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BAG1_ARATH
ID   BAG1_ARATH              Reviewed;         342 AA.
AC   Q0WUQ1; Q9FJ86;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=BAG family molecular chaperone regulator 1;
DE   AltName: Full=Bcl-2-associated athanogene 1;
GN   Name=BAG1; OrderedLocusNames=At5g52060; ORFNames=MSG15.15;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA   Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT   features of the regions of 1,013,767 bp covered by sixteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:297-308(1998).
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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-342.
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 (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   DOI=10.1016/S0168-9452(03)00121-3;
RA   Juqiang Y., Cixin H., Hong Z.;
RT   "The BAG-family proteins in Arabidopsis thaliana.";
RL   Plant Sci. 165:1-7(2003).
RN   [6]
RP   GENE FAMILY.
RX   PubMed=16636050; DOI=10.1074/jbc.m511794200;
RA   Doukhanina E.V., Chen S., van der Zalm E., Godzik A., Reed J.,
RA   Dickman M.B.;
RT   "Identification and functional characterization of the BAG protein family
RT   in Arabidopsis thaliana.";
RL   J. Biol. Chem. 281:18793-18801(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
CC   -!- FUNCTION: Co-chaperone that regulates diverse cellular pathways, such
CC       as programmed cell death and stress responses. {ECO:0000250}.
CC   -!- SUBUNIT: Binds to the ATPase domain of HSP70/HSC70 chaperones.
CC       {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB11054.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB015478; BAB11054.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002688; AED96167.1; -; Genomic_DNA.
DR   EMBL; AK227095; BAE99147.1; -; mRNA.
DR   EMBL; BT030041; ABN04779.1; -; mRNA.
DR   RefSeq; NP_200019.2; NM_124585.4.
DR   PDB; 4HWC; X-ray; 1.80 A; A/B/C/D/E/F=157-241.
DR   PDB; 4HWI; X-ray; 2.27 A; B=66-242.
DR   PDBsum; 4HWC; -.
DR   PDBsum; 4HWI; -.
DR   AlphaFoldDB; Q0WUQ1; -.
DR   SMR; Q0WUQ1; -.
DR   BioGRID; 20526; 1.
DR   STRING; 3702.AT5G52060.1; -.
DR   iPTMnet; Q0WUQ1; -.
DR   PaxDb; Q0WUQ1; -.
DR   PRIDE; Q0WUQ1; -.
DR   ProteomicsDB; 240809; -.
DR   EnsemblPlants; AT5G52060.1; AT5G52060.1; AT5G52060.
DR   GeneID; 835281; -.
DR   Gramene; AT5G52060.1; AT5G52060.1; AT5G52060.
DR   KEGG; ath:AT5G52060; -.
DR   Araport; AT5G52060; -.
DR   TAIR; locus:2173108; AT5G52060.
DR   eggNOG; KOG4361; Eukaryota.
DR   HOGENOM; CLU_043370_1_0_1; -.
DR   OMA; AMPNTNG; -.
DR   OrthoDB; 1266506at2759; -.
DR   PhylomeDB; Q0WUQ1; -.
DR   PRO; PR:Q0WUQ1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q0WUQ1; baseline and differential.
DR   Genevisible; Q0WUQ1; AT.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR   GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IMP:TAIR.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR   Gene3D; 1.20.58.120; -; 1.
DR   IDEAL; IID50190; -.
DR   InterPro; IPR039773; BAG_chaperone_regulator.
DR   InterPro; IPR036533; BAG_dom_sf.
DR   InterPro; IPR003103; BAG_domain.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR12329; PTHR12329; 1.
DR   Pfam; PF02179; BAG; 1.
DR   SMART; SM00264; BAG; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   SUPFAM; SSF63491; SSF63491; 1.
DR   PROSITE; PS51035; BAG; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Phosphoprotein; Reference proteome.
FT   CHAIN           1..342
FT                   /note="BAG family molecular chaperone regulator 1"
FT                   /id="PRO_0000415521"
FT   DOMAIN          65..141
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          160..238
FT                   /note="BAG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         298
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
FT   STRAND          67..73
FT                   /evidence="ECO:0007829|PDB:4HWI"
FT   STRAND          76..82
FT                   /evidence="ECO:0007829|PDB:4HWI"
FT   HELIX           88..99
FT                   /evidence="ECO:0007829|PDB:4HWI"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:4HWI"
FT   STRAND          106..110
FT                   /evidence="ECO:0007829|PDB:4HWI"
FT   TURN            121..125
FT                   /evidence="ECO:0007829|PDB:4HWI"
FT   STRAND          130..136
FT                   /evidence="ECO:0007829|PDB:4HWI"
FT   HELIX           157..183
FT                   /evidence="ECO:0007829|PDB:4HWC"
FT   HELIX           190..207
FT                   /evidence="ECO:0007829|PDB:4HWC"
FT   HELIX           214..240
FT                   /evidence="ECO:0007829|PDB:4HWC"
SQ   SEQUENCE   342 AA;  38191 MW;  E1F103F7230D55E5 CRC64;
     MMKMMRNKPT NLPTAGMTNG GRGSGGGGGG GGRESGGRDL EIRPGGMLVQ KRNPDLDPVG
     PPPPPMIRVR IKYGAVYHEI NISPQASFGE LKKMLTGPTG IHHQDQKLMY KDKERDSKAF
     LDVSGVKDKS KMVLIEDPLS QEKRFLEMRK IAKTEKASKA ISDISLEVDR LGGRVSAFEM
     VTKKGGKIAE KDLVTVIELL MNELIKLDAI VAEGDVKLQR KMQVKRVQNY VETLDALKVK
     NSMANGQQKQ SSTAQRLAPI QEHNNEERQE QKPIQSLMDM PIQYKEKKQE IEEEPRNSGE
     GPFVLDSSAK WETFDHHPVT PLSSTTAKNN AIPPRFNWEF FD
 
 
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