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2AB2E_ARATH
ID   2AB2E_ARATH             Reviewed;         529 AA.
AC   Q84JI6; F4I2K5; Q9ZWB6;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Probable serine/threonine protein phosphatase 2A regulatory subunit B''epsilon;
DE            Short=AtB''epsilon;
GN   Name=B''EPSILON; OrderedLocusNames=At1g03960; ORFNames=F21M11.11;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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, AND NOMENCLATURE.
RX   PubMed=21478440; DOI=10.1105/tpc.110.074278;
RA   Leivar P., Antolin-Llovera M., Ferrero S., Closa M., Arro M., Ferrer A.,
RA   Boronat A., Campos N.;
RT   "Multilevel control of Arabidopsis 3-hydroxy-3-methylglutaryl coenzyme A
RT   reductase by protein phosphatase 2A.";
RL   Plant Cell 23:1494-1511(2011).
CC   -!- FUNCTION: Probable regulatory subunit of type 2A protein phosphatase.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed
CC       of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant
CC       regulatory subunit (PR65 or subunit A), that associates with a variety
CC       of regulatory subunits. Proteins that associate with the core dimer
CC       include three families of regulatory subunits B (the R2/B/PR55/B55,
CC       R3/B''/PR72/PR130/PR59 and R5/B'/B56 families) and cell signaling
CC       molecules (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q84JI6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q84JI6-2; Sequence=VSP_046804;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD10674.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC003027; AAD10674.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE27638.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27639.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM57805.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM57808.1; -; Genomic_DNA.
DR   EMBL; BT004045; AAO42077.1; -; mRNA.
DR   EMBL; BT004945; AAO50478.1; -; mRNA.
DR   PIR; E86170; E86170.
DR   RefSeq; NP_001320288.1; NM_001331448.1. [Q84JI6-2]
DR   RefSeq; NP_001320291.1; NM_001331449.1. [Q84JI6-2]
DR   RefSeq; NP_171892.2; NM_100277.5. [Q84JI6-1]
DR   RefSeq; NP_973757.1; NM_202028.3. [Q84JI6-2]
DR   AlphaFoldDB; Q84JI6; -.
DR   SMR; Q84JI6; -.
DR   BioGRID; 24596; 5.
DR   STRING; 3702.AT1G03960.1; -.
DR   iPTMnet; Q84JI6; -.
DR   PaxDb; Q84JI6; -.
DR   PRIDE; Q84JI6; -.
DR   EnsemblPlants; AT1G03960.1; AT1G03960.1; AT1G03960. [Q84JI6-1]
DR   EnsemblPlants; AT1G03960.2; AT1G03960.2; AT1G03960. [Q84JI6-2]
DR   EnsemblPlants; AT1G03960.3; AT1G03960.3; AT1G03960. [Q84JI6-2]
DR   EnsemblPlants; AT1G03960.4; AT1G03960.4; AT1G03960. [Q84JI6-2]
DR   GeneID; 839361; -.
DR   Gramene; AT1G03960.1; AT1G03960.1; AT1G03960. [Q84JI6-1]
DR   Gramene; AT1G03960.2; AT1G03960.2; AT1G03960. [Q84JI6-2]
DR   Gramene; AT1G03960.3; AT1G03960.3; AT1G03960. [Q84JI6-2]
DR   Gramene; AT1G03960.4; AT1G03960.4; AT1G03960. [Q84JI6-2]
DR   KEGG; ath:AT1G03960; -.
DR   Araport; AT1G03960; -.
DR   TAIR; locus:2024254; AT1G03960.
DR   eggNOG; KOG2562; Eukaryota.
DR   HOGENOM; CLU_019589_3_0_1; -.
DR   InParanoid; Q84JI6; -.
DR   OMA; ITANEMQ; -.
DR   PhylomeDB; Q84JI6; -.
DR   PRO; PR:Q84JI6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q84JI6; baseline and differential.
DR   Genevisible; Q84JI6; AT.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR   GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR041534; EF-hand_13.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   Pfam; PF17958; EF-hand_13; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SUPFAM; SSF47473; SSF47473; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Metal-binding; Reference proteome.
FT   CHAIN           1..529
FT                   /note="Probable serine/threonine protein phosphatase 2A
FT                   regulatory subunit B''epsilon"
FT                   /id="PRO_0000422791"
FT   DOMAIN          381..416
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          58..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         394
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         396
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         398
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         405
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   VAR_SEQ         1..140
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046804"
SQ   SEQUENCE   529 AA;  61239 MW;  AA71B4C3720ED05A CRC64;
     MDIDGVDDDL HILDPELLQL PGLSPSPLKP TSLIADDLFS QWLSLPETAT LVKSLIDDAK
     SGTPTNKSKN LPSVFLSSST PPLSPRSSSG SPRFSRQRTS PPSLHSPLRS LKEPKRQLIP
     QFYYQHGRPP AKELKEQCLS MVDQVFSNYI DGLHVDEFKS ITKQVCKLPS FLSPALFRKI
     DPNCTDIVTR DAFIKYWIDG NMLTMDTASQ IYNILRQQGC SYLRQADFKP VLDELLATHP
     GLEFLRTISE FQERYAETVI YRIFYYINRS GTGCLTLREL RRGNLIAAMQ QLDEEDDINK
     IIRYFSYEHF YVIYCKFWEL DGDHDCFIDK DNLIKYGNNA LTYRIVDRIF SQIPRKFTSK
     VEGKMSYEDF VYFILAEEDK SSEPSLEYWF KCVDLDGNGV ITSNEMQFFF EEQLHRMECI
     TQEAVLFSDI LCQIIDMIGP EKENCITLQD LKGSKLSANV FNILFNLNKF MAFETRDPFL
     IRQEREDPNL TEWDRFAQRE YARLSMEEDV DEVSNGSADV WDEPLEPPF
 
 
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