P38788 (SSZ1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	538 AA.
Sequence status	Complete.
Protein existence	Evidence 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.14
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.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytoplasmic translation Inferred from mutant phenotype PubMed 11929994. Source: SGD rRNA processing Inferred from mutant phenotype PubMed 20368619. Source: SGD regulation of translational fidelity Inferred from mutant phenotype Ref.12. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 10792726. Source: SGD polysome Inferred from direct assay PubMed 16413483. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW unfolded protein binding Inferred from genetic interaction Ref.6. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ZUO1	P32527	7	EBI-24570,EBI-29684

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 538	538	Ribosome-associated complex subunit SSZ1		PRO_0000078400
Regions
	Region	400 – 538	139	Peptide-binding domain Potential
Amino acid modifications
	Modified residue	136	1	Phosphoserine Ref.18
	Modified residue	405	1	Phosphothreonine Ref.17
	Modified residue	477	1	Phosphoserine Ref.15 Ref.16 Ref.17 Ref.18
	Modified residue	480	1	Phosphoserine Ref.13 Ref.15 Ref.16 Ref.17 Ref.18
Experimental info
	Mutagenesis	295	1	S → F: Increases readthrough in translation termination. Ref.12
	Sequence conflict	208	1	V → A in AAT93146. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P38788 [UniParc]. Last modified July 11, 2006. Version 2. Checksum: 07B1A409B213E0B4	FASTA	538	58,238
	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

References

	« Hide 'large scale' referencesShow '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. , 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 204511 / S288c / AB972.
[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. , 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]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, MASS SPECTROMETRY. Strain: YAL6B.
[14]	"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.
[15]	"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, MASS SPECTROMETRY. Strain: ADR376.
[16]	"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-477 AND SER-480, MASS SPECTROMETRY.
[17]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-405; SER-477 AND SER-480, MASS SPECTROMETRY.
[18]	"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-136; SER-477 AND SER-480, MASS SPECTROMETRY.
+	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.
PIR	S46712.
RefSeq	NP_011931.2. NM_001179194.1.
3D structure databases
ProteinModelPortal	P38788.
SMR	P38788. Positions 4-535.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6305N.
IntAct	P38788. 60 interactions.
MINT	MINT-671986.
Proteomic databases
PaxDb	P38788.
PeptideAtlas	P38788.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YHR064C; YHR064C; YHR064C.
GeneID	856461.
KEGG	sce:YHR064C.
Organism-specific databases
CYGD	YHR064c.
SGD	S000001106. SSZ1.
Phylogenomic databases
eggNOG	COG0443.
GeneTree	ENSGT00700000105728.
HOGENOM	HOG000184645.
OMA	TILATAH.
OrthoDB	EOG4R273W.
Enzyme and pathway databases
BioCyc	YEAST:G3O-31115-MONOMER.
Gene expression databases
Genevestigator	P38788.
GermOnline	YHR064C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013126. Hsp_70_fam. [Graphical view]
Pfam	PF00012. HSP70. 1 hit. [Graphical view]
PRINTS	PR00301. HEATSHOCK70.
PROSITE	PS00297. HSP70_1. False negative. PS00329. HSP70_2. False negative. PS01036. HSP70_3. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	982108.

Entry information

Entry name

SSZ1_YEAST

Accession

Primary (citable) accession number: P38788
Secondary accession number(s): D3DL13 , Q6B1F3, Q6TQT7, Q6TQT8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	July 11, 2006
Last modified:	May 29, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program