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Protein

Chaperonin 60 subunit beta 1, chloroplastic

Gene

CPN60B1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds RuBisCO small and large subunits and is implicated in the assembly of the enzyme oligomer. Involved in protein assisted folding. Required for proper plastid division.5 Publications

GO - Molecular functioni

GO - Biological processi

  • cell death Source: TAIR
  • chaperone mediated protein folding requiring cofactor Source: TAIR
  • protein refolding Source: InterPro
  • response to cold Source: TAIR
  • systemic acquired resistance Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperonin 60 subunit beta 1, chloroplastic
Short name:
CPN-60 beta 1
Alternative name(s):
60 kDa chaperonin subunit beta 1
RuBisCO large subunit-binding protein subunit beta, chloroplastic
Gene namesi
Name:CPN60B1
Synonyms:Cpn60-B(3), LEN1
Ordered Locus Names:At1g55490
ORF Names:T5A14.11
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G55490.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: TAIR
  • cytosolic ribosome Source: TAIR
  • membrane Source: TAIR
  • plasma membrane Source: TAIR
  • stromule Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

Normal germination, but chloroplast-division defect and late dwarf phenotype. Lesion formation on leaves when grown under short-day conditions. Cpn60B1 and cpn60B2 double mutant produces small albino seedlings.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5454Chloroplast1 PublicationAdd
BLAST
Chaini55 – 600546Chaperonin 60 subunit beta 1, chloroplasticPRO_0000005022Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011PhosphoserineBy similarity
Modified residuei478 – 4781PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP21240.
PRIDEiP21240.

PTM databases

iPTMnetiP21240.

Expressioni

Tissue specificityi

Expressed in leaves, stems, petioles and flowers.1 Publication

Inductioni

Up-regulated by light. Down-regulated by wounding. Not induced by heat.2 Publications

Gene expression databases

GenevisibleiP21240. AT.

Interactioni

Subunit structurei

Part of the Cpn60 complex composed of 7 alpha and 7 beta subunits. Can also form a complex composed of 14 beta subunits only. Both complexes show ATPase activity. The Cpn60 complex interacts with the Cpn10 complex. Interacts with RAB during heat stress.3 Publications

Protein-protein interaction databases

BioGridi27221. 9 interactions.
IntActiP21240. 2 interactions.
STRINGi3702.AT1G55490.1.

Structurei

3D structure databases

ProteinModelPortaliP21240.
SMRiP21240. Positions 55-581.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the chaperonin (HSP60) family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0356. Eukaryota.
COG0459. LUCA.
HOGENOMiHOG000076290.
InParanoidiP21240.
KOiK04077.
OMAiMIANNAG.
PhylomeDBiP21240.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPiMF_00600. CH60.
InterProiIPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00298. CHAPERONIN60.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02348. GroEL. 1 hit.
PROSITEiPS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21240-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTFTATSS IGSMVAPNGH KSDKKLISKL SSSSFGRRQS VCPRPRRSSS
60 70 80 90 100
AIVCAAKELH FNKDGTTIRR LQAGVNKLAD LVGVTLGPKG RNVVLESKYG
110 120 130 140 150
SPRIVNDGVT VAREVELEDP VENIGAKLVR QAAAKTNDLA GDGTTTSVVL
160 170 180 190 200
AQGFIAEGVK VVAAGANPVL ITRGIEKTAK ALVTELKKMS KEVEDSELAD
210 220 230 240 250
VAAVSAGNND EIGNMIAEAM SKVGRKGVVT LEEGKSAENN LYVVEGMQFD
260 270 280 290 300
RGYISPYFVT DSEKMSVEFD NCKLLLVDKK ITNARDLVGV LEDAIRGGYP
310 320 330 340 350
ILIIAEDIEQ EALATLVVNK LRGTLKIAAL RAPGFGERKS QYLDDIAILT
360 370 380 390 400
GATVIREEVG LSLDKAGKEV LGNASKVVLT KETSTIVGDG STQDAVKKRV
410 420 430 440 450
TQIKNLIEQA EQDYEKEKLN ERIAKLSGGV AVIQVGAQTE TELKEKKLRV
460 470 480 490 500
EDALNATKAA VEEGIVVGGG CTLLRLASKV DAIKATLDND EEKVGADIVK
510 520 530 540 550
RALSYPLKLI AKNAGVNGSV VSEKVLSNDN VKFGYNAATG KYEDLMAAGI
560 570 580 590 600
IDPTKVVRCC LEHAASVAKT FLMSDCVVVE IKEPEPVPVG NPMDNSGYGY
Length:600
Mass (Da):63,809
Last modified:January 10, 2003 - v3
Checksum:i78B10E9B2EE19859
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 2421Y → H in AAA32725 (PubMed:11130712).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC005223 Genomic DNA. Translation: AAD10647.1.
CP002684 Genomic DNA. Translation: AEE33251.1.
CP002684 Genomic DNA. Translation: AEE33252.1.
AF386945 mRNA. Translation: AAK62390.1.
AY081501 mRNA. Translation: AAM10063.1.
AK316889 mRNA. Translation: BAH19596.1.
AK317612 mRNA. Translation: BAH20275.1.
M35598 mRNA. Translation: AAA32725.1.
PIRiB96597.
JT0901.
PW0008.
RefSeqiNP_175945.1. NM_104424.2.
NP_849811.1. NM_179480.2.
UniGeneiAt.19230.

Genome annotation databases

EnsemblPlantsiAT1G55490.1; AT1G55490.1; AT1G55490.
AT1G55490.2; AT1G55490.2; AT1G55490.
GeneIDi841996.
GrameneiAT1G55490.1; AT1G55490.1; AT1G55490.
AT1G55490.2; AT1G55490.2; AT1G55490.
KEGGiath:AT1G55490.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC005223 Genomic DNA. Translation: AAD10647.1.
CP002684 Genomic DNA. Translation: AEE33251.1.
CP002684 Genomic DNA. Translation: AEE33252.1.
AF386945 mRNA. Translation: AAK62390.1.
AY081501 mRNA. Translation: AAM10063.1.
AK316889 mRNA. Translation: BAH19596.1.
AK317612 mRNA. Translation: BAH20275.1.
M35598 mRNA. Translation: AAA32725.1.
PIRiB96597.
JT0901.
PW0008.
RefSeqiNP_175945.1. NM_104424.2.
NP_849811.1. NM_179480.2.
UniGeneiAt.19230.

3D structure databases

ProteinModelPortaliP21240.
SMRiP21240. Positions 55-581.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi27221. 9 interactions.
IntActiP21240. 2 interactions.
STRINGi3702.AT1G55490.1.

PTM databases

iPTMnetiP21240.

Proteomic databases

PaxDbiP21240.
PRIDEiP21240.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G55490.1; AT1G55490.1; AT1G55490.
AT1G55490.2; AT1G55490.2; AT1G55490.
GeneIDi841996.
GrameneiAT1G55490.1; AT1G55490.1; AT1G55490.
AT1G55490.2; AT1G55490.2; AT1G55490.
KEGGiath:AT1G55490.

Organism-specific databases

TAIRiAT1G55490.

Phylogenomic databases

eggNOGiKOG0356. Eukaryota.
COG0459. LUCA.
HOGENOMiHOG000076290.
InParanoidiP21240.
KOiK04077.
OMAiMIANNAG.
PhylomeDBiP21240.

Miscellaneous databases

PROiP21240.

Gene expression databases

GenevisibleiP21240. AT.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPiMF_00600. CH60.
InterProiIPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00298. CHAPERONIN60.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02348. GroEL. 1 hit.
PROSITEiPS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of genes encoding chaperonin 60 beta from Arabidopsis thaliana."
    Zabaleta E., Oropeza A., Jimenez B., Salerno G., Crespi M., Herrera-Estrella L.
    Gene 111:175-181(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Unique composition of plastid chaperonin-60: alpha and beta polypeptide-encoding genes are highly divergent."
    Martel R., Cloney L.P., Pelcher L.E., Hemmingsen S.M.
    Gene 94:181-187(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 127-312.
    Strain: cv. Columbia.
  7. "Association of Rubisco activase with chaperonin-60beta: a possible mechanism for protecting photosynthesis during heat stress."
    Salvucci M.E.
    J. Exp. Bot. 59:1923-1933(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PROTEIN SEQUENCE OF 55-68, INTERACTION WITH RAB.
  8. "Differential involvement of the circadian clock in the expression of genes required for ribulose-1,5-bisphosphate carboxylase/oxygenase synthesis, assembly, and activation in Arabidopsis thaliana."
    Pilgrim M.L., McClung C.R.
    Plant Physiol. 103:553-564(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY LIGHT.
  9. "Expression of one of the members of the Arabidopsis chaperonin 60 beta gene family is developmentally regulated and wound-repressible."
    Zabaleta E., Assad N., Oropeza A., Salerno G., Herrera-Estrella L.
    Plant Mol. Biol. 24:195-202(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION BY WOUNDING AND HEAT.
  10. "Functional characterization of the higher plant chloroplast chaperonins."
    Viitanen P.V., Schmidt M., Buchner J., Suzuki T., Vierling E., Dickson R., Lorimer G.H., Gatenby A., Soll J.
    J. Biol. Chem. 270:18158-18164(1995)
    Cited for: FUNCTION, INTERACTION.
  11. "Arabidopsis thaliana type I and II chaperonins."
    Hill J.E., Hemmingsen S.M.
    Cell Stress Chaperones 6:190-200(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  12. "Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana."
    Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.
    Mol. Cell. Proteomics 2:325-345(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Wassilewskija.
  13. "Deletion of a chaperonin 60 beta gene leads to cell death in the Arabidopsis lesion initiation 1 mutant."
    Ishikawa A., Tanaka H., Nakai M., Asahi T.
    Plant Cell Physiol. 44:255-261(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  14. "Plastid chaperonin proteins Cpn60 alpha and Cpn60 beta are required for plastid division in Arabidopsis thaliana."
    Suzuki K., Nakanishi H., Bower J., Yoder D.W., Osteryoung K.W., Miyagishima S.Y.
    BMC Plant Biol. 9:38-38(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  15. "Differential effects of co-chaperonin homologs on cpn60 oligomers."
    Bonshtien A.L., Parnas A., Sharkia R., Niv A., Mizrahi I., Azem A., Weiss C.
    Cell Stress Chaperones 14:509-519(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN CPN60 COMPLEX.
  16. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "A chaperonin subunit with unique structures is essential for folding of a specific substrate."
    Peng L., Fukao Y., Myouga F., Motohashi R., Shinozaki K., Shikanai T.
    PLoS Biol. 9:E1001040-E1001040(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiCPNB1_ARATH
AccessioniPrimary (citable) accession number: P21240
Secondary accession number(s): B9DFS9, B9DHQ8, Q9SAV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 10, 2003
Last modified: February 17, 2016
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Assisted protein folding requires ATP hydrolysis, but not K+ ions.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.