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P38788 (SSZ1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribosome-associated complex subunit SSZ1
Alternative name(s):
DnaK-related protein SSZ1
Heat shock protein 70 homolog SSZ1
Pleiotropic drug resistance protein 13
Gene names
Name:SSZ1
Synonyms:PDR13
Ordered Locus Names:YHR064C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length538 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain. SSZ1 is required for ZUO1 to function efficiently as a J-protein for SSB1/SSB2. Also involved in pleiotropic drug resistance by post-translational activation of transcription factor PDR1. Ref.8 Ref.12 Ref.13

Subunit structure

RAC is a heterodimer of the Hsp70/DnaK-type chaperone SSZ1 and the Hsp40/DnaJ-type chaperone ZUO1. RAC associates with ribosomes via ZUO1. Ref.7

Subcellular location

Cytoplasm Ref.10.

Domain

Neither ATP binding nor ATP hydrolysis is required for SSZ1 function.

Does not seem to bind unfolded protein substrates, as its C-terminal putative peptide-binding domain is not required for its function.

Miscellaneous

Present with 73600 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the heat shock protein 70 family.

Sequence caution

The sequence AAB68391.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAT93146.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ZUO1P325277EBI-24570,EBI-29684

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 538538Ribosome-associated complex subunit SSZ1
PRO_0000078400

Regions

Region400 – 538139Peptide-binding domain Potential

Amino acid modifications

Modified residue4771Phosphoserine Ref.14 Ref.16 Ref.17
Modified residue4801Phosphoserine Ref.14 Ref.15 Ref.16 Ref.17

Experimental info

Mutagenesis2951S → F: Increases readthrough in translation termination. Ref.12
Sequence conflict2081V → A in AAT93146. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P38788 [UniParc].

Last modified July 11, 2006. Version 2.
Checksum: 07B1A409B213E0B4

FASTA53858,238
        10         20         30         40         50         60 
MSSPVIGITF GNTSSSIAYI NPKNDVDVIA NPDGERAIPS ALSYVGEDEY HGGQALQQLI 

        70         80         90        100        110        120 
RNPKNTIINF RDFIGLPFDK CDVSKCANGA PAVEVDGKVG FVISRGEGKE EKLTVDEVVS 

       130        140        150        160        170        180 
RHLNRLKLAA EDYIGSAVKE AVLTVPTNFS EEQKTALKAS AAKIGLQIVQ FINEPSAALL 

       190        200        210        220        230        240 
AHAEQFPFEK DVNVVVADFG GIRSDAAVIA VRNGIFTILA TAHDLSLGGD NLDTELVEYF 

       250        260        270        280        290        300 
ASEFQKKYQA NPRKNARSLA KLKANSSITK KTLSNATSAT ISIDSLADGF DYHASINRMR 

       310        320        330        340        350        360 
YELVANKVFA QFSSFVDSVI AKAELDPLDI DAVLLTGGVS FTPKLTTNLE YTLPESVEIL 

       370        380        390        400        410        420 
GPQNKNASNN PNELAASGAA LQARLISDYD ADELAEALQP VIVNTPHLKK PIGLIGAKGE 

       430        440        450        460        470        480 
FHPVLLAETS FPVQKKLTLK QAKGDFLIGV YEGDHHIEEK TLEPIPKEEN AEEDDESEWS 

       490        500        510        520        530 
DDEPEVVREK LYTLGTKLME LGIKNANGVE IIFNINKDGA LRVTARDLKT GNAVKGEL 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Verification of 3' and 5' ends of S. cerevisiae transcripts."
Kennedy M.C., Dietrich F.S.
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-72 AND 504-538.
Strain: ATCC 204511 / S288c / AB972.
[5]"Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels."
Shevchenko A., Jensen O.N., Podtelejnikov A.V., Sagliocco F., Wilm M., Vorm O., Mortensen P., Shevchenko A., Boucherie H., Mann M.
Proc. Natl. Acad. Sci. U.S.A. 93:14440-14445(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[6]"Yeast Pdr13p and Zuo1p molecular chaperones are new functional Hsp70 and Hsp40 partners."
Michimoto T., Aoki T., Toh-e A., Kikuchi Y.
Gene 257:131-137(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZUO1.
[7]"RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin."
Gautschi M., Lilie H., Fuenfschilling U., Mun A., Ross S., Lithgow T., Ruecknagel P., Rospert S.
Proc. Natl. Acad. Sci. U.S.A. 98:3762-3767(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN RAC.
[8]"The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain."
Hundley H., Eisenman H., Walter W., Evans T., Hotokezaka Y., Wiedmann M., Craig E.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4203-4208(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Sequencing and comparison of yeast species to identify genes and regulatory elements."
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[10]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]"The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae."
Rakwalska M., Rospert S.
Mol. Cell. Biol. 24:9186-9197(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-295.
[13]"The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1."
Huang P., Gautschi M., Walter W., Rospert S., Craig E.A.
Nat. Struct. Mol. Biol. 12:497-504(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ATP-BINDING.
[14]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[15]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00061 Genomic DNA. Translation: AAB68391.1. Different initiation.
AY693127 Genomic DNA. Translation: AAT93146.1. Different initiation.
AY389300 mRNA. Translation: AAQ97232.1.
AY389301 mRNA. Translation: AAQ97233.1.
BK006934 Genomic DNA. Translation: DAA06757.1.
PIRS46712.
RefSeqNP_011931.2. NM_001179194.1.

3D structure databases

ProteinModelPortalP38788.
SMRP38788. Positions 4-535.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36496. 94 interactions.
DIPDIP-6305N.
IntActP38788. 56 interactions.
MINTMINT-671986.

Proteomic databases

PaxDbP38788.
PeptideAtlasP38788.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR064C; YHR064C; YHR064C.
GeneID856461.
KEGGsce:YHR064C.

Organism-specific databases

CYGDYHR064c.
SGDS000001106. SSZ1.

Phylogenomic databases

eggNOGCOG0443.
GeneTreeENSGT00740000115930.
HOGENOMHOG000184645.
OrthoDBEOG7P02SZ.

Enzyme and pathway databases

BioCycYEAST:G3O-31115-MONOMER.

Gene expression databases

GenevestigatorP38788.

Family and domain databases

InterProIPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
ProtoNetSearch...

Other

NextBio982108.

Entry information

Entry nameSSZ1_YEAST
AccessionPrimary (citable) accession number: P38788
Secondary accession number(s): D3DL13 expand/collapse secondary AC list , Q6B1F3, Q6TQT7, Q6TQT8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 11, 2006
Last modified: March 19, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families