GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

YEAST:HST1

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) HST1
Protein Name(s) NAD-dependent protein deacetylase HST1

Homologous to SIR2 protein 1 Regulatory protein SIR2 homolog 1

External Links
UniProt P53685
EMBL U39041
L47120
Z74810
BK006948
PIR S59698
RefSeq NP_014573.1
ProteinModelPortal P53685
SMR P53685
BioGrid 34333
DIP DIP-6757N
IntAct P53685
MINT MINT-639447
STRING 4932.YOL068C
MaxQB P53685
PaxDb P53685
PeptideAtlas P53685
EnsemblFungi [example_ID YOL068C]
GeneID 854086
KEGG sce:YOL068C
CYGD YOL068c
SGD S000005429
eggNOG COG0846
GeneTree ENSGT00740000115330
HOGENOM HOG000191845
InParanoid P53685
KO K11121
OrthoDB EOG7MWH64
BioCyc YEAST:G3O-33473-MONOMER
Reactome REACT_205607
SABIO-RK P53685
NextBio 975731
Proteomes UP000002311
Genevestigator P53685
GO GO:0034967
GO:0070403
GO:0017136
GO:0045129
GO:0008270
GO:0006342
GO:0016575
GO:0045950
GO:0030435
GO:0006351
Gene3D 3.30.1600.10
3.40.50.1220
InterPro IPR029035
IPR007654
IPR003000
IPR026591
IPR026590
PANTHER PTHR11085
Pfam PF04574
PF02146
SUPFAM SSF52467
PROSITE PS50305

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0070623

regulation of thiamine biosynthetic process

PMID:20439498[1]

ECO:0000315

P

Figure 7A illusterates an increase in intracellular thiamine levels in the mutant Hst1 representing that cellular thiamine homeostasis in yeast requires Hst1.

complete
CACAO 4730

involved_in

GO:0030466

chromatin silencing at silent mating-type cassette

PMID:27185881[2]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000002200,SGD:S000002718

P

Seeded From UniProt

complete

involved_in

GO:0070623

regulation of thiamine biosynthetic process

PMID:20439498[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016575

histone deacetylation

PMID:11313477[3]

ECO:0000314

direct assay evidence used in manual assertion

P

has_direct_input:(UniProtKB:P02309)

Seeded From UniProt

complete

enables

GO:0017136

NAD-dependent histone deacetylase activity

PMID:11313477[3]

ECO:0000314

direct assay evidence used in manual assertion

F

has_direct_input:(UniProtKB:P02309)

Seeded From UniProt

complete

involved_in

GO:0045950

negative regulation of mitotic recombination

PMID:16051752[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0045129

NAD-independent histone deacetylase activity

PMID:11711434[5]

ECO:0000314

direct assay evidence used in manual assertion

F

has_direct_input:(UniProtKB:P02309)

Seeded From UniProt

complete

part_of

GO:0034967

Set3 complex

PMID:11711434[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0017136

NAD-dependent histone deacetylase activity

PMID:11711434[5]

ECO:0000314

direct assay evidence used in manual assertion

F

has_direct_input:(UniProtKB:P02309)

Seeded From UniProt

complete

involved_in

GO:0016575

histone deacetylation

PMID:11711434[5]

ECO:0000314

direct assay evidence used in manual assertion

P

has_direct_input:(UniProtKB:P02309)

Seeded From UniProt

complete

involved_in

GO:0030466

chromatin silencing at silent mating-type cassette

PMID:11313477[3]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P06700
UniProtKB:P46676

P

Seeded From UniProt

complete

involved_in

GO:0030466

chromatin silencing at silent mating-type cassette

PMID:11313477[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0070403

NAD+ binding

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000119154
PomBase:SPBC16D10.07c
UniProtKB:Q8IXJ6

F

Seeded From UniProt

complete

enables

GO:0046970

NAD-dependent histone deacetylase activity (H4-K16 specific)

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000872240
PomBase:SPBC16D10.07c
SGD:S000002200
UniProtKB:C8V3W5

F

Seeded From UniProt

complete

part_of

GO:0034967

Set3 complex

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000872240
SGD:S000005429

C

Seeded From UniProt

complete

part_of

GO:0031618

nuclear pericentric heterochromatin

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000872240
PomBase:SPBC16D10.07c

C

Seeded From UniProt

complete

enables

GO:0017136

NAD-dependent histone deacetylase activity

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0024291
FB:FBgn0038788
MGI:MGI:2135607
PANTHER:PTN000119154
SGD:S000002200
SGD:S000005429
SGD:S000005551
SGD:S000005936
UniProtKB:Q96EB6

F

Seeded From UniProt

complete

enables

GO:0017136

NAD-dependent histone deacetylase activity

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0024291
FB:FBgn0038788
MGI:MGI:2135607
PANTHER:PTN000119154
SGD:S000002200
SGD:S000005429
SGD:S000005551
SGD:S000005936
UniProtKB:Q8IXJ6
UniProtKB:Q96EB6

F

Seeded From UniProt

complete

part_of

GO:0005730

nucleolus

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000872240
SGD:S000002200

C

Seeded From UniProt

complete

part_of

GO:0005724

nuclear telomeric heterochromatin

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000872240
SGD:S000002200

C

Seeded From UniProt

complete

part_of

GO:0005720

nuclear heterochromatin

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000872240
SGD:S000002200

C

Seeded From UniProt

complete

part_of

GO:0005677

chromatin silencing complex

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000872240
SGD:S000002200

C

Seeded From UniProt

complete

part_of

GO:0000790

nuclear chromatin

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000872240
PomBase:SPBC16D10.07c

C

Seeded From UniProt

complete

involved_in

GO:0070933

histone H4 deacetylation

GO_REF:0000108

ECO:0000364

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

GO:0046970

P

Seeded From UniProt

complete

enables

GO:0070403

NAD+ binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003000

F

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:0030435

sporulation resulting in formation of a cellular spore

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0749

P

Seeded From UniProt

complete

involved_in

GO:0006325

chromatin organization

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0156

P

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

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

edit table

Notes

References

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

  1. ↑ 1.0 1.1 Li, M et al. (2010) Thiamine biosynthesis in Saccharomyces cerevisiae is regulated by the NAD+-dependent histone deacetylase Hst1. Mol. Cell. Biol. 30 3329-41 PubMed GONUTS page
  2. ↑ Chen, YF et al. (2016) Determinants of Sir2-Mediated, Silent Chromatin Cohesion. Mol. Cell. Biol. 36 2039-50 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 3.3 Sutton, A et al. (2001) A novel form of transcriptional silencing by Sum1-1 requires Hst1 and the origin recognition complex. Mol. Cell. Biol. 21 3514-22 PubMed GONUTS page
  4. ↑ Lamming, DW et al. (2005) HST2 mediates SIR2-independent life-span extension by calorie restriction. Science 309 1861-4 PubMed GONUTS page
  5. ↑ 5.0 5.1 5.2 5.3 Pijnappel, WW et al. (2001) The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and Hst1, and is a meiotic-specific repressor of the sporulation gene program. Genes Dev. 15 2991-3004 PubMed GONUTS page
  6. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
Retrieved from "https://gowiki.tamu.edu/wiki/index.php?title=YEAST:HST1&oldid=5956943"