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YEAST:UBP6

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) UBP6
Protein Name(s) Ubiquitin carboxyl-terminal hydrolase 6

Deubiquitinating enzyme 6 Ubiquitin thioesterase 6 Ubiquitin-specific-processing protease 6

External Links
UniProt P43593
EMBL D50617
BK006940
PIR S56265
RefSeq NP_116665.1
PDB 1VJV
PDBsum 1VJV
ProteinModelPortal P43593
SMR P43593
BioGrid 31160
DIP DIP-6731N
IntAct P43593
MINT MINT-619095
STRING 4932.YFR010W
MEROPS C19.079
MoonProt P43593
MaxQB P43593
PaxDb P43593
PeptideAtlas P43593
EnsemblFungi [example_ID YFR010W]
GeneID 850562
KEGG sce:YFR010W
CYGD YFR010w
SGD S000001906
eggNOG NOG286607
GeneTree ENSGT00390000009615
HOGENOM HOG000202292
InParanoid P43593
KO K11843
OMA ELCTTEL
OrthoDB EOG789CMF
BioCyc YEAST:G3O-30463-MONOMER
EvolutionaryTrace P43593
NextBio 966361
PRO PR:P43593
Proteomes UP000002311
Genevestigator P43593
GO GO:0000502
GO:0005838
GO:0004843
GO:1901799
GO:0016579
GO:0006511
InterPro IPR001394
IPR000626
IPR029071
IPR018200
IPR028889
Pfam PF00443
SMART SM00213
SUPFAM SSF54236
PROSITE PS00972
PS00973
PS50235

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0032434

regulation of proteasomal ubiquitin-dependent protein catabolic process

PMID:21658604[1]

ECO:0000315

P

Figure 5(A) The immunoblot analysis indicates that the blot of Ubp6 mutant accumulates ubiquitylated proteins unlike the wild type cells. Figure 4 (D) Double deletion of Ubp6 and hsm3 shows the most noticeable growth defect due to lack of proteasomal assembly.

complete
CACAO 4640

involved_in

GO:0072671

mitochondria-associated ubiquitin-dependent protein catabolic process

PMID:21070972[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

has_input:(UniProtKB:P07213)|has_input:(UniProtKB:P53083)|has_input:(UniProtKB:P28737)

Seeded From UniProt

complete

involved_in

GO:0032434

regulation of proteasomal ubiquitin-dependent protein catabolic process

PMID:21658604[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1901799

negative regulation of proteasomal protein catabolic process

PMID:17018280[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016579

protein deubiquitination

PMID:14581483[4]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000001900

P

Seeded From UniProt

complete

involved_in

GO:0016579

protein deubiquitination

PMID:12408819[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005838

proteasome regulatory particle

PMID:11029046[6]

ECO:0000353

physical interaction evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004843

thiol-dependent ubiquitin-specific protease activity

PMID:12408819[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004843

thiol-dependent ubiquitin-specific protease activity

PMID:17018280[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004843

thiol-dependent ubiquitin-specific protease activity

PMID:12408819[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004843

thiol-dependent ubiquitin-specific protease activity

PMID:17018280[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0000502

proteasome complex

PMID:12408819[5]

ECO:0000353

physical interaction evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006511

ubiquitin-dependent protein catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR018200

P

Seeded From UniProt

complete

involved_in

GO:0016579

protein deubiquitination

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001394

P

Seeded From UniProt

complete

enables

GO:0036459

thiol-dependent ubiquitinyl hydrolase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001394
InterPro:IPR018200

F

Seeded From UniProt

complete

enables

GO:0036459

thiol-dependent ubiquitinyl hydrolase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.4.19.12

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

enables

GO:0008234

cysteine-type peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0788

F

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 Sakata, E et al. (2011) The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle. Mol. Cell 42 637-49 PubMed GONUTS page
  2. Heo, JM et al. (2010) A stress-responsive system for mitochondrial protein degradation. Mol. Cell 40 465-80 PubMed GONUTS page
  3. 3.0 3.1 3.2 Hanna, J et al. (2006) Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation. Cell 127 99-111 PubMed GONUTS page
  4. Guterman, A & Glickman, MH (2004) Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome. J. Biol. Chem. 279 1729-38 PubMed GONUTS page
  5. 5.0 5.1 5.2 5.3 Leggett, DS et al. (2002) Multiple associated proteins regulate proteasome structure and function. Mol. Cell 10 495-507 PubMed GONUTS page
  6. Verma, R et al. (2000) Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol. Biol. Cell 11 3425-39 PubMed GONUTS page