P08153 (SWI5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcriptional factor SWI5

Gene names

Name:	SWI5
Ordered Locus Names:	YDR146C
ORF Names:	YD8358.03C

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

General annotation (Comments)

Function	Determines the mother-cell-specific transcription of the HO endonuclease gene that is responsible for the initiation of mating-type switching in yeast. Recognizes a specific sequence in the promoter of the HO gene. Activates EGT2 transcription in a concentration-dependent manner. Synthesized during G2 and early mitosis.
Subcellular location	Nucleus. Cytoplasm. Note: Nuclear in G1, cytoplasmic in S, G2 and M cell cycle phases. Ref.6
Post-translational modification	Cell cycle-dependent phosphorylation of three serine residues prevents SWI5 from entering the nucleus, and it accumulates in the cytoplasm. As a consequence of CDC28 kinase inactivation at the end of anaphase, the three serine residues are dephosphorylated and SWI5 enters the nucleus to activate transcription. It is then rapidly degraded. Threonine phosphorylation also seems to occur. Ref.6 Ref.7 Phosphorylated by PHO85. Ref.6 Ref.7
Miscellaneous	Present with 688 molecules/cell in log phase SD medium.
Sequence similarities	Contains 1 A.T hook DNA-binding domain. Contains 3 C2H2-type zinc fingers.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of mating type switching Inferred from mutant phenotype PubMed 6436497. Source: SGD positive regulation of transcription on exit from mitosis, from RNA polymerase II promoter Inferred from mutant phenotype PubMed 9017392PubMed 9529390. Source: SGD regulation of transcription involved in G1 phase of mitotic cell cycle Inferred from mutant phenotype PubMed 10409653. Source: SGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay PubMed 8816483. Source: SGD nucleus Inferred from direct assay PubMed 8816483. Source: SGD
Molecular_function	RNA polymerase II distal enhancer sequence-specific DNA binding Inferred from direct assay Ref.1. Source: SGD mediator complex binding Inferred from mutant phenotype PubMed 11562354. Source: SGD sequence-specific transcription regulatory region DNA binding RNA polymerase II transcription factor recruiting transcription factor activity Inferred from mutant phenotype PubMed 10319811PubMed 11562354. Source: SGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 709

709

Transcriptional factor SWI5

PRO_0000046855

Regions

Zinc finger

550 – 574

25

C2H2-type 1

Zinc finger

580 – 604

25

C2H2-type 2

Zinc finger

609 – 632

24

C2H2-type 3

DNA binding

647 – 659

13

A.T hook Ref.5

Motif

635 – 659

25

Nuclear localization signal Potential

Amino acid modifications

Modified residue

278

1

Phosphoserine Ref.11

Modified residue

492

1

Phosphoserine Ref.9 Ref.12

Modified residue

505

1

Phosphoserine Ref.10 Ref.11 Ref.12

Modified residue

522

1

Phosphoserine; by CDC28

Modified residue

646

1

Phosphoserine; by CDC28 Ref.10

Modified residue

664

1

Phosphoserine; by CDC28

Experimental info

Mutagenesis

522

1

S → A: Constitutive nuclear entry; when associated with A-646 and A-664.

Mutagenesis

646

1

S → A: Constitutive nuclear entry; when associated with A-522 and A-664.

Mutagenesis

664

1

S → A: Constitutive nuclear entry; when associated with A-522 and A-646.

Sequence conflict

514

1

E → K in AAU09695. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

709

Helix Strand Turn

Details...

Helix

538 – 540

3

Beta strand

543 – 545

3

Turn

546 – 548

3

Beta strand

549 – 551

3

Beta strand

563 – 566

4

Helix

567 – 574

8

Turn

575 – 577

3

Beta strand

591 – 594

4

Helix

595 – 601

7

Helix

602 – 604

3

Sequences

	Sequence		Length	Mass (Da)
	P08153 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: BEF5ED5BFB6E30F6	FASTA	709	79,775
	10 20 30 40 50 60 MDTSNSWFDA SKVQSLNFDL QTNSYYSNAR GSDPSSYAIE GEYKTLATDD LGNILNLNYG 70 80 90 100 110 120 ETNEVIMNEI NDLNLPLGPL SDEKSVKVST FSELIGNDWQ SMNFDLENNS REVTLNATSL 130 140 150 160 170 180 LNENRLNQDS GMTVYQKTMS DKPHDEKKIS MADNLLSTIN KSEINKGFDR NLGELLLQQQ 190 200 210 220 230 240 QELREQLRAQ QEANKKLELE LKQTQYKQQQ LQATLENSDG PQFLSPKRKI SPASENVEDV 250 260 270 280 290 300 YANSLSPMIS PPMSNTSFTG SPSRRNNRQK YCLQRKNSSG TVGPLCFQEL NEGFNDSLIS 310 320 330 340 350 360 PKKIRSNPNE NLSSKTKFIT PFTPKSRVSS ATSNSANITP NNLRLDFKIN VEDQESEYSE 370 380 390 400 410 420 KPLGLGIELL GKPGPSPTKS VSLKSASVDI MPTIPGSVNN TPSVNKVSLS SSYIDQYTPR 430 440 450 460 470 480 GKQLHFSSIS ENALGINAAT PHLKPPSQQA RHREGVFNDL DPNVLTKNTD NEGDDNEENE 490 500 510 520 530 540 PESRFVISET PSPVLKSQSK YEGRSPQFGT HIKEINTYTT NSPSKITRKL TTLPRGSIDK 550 560 570 580 590 600 YVKEMPDKTF ECLFPGCTKT FKRRYNIRSH IQTHLEDRPY SCDHPGCDKA FVRNHDLIRH 610 620 630 640 650 660 KKSHQEKAYA CPCGKKFNRE DALVVHRSRM ICSGGKKYEN VVIKRSPRKR GRPRKDGTSS 670 680 690 700 VSSSPIKENI NKDHNGQLMF KLEDQLRRER SYDGNGTGIM VSPMKTNQR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a transcription factor involved in mother cell specific transcription of the yeast HO gene." Stillman D.J., Bankier A.T., Seddon A., Groenhout E.G., Nasmyth K.A. EMBO J. 7:485-494(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: S288c / FY1678.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Zinc-finger motifs expressed in E. coli and folded in vitro direct specific binding to DNA." Nagai K., Nakaseko Y., Nasmyth K.A., Rhodes D. Nature 332:284-286(1988) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING.
[6]	"The role of phosphorylation and the CDC28 protein kinase in cell cycle-regulated nuclear import of the S. cerevisiae transcription factor SWI5." Moll T., Tebb G., Surana U., Robitsch H., Nasmyth K. Cell 66:743-758(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, MUTAGENESIS, SUBCELLULAR LOCATION.
[7]	"Interactions between Pho85 cyclin-dependent kinase complexes and the Swi5 transcription factor in budding yeast." Measday V., McBride H., Moffat J., Stillman D., Andrews B.J. Mol. Microbiol. 35:825-834(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY PHO85.
[8]	"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].
[9]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, MASS SPECTROMETRY. Strain: YAL6B.
[10]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505 AND SER-646, MASS SPECTROMETRY.
[11]	"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-278 AND SER-505, MASS SPECTROMETRY.
[12]	"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-492 AND SER-505, MASS SPECTROMETRY.
[13]	"Solution structures of two zinc-finger domains from SWI5 obtained using two-dimensional 1H nuclear magnetic resonance spectroscopy. A zinc-finger structure with a third strand of beta-sheet." Neuhaus D., Nakaseko Y., Schwabe J.W.R., Klug A. J. Mol. Biol. 228:637-651(1992) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 540-608.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X06978 Genomic DNA. Translation: CAA30040.1.
Z50046 Genomic DNA. Translation: CAA90369.1.
AY723778 Genomic DNA. Translation: AAU09695.1.
BK006938 Genomic DNA. Translation: DAA11989.1.

PIR

TWBYS5. S00342.

RefSeq

NP_010430.1. NM_001180453.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NCS	NMR	-	A	532-578	[»]
1ZFD	NMR	-	A	577-608	[»]

ProteinModelPortal

P08153.

SMR

P08153. Positions 532-627, 631-707.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1461N.

IntAct

P08153. 17 interactions.

MINT

MINT-399696.

STRING

4932.YDR146C.

Proteomic databases

PaxDb

P08153.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR146C; YDR146C; YDR146C.

GeneID

851724.

KEGG

sce:YDR146C.

Organism-specific databases

CYGD

YDR146c.

SGD

S000002553. SWI5.

Phylogenomic databases

eggNOG

COG5048.

GeneTree

ENSGT00700000104901.

HOGENOM

HOG000001123.

KO

K09202.

OrthoDB

EOG49KK17.

Enzyme and pathway databases

BioCyc

YEAST:G3O-29743-MONOMER.

Gene expression databases

Genevestigator

P08153.

GermOnline

YDR146C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.30.160.60. 2 hits.

InterPro

IPR017956. AT_hook_DNA-bd_motif.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]

Pfam

PF00096. zf-C2H2. 2 hits.
[Graphical view]

SMART

SM00384. AT_hook. 1 hit.
SM00355. ZnF_C2H2. 2 hits.
[Graphical view]

PROSITE

PS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P08153.

NextBio

969436.

Entry information

Entry name

SWI5_YEAST

Accession

Primary (citable) accession number: P08153
Secondary accession number(s): D6VSC9, E9P945

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	May 29, 2013
This is version 158 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program