YEAST:RPB1

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	RPO21 (synonyms: RPB1, RPB220, SUA8)
Protein Name(s)	DNA-directed RNA polymerase II subunit RPB1 RNA polymerase II subunit 1 RNA polymerase II subunit B1 DNA-directed RNA polymerase III largest subunit RNA polymerase II subunit B220
External Links
UniProt	P04050
EMBL	X03128 X96876 Z74188 U27182 BK006938
PIR	S67686
RefSeq	NP_010141.1
PDB	1I3Q 1I50 1I6H 1K83 1NIK 1NT9 1PQV 1R5U 1R9S 1R9T 1SFO 1TWA 1TWC 1TWF 1TWG 1TWH 1WCM 1Y1V 1Y1W 1Y1Y 1Y77 2B63 2B8K 2E2H 2E2I 2E2J 2JA5 2JA6 2JA7 2JA8 2L0I 2LO6 2NVQ 2NVT 2NVX 2NVY 2NVZ 2R7Z 2R92 2R93 2VUM 2YU9 3CQZ 3FKI 3GTG 3GTJ 3GTK 3GTL 3GTM 3GTO 3GTP 3GTQ 3H3V 3HOU 3HOV 3HOW 3HOX 3HOY 3HOZ 3I4M 3I4N 3J0K 3J1N 3K1F 3K7A 3M3Y 3M4O 3PO2 3PO3 3QT1 3RZD 3RZO 3S14 3S15 3S16 3S17 3S1M 3S1N 3S1Q 3S1R 3S2D 3S2H 4A3B 4A3C 4A3D 4A3E 4A3F 4A3G 4A3I 4A3J 4A3K 4A3L 4A3M 4A93 4BBR 4BBS 4BXX 4BXZ 4BY1 4BY7 4GWQ
PDBsum	1I3Q 1I50 1I6H 1K83 1NIK 1NT9 1PQV 1R5U 1R9S 1R9T 1SFO 1TWA 1TWC 1TWF 1TWG 1TWH 1WCM 1Y1V 1Y1W 1Y1Y 1Y77 2B63 2B8K 2E2H 2E2I 2E2J 2JA5 2JA6 2JA7 2JA8 2L0I 2LO6 2NVQ 2NVT 2NVX 2NVY 2NVZ 2R7Z 2R92 2R93 2VUM 2YU9 3CQZ 3FKI 3GTG 3GTJ 3GTK 3GTL 3GTM 3GTO 3GTP 3GTQ 3H3V 3HOU 3HOV 3HOW 3HOX 3HOY 3HOZ 3I4M 3I4N 3J0K 3J1N 3K1F 3K7A 3M3Y 3M4O 3PO2 3PO3 3QT1 3RZD 3RZO 3S14 3S15 3S16 3S17 3S1M 3S1N 3S1Q 3S1R 3S2D 3S2H 4A3B 4A3C 4A3D 4A3E 4A3F 4A3G 4A3I 4A3J 4A3K 4A3L 4A3M 4A93 4BBR 4BBS 4BXX 4BXZ 4BY1 4BY7 4GWQ
ProteinModelPortal	P04050
BioGrid	31921
DIP	DIP-611N
IntAct	P04050
MINT	MINT-432838
MaxQB	P04050
PaxDb	P04050
PeptideAtlas	P04050
EnsemblFungi	[example_ID YDL140C]
GeneID	851415
KEGG	sce:YDL140C
CYGD	YDL140c
SGD	S000002299
eggNOG	COG0086
GeneTree	ENSGT00770000120757
HOGENOM	HOG000222975
InParanoid	P04050
KO	K03006
OMA	ENTMLEN
OrthoDB	EOG780RVQ
BioCyc	YEAST:G3O-29539-MONOMER
Reactome	REACT_191540 REACT_229646 REACT_232590 REACT_235070 REACT_236803 REACT_240372 REACT_247354 REACT_249293 REACT_249645 REACT_250507 REACT_252915 REACT_257112 REACT_261636
EvolutionaryTrace	P04050
NextBio	968606
PRO	PR:P04050
Proteomes	UP000002311
Genevestigator	P04050
GO	GO:0005665 GO:0003677 GO:0003899 GO:0046872 GO:0006366 GO:0001172 GO:0019985
InterPro	IPR000722 IPR000684 IPR006592 IPR007080 IPR007066 IPR007083 IPR007081 IPR007075 IPR007073
Pfam	PF04997 PF00623 PF04983 PF05000 PF04998 PF04992 PF04990 PF05001
SMART	SM00663
PROSITE	PS00115

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
part_of	GO:0005739	mitochondrion	PMID:16823961^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:22842922^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:14576278^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0010494	cytoplasmic stress granule	PMID:26777405^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:26945063^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:23438601^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0019985	translesion synthesis	PMID:22405652^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006366	transcription by RNA polymerase II	PMID:3299050^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005665	RNA polymerase II, core complex	PMID:2186966^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005665	RNA polymerase II, core complex	PMID:2183013^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005665	RNA polymerase II, core complex	PMID:1331084^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
contributes_to	GO:0003968	RNA-directed 5'-3' RNA polymerase activity	PMID:18004386^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
contributes_to	GO:0001055	RNA polymerase II activity	PMID:8288647^[13]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005665	RNA polymerase II, core complex	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003277 PANTHER:PTN000453465 PomBase:SPBC28F2.12 SGD:S000002299 TAIR:locus:2125319 UniProtKB:P24928	C	Seeded From UniProt	complete
contributes_to	GO:0003899	DNA-directed 5'-3' RNA polymerase activity	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003277 PANTHER:PTN000453461 RGD:620824	F	Seeded From UniProt	complete
contributes_to	GO:0001055	RNA polymerase II activity	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000453465 SGD:S000002299 WB:WBGene00000123	F	Seeded From UniProt	complete
	GO:0035067	negative regulation of histone acetylation	PMID:23401858^[15]	ECO:0000315			P	Figure 7 shows ctk1 mutants had increased histone acetylation.	complete CACAO 7233
involved_in	GO:0001172	transcription, RNA-templated	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003968	P	Seeded From UniProt	complete
	GO:0005634	nucleus	PMID:23438601^[6]	ECO:0000314			C	Figure 4A illustrates the intracellular localization of the RNA polymerase ll subunit 1 mainly in the nucleus in the wild-type strain, while the mutants were found in the cytoplasm.	complete CACAO 7489
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000684 InterPro:IPR000722 InterPro:IPR006592 InterPro:IPR007066 InterPro:IPR007073 InterPro:IPR007075 InterPro:IPR007080 InterPro:IPR007081 InterPro:IPR007083	F	Seeded From UniProt	complete
enables	GO:0003899	DNA-directed 5'-3' RNA polymerase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000722 InterPro:IPR006592 InterPro:IPR007066 InterPro:IPR007073 InterPro:IPR007075 InterPro:IPR007080 InterPro:IPR007081 InterPro:IPR007083	F	Seeded From UniProt	complete
part_of	GO:0005665	RNA polymerase II, core complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000684	C	Seeded From UniProt	complete
involved_in	GO:0006351	transcription, DNA-templated	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000722 InterPro:IPR006592 InterPro:IPR007066 InterPro:IPR007073 InterPro:IPR007075 InterPro:IPR007080 InterPro:IPR007081 InterPro:IPR007083	P	Seeded From UniProt	complete
involved_in	GO:0006366	transcription by RNA polymerase II	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000684	P	Seeded From UniProt	complete
enables	GO:0003899	DNA-directed 5'-3' RNA polymerase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.7.6	F	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
enables	GO:0016779	nucleotidyltransferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0548	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
enables	GO:0003899	DNA-directed 5'-3' RNA polymerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0240	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:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
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Notes

References

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

↑ 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
↑ Jain, S et al. (2016) ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure. Cell 164 487-98 PubMed GONUTS page
↑ Crickard, JB et al. (2016) Biochemical Analysis of Yeast Suppressor of Ty 4/5 (Spt4/5) Reveals the Importance of Nucleic Acid Interactions in the Prevention of RNA Polymerase II Arrest. J. Biol. Chem. 291 9853-70 PubMed GONUTS page
↑ ^6.0 ^6.1 Gómez-Navarro, N et al. (2013) Rtp1p is a karyopherin-like protein required for RNA polymerase II biogenesis. Mol. Cell. Biol. 33 1756-67 PubMed GONUTS page
↑ Walmacq, C et al. (2012) Mechanism of translesion transcription by RNA polymerase II and its role in cellular resistance to DNA damage. Mol. Cell 46 18-29 PubMed GONUTS page
↑ Nonet, M et al. (1987) Eucaryotic RNA polymerase conditional mutant that rapidly ceases mRNA synthesis. Mol. Cell. Biol. 7 1602-11 PubMed GONUTS page
↑ Woychik, NA et al. (1990) Subunits shared by eukaryotic nuclear RNA polymerases. Genes Dev. 4 313-23 PubMed GONUTS page
↑ Kolodziej, PA et al. (1990) RNA polymerase II subunit composition, stoichiometry, and phosphorylation. Mol. Cell. Biol. 10 1915-20 PubMed GONUTS page
↑ Sayre, MH et al. (1992) Reconstitution of transcription with five purified initiation factors and RNA polymerase II from Saccharomyces cerevisiae. J. Biol. Chem. 267 23376-82 PubMed GONUTS page
↑ Lehmann, E et al. (2007) Molecular basis of RNA-dependent RNA polymerase II activity. Nature 450 445-9 PubMed GONUTS page
↑ Christie, KR et al. (1994) Purified yeast RNA polymerase II reads through intrinsic blocks to elongation in response to the yeast TFIIS analogue, P37. J. Biol. Chem. 269 936-43 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Xue, YM et al. (2013) Histone chaperones Nap1 and Vps75 regulate histone acetylation during transcription elongation. Mol. Cell. Biol. 33 1645-56 PubMed GONUTS page

[PMID:16823961-1] 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:22842922-2] 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:14576278-3] 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:26777405-4] Jain, S et al. (2016) ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure. Cell 164 487-98 PubMed GONUTS page

[PMID:26945063-5] Crickard, JB et al. (2016) Biochemical Analysis of Yeast Suppressor of Ty 4/5 (Spt4/5) Reveals the Importance of Nucleic Acid Interactions in the Prevention of RNA Polymerase II Arrest. J. Biol. Chem. 291 9853-70 PubMed GONUTS page

[PMID:23438601-6] 6.0 ^6.1 Gómez-Navarro, N et al. (2013) Rtp1p is a karyopherin-like protein required for RNA polymerase II biogenesis. Mol. Cell. Biol. 33 1756-67 PubMed GONUTS page

[PMID:22405652-7] Walmacq, C et al. (2012) Mechanism of translesion transcription by RNA polymerase II and its role in cellular resistance to DNA damage. Mol. Cell 46 18-29 PubMed GONUTS page

[PMID:3299050-8] Nonet, M et al. (1987) Eucaryotic RNA polymerase conditional mutant that rapidly ceases mRNA synthesis. Mol. Cell. Biol. 7 1602-11 PubMed GONUTS page

[PMID:2186966-9] Woychik, NA et al. (1990) Subunits shared by eukaryotic nuclear RNA polymerases. Genes Dev. 4 313-23 PubMed GONUTS page

[PMID:2183013-10] Kolodziej, PA et al. (1990) RNA polymerase II subunit composition, stoichiometry, and phosphorylation. Mol. Cell. Biol. 10 1915-20 PubMed GONUTS page

[PMID:1331084-11] Sayre, MH et al. (1992) Reconstitution of transcription with five purified initiation factors and RNA polymerase II from Saccharomyces cerevisiae. J. Biol. Chem. 267 23376-82 PubMed GONUTS page

[PMID:18004386-12] Lehmann, E et al. (2007) Molecular basis of RNA-dependent RNA polymerase II activity. Nature 450 445-9 PubMed GONUTS page

[PMID:8288647-13] Christie, KR et al. (1994) Purified yeast RNA polymerase II reads through intrinsic blocks to elongation in response to the yeast TFIIS analogue, P37. J. Biol. Chem. 269 936-43 PubMed GONUTS page

[PMID:21873635-14] 14.0 ^14.1 ^14.2 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:23401858-15] Xue, YM et al. (2013) Histone chaperones Nap1 and Vps75 regulate histone acetylation during transcription elongation. Mol. Cell. Biol. 33 1645-56 PubMed GONUTS page

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YEAST:RPB1

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