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YEAST:ORM2

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) ORM2
Protein Name(s) Protein ORM2
External Links
UniProt Q06144
EMBL U19028
AY692908
BK006945
PIR S51352
RefSeq NP_013454.1
ProteinModelPortal Q06144
BioGrid 31612
DIP DIP-5579N
IntAct Q06144
MINT MINT-573025
STRING 4932.YLR350W
MaxQB Q06144
PaxDb Q06144
EnsemblFungi [example_ID YLR350W]
GeneID 851064
KEGG sce:YLR350W
CYGD YLR350w
SGD S000004342
eggNOG COG5081
GeneTree ENSGT00390000015817
HOGENOM HOG000192740
InParanoid Q06144
OrthoDB EOG7RFTVM
BioCyc YEAST:G3O-32425-MONOMER
NextBio 967696
Proteomes UP000002311
Genevestigator Q06144
GO GO:0005783
GO:0005789
GO:0016021
GO:0035339
GO:0090156
GO:0090155
GO:0006986
InterPro IPR029887
IPR007203
PANTHER PTHR12665
PTHR12665:SF7
Pfam PF04061
PIRSF PIRSF018147

Annotations

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

part_of

GO:0005783

endoplasmic reticulum

PMID:14562095[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0090155

negative regulation of sphingolipid biosynthetic process

PMID:20182505[2]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000002469
SGD:S000003270

P

Seeded From UniProt

complete

involved_in

GO:0090155

negative regulation of sphingolipid biosynthetic process

PMID:20182505[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0035339

SPOTS complex

PMID:20182505[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006986

response to unfolded protein

PMID:12093374[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006986

response to unfolded protein

PMID:12093374[3]

ECO:0000250

sequence similarity evidence used in manual assertion

P

Seeded From UniProt

Missing: with/from

part_of

GO:0005783

endoplasmic reticulum

PMID:20182505[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003674

molecular_function

GO_REF:0000015

ECO:0000307

no biological data found used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0090156

cellular sphingolipid homeostasis

PMID:20182505[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0090155

negative regulation of sphingolipid biosynthetic process

PMID:20182505[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0035339

SPOTS complex

PMID:20182505[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

PMID:20182505[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:1900060

negative regulation of ceramide biosynthetic process

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:1913862
PANTHER:PTN000292374
UniProtKB:Q53FV1
UniProtKB:Q8N138
UniProtKB:Q9P0S3

P

Seeded From UniProt

complete

involved_in

GO:0090156

cellular sphingolipid homeostasis

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000292374
SGD:S000003270
SGD:S000004342
TAIR:locus:2035352
UniProtKB:Q9FHY3

P

Seeded From UniProt

complete

part_of

GO:0035339

SPOTS complex

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000292374
SGD:S000003270
SGD:S000004342
UniProtKB:Q8N138

C

Seeded From UniProt

complete

involved_in

GO:0006672

ceramide metabolic process

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000292374
UniProtKB:Q53FV1
UniProtKB:Q8N138
UniProtKB:Q9P0S3

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:28183979[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q06144

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:20182505[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q06144

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:18467557[6]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q06144

F

Seeded From UniProt

complete

part_of

GO:0005789

endoplasmic reticulum membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR007203

C

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR007203

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0256

C

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

part_of

GO:0005789

endoplasmic reticulum membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0097

C

Seeded From UniProt

complete

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Notes

References

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

  1. ↑ Huh, WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425 686-91 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 2.8 Breslow, DK et al. (2010) Orm family proteins mediate sphingolipid homeostasis. Nature 463 1048-53 PubMed GONUTS page
  3. ↑ 3.0 3.1 Hjelmqvist, L et al. (2002) ORMDL proteins are a conserved new family of endoplasmic reticulum membrane proteins. Genome Biol. 3 RESEARCH0027 PubMed GONUTS page
  4. ↑ 4.0 4.1 4.2 4.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  5. ↑ Diss, G et al. (2017) Gene duplication can impart fragility, not robustness, in the yeast protein interaction network. Science 355 630-634 PubMed GONUTS page
  6. ↑ Tarassov, K et al. (2008) An in vivo map of the yeast protein interactome. Science 320 1465-70 PubMed GONUTS page
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