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YEAST:MAS5

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) YDJ1 (synonyms: MAS5)
Protein Name(s) Mitochondrial protein import protein MAS5

Yeast dnaJ protein 1

External Links
UniProt P25491
EMBL X56560
S74758
U12141
Z71340
BK006947
PIR S26703
RefSeq NP_014335.1
PDB 1NLT
1XAO
PDBsum 1NLT
1XAO
ProteinModelPortal P25491
SMR P25491
BioGrid 35759
DIP DIP-2251N
IntAct P25491
MINT MINT-603538
STRING 4932.YNL064C
MaxQB P25491
PaxDb P25491
PeptideAtlas P25491
EnsemblFungi [example_ID YNL064C]
GeneID 855661
KEGG sce:YNL064C
CYGD YNL064c
SGD S000005008
eggNOG COG0484
GeneTree ENSGT00490000043321
HOGENOM HOG000226718
InParanoid P25491
KO K09503
OMA HVSGDWL
OrthoDB EOG77M90H
BioCyc YEAST:G3O-33094-MONOMER
EvolutionaryTrace P25491
NextBio 979926
PRO PR:P25491
Proteomes UP000002311
Genevestigator P25491
GO GO:0005829
GO:0048471
GO:0072380
GO:0005524
GO:0001671
GO:0046872
GO:0051082
GO:0006458
GO:0030433
GO:0032781
GO:0042026
GO:0045047
GO:0006626
GO:0009408
Gene3D 1.10.287.110
2.10.230.10
HAMAP MF_01152
InterPro IPR012724
IPR002939
IPR001623
IPR018253
IPR008971
IPR001305
Pfam PF01556
PF00226
PF00684
PRINTS PR00625
SMART SM00271
SUPFAM SSF46565
SSF49493
SSF57938
PROSITE PS00636
PS50076
PS51188

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0005829

cytosol

PMID:26928762[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0051131

chaperone-mediated protein complex assembly

PMID:10811660[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0035719

tRNA import into nucleus

PMID:25853343[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

happens_during:(GO:0009267)

Seeded From UniProt

complete

involved_in

GO:0006511

ubiquitin-dependent protein catabolic process

PMID:25344756[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

happens_during:(GO:0034605)

Seeded From UniProt

complete

part_of

GO:0072380

TRC complex

PMID:20850366[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:9774392[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0048471

perinuclear region of cytoplasm

PMID:1869583[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0045047

protein targeting to ER

PMID:1473150[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042026

protein refolding

PMID:9674429[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0030433

ubiquitin-dependent ERAD pathway

PMID:15252059[10]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0030433

ubiquitin-dependent ERAD pathway

PMID:15342786[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006626

protein targeting to mitochondrion

PMID:1729605[12]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006458

'de novo' protein folding

PMID:10567418[13]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:8144572[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:1869583[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0001671

ATPase activator activity

PMID:1400408[15]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0001671

ATPase activator activity

PMID:15342786[11]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[16]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001531327
PomBase:SPBC1734.11
RGD:71001
SGD:S000005008
TAIR:locus:505006628
UniProtKB:O60884
UniProtKB:P31689
UniProtKB:Q8WW22
UniProtKB:Q94AW8

C

Seeded From UniProt

complete

involved_in

GO:0032781

positive regulation of ATPase activity

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0001671

P

Seeded From UniProt

complete

involved_in

GO:0032781

positive regulation of ATPase activity

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0001671

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012724

F

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR008971
InterPro:IPR012724

P

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012724

P

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001305

F

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001305
InterPro:IPR008971
InterPro:IPR012724

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0015031

protein transport

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0653

P

Seeded From UniProt

complete

part_of

GO:0048471

perinuclear region of cytoplasm

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0198

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Yofe, I et al. (2016) One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy. Nat. Methods 13 371-378 PubMed GONUTS page
  2. Weaver, AJ et al. (2000) Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone. J. Biol. Chem. 275 23045-52 PubMed GONUTS page
  3. Takano, A et al. (2015) Cytosolic Hsp70 and co-chaperones constitute a novel system for tRNA import into the nucleus. Elife 4 PubMed GONUTS page
  4. Fang, NN et al. (2014) Rsp5/Nedd4 is the main ubiquitin ligase that targets cytosolic misfolded proteins following heat stress. Nat. Cell Biol. 16 1227-37 PubMed GONUTS page
  5. Wang, F et al. (2010) A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol. Cell 40 159-71 PubMed GONUTS page
  6. Lu, Z & Cyr, DM (1998) Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1. J. Biol. Chem. 273 27824-30 PubMed GONUTS page
  7. 7.0 7.1 Caplan, AJ & Douglas, MG (1991) Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J. Cell Biol. 114 609-21 PubMed GONUTS page
  8. Caplan, AJ et al. (1992) YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71 1143-55 PubMed GONUTS page
  9. Glover, JR & Lindquist, S (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94 73-82 PubMed GONUTS page
  10. Huyer, G et al. (2004) Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein. J. Biol. Chem. 279 38369-78 PubMed GONUTS page
  11. 11.0 11.1 Youker, RT et al. (2004) Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast. Mol. Biol. Cell 15 4787-97 PubMed GONUTS page
  12. Atencio, DP & Yaffe, MP (1992) MAS5, a yeast homolog of DnaJ involved in mitochondrial protein import. Mol. Cell. Biol. 12 283-91 PubMed GONUTS page
  13. Meacham, GC et al. (1999) Mutations in the yeast Hsp40 chaperone protein Ydj1 cause defects in Axl1 biogenesis and pro-a-factor processing. J. Biol. Chem. 274 34396-402 PubMed GONUTS page
  14. Cyr, DM & Douglas, MG (1994) Differential regulation of Hsp70 subfamilies by the eukaryotic DnaJ homologue YDJ1. J. Biol. Chem. 269 9798-804 PubMed GONUTS page
  15. Cyr, DM et al. (1992) Regulation of Hsp70 function by a eukaryotic DnaJ homolog. J. Biol. Chem. 267 20927-31 PubMed GONUTS page
  16. Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page