Q12692 (H2AZ_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H2A.Z

Gene names

Name:	HTZ1
Synonyms:	H2AZ, HTA3
Ordered Locus Names:	YOL012C
ORF Names:	O2345

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	134 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Variant histone H2A which can replace H2A in some nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. This variant is enriched at promoters, it may keep them in a repressed state until the appropriate activation signal is received. Near telomeres, it may counteract gene silencing caused by the spread of heterochromatin proteins. Required for the RNA polymerase II and SPT15/TBP recruitment to the target genes. Involved in chromosome stability. Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20
Subunit structure	The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. H2A or its variant H2A.Z forms an heterodimer with H2B. H2A.Z associates with the VPS72/SWC2 subunit of the SWR1 chromatin remodeling complex. Interacts also with RBP1/DNA-directed RNA polymerase II largest subunit. Interacts with NAP1. Ref.9 Ref.16 Ref.18 Ref.22
Subcellular location	Nucleus. Chromosome Ref.12.
Post-translational modification	Acetylated by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex, and/or by GCN5, a component of the SAGA complex, to form H2A.ZK3Ac, H2A.ZK8Ac, H2A.ZK10Ac and H2A.ZK14Ac once deposited into chromatin. Acetylation is required for function at telomeres. H2A.ZK14Ac is acetylated at the promoters of active genes.
Miscellaneous	Present with 2840 molecules/cell in log phase SD medium. Ref.13 In contrast to H2A1 and H2A2, appears to be weakly or not sumoylated.
Sequence similarities	Belongs to the histone H2A family.
Caution	To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions refering to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H2A.ZK3ac = acetylated Lys-4; H2A.ZK8ac = acetylated Lys-9; H2A.ZK10ac = acetylated Lys-11; H2A.ZK14ac = acetylated Lys-15.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
Molecular function	Activator Chromatin regulator
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW chromatin silencing at silent mating-type cassette Inferred from genetic interaction Ref.7. Source: SGD nuclear-transcribed mRNA catabolic process, non-stop decay Inferred from mutant phenotype. Source: SGD nucleosome assembly Inferred from electronic annotation. Source: InterPro regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.6. Source: SGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromatin assembly complex Inferred from physical interaction Ref.7. Source: SGD nuclear chromatin Inferred from physical interaction Ref.6Ref.7. Source: SGD nucleosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin binding Inferred from direct assay Ref.6. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-8080,EBI-8080
BDF1	P35817	4	EBI-8080,EBI-3493
HHO1	P53551	3	EBI-8080,EBI-8064
MPS3	P47069	3	EBI-8080,EBI-25811
SWR1	Q05471	8	EBI-8080,EBI-22102

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 134

133

Histone H2A.Z

PRO_0000055340

Regions

Region

98 – 108

11

Interaction with VPS72

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.4

Modified residue

4

1

N6-acetyllysine Ref.4 Ref.20

Modified residue

9

1

N6-acetyllysine Ref.4 Ref.20

Modified residue

11

1

N6-acetyllysine Ref.4 Ref.20

Modified residue

15

1

N6-acetyllysine Ref.4 Ref.20

Secondary structure

1

.

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134

Helix Strand Turn

Details...

Helix

2 – 19

18

Beta strand

21 – 23

3

Helix

25 – 28

4

Helix

35 – 44

10

Turn

54 – 56

3

Helix

57 – 82

26

Helix

89 – 97

9

Helix

100 – 106

7

Turn

111 – 113

3

Sequences

	Sequence		Length	Mass (Da)
	Q12692 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 1D8FCEE3C8A504E7	FASTA	134	14,283
	10 20 30 40 50 60 MSGKAHGGKG KSGAKDSGSL RSQSSSARAG LQFPVGRIKR YLKRHATGRT RVGSKAAIYL 70 80 90 100 110 120 TAVLEYLTAE VLELAGNAAK DLKVKRITPR HLQLAIRGDD ELDSLIRATI ASGGVLPHIN 130 KALLLKVEKK GSKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"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: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Acetylation of H2AZ Lys 14 is associated with genome-wide gene activity in yeast." Millar C.B., Xu F., Zhang K., Grunstein M. Genes Dev. 20:711-722(2006) [PubMed: 16543223] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21, ACETYLATION AT SER-2; LYS-4; LYS-9; LYS-11 AND LYS-15, MASS SPECTROMETRY, FUNCTION.
[5]	"A likely histone H2A.F/Z variant in Saccharomyces cerevisiae." Jackson J.D., Falciano V.T., Gorovsky M.A. Trends Biochem. Sci. 21:466-467(1996) [PubMed: 9009827] [Abstract] Cited for: SIMILARITY TO VARIANT H2A, GENE NAME.
[6]	"Histone H2A.Z regulates transcription and is partially redundant with nucleosome remodeling complexes." Santisteban M.S., Kalashnikova T., Smith M.M. Cell 103:411-422(2000) [PubMed: 11081628] [Abstract] Cited for: FUNCTION.
[7]	"A histone variant, Htz1p, and a Sir1p-like protein, Esc2p, mediate silencing at HMR." Dhillon N., Kamakaka R.T. Mol. Cell 6:769-780(2000) [PubMed: 11090616] [Abstract] Cited for: FUNCTION.
[8]	"Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants." Jackson J.D., Gorovsky M.A. Nucleic Acids Res. 28:3811-3816(2000) [PubMed: 11000274] [Abstract] Cited for: FUNCTION.
[9]	"H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions." Adam M., Robert F., Larochelle M., Gaudreau L. Mol. Cell. Biol. 21:6270-6279(2001) [PubMed: 11509669] [Abstract] Cited for: FUNCTION, INTERACTION WITH RPB1.
[10]	"Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin." Meneghini M.D., Wu M., Madhani H.D. Cell 112:725-736(2003) [PubMed: 12628191] [Abstract] Cited for: FUNCTION.
[11]	"A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1." Krogan N.J., Keogh M.-C., Datta N., Sawa C., Ryan O.W., Ding H., Haw R.A., Pootoolal J., Tong A., Canadien V., Richards D.P., Wu X., Emili A., Hughes T.R., Buratowski S., Greenblatt J.F. Mol. Cell 12:1565-1576(2003) [PubMed: 14690608] [Abstract] Cited for: FUNCTION OF THE SWR1 COMPLEX, IDENTIFICATION IN THE SWR1 COMPLEX, MASS SPECTROMETRY.
[12]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[13]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[14]	"A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin." Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W., Jennings J.L., Link A.J., Madhani H.D., Rine J. PLoS Biol. 2:587-599(2004) [PubMed: 15045029] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE SWR1 COMPLEX, MASS SPECTROMETRY.
[15]	"Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4." Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y., Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A., Buratowski S., Hieter P., Greenblatt J.F. Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004) [PubMed: 15353583] [Abstract] Cited for: FUNCTION.
[16]	"ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex." Mizuguchi G., Shen X., Landry J., Wu W.-H., Sen S., Wu C. Science 303:343-348(2004) [PubMed: 14645854] [Abstract] Cited for: IDENTIFICATION IN THE SWR1 COMPLEX, FUNCTION OF THE SWR1 COMPLEX, INTERACTION WITH HISTONE H2B, MASS SPECTROMETRY.
[17]	"Histone variant H2A.Z marks the 5' ends of both active and inactive genes in euchromatin." Raisner R.M., Hartley P.D., Meneghini M.D., Bao M.Z., Liu C.L., Schreiber S.L., Rando O.J., Madhani H.D. Cell 123:233-248(2005) [PubMed: 16239142] [Abstract] Cited for: FUNCTION.
[18]	"Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange." Wu W.-H., Alami S., Luk E., Wu C.-H., Sen S., Mizuguchi G., Wei D., Wu C. Nat. Struct. Mol. Biol. 12:1064-1071(2005) [PubMed: 16299513] [Abstract] Cited for: INTERACTION WITH VPS72.
[19]	"Preferential occupancy of histone variant H2AZ at inactive promoters influences local histone modifications and chromatin remodeling." Li B., Pattenden S.G., Lee D., Gutierrez J., Chen J., Seidel C., Gerton J., Workman J.L. Proc. Natl. Acad. Sci. U.S.A. 102:18385-18390(2005) [PubMed: 16344463] [Abstract] Cited for: FUNCTION.
[20]	"Telomeric heterochromatin boundaries require NuA4-dependent acetylation of histone variant H2A.Z in Saccharomyces cerevisiae." Babiarz J.E., Halley J.E., Rine J. Genes Dev. 20:700-710(2006) [PubMed: 16543222] [Abstract] Cited for: ACETYLATION AT LYS-4; LYS-9; LYS-11 AND LYS-15, MASS SPECTROMETRY, FUNCTION.
[21]	"Histone sumoylation is a negative regulator in Saccharomyces cerevisiae and shows dynamic interplay with positive-acting histone modifications." Nathan D., Ingvarsdottir K., Sterner D.E., Bylebyl G.R., Dokmanovic M., Dorsey J.A., Whelan K.A., Krsmanovic M., Lane W.S., Meluh P.B., Johnson E.S., Berger S.L. Genes Dev. 20:966-976(2006) [PubMed: 16598039] [Abstract] Cited for: LACK OF SUMOYLATION.
[22]	"Phosphorylation by casein kinase 2 regulates Nap1 localization and function." Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., Pemberton L.F. Mol. Cell. Biol. 28:1313-1325(2008) [PubMed: 18086883] [Abstract] Cited for: INTERACTION WITH NAP1, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z74754 Genomic DNA. Translation: CAA99011.1.
AY558000 Genomic DNA. Translation: AAS56326.1.
BK006948 Genomic DNA. Translation: DAA10771.1.

PIR

S66694.

RefSeq

NP_014631.1. NM_001183266.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FSB	model	-	A	104-134	[»]
			C/G	1-134	[»]
2JSS	NMR	-	A	23-119	[»]

ProteinModelPortal

Q12692.

SMR

Q12692. Positions 28-119.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1381N.

IntAct

Q12692. 129 interactions.

MINT

MINT-387304.

STRING

Q12692.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOL012C; YOL012C; YOL012C.

GeneID

854150.

KEGG

sce:YOL012C.

NMPDR

fig|4932.3.peg.5726.

Organism-specific databases

SGD

S000005372. HTZ1.

Phylogenomic databases

eggNOG

fuNOG10534.

GeneTree

EFGT00050000005745.

HOGENOM

HBG610736.

OMA

FGGVLPH.

OrthoDB

EOG49632H.

Gene expression databases

ArrayExpress

Q12692.

Genevestigator

Q12692.

GermOnline

YOL012C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view]

Gene3D

G3DSA:1.10.20.10. Histone-fold. 1 hit.

KO

K11251.

Pfam

PF00125. Histone. 1 hit.
[Graphical view]

PRINTS

PR00620. HISTONEH2A.

SMART

SM00414. H2A. 1 hit.
[Graphical view]

SUPFAM

SSF47113. Histone-fold. 1 hit.

PROSITE

PS00046. HISTONE_H2A. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

975902.

Entry information

Entry name

H2AZ_YEAST

Accession

Primary (citable) accession number: Q12692
Secondary accession number(s): D6W255

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program