q9FPW6; -.
DR   BioGRID; 10647; 6.
DR   IntAct; Q9FPW6; 6.
DR   STRING; 3702.AT3G61600.1; -.
DR   PaxDb; Q9FPW6; -.
DR   PRIDE; Q9FPW6; -.
DR   ProteomicsDB; 234793; -. [Q9FPW6-1]
DR   EnsemblPlants; AT3G61600.1; AT3G61600.1; AT3G61600. [Q9FPW6-1]
DR   EnsemblPlants; AT3G61600.2; AT3G61600.2; AT3G61600. [Q9FPW6-2]
DR   GeneID; 825333; -.
DR   Gramene; AT3G61600.1; AT3G61600.1; AT3G61600. [Q9FPW6-1]
DR   Gramene; AT3G61600.2; AT3G61600.2; AT3G61600. [Q9FPW6-2]
DR   KEGG; ath:AT3G61600; -.
DR   Araport; AT3G61600; -.
DR   TAIR; locus:2082827; AT3G61600.
DR   eggNOG; ENOG502QT6M; Eukaryota.
DR   HOGENOM; CLU_024600_2_0_1; -.
DR   InParanoid; Q9FPW6; -.
DR   OMA; NENQPDM; -.
DR   PhylomeDB; Q9FPW6; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9FPW6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9FPW6; baseline and differential.
DR   Genevisible; Q9FPW6; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:TAIR.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR   GO; GO:0010114; P:response to red light; IGI:TAIR.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR011705; BACK.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR045890; POB1-like.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   PANTHER; PTHR46336; PTHR46336; 1.
DR   Pfam; PF07707; BACK; 1.
DR   Pfam; PF00651; BTB; 1.
DR   SMART; SM00875; BACK; 1.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..561
FT                   /note="BTB/POZ domain-containing protein POB1"
FT                   /id="PRO_0000406781"
FT   DOMAIN          145..214
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          268..360
FT                   /note="BACK"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         558..561
FT                   /note="STDP -> LEED (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12008900, ECO:0000303|Ref.5"
FT                   /id="VSP_040845"
SQ   SEQUENCE   561 AA;  63066 MW;  3DD33C26CDA2A36C CRC64;
     MRGTTENTDL FDPKTQMDPD FTRHGSSSDG DFGFAFNDSN FSDRLLRIEI MGGPSDSRSE
     VEGCTSIADW ARHRKRRRED IKKESGVTIS DIVACPEEQI LTDEQPDMDG CPGGENPDDE
     GGEAMVEEAL SGDEEETSSE PNWGMDCSTV VRVKELHISS PILAAKSPFF YKLFSNGMRE
     SEQRHVTLRI NASEEAALME LLNFMYSNAV SVTTAPALLD VLMAADKFEV ASCMRYCSRL
     LRNMPMTPES ALLYLELPSS VLMAKAVQPL TDAAKQFLAA RYKDITKFHE EVMSLPLAGI
     EAILSSDELQ IASEDAVYDF ILKWARAQYP CLEERREILG SRLALSIRFP FMTCRKLKKV
     LTCSDFEHEI ASKLVLEALF FKAEAPHRQR SLASEESASL NRRLIERAYK YRPVKVVEFE
     LPRPQCVVYL DLKREECGGL FPSGRVYSQA FHLGGQGFFL SAHCNMDQQS SFHCFGLFLG
     MQEKGSVSFG VDYEFSARSK PAEDFISKYK GNYTFTGGKA VGYRNLFGVP WTSFIAEDSQ
     YFINGILHLR AELTIKRSTD P
 
 
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