YEAST:MOT1

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	MOT1
Protein Name(s)	TATA-binding protein-associated factor MOT1 TBP-associated factor MOT1 Modifier of transcription 1
External Links
UniProt	P32333
EMBL	M83224 U41849 BK006949
PIR	S22775
RefSeq	NP_015243.1
ProteinModelPortal	P32333
SMR	P32333
BioGrid	36099
DIP	DIP-2418N
IntAct	P32333
MINT	MINT-623118
STRING	4932.YPL082C
MaxQB	P32333
PaxDb	P32333
PeptideAtlas	P32333
PRIDE	P32333
EnsemblFungi	[example_ID YPL082C]
GeneID	856023
KEGG	sce:YPL082C
CYGD	YPL082c
SGD	S000006003
eggNOG	COG0553
GeneTree	ENSGT00630000089754
HOGENOM	HOG000210415
InParanoid	P32333
KO	K15192
OMA	QRSRDVD
OrthoDB	EOG7WDN9S
BioCyc	YEAST:G3O-33988-MONOMER
NextBio	980935
PRO	PR:P32333
Proteomes	UP000002311
Genevestigator	P32333
GO	GO:0005739 GO:0000228 GO:0005634 GO:0005524 GO:0016887 GO:0003677 GO:0004386 GO:0017025 GO:0006200 GO:0045892 GO:0045898 GO:0006357 GO:0006364 GO:0042790
Gene3D	1.25.10.10 3.40.50.300
InterPro	IPR011989 IPR016024 IPR022707 IPR014001 IPR001650 IPR027417 IPR000330
Pfam	PF12054 PF00271 PF00176
SMART	SM00487 SM00490
SUPFAM	SSF48371 SSF52540
PROSITE	PS51192 PS51194

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:2000233	negative regulation of rRNA processing	PMID:17296733^[1]	ECO:0000314			P	Figure 2: Reduced rRNA synthesis and processing in mot1 cells	complete CACAO 6146
part_of	GO:0005739	mitochondrion	PMID:16823961^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:22842922^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:14576278^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:24459134^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045898	regulation of RNA polymerase II transcriptional preinitiation complex assembly	PMID:15861138^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045898	regulation of RNA polymerase II transcriptional preinitiation complex assembly	PMID:21976730^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042790	nucleolar large rRNA transcription by RNA polymerase I	PMID:17296733^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042790	nucleolar large rRNA transcription by RNA polymerase I	PMID:17296733^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0017025	TBP-class protein binding	PMID:8083216^[8]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000000950	F	Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:9234740^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006364	rRNA processing	PMID:17296733^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006357	regulation of transcription by RNA polymerase II	PMID:9234740^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21976730^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:22298788^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0000228	nuclear chromosome	PMID:11880621^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000330	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
part_of	GO:0005739	mitochondrion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496 UniProtKB-SubCell:SL-0173	C	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	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
enables	GO:0004386	helicase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0347	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 ^1.2 ^1.3 Dasgupta, A et al. (2007) Regulation of rRNA synthesis by TATA-binding protein-associated factor Mot1. Mol. Cell. Biol. 27 2886-96 PubMed GONUTS page
↑ Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page
↑ Tkach, JM et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat. Cell Biol. 14 966-76 PubMed GONUTS page
↑ Sickmann, A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. U.S.A. 100 13207-12 PubMed GONUTS page
↑ Koster, MJ et al. (2014) Suppression of intragenic transcription requires the MOT1 and NC2 regulators of TATA-binding protein. Nucleic Acids Res. 42 4220-9 PubMed GONUTS page
↑ Dasgupta, A et al. (2005) Mot1-mediated control of transcription complex assembly and activity. EMBO J. 24 1717-29 PubMed GONUTS page
↑ ^7.0 ^7.1 Spedale, G et al. (2012) Tight cooperation between Mot1p and NC2β in regulating genome-wide transcription, repression of transcription following heat shock induction and genetic interaction with SAGA. Nucleic Acids Res. 40 996-1008 PubMed GONUTS page
↑ Poon, D et al. (1994) Yeast Taf170 is encoded by MOT1 and exists in a TATA box-binding protein (TBP)-TBP-associated factor complex distinct from transcription factor IID. J. Biol. Chem. 269 23135-40 PubMed GONUTS page
↑ ^9.0 ^9.1 Auble, DT et al. (1997) Molecular analysis of the SNF2/SWI2 protein family member MOT1, an ATP-driven enzyme that dissociates TATA-binding protein from DNA. Mol. Cell. Biol. 17 4842-51 PubMed GONUTS page
↑ Moyle-Heyrman, G et al. (2012) Two-step mechanism for modifier of transcription 1 (Mot1) enzyme-catalyzed displacement of TATA-binding protein (TBP) from DNA. J. Biol. Chem. 287 9002-12 PubMed GONUTS page
↑ Dasgupta, A et al. (2002) Mot1 activates and represses transcription by direct, ATPase-dependent mechanisms. Proc. Natl. Acad. Sci. U.S.A. 99 2666-71 PubMed GONUTS page

[PMID:17296733-1] 1.0 ^1.1 ^1.2 ^1.3 Dasgupta, A et al. (2007) Regulation of rRNA synthesis by TATA-binding protein-associated factor Mot1. Mol. Cell. Biol. 27 2886-96 PubMed GONUTS page

[PMID:16823961-2] Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page

[PMID:22842922-3] Tkach, JM et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat. Cell Biol. 14 966-76 PubMed GONUTS page

[PMID:14576278-4] Sickmann, A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. U.S.A. 100 13207-12 PubMed GONUTS page

[PMID:24459134-5] Koster, MJ et al. (2014) Suppression of intragenic transcription requires the MOT1 and NC2 regulators of TATA-binding protein. Nucleic Acids Res. 42 4220-9 PubMed GONUTS page

[PMID:15861138-6] Dasgupta, A et al. (2005) Mot1-mediated control of transcription complex assembly and activity. EMBO J. 24 1717-29 PubMed GONUTS page

[PMID:21976730-7] 7.0 ^7.1 Spedale, G et al. (2012) Tight cooperation between Mot1p and NC2β in regulating genome-wide transcription, repression of transcription following heat shock induction and genetic interaction with SAGA. Nucleic Acids Res. 40 996-1008 PubMed GONUTS page

[PMID:8083216-8] Poon, D et al. (1994) Yeast Taf170 is encoded by MOT1 and exists in a TATA box-binding protein (TBP)-TBP-associated factor complex distinct from transcription factor IID. J. Biol. Chem. 269 23135-40 PubMed GONUTS page

[PMID:9234740-9] 9.0 ^9.1 Auble, DT et al. (1997) Molecular analysis of the SNF2/SWI2 protein family member MOT1, an ATP-driven enzyme that dissociates TATA-binding protein from DNA. Mol. Cell. Biol. 17 4842-51 PubMed GONUTS page

[PMID:22298788-10] Moyle-Heyrman, G et al. (2012) Two-step mechanism for modifier of transcription 1 (Mot1) enzyme-catalyzed displacement of TATA-binding protein (TBP) from DNA. J. Biol. Chem. 287 9002-12 PubMed GONUTS page

[PMID:11880621-11] Dasgupta, A et al. (2002) Mot1 activates and represses transcription by direct, ATPase-dependent mechanisms. Proc. Natl. Acad. Sci. U.S.A. 99 2666-71 PubMed GONUTS page

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YEAST:MOT1

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