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P25491 (MAS5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Mitochondrial protein import protein MAS5
Alternative name(s):
Yeast dnaJ protein 1
Gene names
Name:YDJ1
Synonyms:MAS5
Ordered Locus Names:YNL064C
ORF Names:N2418, YNL2418C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably involved in mitochondrial protein import. Is also required for efficient translocation of pre-pro-alpha-factor. Involved in heme regulation of HAP1, as a component of the high-molecular-weight (HMC) complex. Ref.8

Subunit structure

Homodimer. Interacts with HAP1. Component of the HMC including HAP1, SRO9 and YDJ1. Ref.8 Ref.13

Subcellular location

Cytoplasm. Cytoplasmperinuclear region. Note: Concentrated in a perinuclear ring as well as in the cytoplasm. Ref.1 Ref.9

Induction

YDJ1 is a heat shock gene whose expression increases moderately at elevated temperatures. HAMAP-Rule MF_01152

Miscellaneous

Present with 119000 molecules/cell in log phase SD medium.

Sequence similarities

Contains 1 CR-type zinc finger.

Contains 1 J domain.

Ontologies

Keywords
   Biological processProtein transport
Stress response
Transport
   Cellular componentCytoplasm
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChaperone
   PTMLipoprotein
Methylation
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' protein folding

Inferred from mutant phenotype PubMed 10567418. Source: SGD

ER-associated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 15252059PubMed 15342786. Source: SGD

positive regulation of ATPase activity

Inferred from direct assay PubMed 1400408PubMed 15342786. Source: GOC

protein refolding

Inferred from direct assay PubMed 9674429. Source: SGD

protein targeting to ER

Inferred from mutant phenotype PubMed 1473150. Source: SGD

protein targeting to mitochondrion

Inferred from mutant phenotype Ref.2. Source: SGD

response to heat

Inferred from electronic annotation. Source: InterPro

   Cellular_componentTRC complex

Inferred from direct assay PubMed 20850366. Source: SGD

cytosol

Inferred from direct assay Ref.1PubMed 8144572. Source: SGD

perinuclear region of cytoplasm

Inferred from direct assay Ref.1. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

ATPase activator activity

Inferred from direct assay PubMed 1400408PubMed 15342786. Source: SGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

unfolded protein binding

Inferred from direct assay PubMed 9774392. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MDY2Q122852EBI-10420,EBI-34904
SGT2Q121182EBI-10420,EBI-31784
SUP35Q7LKB13EBI-10420,EBI-8411471From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 406406Mitochondrial protein import protein MAS5 HAMAP-Rule MF_01152
PRO_0000071093
Propeptide407 – 4093Removed in mature form Probable
PRO_0000396684

Regions

Domain4 – 7269J
Repeat143 – 1508CXXCXGXG motif HAMAP-Rule MF_01152
Repeat159 – 1668CXXCXGXG motif HAMAP-Rule MF_01152
Repeat185 – 1928CXXCXGXG motif HAMAP-Rule MF_01152
Repeat201 – 2088CXXCXGXG motif HAMAP-Rule MF_01152
Zinc finger130 – 21384CR-type HAMAP-Rule MF_01152
Region1 – 172172Necessary for HAP1 repression in the absence of heme HAMAP-Rule MF_01152
Region135 – 1373Substrate binding HAMAP-Rule MF_01152
Region215 – 2162Substrate binding HAMAP-Rule MF_01152
Region247 – 2493Substrate binding HAMAP-Rule MF_01152
Compositional bias73 – 10331Gly-rich HAMAP-Rule MF_01152

Sites

Metal binding1431Zinc 1
Metal binding1461Zinc 1
Metal binding1591Zinc 2
Metal binding1621Zinc 2
Metal binding1851Zinc 2
Metal binding1881Zinc 2
Metal binding2011Zinc 1
Metal binding2041Zinc 1
Binding site1161Substrate; via amide nitrogen
Site3351Involved in dimerization

Amino acid modifications

Modified residue4061Cysteine methyl ester Probable
Lipidation4061S-farnesyl cysteine Ref.7

Experimental info

Mutagenesis3351F → D: Prevents dimerization. Ref.13

Secondary structure

................................................. 409
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25491 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: E4539F3618DD9CF2

FASTA40944,671
        10         20         30         40         50         60 
MVKETKFYDI LGVPVTATDV EIKKAYRKCA LKYHPDKNPS EEAAEKFKEA SAAYEILSDP 

        70         80         90        100        110        120 
EKRDIYDQFG EDGLSGAGGA GGFPGGGFGF GDDIFSQFFG AGGAQRPRGP QRGKDIKHEI 

       130        140        150        160        170        180 
SASLEELYKG RTAKLALNKQ ILCKECEGRG GKKGAVKKCT SCNGQGIKFV TRQMGPMIQR 

       190        200        210        220        230        240 
FQTECDVCHG TGDIIDPKDR CKSCNGKKVE NERKILEVHV EPGMKDGQRI VFKGEADQAP 

       250        260        270        280        290        300 
DVIPGDVVFI VSERPHKSFK RDGDDLVYEA EIDLLTAIAG GEFALEHVSG DWLKVGIVPG 

       310        320        330        340        350        360 
EVIAPGMRKV IEGKGMPIPK YGGYGNLIIK FTIKFPENHF TSEENLKKLE EILPPRIVPA 

       370        380        390        400 
IPKKATVDEC VLADFDPAKY NRTRASRGGA NYDSDEEEQG GEGVQCASQ 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein."
Caplan A.J., Douglas M.G.
J. Cell Biol. 114:609-621(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
[2]"MAS5, a yeast homolog of DnaJ involved in mitochondrial protein import."
Atencio D.P., Yaffe M.P.
Mol. Cell. Biol. 12:283-291(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The sequence of a 44 420 bp fragment located on the left arm of chromosome XIV from Saccharomyces cerevisiae."
Bergez P., Doignon F., Crouzet M.
Yeast 11:967-974(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: S288c / FY1676.
[4]Erratum
Bergez P., Doignon F., Crouzet M.
Yeast 12:297-297(1996) [PubMed] [Europe PMC] [Abstract]
[5]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[7]"Farnesylation of YDJ1p is required for function at elevated growth temperatures in Saccharomyces cerevisiae."
Caplan A.J., Tsai J., Casey P.J., Douglas M.G.
J. Biol. Chem. 267:18890-18895(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-406.
[8]"The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme."
Hon T., Lee H.C., Hach A., Johnson J.L., Craig E.A., Erdjument-Bromage H., Tempst P., Zhang L.
Mol. Cell. Biol. 21:7923-7932(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[9]"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].
[10]"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].
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate."
Li J., Qian X., Sha B.
Structure 11:1475-1483(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 103-350 IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT, MUTAGENESIS OF PHE-335.
[14]"The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 reveals novel dimerization motif for Hsp40."
Wu Y., Li J., Jin Z., Fu Z., Sha B.
J. Mol. Biol. 346:1005-1011(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 258-378.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56560 Genomic DNA. Translation: CAA39910.1.
S74758 Genomic DNA. Translation: AAB20771.1.
U12141 Genomic DNA. Translation: AAA99647.1.
Z71340 Genomic DNA. Translation: CAA95937.1.
BK006947 Genomic DNA. Translation: DAA10482.1.
PIRS26703.
RefSeqNP_014335.1. NM_001182902.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NLTX-ray2.70A103-350[»]
1XAOX-ray2.07A/B258-378[»]
ProteinModelPortalP25491.
SMRP25491. Positions 1-71, 110-378.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35759. 484 interactions.
DIPDIP-2251N.
IntActP25491. 14 interactions.
MINTMINT-603538.
STRING4932.YNL064C.

Proteomic databases

PaxDbP25491.
PeptideAtlasP25491.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL064C; YNL064C; YNL064C.
GeneID855661.
KEGGsce:YNL064C.

Organism-specific databases

CYGDYNL064c.
SGDS000005008. YDJ1.

Phylogenomic databases

eggNOGCOG0484.
GeneTreeENSGT00490000043321.
HOGENOMHOG000226718.
KOK09503.
OMAHFTSEEN.
OrthoDBEOG77M90H.

Enzyme and pathway databases

BioCycYEAST:G3O-33094-MONOMER.

Gene expression databases

GenevestigatorP25491.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPMF_01152. DnaJ.
InterProIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamPF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
SSF57938. SSF57938. 1 hit.
PROSITEPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25491.
NextBio979926.
PROP25491.

Entry information

Entry nameMAS5_YEAST
AccessionPrimary (citable) accession number: P25491
Secondary accession number(s): D6W1B6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 16, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references