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Y2626_ARATH
ID   Y2626_ARATH             Reviewed;         561 AA.
AC   O82343; Q56WV2; Q8LG00; Q94AI9;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=BTB/POZ domain-containing protein At2g46260;
GN   OrderedLocusNames=At2g46260; ORFNames=T3F17.9;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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].
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-561.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) 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       O82343; Q6NLH4: BBX29; NbExp=3; IntAct=EBI-15192211, EBI-15192709;
CC       O82343; Q9FVC1: SVP; NbExp=3; IntAct=EBI-15192211, EBI-592058;
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=AAM61110.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD94357.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC005397; AAC62880.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10666.1; -; Genomic_DNA.
DR   EMBL; AY046011; AAK76685.1; -; mRNA.
DR   EMBL; AY079398; AAL85129.1; -; mRNA.
DR   EMBL; AY084542; AAM61110.1; ALT_INIT; mRNA.
DR   EMBL; AK221929; BAD94357.1; ALT_INIT; mRNA.
DR   PIR; F84900; F84900.
DR   RefSeq; NP_566069.1; NM_130189.3.
DR   AlphaFoldDB; O82343; -.
DR   SMR; O82343; -.
DR   BioGRID; 4569; 10.
DR   IntAct; O82343; 8.
DR   STRING; 3702.AT2G46260.1; -.
DR   PaxDb; O82343; -.
DR   PRIDE; O82343; -.
DR   ProteomicsDB; 242360; -.
DR   EnsemblPlants; AT2G46260.1; AT2G46260.1; AT2G46260.
DR   GeneID; 819234; -.
DR   Gramene; AT2G46260.1; AT2G46260.1; AT2G46260.
DR   KEGG; ath:AT2G46260; -.
DR   Araport; AT2G46260; -.
DR   TAIR; locus:2063026; AT2G46260.
DR   eggNOG; ENOG502QT6M; Eukaryota.
DR   HOGENOM; CLU_024600_2_0_1; -.
DR   InParanoid; O82343; -.
DR   OMA; LDECENQ; -.
DR   OrthoDB; 462254at2759; -.
DR   PhylomeDB; O82343; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:O82343; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O82343; baseline and differential.
DR   Genevisible; O82343; AT.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0010114; P:response to red light; IGI:TAIR.
DR   Gene3D; 2.60.210.10; -; 1.
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   InterPro; IPR008974; TRAF-like.
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   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..561
FT                   /note="BTB/POZ domain-containing protein At2g46260"
FT                   /id="PRO_0000406780"
FT   DOMAIN          143..212
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          266..358
FT                   /note="BACK"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   561 AA;  63037 MW;  D687F7F85170C5EC CRC64;
     MRGSNNTDLF DPKTEMDSNF SRHGSSSEGD FGFAFNDSNF SDRLLRIEIL GGPSDSRSDA
     EGCTSIADWA RHRKRRREDN KKDNGVAISD IVACAEEQIL TDNNQPDMDD APGGDNLDDE
     GEAMVEEALS GDDDASSEPN WGIDCSTVVR VKELHISSPI LAAKSPFFYK LFSNGMRESE
     QRHVTLRISA QEEGALMELL NFMYSNSLSV TTAPALLDVL MAADKFEVAS CMRYCSRLLR
     NMPMTPDSAL LYLELPSSVL MAEAVQPLTD AAKQFLASRY KDITKFHDEV MALPLAGIEA
     ILSSDDLQIA SEDAVYDFVL KWARGQYSSL EDRREILGSR LALYIRFPYM TCRKLKKVLT
     CSDFEHEVAS KQVLEALFFK AEAPHRQRIL AAEGSDSMNR RFIERAYKYR PVKVVEFELP
     RPQCVVYLDL KREECAGLFP SGRVYSQAFH LGGQGFFLSA HCNMDQQSSF HCFGLFLGMQ
     EKGAVSFGVD YEFAARDKST KEEYVSKYKG NYTFTGGKAV GYRNLFGIPW TSFIAEDSQH
     FINGILHLRA ELTIKRSSDL H
 
 
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