P53165 (SGF73_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SAGA-associated factor 73

Alternative name(s):
73 kDa SAGA-associated factor
SAGA histone acetyltransferase complex 73 kDa subunit

Gene names

Name:	SGF73
Ordered Locus Names:	YGL066W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	657 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions as component of the transcription regulatory histone acetylation (HAT) complex SAGA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs).
Subunit structure	Component of the 1.8 MDa SAGA complex, which consists of at least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12, TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2 copies. SAGA is built of 5 distinct domains with specialized functions. Domain I (containing TRA1) probably represents the activator interaction surface. Domain II (containing TAF5 and TAF6, and probably TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily an architectural role. Domain III also harbors the HAT activity. Domain V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-interacting module, which may be associated transiently with SAGA. Ref.5
Subcellular location	Nucleus Probable.
Miscellaneous	Present with 486 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the ataxin-7 family. Contains 1 SCA7 domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone acetylation Inferred from mutant phenotype PubMed 15932941. Source: SGD histone deubiquitination Inferred from mutant phenotype PubMed 19226466. Source: SGD mRNA export from nucleus Inferred from mutant phenotype PubMed 18488019. Source: SGD positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Inferred from mutant phenotype PubMed 17090597. Source: SGD protein complex assembly Inferred from mutant phenotype PubMed 19226466. Source: SGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	DUBm complex Inferred from direct assay PubMed 20395473. Source: SGD SAGA complex Inferred from direct assay Ref.5PubMed 17090597. Source: SGD SLIK (SAGA-like) complex Inferred from physical interaction PubMed 15932941. Source: SGD
Molecular_function	enzyme activator activity Inferred from direct assay PubMed 18488019. Source: SGD structural molecule activity Inferred from mutant phenotype PubMed 15932941. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 657

657

SAGA-associated factor 73

PRO_0000202764

Regions

Domain

220 – 286

67

SCA7

Compositional bias

141 – 150

10

Poly-Asp

Compositional bias

153 – 162

10

Poly-Asp

Compositional bias

466 – 476

11

Poly-Gln

Compositional bias

517 – 526

10

Poly-Gln

Amino acid modifications

Modified residue

22

1

Phosphoserine Ref.8

Modified residue

182

1

Phosphoserine Ref.7 Ref.8

Modified residue

184

1

Phosphoserine Ref.7 Ref.8

Modified residue

187

1

Phosphoserine Ref.8

Secondary structure

1

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657

Helix Strand Turn

Details...

Beta strand

7 – 11

5

Helix

13 – 18

6

Turn

19 – 22

4

Beta strand

28 – 30

3

Helix

32 – 35

4

Helix

36 – 41

6

Beta strand

47 – 49

3

Helix

51 – 57

7

Beta strand

70 – 72

3

Beta strand

76 – 78

3

Turn

79 – 81

3

Beta strand

84 – 86

3

Helix

87 – 89

3

Turn

90 – 92

3

Sequences

	Sequence		Length	Mass (Da)
	P53165 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 4618E2E47824321D	FASTA	657	72,878
	10 20 30 40 50 60 MRSGDAEIKG IKPKVIEEYS LSQGSGPSND SWKSLMSSAK DTPLQYDHMN RESLKKYFNP 70 80 90 100 110 120 NAQLIEDPLD KPIQYRVCEK CGKPLALTAI VDHLENHCAG ASGKSSTDPR DESTRETIRN 130 140 150 160 170 180 GVESTGRNNN DDDNSNDNNN DDDDDDDNDD NEDDDDADDD DDNSNGANYK KNDSSFNPLK 190 200 210 220 230 240 RSTSMESANT PNMDTKRSKT GTPQTFSSSI KKQKKVKQRN PTEKHLIDFN KQCGVELPEG 250 260 270 280 290 300 GYCARSLTCK SHSMGAKRAV SGRSKPYDVL LADYHREHQT KIGAAAEKRA KQQELQKLQK 310 320 330 340 350 360 QIQKEQKKHT QQQKQGQRSK QRNVNGGKSA KNGGKSTVHN GNNINEIGHV NLTPEEETTQ 370 380 390 400 410 420 VLNGVSRSFP LPLESTVLSS VRYRTKYFRM REMFASSFSV KPGYTSPGYG AIHSRVGCLD 430 440 450 460 470 480 LDRTTDYKFR VRTPQPINHL TNQNLNPKQI QRLQQQRALQ AQLLSQQQQQ QQQQQQHHSP 490 500 510 520 530 540 QAQAQASTQQ PTQGMVPNHF PGGATNSSFN ANVSSKQIQQ QQQQQQHKSQ DTGLTPLEIQ 550 560 570 580 590 600 SQQQKLRQQQ LQQQKFEAAA SYLANATKLM QESNQDSHLS GTHNNNSSKN GNNNLMTMKA 610 620 630 640 650 SISSPNTSVN SIQSPPSVNS VNGSGQGVST GINVSGNNGR IEVGIGNSVN PYNGRIN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII." Rieger M., Brueckner M., Schaefer M., Mueller-Auer S. Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes." Feuermann M., de Montigny J., Potier S., Souciet J.-L. Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 115-657. Strain: ATCC 204508 / S288c.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Proteomics of the eukaryotic transcription machinery: identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry." Sanders S.L., Jennings J., Canutescu A., Link A.J., Weil P.A. Mol. Cell. Biol. 22:4723-4738(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE SAGA COMPLEX.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-184, MASS SPECTROMETRY.
[8]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-182; SER-184 AND SER-187, MASS SPECTROMETRY.
[9]	"Molecular architecture of the S. cerevisiae SAGA complex." Wu P.Y., Ruhlmann C., Winston F., Schultz P. Mol. Cell 15:199-208(2004) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z72588 Genomic DNA. Translation: CAA96770.1.
Z72587 Genomic DNA. Translation: CAA96769.1.
BK006941 Genomic DNA. Translation: DAA08036.1.

PIR

S64073.

RefSeq

NP_011449.1. NM_001180931.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LO3	NMR	-	A	59-102	[»]
3M99	X-ray	2.70	D	1-104	[»]
3MHH	X-ray	2.45	E	1-96	[»]
3MHS	X-ray	1.89	E	1-96	[»]
4FIP	X-ray	2.69	D/H	1-96	[»]
4FJC	X-ray	2.83	D/H	1-96	[»]
4FK5	X-ray	2.03	E	1-96	[»]

ProteinModelPortal

P53165.

SMR

P53165. Positions 5-96.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5211N.

IntAct

P53165. 90 interactions.

MINT

MINT-548904.

STRING

4932.YGL066W.

Proteomic databases

PaxDb

P53165.

PeptideAtlas

P53165.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGL066W; YGL066W; YGL066W.

GeneID

852814.

KEGG

sce:YGL066W.

Organism-specific databases

CYGD

YGL066w.

SGD

S000003034. SGF73.

Phylogenomic databases

eggNOG

NOG285209.

HOGENOM

HOG000142039.

KO

K11365.

OMA

MREMFAS.

OrthoDB

EOG4HDX4B.

Gene expression databases

Genevestigator

P53165.

GermOnline

YGL066W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR013243. SCA7_dom.
[Graphical view]

Pfam

PF08313. SCA7. 1 hit.
[Graphical view]

PROSITE

PS51505. SCA7. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P53165.

NextBio

972348.

Entry information

Entry name

SGF73_YEAST

Accession

Primary (citable) accession number: P53165
Secondary accession number(s): D6VU75

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program