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Protein

Co-chaperone protein SBA1

Gene

SBA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a co-chaperone.1 Publication

GO - Molecular functioni

  • chaperone binding Source: SGD

GO - Biological processi

  • negative regulation of DNA binding Source: SGD
  • positive regulation of telomere maintenance via telomerase Source: SGD
  • protein folding Source: SGD
  • regulation of telomerase activity Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

BioCyciYEAST:G3O-31901-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Co-chaperone protein SBA1
Gene namesi
Name:SBA1
Ordered Locus Names:YKL117W
ORF Names:YKL518
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL117W.
SGDiS000001600. SBA1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 216215Co-chaperone protein SBA1PRO_0000218959Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP28707.
PeptideAtlasiP28707.
TopDownProteomicsiP28707.

2D gel databases

SWISS-2DPAGEP28707.

Interactioni

Subunit structurei

Interacts with HSP82.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP82P028294EBI-26838,EBI-8659

GO - Molecular functioni

  • chaperone binding Source: SGD

Protein-protein interaction databases

BioGridi34018. 331 interactions.
DIPiDIP-2311N.
IntActiP28707. 10 interactions.
MINTiMINT-511012.

Structurei

Secondary structure

1
216
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 193Combined sources
Beta strandi23 – 297Combined sources
Beta strandi33 – 375Combined sources
Beta strandi44 – 496Combined sources
Beta strandi63 – 653Combined sources
Beta strandi67 – 704Combined sources
Beta strandi77 – 848Combined sources
Beta strandi91 – 966Combined sources
Beta strandi98 – 1014Combined sources
Beta strandi107 – 1104Combined sources
Beta strandi115 – 1195Combined sources
Turni121 – 1233Combined sources
Beta strandi127 – 1315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CG9X-ray3.10X/Y2-135[»]
ProteinModelPortaliP28707.
SMRiP28707. Positions 12-135.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP28707.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 108104CSPROSITE-ProRule annotationAdd
BLAST
Repeati141 – 15616Add
BLAST
Repeati160 – 17415Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi203 – 21311Poly-GluAdd
BLAST

Sequence similaritiesi

Belongs to the p23/wos2 family.Curated
Contains 1 CS domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00830000129169.
HOGENOMiHOG000177563.
InParanoidiP28707.
OMAiDFSKWVD.
OrthoDBiEOG7W9S6F.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51203. CS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P28707-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDKVINPQV AWAQRSSTTD PERNYVLITV SIADCDAPEL TIKPSYIELK
60 70 80 90 100
AQSKPHVGDE NVHHYQLHID LYKEIIPEKT MHKVANGQHY FLKLYKKDLE
110 120 130 140 150
SEYWPRLTKE KVKYPYIKTD FDKWVDEDEQ DEVEAEGNDA AQGMDFSQMM
160 170 180 190 200
GGAGGAGGAG GMDFSQMMGG AGGAGSPDMA QLQQLLAQSG GNLDMGDFKE
210
NDEEDEEEEI EPEVKA
Length:216
Mass (Da):24,082
Last modified:January 23, 2007 - v3
Checksum:iC51CDE30BF2FA945
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S93804 Genomic DNA. Translation: AAB22000.1.
Z28117 Genomic DNA. Translation: CAA81957.1.
BK006944 Genomic DNA. Translation: DAA09042.1.
PIRiS27382.
RefSeqiNP_012805.1. NM_001179683.1.

Genome annotation databases

EnsemblFungiiYKL117W; YKL117W; YKL117W.
GeneIDi853743.
KEGGisce:YKL117W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S93804 Genomic DNA. Translation: AAB22000.1.
Z28117 Genomic DNA. Translation: CAA81957.1.
BK006944 Genomic DNA. Translation: DAA09042.1.
PIRiS27382.
RefSeqiNP_012805.1. NM_001179683.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CG9X-ray3.10X/Y2-135[»]
ProteinModelPortaliP28707.
SMRiP28707. Positions 12-135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34018. 331 interactions.
DIPiDIP-2311N.
IntActiP28707. 10 interactions.
MINTiMINT-511012.

2D gel databases

SWISS-2DPAGEP28707.

Proteomic databases

MaxQBiP28707.
PeptideAtlasiP28707.
TopDownProteomicsiP28707.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL117W; YKL117W; YKL117W.
GeneIDi853743.
KEGGisce:YKL117W.

Organism-specific databases

EuPathDBiFungiDB:YKL117W.
SGDiS000001600. SBA1.

Phylogenomic databases

GeneTreeiENSGT00830000129169.
HOGENOMiHOG000177563.
InParanoidiP28707.
OMAiDFSKWVD.
OrthoDBiEOG7W9S6F.

Enzyme and pathway databases

BioCyciYEAST:G3O-31901-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP28707.
NextBioi974798.
PROiP28707.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51203. CS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of a 10.7 kb segment of yeast chromosome XI identifies the APN1 and the BAF1 loci and reveals one tRNA gene and several new open reading frames including homologs to RAD2 and kinases."
    Jacquier A., Legrain P., Dujon B.
    Yeast 8:121-132(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
    Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
    Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT SER-2.
  5. "The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies."
    Freeman B.C., Felts S.J., Toft D.O., Yamamoto K.R.
    Genes Dev. 14:422-434(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex."
    Ali M.M., Roe S.M., Vaughan C.K., Meyer P., Panaretou B., Piper P.W., Prodromou C., Pearl L.H.
    Nature 440:1013-1017(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 2-135 IN COMPLEX WITH HSP82.

Entry informationi

Entry nameiSBA1_YEAST
AccessioniPrimary (citable) accession number: P28707
Secondary accession number(s): D6VXH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 33700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

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.