YEAST:SEN1

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	SEN1
Protein Name(s)	Helicase SEN1 tRNA-splicing endonuclease positive effector
External Links
UniProt	Q00416
EMBL	U20939 U21094 M74589 BK006945
PIR	S53416
RefSeq	NP_013534.3
ProteinModelPortal	Q00416
SMR	Q00416
BioGrid	31689
DIP	DIP-881N
IntAct	Q00416
MINT	MINT-427565
iPTMnet	Q00416
MaxQB	Q00416
PeptideAtlas	Q00416
TopDownProteomics	Q00416
EnsemblFungi	YLR430W
GeneID	851150
KEGG	sce:YLR430W
EuPathDB	FungiDB:YLR430W
SGD	S000004422
GeneTree	ENSGT00830000128421
HOGENOM	HOG000246755
InParanoid	Q00416
KO	K10706
OMA	EIIIMSC
OrthoDB	EOG70PC5T
BioCyc	YEAST:G3O-32489-MONOMER
PRO	PR:Q00416
Proteomes	UP000002311
GO	GO:0005737 GO:0035649 GO:0005634 GO:0005657 GO:0005524 GO:0032575 GO:0008094 GO:0019904 GO:0008186 GO:0017116 GO:0032508 GO:0045005 GO:0006353 GO:0031124 GO:0006378 GO:1990248 GO:0006364 GO:0031126 GO:0016180 GO:0006369 GO:0008033
Gene3D	3.40.50.300
InterPro	IPR024481 IPR027417
Pfam	PF12726
SUPFAM	SSF52540

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0060257	negative regulation of flocculation	PMID:26364722^[1]	ECO:0000315			P	Flocculation was monitored through growth assays and was measured by rate of sedimentation. It was found that the amount of flocculation as well as the rate of flocculation was greater in the SEN1 mutants that in wild type cells (Figure 1A and 1B).	complete CACAO 12170
enables	GO:0003729	mRNA binding	PMID:23222640^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006283	transcription-coupled nucleotide-excision repair	PMID:27179024^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P06779,UniProtKB:P32914	P	Seeded From UniProt	complete
involved_in	GO:0006283	transcription-coupled nucleotide-excision repair	PMID:27179024^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P06779,UniProtKB:P40352	P	Seeded From UniProt	complete
involved_in	GO:0006283	transcription-coupled nucleotide-excision repair	PMID:27179024^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P06779	P	Seeded From UniProt	complete
enables	GO:0033682	ATP-dependent 5'-3' DNA/RNA helicase activity	PMID:26198638^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0043141	ATP-dependent 5'-3' DNA helicase activity	PMID:26198638^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:1990248	regulation of transcription from RNA polymerase II promoter in response to DNA damage	PMID:23741394^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045005	DNA-dependent DNA replication maintenance of fidelity	PMID:23141540^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0035649	Nrd1 complex	PMID:16427013^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0032575	ATP-dependent 5'-3' RNA helicase activity	PMID:10545196^[8]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q92355	F	Seeded From UniProt	complete
involved_in	GO:0031126	snoRNA 3'-end processing	PMID:11565036^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0031124	mRNA 3'-end processing	PMID:11565036^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:22286094^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:22286094^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0016180	snRNA processing	PMID:9365256^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008186	RNA-dependent ATPase activity	PMID:10545196^[8]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q92355	F	Seeded From UniProt	complete
enables	GO:0008094	DNA-dependent ATPase activity	PMID:10545196^[8]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q92355	F	Seeded From UniProt	complete
involved_in	GO:0008033	tRNA processing	PMID:9365256^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006378	mRNA polyadenylation	PMID:22123738^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006369	termination of RNA polymerase II transcription	PMID:17157256^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006364	rRNA processing	PMID:9365256^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006353	DNA-templated transcription, termination	PMID:23748379^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:23222640^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005657	replication fork	PMID:23141540^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:23222640^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:8544822^[15]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0045454	cell redox homeostasis	PMID:27718307^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045005	DNA-dependent DNA replication maintenance of fidelity	PMID:21873635^[17]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002474780 SGD:S000004422	P	Seeded From UniProt	complete
enables	GO:0043141	ATP-dependent 5'-3' DNA helicase activity	PMID:21873635^[17]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002474780 SGD:S000004422	F	Seeded From UniProt	complete
part_of	GO:0035861	site of double-strand break	PMID:21873635^[17]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002474780 PomBase:SPBC29A10.10c	C	Seeded From UniProt	complete
enables	GO:0033682	ATP-dependent 5'-3' DNA/RNA helicase activity	PMID:21873635^[17]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002474780 PomBase:SPAC6G9.10c SGD:S000004422	F	Seeded From UniProt	complete
enables	GO:0032575	ATP-dependent 5'-3' RNA helicase activity	PMID:21873635^[17]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002474780 PomBase:SPAC6G9.10c	F	Seeded From UniProt	complete
involved_in	GO:0008033	tRNA processing	PMID:21873635^[17]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002474780 SGD:S000004422	P	Seeded From UniProt	complete
involved_in	GO:0006283	transcription-coupled nucleotide-excision repair	PMID:21873635^[17]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002474780 SGD:S000004422	P	Seeded From UniProt	complete
part_of	GO:0005657	replication fork	PMID:21873635^[17]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002474780 SGD:S000004422	C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[17]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002474780 SGD:S000004422	C	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:21873635^[17]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000094509 UniProtKB:Q92900 UniProtKB:Q9HCE1	F	Seeded From UniProt	complete
involved_in	GO:0032508	DNA duplex unwinding	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0043141	P	Seeded From UniProt	complete
involved_in	GO:0032508	DNA duplex unwinding	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0043141	P	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
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
involved_in	GO:0006397	mRNA processing	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0507	P	Seeded From UniProt	complete
involved_in	GO:0006364	rRNA processing	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0698	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
involved_in	GO:0008033	tRNA processing	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0819	P	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.

↑ Singh, V et al. (2015) Flocculation in Saccharomyces cerevisiae is regulated by RNA/DNA helicase Sen1p. FEBS Lett. 589 3165-74 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Mitchell, SF et al. (2013) Global analysis of yeast mRNPs. Nat. Struct. Mol. Biol. 20 127-33 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Li, W et al. (2016) Sen1, the yeast homolog of human senataxin, plays a more direct role than Rad26 in transcription coupled DNA repair. Nucleic Acids Res. 44 6794-802 PubMed GONUTS page
↑ ^4.0 ^4.1 Martin-Tumasz, S & Brow, DA (2015) Saccharomyces cerevisiae Sen1 Helicase Domain Exhibits 5'- to 3'-Helicase Activity with a Preference for Translocation on DNA Rather than RNA. J. Biol. Chem. 290 22880-9 PubMed GONUTS page
↑ Golla, U et al. (2013) Sen1p contributes to genomic integrity by regulating expression of ribonucleotide reductase 1 (RNR1) in Saccharomyces cerevisiae. PLoS ONE 8 e64798 PubMed GONUTS page
↑ ^6.0 ^6.1 Alzu, A et al. (2012) Senataxin associates with replication forks to protect fork integrity across RNA-polymerase-II-transcribed genes. Cell 151 835-46 PubMed GONUTS page
↑ Vasiljeva, L & Buratowski, S (2006) Nrd1 interacts with the nuclear exosome for 3' processing of RNA polymerase II transcripts. Mol. Cell 21 239-48 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Kim, HD et al. (1999) The sen1(+) gene of Schizosaccharomyces pombe, a homologue of budding yeast SEN1, encodes an RNA and DNA helicase. Biochemistry 38 14697-710 PubMed GONUTS page
↑ ^9.0 ^9.1 Steinmetz, EJ et al. (2001) RNA-binding protein Nrd1 directs poly(A)-independent 3'-end formation of RNA polymerase II transcripts. Nature 413 327-31 PubMed GONUTS page
↑ ^10.0 ^10.1 Chinchilla, K et al. (2012) Interactions of Sen1, Nrd1, and Nab3 with multiple phosphorylated forms of the Rpb1 C-terminal domain in Saccharomyces cerevisiae. Eukaryotic Cell 11 417-29 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Ursic, D et al. (1997) The yeast SEN1 gene is required for the processing of diverse RNA classes. Nucleic Acids Res. 25 4778-85 PubMed GONUTS page
↑ Beggs, S et al. (2012) The PolyA tail length of yeast histone mRNAs varies during the cell cycle and is influenced by Sen1p and Rrp6p. Nucleic Acids Res. 40 2700-11 PubMed GONUTS page
↑ Steinmetz, EJ et al. (2006) Genome-wide distribution of yeast RNA polymerase II and its control by Sen1 helicase. Mol. Cell 24 735-46 PubMed GONUTS page
↑ Porrua, O & Libri, D (2013) A bacterial-like mechanism for transcription termination by the Sen1p helicase in budding yeast. Nat. Struct. Mol. Biol. 20 884-91 PubMed GONUTS page
↑ Ursic, D et al. (1995) Inactivation of the yeast Sen1 protein affects the localization of nucleolar proteins. Mol. Gen. Genet. 249 571-84 PubMed GONUTS page
↑ Sariki, SK et al. (2016) Sen1, the homolog of human Senataxin, is critical for cell survival through regulation of redox homeostasis, mitochondrial function, and the TOR pathway in Saccharomyces cerevisiae. FEBS J. 283 4056-4083 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 ^17.4 ^17.5 ^17.6 ^17.7 ^17.8 ^17.9 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:26364722-1] Singh, V et al. (2015) Flocculation in Saccharomyces cerevisiae is regulated by RNA/DNA helicase Sen1p. FEBS Lett. 589 3165-74 PubMed GONUTS page

[PMID:23222640-2] 2.0 ^2.1 ^2.2 Mitchell, SF et al. (2013) Global analysis of yeast mRNPs. Nat. Struct. Mol. Biol. 20 127-33 PubMed GONUTS page

[PMID:27179024-3] 3.0 ^3.1 ^3.2 Li, W et al. (2016) Sen1, the yeast homolog of human senataxin, plays a more direct role than Rad26 in transcription coupled DNA repair. Nucleic Acids Res. 44 6794-802 PubMed GONUTS page

[PMID:26198638-4] 4.0 ^4.1 Martin-Tumasz, S & Brow, DA (2015) Saccharomyces cerevisiae Sen1 Helicase Domain Exhibits 5'- to 3'-Helicase Activity with a Preference for Translocation on DNA Rather than RNA. J. Biol. Chem. 290 22880-9 PubMed GONUTS page

[PMID:23741394-5] Golla, U et al. (2013) Sen1p contributes to genomic integrity by regulating expression of ribonucleotide reductase 1 (RNR1) in Saccharomyces cerevisiae. PLoS ONE 8 e64798 PubMed GONUTS page

[PMID:23141540-6] 6.0 ^6.1 Alzu, A et al. (2012) Senataxin associates with replication forks to protect fork integrity across RNA-polymerase-II-transcribed genes. Cell 151 835-46 PubMed GONUTS page

[PMID:16427013-7] Vasiljeva, L & Buratowski, S (2006) Nrd1 interacts with the nuclear exosome for 3' processing of RNA polymerase II transcripts. Mol. Cell 21 239-48 PubMed GONUTS page

[PMID:10545196-8] 8.0 ^8.1 ^8.2 Kim, HD et al. (1999) The sen1(+) gene of Schizosaccharomyces pombe, a homologue of budding yeast SEN1, encodes an RNA and DNA helicase. Biochemistry 38 14697-710 PubMed GONUTS page

[PMID:11565036-9] 9.0 ^9.1 Steinmetz, EJ et al. (2001) RNA-binding protein Nrd1 directs poly(A)-independent 3'-end formation of RNA polymerase II transcripts. Nature 413 327-31 PubMed GONUTS page

[PMID:22286094-10] 10.0 ^10.1 Chinchilla, K et al. (2012) Interactions of Sen1, Nrd1, and Nab3 with multiple phosphorylated forms of the Rpb1 C-terminal domain in Saccharomyces cerevisiae. Eukaryotic Cell 11 417-29 PubMed GONUTS page

[PMID:9365256-11] 11.0 ^11.1 ^11.2 Ursic, D et al. (1997) The yeast SEN1 gene is required for the processing of diverse RNA classes. Nucleic Acids Res. 25 4778-85 PubMed GONUTS page

[PMID:22123738-12] Beggs, S et al. (2012) The PolyA tail length of yeast histone mRNAs varies during the cell cycle and is influenced by Sen1p and Rrp6p. Nucleic Acids Res. 40 2700-11 PubMed GONUTS page

[PMID:17157256-13] Steinmetz, EJ et al. (2006) Genome-wide distribution of yeast RNA polymerase II and its control by Sen1 helicase. Mol. Cell 24 735-46 PubMed GONUTS page

[PMID:23748379-14] Porrua, O & Libri, D (2013) A bacterial-like mechanism for transcription termination by the Sen1p helicase in budding yeast. Nat. Struct. Mol. Biol. 20 884-91 PubMed GONUTS page

[PMID:8544822-15] Ursic, D et al. (1995) Inactivation of the yeast Sen1 protein affects the localization of nucleolar proteins. Mol. Gen. Genet. 249 571-84 PubMed GONUTS page

[PMID:27718307-16] Sariki, SK et al. (2016) Sen1, the homolog of human Senataxin, is critical for cell survival through regulation of redox homeostasis, mitochondrial function, and the TOR pathway in Saccharomyces cerevisiae. FEBS J. 283 4056-4083 PubMed GONUTS page

[PMID:21873635-17] 17.0 ^17.1 ^17.2 ^17.3 ^17.4 ^17.5 ^17.6 ^17.7 ^17.8 ^17.9 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:SEN1

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