P22082 (SNF2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription regulatory protein SNF2
EC=3.6.4.-

Alternative name(s):
ATP-dependent helicase SNF2
Regulatory protein GAM1
Regulatory protein SWI2
SWI/SNF complex component SNF2
Transcription factor TYE3

Gene names

Name:	SNF2
Synonyms:	GAM1, RIC1, SWI2, TYE3
Ordered Locus Names:	YOR290C

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	1703 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in transcriptional activation. Catalytic component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subunit structure	Component of the SWI/SNF global transcription activator complex. The 1.14 MDa SWI/SNF complex is composed of 11 different subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73, ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82; and three copies of TAF14/SWP29.
Subcellular location	Nucleus.
Miscellaneous	Present with 217 molecules/cell in log phase SD medium.
Sequence similarities	Contains 3 A.T hook DNA-binding domains. Contains 1 bromo domain. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 HSA domain. Contains 1 QLQ domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Bromodomain Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Activator Helicase Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from direct assay PubMed 17188033PubMed 8127913PubMed 8458575. Source: GOC ATP-dependent chromatin remodeling Inferred from direct assay PubMed 8016655. Source: SGD DNA-dependent DNA replication Inferred from mutant phenotype PubMed 10198436. Source: SGD cellular alcohol catabolic process Inferred from mutant phenotype PubMed 1339306. Source: SGD chromatin remodeling Inferred from mutant phenotype PubMed 1459453. Source: SGD double-strand break repair Inferred from mutant phenotype PubMed 16024655. Source: SGD nucleosome mobilization Inferred from direct assay PubMed 17496903. Source: SGD positive regulation of mating type switching Inferred from mutant phenotype PubMed 6436497. Source: SGD positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 1339306PubMed 17681272PubMed 3542227PubMed 8016655. Source: SGD positive regulation of transcription from RNA polymerase II promoter in response to amino acid starvation Inferred from mutant phenotype PubMed 10549298. Source: SGD strand invasion Inferred from mutant phenotype PubMed 19766565. Source: SGD sucrose catabolic process Inferred from mutant phenotype PubMed 1339306PubMed 6392017. Source: SGD transcription, DNA-templated Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	SWI/SNF complex Inferred from direct assay PubMed 18644858PubMed 8016655PubMed 8127913PubMed 8159677. Source: SGD nucleus Inferred from direct assay Ref.1PubMed 22932476. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-dependent ATPase activity Inferred from direct assay PubMed 8127913PubMed 8458575. Source: SGD RNA polymerase II activating transcription factor binding Inferred from physical interaction PubMed 11865042. Source: SGD helicase activity Inferred from electronic annotation. Source: UniProtKB-KW histone acetyl-lysine binding Inferred from direct assay PubMed 20126658. Source: SGD nucleosomal DNA binding Inferred from direct assay PubMed 18644858. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HMT1	P38074	3	EBI-17526,EBI-8394
SNF11	P38956	3	EBI-17526,EBI-17560
SWI3	P32591	6	EBI-17526,EBI-18622

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1703

1703

Transcription regulatory protein SNF2

PRO_0000074358

Regions

Domain

247 – 282

36

QLQ

Domain

588 – 661

74

HSA

Domain

779 – 944

166

Helicase ATP-binding

Domain

1091 – 1254

164

Helicase C-terminal

Domain

1568 – 1638

71

Bromo

Nucleotide binding

792 – 799

8

ATP By similarity

DNA binding

1446 – 1456

11

A.T hook 1

DNA binding

1502 – 1513

12

A.T hook 2

DNA binding

1516 – 1526

11

A.T hook 3

Motif

894 – 897

4

DEGH box

Compositional bias

55 – 68

14

Gln-rich

Compositional bias

207 – 239

33

Ala/Gln-rich

Amino acid modifications

Modified residue

358

1

Phosphoserine Ref.10 Ref.11 Ref.12

Modified residue

383

1

Phosphothreonine Ref.12

Modified residue

716

1

Phosphoserine Ref.11 Ref.12

Modified residue

1340

1

Phosphoserine Ref.11

Secondary structure

1

.

.

.

1703

Helix Strand Turn

Details...

Helix

593 – 657

65

Sequences

	Sequence		Length	Mass (Da)
	P22082 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 84B8BC595C8F3E6D	FASTA	1,703	194,051
	10 20 30 40 50 60 MNIPQRQFSN EEVNRCYLRW QHLRNEHGMN APSVPEFIYL TKVLQFAAKQ RQELQMQRQQ 70 80 90 100 110 120 QGISGSQQNI VPNSSDQAEL PNNASSHISA SASPHLAPNM QLNGNETFST SAHQSPIMQT 130 140 150 160 170 180 QMPLNSNGGN NMLPQRQSSV GSLNATNFSP TPANNGENAA EKPDNSNHNN LNLNNSELQP 190 200 210 220 230 240 QNRSLQEHNI QDSNVMPGSQ INSPMPQQAQ MQQAQFQAQQ AQQAQQAQQA QQAQARLQQG 250 260 270 280 290 300 RRLPMTMFTA EQSELLKAQI TSLKCLVNRK PIPFEFQAVI QKSINHPPDF KRMLLSLSEF 310 320 330 340 350 360 ARRRQPTDQN NQSNLNGGNN TQQPGTNSHY NNTNTDNVSG LTRNAPLDSK DENFASVSPA 370 380 390 400 410 420 GPSSVHNAKN GTLDKNSQTV SGTPITQTES KKEENETISN VAKTAPNSNK THTEQNNPPK 430 440 450 460 470 480 PQKPVPLNVL QDQYKEGIKV VDIDDPDMMV DSFTMPNISH SNIDYQTLLA NSDHAKFTIE 490 500 510 520 530 540 PGVLPVGIDT HTATDIYQTL IALNLDTTVN DCLDKLLNDE CTESTRENAL YDYYALQLLP 550 560 570 580 590 600 LQKAVRGHVL QFEWHQNSLL TNTHPNFLSK IRNINVQDAL LTNQLYKNHE LLKLERKKTE 610 620 630 640 650 660 AVARLKSMNK SAINQYNRRQ DKKNKRLKFG HRLIATHTNL ERDEQKRAEK KAKERLQALK 670 680 690 700 710 720 ANDEEAYIKL LDQTKDTRIT HLLRQTNAFL DSLTRAVKDQ QKYTKEMIDS HIKEASEEVD 730 740 750 760 770 780 DLSMVPKMKD EEYDDDDDNS NVDYYNVAHR IKEDIKKQPS ILVGGTLKDY QIKGLQWMVS 790 800 810 820 830 840 LFNNHLNGIL ADEMGLGKTI QTISLLTYLY EMKNIRGPYL VIVPLSTLSN WSSEFAKWAP 850 860 870 880 890 900 TLRTISFKGS PNERKAKQAK IRAGEFDVVL TTFEYIIKER ALLSKVKWVH MIIDEGHRMK 910 920 930 940 950 960 NAQSKLSLTL NTHYHADYRL ILTGTPLQNN LPELWALLNF VLPKIFNSVK SFDEWFNTPF 970 980 990 1000 1010 1020 ANTGGQDKIE LSEEETLLVI RRLHKVLRPF LLRRLKKDVE KELPDKVEKV VKCKMSALQQ 1030 1040 1050 1060 1070 1080 IMYQQMLKYR RLFIGDQNNK KMVGLRGFNN QIMQLKKICN HPFVFEEVED QINPTRETND 1090 1100 1110 1120 1130 1140 DIWRVAGKFE LLDRILPKLK ATGHRVLIFF QMTQIMDIME DFLRYINIKY LRLDGHTKSD 1150 1160 1170 1180 1190 1200 ERSELLRLFN APDSEYLCFI LSTRAGGLGL NLQTADTVII FDTDWNPHQD LQAQDRAHRI 1210 1220 1230 1240 1250 1260 GQKNEVRILR LITTNSVEEV ILERAYKKLD IDGKVIQAGK FDNKSTSEEQ EALLRSLLDA 1270 1280 1290 1300 1310 1320 EEERRKKRES GVEEEEELKD SEINEILARN DEEMAVLTRM DEDRSKKEEE LGVKSRLLEK 1330 1340 1350 1360 1370 1380 SELPDIYSRD IGAELKREES ESAAVYNGRG ARERKTATYN DNMSEEQWLR QFEVSDDEKN 1390 1400 1410 1420 1430 1440 DKQARKQRTK KEDKSEAIDG NGEIKGENID ADNDGPRINN ISAEDRADTD LAMNDDDFLS 1450 1460 1470 1480 1490 1500 KKRKAGRPRG RPKKVKLEGS ENSEPPALES SPVTGDNSPS EDFMDIPKPR TAGKTSVKSA 1510 1520 1530 1540 1550 1560 RTSTRGRGRG RGRGRGRGRG RGRPPKARNG LDYVRTPAAA TSPIDIREKV AKQALDLYHF 1570 1580 1590 1600 1610 1620 ALNYENEAGR KLSDIFLSKP SKALYPDYYM IIKYPVAFDN INTHIETLAY NSLKETLQDF 1630 1640 1650 1660 1670 1680 HLIFSNARIY NTEGSVVYED SLELEKVVTK KYCEIMGDNS QLDFTEFDEQ YGTRPLVLPP 1690 1700 VVTSSVAESF TDEADSSMTE ASV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional interdependence of the yeast SNF2, SNF5, and SNF6 proteins in transcriptional activation." Laurent B.C., Treitel M.A., Carlson M. Proc. Natl. Acad. Sci. U.S.A. 88:2687-2691(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"The GAM1/SNF2 gene of Saccharomyces cerevisiae encodes a highly charged nuclear protein required for transcription of the STA1 gene." Yoshimoto H., Yamashita I. Mol. Gen. Genet. 228:270-280(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 38626 / AH22 / NRRL Y-12843.
[3]	"The SNF2/SWI2/GAM1/TYE3/RIC1 gene is involved in the coordinate regulation of phospholipid synthesis in Saccharomyces cerevisiae." Kodaki T., Hosaka K., Nikawa J., Yamashita S. J. Biochem. 117:362-368(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 26787 / X2180-1B.
[4]	"DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of Saccharomyces cerevisiae." Cheret G., Bernardi A., Sor F.J. Yeast 12:1059-1064(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[7]	"Sequence and analysis of a 36.2 kb fragment from the right arm of yeast chromosome XV reveals 19 open reading frames including SNF2 (5' end), CPA1, SLY41, a putative transport ATPase, a putative ribosomal protein and an SNF2 homologue." Poirey R., Cziepluch C., Tobiasch E., Pujol A., Kordes E., Jauniaux J.-C. Yeast 13:479-482(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-309. Strain: ATCC 96604 / S288c / FY1679.
[8]	"Functional analysis of the DNA-stimulated ATPase domain of yeast SWI2/SNF2." Richmond E., Peterson C.L. Nucleic Acids Res. 24:3685-3692(1996) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[9]	"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].
[10]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: ADR376.
[11]	"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-358; SER-716 AND SER-1340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution." Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O. Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; THR-383 AND SER-716, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Sites of ubiquitin attachment in Saccharomyces cerevisiae." Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S. Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Structural analysis of the yeast SWI/SNF chromatin remodeling complex." Smith C.L., Horowitz-Scherer R., Flanagan J.F., Woodcock C.L., Peterson C.L. Nat. Struct. Biol. 10:141-145(2003) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF THE SWI/SNF COMPLEX, ELECTRON MICROSCOPY OF THE SWI/SNF COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M61703 Genomic DNA. Translation: AAA35059.1.
X57837 Genomic DNA. Translation: CAA40969.1.
D90459 Genomic DNA. Translation: BAA14423.1.
X89633 Genomic DNA. Translation: CAA61793.1.
Z75198 Genomic DNA. Translation: CAA99517.1.
Z75199 Genomic DNA. Translation: CAA99519.1.
BK006948 Genomic DNA. Translation: DAA11054.1.

PIR

S15047.

RefSeq

NP_014933.3. NM_001183709.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4I6M	X-ray	2.80	C	575-667	[»]

ProteinModelPortal

P22082.

SMR

P22082. Positions 592-660, 752-1294, 1565-1655.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

34678. 142 interactions.

DIP

DIP-1150N.

IntAct

P22082. 42 interactions.

MINT

MINT-600461.

STRING

4932.YOR290C.

Proteomic databases

PaxDb

P22082.

PeptideAtlas

P22082.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOR290C; YOR290C; YOR290C.

GeneID

854465.

KEGG

sce:YOR290C.

Organism-specific databases

CYGD

YOR290c.

SGD

S000005816. SNF2.

Phylogenomic databases

eggNOG

COG0553.

GeneTree

ENSGT00750000117971.

HOGENOM

HOG000172362.

KO

K11786.

OMA

FVYEEVE.

OrthoDB

EOG7M98QM.

Enzyme and pathway databases

BioCyc

YEAST:G3O-33775-MONOMER.

Gene expression databases

Genevestigator

P22082.

Family and domain databases

Gene3D

1.20.920.10. 1 hit.
3.40.50.300. 2 hits.

InterPro

IPR017956. AT_hook_DNA-bd_motif.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR014978. Gln-Leu-Gln_QLQ.
IPR014012. Helicase/SANT-assoc_DNA-bd.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]

Pfam

PF00439. Bromodomain. 1 hit.
PF00271. Helicase_C. 1 hit.
PF08880. QLQ. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00384. AT_hook. 2 hits.
SM00297. BROMO. 1 hit.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00951. QLQ. 1 hit.
[Graphical view]

SUPFAM

SSF47370. SSF47370. 1 hit.
SSF52540. SSF52540. 2 hits.

PROSITE

PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51204. HSA. 1 hit.
PS51666. QLQ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

976750.

Entry information

Entry name

SNF2_YEAST

Accession

Primary (citable) accession number: P22082
Secondary accession number(s): D6W2Y8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	April 16, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program