YEAST:ROT1

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	ROT1
Protein Name(s)	Protein ROT1 Reversal of TOR2 lethality protein 1
External Links
UniProt	Q03691
EMBL	Z48755 BK006946
PIR	S59441
RefSeq	NP_013927.1
BioGrid	35378
DIP	DIP-2676N
IntAct	Q03691
MINT	MINT-490710
PeptideAtlas	Q03691
EnsemblFungi	[example_ID YMR200W]
GeneID	855240
KEGG	sce:YMR200W
EuPathDB	FungiDB:YMR200W
SGD	S000004813
HOGENOM	HOG000246668
InParanoid	Q03691
OMA	SRYVQST
OrthoDB	EOG7FBRV8
BioCyc	YEAST:G3O-32887-MONOMER
NextBio	978792
PRO	PR:Q03691
Proteomes	UP000002311
GO	GO:0005789 GO:0016021 GO:0051082 GO:0006458 GO:0007118 GO:0030968 GO:0030950 GO:0009272 GO:0006457 GO:0006487 GO:0035269
InterPro	IPR019623
Pfam	PF10681
PIRSF	PIRSF017290

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0005789	endoplasmic reticulum membrane	PMID:16567426^[1]	ECO:0000314			C	Figure 1 E shows Rot1p is localized in the ER membrane.	complete CACAO 11232
part_of	GO:0005783	endoplasmic reticulum	PMID:26928762^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:14562095^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:18508919^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:18508919^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0035269	protein O-linked mannosylation	PMID:22492205^[5]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000005611	P	Seeded From UniProt	complete
involved_in	GO:0034975	protein folding in endoplasmic reticulum	PMID:16874095^[6]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000003571	P	Seeded From UniProt	complete
involved_in	GO:0030950	establishment or maintenance of actin cytoskeleton polarity	PMID:17606994^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009272	fungal-type cell wall biogenesis	PMID:9545237^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007118	budding cell apical bud growth	PMID:17606994^[7]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000006323	P	Seeded From UniProt	complete
involved_in	GO:0007118	budding cell apical bud growth	PMID:17606994^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006487	protein N-linked glycosylation	PMID:22492205^[5]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000005611	P	Seeded From UniProt	complete
involved_in	GO:0006487	protein N-linked glycosylation	PMID:22492205^[5]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000005611	P	Seeded From UniProt	complete
involved_in	GO:0006458	'de novo' protein folding	PMID:18508919^[4]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000001143 SGD:S000006363	P	Seeded From UniProt	complete
involved_in	GO:0006458	'de novo' protein folding	PMID:18508919^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	PMID:16874095^[6]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000003571	P	Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	PMID:16567426^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001999053 SGD:S000004813	F	Seeded From UniProt	complete
involved_in	GO:0035269	protein O-linked mannosylation	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001999053 SGD:S000004813	P	Seeded From UniProt	complete
involved_in	GO:0009272	fungal-type cell wall biogenesis	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001999053 SGD:S000004813	P	Seeded From UniProt	complete
involved_in	GO:0007118	budding cell apical bud growth	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001999057 SGD:S000004813	P	Seeded From UniProt	complete
involved_in	GO:0006487	protein N-linked glycosylation	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001999053 SGD:S000004813	P	Seeded From UniProt	complete
involved_in	GO:0006458	'de novo' protein folding	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001999053 SGD:S000004813	P	Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001999053 SGD:S000004813	C	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR019623	C	Seeded From UniProt	complete
involved_in	GO:0006458	'de novo' protein folding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR019623	P	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: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: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: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.

↑ ^1.0 ^1.1 Takeuchi, M et al. (2006) Saccharomyces cerevisiae Rot1p is an ER-localized membrane protein that may function with BiP/Kar2p in protein folding. J. Biochem. 139 597-605 PubMed GONUTS page
↑ 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
↑ Huh, WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425 686-91 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 Takeuchi, M et al. (2008) Saccharomyces cerevisiae Rot1 is an essential molecular chaperone in the endoplasmic reticulum. Mol. Biol. Cell 19 3514-25 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Pasikowska, M et al. (2012) The essential endoplasmic reticulum chaperone Rot1 is required for protein N- and O-glycosylation in yeast. Glycobiology 22 939-47 PubMed GONUTS page
↑ ^6.0 ^6.1 Takeuchi, M et al. () Causal links between protein folding in the ER and events along the secretory pathway. Autophagy 2 323-4 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Juanes, MA et al. (2007) Rot1 plays an antagonistic role to Clb2 in actin cytoskeleton dynamics throughout the cell cycle. J. Cell. Sci. 120 2390-401 PubMed GONUTS page
↑ Bickle, M et al. (1998) Cell wall integrity modulates RHO1 activity via the exchange factor ROM2. EMBO J. 17 2235-45 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 ^9.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:16567426-1] 1.0 ^1.1 Takeuchi, M et al. (2006) Saccharomyces cerevisiae Rot1p is an ER-localized membrane protein that may function with BiP/Kar2p in protein folding. J. Biochem. 139 597-605 PubMed GONUTS page

[PMID:26928762-2] 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

[PMID:14562095-3] Huh, WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425 686-91 PubMed GONUTS page

[PMID:18508919-4] 4.0 ^4.1 ^4.2 ^4.3 Takeuchi, M et al. (2008) Saccharomyces cerevisiae Rot1 is an essential molecular chaperone in the endoplasmic reticulum. Mol. Biol. Cell 19 3514-25 PubMed GONUTS page

[PMID:22492205-5] 5.0 ^5.1 ^5.2 Pasikowska, M et al. (2012) The essential endoplasmic reticulum chaperone Rot1 is required for protein N- and O-glycosylation in yeast. Glycobiology 22 939-47 PubMed GONUTS page

[PMID:16874095-6] 6.0 ^6.1 Takeuchi, M et al. () Causal links between protein folding in the ER and events along the secretory pathway. Autophagy 2 323-4 PubMed GONUTS page

[PMID:17606994-7] 7.0 ^7.1 ^7.2 Juanes, MA et al. (2007) Rot1 plays an antagonistic role to Clb2 in actin cytoskeleton dynamics throughout the cell cycle. J. Cell. Sci. 120 2390-401 PubMed GONUTS page

[PMID:9545237-8] Bickle, M et al. (1998) Cell wall integrity modulates RHO1 activity via the exchange factor ROM2. EMBO J. 17 2235-45 PubMed GONUTS page

[PMID:21873635-9] 9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 ^9.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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YEAST:ROT1

Contents

Annotations

Notes

References

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