YEAST:PAF1

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	PAF1
Protein Name(s)	RNA polymerase II-associated protein 1 Protein PAF1
External Links
UniProt	P38351
EMBL	X76053 Z36148 BK006936
PIR	S44541
RefSeq	NP_009838.1
ProteinModelPortal	P38351
BioGrid	32973
DIP	DIP-1149N
IntAct	P38351
MINT	MINT-600620
MaxQB	P38351
PaxDb	P38351
PeptideAtlas	P38351
PRIDE	P38351
EnsemblFungi	[example_ID YBR279W]
GeneID	852582
KEGG	sce:YBR279W
EuPathDB	FungiDB:YBR279W
SGD	S000000483
eggNOG	NOG276051
HOGENOM	HOG000000738
InParanoid	P38351
KO	K15174
OMA	DEWISMY
OrthoDB	EOG7F2534
BioCyc	YEAST:G3O-29199-MONOMER
NextBio	971727
PRO	PR:P38351
Proteomes	UP000002311
GO	GO:0016593 GO:0005634 GO:0035327 GO:0003682 GO:1990269 GO:0000993 GO:0000983 GO:0001076 GO:0001089 GO:0000183 GO:0006353 GO:0070911 GO:0016570 GO:0031124 GO:0045910 GO:0000122 GO:2001255 GO:2001165 GO:2001209 GO:0032968 GO:0031938 GO:2001173 GO:2001166 GO:0051569 GO:2001163 GO:0006357 GO:0000083 GO:0090262 GO:0006364 GO:0031126 GO:0001015 GO:0006362 GO:0006368 GO:0006360
InterPro	IPR007133
PANTHER	PTHR23188
Pfam	PF03985

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0000122	negative regulation of transcription from RNA polymerase II promoter	PMID:22252319^[1]	ECO:0000315			P		Figure 1 shows greater ARG1 expression caused Paf1 deletion. This is due to Paf1 mediated negative regulation of RNA polymerase II.	complete CACAO 11166
involved_in	GO:2001255	positive regulation of histone H3-K36 trimethylation	PMID:17948059^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2001209	positive regulation of transcription elongation from RNA polymerase I promoter	PMID:20299458^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2001173	regulation of histone H2B conserved C-terminal lysine ubiquitination	PMID:19531475^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2001166	regulation of histone H2B ubiquitination	PMID:12876294^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2001165	positive regulation of phosphorylation of RNA polymerase II C-terminal domain serine 2 residues	PMID:18469135^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2001163	regulation of phosphorylation of RNA polymerase II C-terminal domain serine 2 residues	PMID:15149594^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:1990269	RNA polymerase II C-terminal domain phosphoserine binding	PMID:22796944^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0090262	regulation of transcription-coupled nucleotide-excision repair	PMID:21737840^[9]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000000318	P		Seeded From UniProt	complete
involved_in	GO:0070911	global genome nucleotide-excision repair	PMID:21737840^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051569	regulation of histone H3-K4 methylation	PMID:12876294^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051569	regulation of histone H3-K4 methylation	PMID:12667454^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051569	regulation of histone H3-K4 methylation	PMID:15180994^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045910	negative regulation of DNA recombination	PMID:9891041^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0035327	transcriptionally active chromatin	PMID:11983171^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0032968	positive regulation of transcription elongation from RNA polymerase II promoter	PMID:14710186^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031938	regulation of chromatin silencing at telomere	PMID:12667454^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031938	regulation of chromatin silencing at telomere	PMID:18194564^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031126	snoRNA 3'-end processing	PMID:16246725^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031124	mRNA 3'-end processing	PMID:15149594^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016593	Cdc73/Paf1 complex	PMID:11884586^[17]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000004410 SGD:S000005505	C		Seeded From UniProt	complete
part_of	GO:0016593	Cdc73/Paf1 complex	PMID:11927560^[18]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000003213	C		Seeded From UniProt	complete
part_of	GO:0016593	Cdc73/Paf1 complex	PMID:9032243^[19]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000004410	C		Seeded From UniProt	complete
involved_in	GO:0006368	transcription elongation from RNA polymerase II promoter	PMID:11927560^[18]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000003011 SGD:S000003175 SGD:S000003295 SGD:S000004470	P		Seeded From UniProt	complete
involved_in	GO:0006368	transcription elongation from RNA polymerase II promoter	PMID:11927560^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006364	rRNA processing	PMID:20299458^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006362	transcription elongation from RNA polymerase I promoter	PMID:19164765^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006360	transcription by RNA polymerase I	PMID:20299458^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000005192	P		Seeded From UniProt	complete
involved_in	GO:0006360	transcription by RNA polymerase I	PMID:20299458^[3]	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:11884586^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006353	DNA-templated transcription, termination	PMID:23109428^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0009302)	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:15149594^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:15643076^[22]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	PMID:11983171^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0001015	snoRNA transcription by RNA polymerase II	PMID:16246725^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0001015	snoRNA transcription by RNA polymerase II	PMID:16246725^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0000993	RNA polymerase II complex binding	PMID:16581788^[23]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000002299	F		Seeded From UniProt	complete
involved_in	GO:0000183	chromatin silencing at rDNA	PMID:16582434^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:15180994^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000083	regulation of transcription involved in G1/S transition of mitotic cell cycle	PMID:10219085^[25]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0035327	transcriptionally active chromatin	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0010750 PANTHER:PTN000573292 SGD:S000000483	C		Seeded From UniProt	complete
part_of	GO:0016593	Cdc73/Paf1 complex	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0010750 PANTHER:PTN000573292 PomBase:SPAC664.03 SGD:S000000483 UniProtKB:Q8N7H5	C		Seeded From UniProt	complete
enables	GO:0003682	chromatin binding	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1923988 PANTHER:PTN000573292 SGD:S000000483	F		Seeded From UniProt	complete
enables	GO:0000993	RNA polymerase II complex binding	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000573292 SGD:S000000483 UniProtKB:Q8N7H5	F		Seeded From UniProt	complete
involved_in	GO:0006368	transcription elongation from RNA polymerase II promoter	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR007133	P		Seeded From UniProt	complete
involved_in	GO:0016570	histone modification	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR007133	P		Seeded From UniProt	complete
part_of	GO:0016593	Cdc73/Paf1 complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR007133	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539	C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0190	C		Seeded From UniProt	complete
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Notes

References

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

↑ Crisucci, EM & Arndt, KM (2012) Paf1 restricts Gcn4 occupancy and antisense transcription at the ARG1 promoter. Mol. Cell. Biol. 32 1150-63 PubMed GONUTS page
↑ Chu, Y et al. (2007) Regulation of histone modification and cryptic transcription by the Bur1 and Paf1 complexes. EMBO J. 26 4646-56 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Zhang, Y et al. (2010) The RNA polymerase-associated factor 1 complex (Paf1C) directly increases the elongation rate of RNA polymerase I and is required for efficient regulation of rRNA synthesis. J. Biol. Chem. 285 14152-9 PubMed GONUTS page
↑ Kim, J & Roeder, RG (2009) Direct Bre1-Paf1 complex interactions and RING finger-independent Bre1-Rad6 interactions mediate histone H2B ubiquitylation in yeast. J. Biol. Chem. 284 20582-92 PubMed GONUTS page
↑ ^5.0 ^5.1 Wood, A et al. (2003) The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J. Biol. Chem. 278 34739-42 PubMed GONUTS page
↑ Nordick, K et al. (2008) Direct interactions between the Paf1 complex and a cleavage and polyadenylation factor are revealed by dissociation of Paf1 from RNA polymerase II. Eukaryotic Cell 7 1158-67 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Mueller, CL et al. (2004) The Paf1 complex has functions independent of actively transcribing RNA polymerase II. Mol. Cell 14 447-56 PubMed GONUTS page
↑ Qiu, H et al. (2012) Pol II CTD kinases Bur1 and Kin28 promote Spt5 CTR-independent recruitment of Paf1 complex. EMBO J. 31 3494-505 PubMed GONUTS page
↑ ^9.0 ^9.1 Tatum, D et al. (2011) Diverse roles of RNA polymerase II-associated factor 1 complex in different subpathways of nucleotide excision repair. J. Biol. Chem. 286 30304-13 PubMed GONUTS page
↑ ^10.0 ^10.1 Krogan, NJ et al. (2003) The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Mol. Cell 11 721-9 PubMed GONUTS page
↑ ^11.0 ^11.1 Carvin, CD & Kladde, MP (2004) Effectors of lysine 4 methylation of histone H3 in Saccharomyces cerevisiae are negative regulators of PHO5 and GAL1-10. J. Biol. Chem. 279 33057-62 PubMed GONUTS page
↑ Chang, M et al. (1999) A complex containing RNA polymerase II, Paf1p, Cdc73p, Hpr1p, and Ccr4p plays a role in protein kinase C signaling. Mol. Cell. Biol. 19 1056-67 PubMed GONUTS page
↑ ^13.0 ^13.1 Pokholok, DK et al. (2002) Exchange of RNA polymerase II initiation and elongation factors during gene expression in vivo. Mol. Cell 9 799-809 PubMed GONUTS page
↑ Rondón, AG et al. (2004) Molecular evidence indicating that the yeast PAF complex is required for transcription elongation. EMBO Rep. 5 47-53 PubMed GONUTS page
↑ Marton, HA & Desiderio, S (2008) The Paf1 complex promotes displacement of histones upon rapid induction of transcription by RNA polymerase II. BMC Mol. Biol. 9 4 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Sheldon, KE et al. (2005) A Requirement for the Saccharomyces cerevisiae Paf1 complex in snoRNA 3' end formation. Mol. Cell 20 225-36 PubMed GONUTS page
↑ ^17.0 ^17.1 Mueller, CL & Jaehning, JA (2002) Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex. Mol. Cell. Biol. 22 1971-80 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 Squazzo, SL et al. (2002) The Paf1 complex physically and functionally associates with transcription elongation factors in vivo. EMBO J. 21 1764-74 PubMed GONUTS page
↑ Shi, X et al. (1997) Cdc73p and Paf1p are found in a novel RNA polymerase II-containing complex distinct from the Srbp-containing holoenzyme. Mol. Cell. Biol. 17 1160-9 PubMed GONUTS page
↑ Zhang, Y et al. (2009) The Paf1 complex is required for efficient transcription elongation by RNA polymerase I. Proc. Natl. Acad. Sci. U.S.A. 106 2153-8 PubMed GONUTS page
↑ Tomson, BN et al. (2013) Effects of the Paf1 complex and histone modifications on snoRNA 3'-end formation reveal broad and locus-specific regulation. Mol. Cell. Biol. 33 170-82 PubMed GONUTS page
↑ Porter, SE et al. (2005) Separation of the Saccharomyces cerevisiae Paf1 complex from RNA polymerase II results in changes in its subnuclear localization. Eukaryotic Cell 4 209-20 PubMed GONUTS page
↑ Qiu, H et al. (2006) The Spt4p subunit of yeast DSIF stimulates association of the Paf1 complex with elongating RNA polymerase II. Mol. Cell. Biol. 26 3135-48 PubMed GONUTS page
↑ Mueller, JE et al. (2006) The requirements for COMPASS and Paf1 in transcriptional silencing and methylation of histone H3 in Saccharomyces cerevisiae. Genetics 173 557-67 PubMed GONUTS page
↑ Koch, C et al. (1999) A role for Ctr9p and Paf1p in the regulation G1 cyclin expression in yeast. Nucleic Acids Res. 27 2126-34 PubMed GONUTS page
↑ ^26.0 ^26.1 ^26.2 ^26.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:22252319-1] Crisucci, EM & Arndt, KM (2012) Paf1 restricts Gcn4 occupancy and antisense transcription at the ARG1 promoter. Mol. Cell. Biol. 32 1150-63 PubMed GONUTS page

[PMID:17948059-2] Chu, Y et al. (2007) Regulation of histone modification and cryptic transcription by the Bur1 and Paf1 complexes. EMBO J. 26 4646-56 PubMed GONUTS page

[PMID:20299458-3] 3.0 ^3.1 ^3.2 ^3.3 Zhang, Y et al. (2010) The RNA polymerase-associated factor 1 complex (Paf1C) directly increases the elongation rate of RNA polymerase I and is required for efficient regulation of rRNA synthesis. J. Biol. Chem. 285 14152-9 PubMed GONUTS page

[PMID:19531475-4] Kim, J & Roeder, RG (2009) Direct Bre1-Paf1 complex interactions and RING finger-independent Bre1-Rad6 interactions mediate histone H2B ubiquitylation in yeast. J. Biol. Chem. 284 20582-92 PubMed GONUTS page

[PMID:12876294-5] 5.0 ^5.1 Wood, A et al. (2003) The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J. Biol. Chem. 278 34739-42 PubMed GONUTS page

[PMID:18469135-6] Nordick, K et al. (2008) Direct interactions between the Paf1 complex and a cleavage and polyadenylation factor are revealed by dissociation of Paf1 from RNA polymerase II. Eukaryotic Cell 7 1158-67 PubMed GONUTS page

[PMID:15149594-7] 7.0 ^7.1 ^7.2 Mueller, CL et al. (2004) The Paf1 complex has functions independent of actively transcribing RNA polymerase II. Mol. Cell 14 447-56 PubMed GONUTS page

[PMID:22796944-8] Qiu, H et al. (2012) Pol II CTD kinases Bur1 and Kin28 promote Spt5 CTR-independent recruitment of Paf1 complex. EMBO J. 31 3494-505 PubMed GONUTS page

[PMID:21737840-9] 9.0 ^9.1 Tatum, D et al. (2011) Diverse roles of RNA polymerase II-associated factor 1 complex in different subpathways of nucleotide excision repair. J. Biol. Chem. 286 30304-13 PubMed GONUTS page

[PMID:12667454-10] 10.0 ^10.1 Krogan, NJ et al. (2003) The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Mol. Cell 11 721-9 PubMed GONUTS page

[PMID:15180994-11] 11.0 ^11.1 Carvin, CD & Kladde, MP (2004) Effectors of lysine 4 methylation of histone H3 in Saccharomyces cerevisiae are negative regulators of PHO5 and GAL1-10. J. Biol. Chem. 279 33057-62 PubMed GONUTS page

[PMID:9891041-12] Chang, M et al. (1999) A complex containing RNA polymerase II, Paf1p, Cdc73p, Hpr1p, and Ccr4p plays a role in protein kinase C signaling. Mol. Cell. Biol. 19 1056-67 PubMed GONUTS page

[PMID:11983171-13] 13.0 ^13.1 Pokholok, DK et al. (2002) Exchange of RNA polymerase II initiation and elongation factors during gene expression in vivo. Mol. Cell 9 799-809 PubMed GONUTS page

[PMID:14710186-14] Rondón, AG et al. (2004) Molecular evidence indicating that the yeast PAF complex is required for transcription elongation. EMBO Rep. 5 47-53 PubMed GONUTS page

[PMID:18194564-15] Marton, HA & Desiderio, S (2008) The Paf1 complex promotes displacement of histones upon rapid induction of transcription by RNA polymerase II. BMC Mol. Biol. 9 4 PubMed GONUTS page

[PMID:16246725-16] 16.0 ^16.1 ^16.2 Sheldon, KE et al. (2005) A Requirement for the Saccharomyces cerevisiae Paf1 complex in snoRNA 3' end formation. Mol. Cell 20 225-36 PubMed GONUTS page

[PMID:11884586-17] 17.0 ^17.1 Mueller, CL & Jaehning, JA (2002) Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex. Mol. Cell. Biol. 22 1971-80 PubMed GONUTS page

[PMID:11927560-18] 18.0 ^18.1 ^18.2 Squazzo, SL et al. (2002) The Paf1 complex physically and functionally associates with transcription elongation factors in vivo. EMBO J. 21 1764-74 PubMed GONUTS page

[PMID:9032243-19] Shi, X et al. (1997) Cdc73p and Paf1p are found in a novel RNA polymerase II-containing complex distinct from the Srbp-containing holoenzyme. Mol. Cell. Biol. 17 1160-9 PubMed GONUTS page

[PMID:19164765-20] Zhang, Y et al. (2009) The Paf1 complex is required for efficient transcription elongation by RNA polymerase I. Proc. Natl. Acad. Sci. U.S.A. 106 2153-8 PubMed GONUTS page

[PMID:23109428-21] Tomson, BN et al. (2013) Effects of the Paf1 complex and histone modifications on snoRNA 3'-end formation reveal broad and locus-specific regulation. Mol. Cell. Biol. 33 170-82 PubMed GONUTS page

[PMID:15643076-22] Porter, SE et al. (2005) Separation of the Saccharomyces cerevisiae Paf1 complex from RNA polymerase II results in changes in its subnuclear localization. Eukaryotic Cell 4 209-20 PubMed GONUTS page

[PMID:16581788-23] Qiu, H et al. (2006) The Spt4p subunit of yeast DSIF stimulates association of the Paf1 complex with elongating RNA polymerase II. Mol. Cell. Biol. 26 3135-48 PubMed GONUTS page

[PMID:16582434-24] Mueller, JE et al. (2006) The requirements for COMPASS and Paf1 in transcriptional silencing and methylation of histone H3 in Saccharomyces cerevisiae. Genetics 173 557-67 PubMed GONUTS page

[PMID:10219085-25] Koch, C et al. (1999) A role for Ctr9p and Paf1p in the regulation G1 cyclin expression in yeast. Nucleic Acids Res. 27 2126-34 PubMed GONUTS page

[PMID:21873635-26] 26.0 ^26.1 ^26.2 ^26.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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YEAST:PAF1

Contents

Annotations

Notes

References

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