P0C0S5 (H2AZ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H2A.Z
Short name=H2A/z

Gene names

Name:	H2AFZ
Synonyms:	H2AZ

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	128 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 replaces conventional H2A in a subset of 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. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division. Ref.9
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 H2AFZ forms an heterodimer with H2B. H2AFZ interacts with INCENP By similarity.
Subcellular location	Nucleus. Chromosome.
Post-translational modification	Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression. Acetylated on Lys-5, Lys-8 and Lys-12 during interphase. Acetylation disappears at mitosis By similarity. Not phosphorylated By similarity.
Sequence similarities	Belongs to the histone H2A family.
Mass spectrometry	Molecular mass is 13413.4 Da from positions 2 - 128. Determined by ESI. Monoisotopic, not modified. Ref.10

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular component	nucleosome Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay. Source: MGI
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 128

127

Histone H2A.Z

PRO_0000055297

Regions

Region

2 – 17

16

Required for interaction with INCENP By similarity

Region

93 – 103

11

Required for interaction with INCENP By similarity

Amino acid modifications

Modified residue

5

1

N6-acetyllysine Ref.11 Ref.12 Ref.13 Ref.14

Modified residue

8

1

N6-acetyllysine Ref.11 Ref.12 Ref.13 Ref.14

Modified residue

12

1

N6-acetyllysine Ref.11 Ref.13 Ref.14

Modified residue

14

1

N6-acetyllysine Ref.11 Ref.14

Cross-link

122

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

128

Helix Strand Turn

Details...

Helix

20 – 24

5

Turn

25

1

Helix

30 – 39

10

Turn

40

1

Turn

49 – 50

2

Helix

51 – 75

25

Turn

76 – 78

3

Helix

84 – 93

10

Helix

95 – 100

6

Turn

106 – 107

2

Helix

116 – 118

3

Sequences

	Sequence		Length	Mass (Da)
	P0C0S5 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E024E53818230371	FASTA	128	13,553
	10 20 30 40 50 60 MAGGKAGKDS GKAKTKAVSR SQRAGLQFPV GRIHRHLKSR TTSHGRVGAT AAVYSAAILE 70 80 90 100 110 120 YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG KKGQQKTV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of cDNAs for mammalian H2A.Z, an evolutionarily diverged but highly conserved basal histone H2A isoprotein species." Hatch C.L., Bonner W.M. Nucleic Acids Res. 16:1113-1124(1988) [PubMed: 3344202] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"The human histone H2A.Z gene. Sequence and regulation." Hatch C.L., Bonner W.M. J. Biol. Chem. 265:15211-15218(1990) [PubMed: 1697587] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Tongue.
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Skeletal muscle and Uterus.
[8]	"Histone ubiquitination: a tagging tail unfolds?" Jason L.J.M., Moore S.C., Lewis J.D., Lindsey G., Ausio J. Bioessays 24:166-174(2002) [PubMed: 11835281] [Abstract] Cited for: UBIQUITINATION AT LYS-122.
[9]	"Transcription-induced chromatin remodeling at the c-myc gene involves the local exchange of histone H2A.Z." Farris S.D., Rubio E.D., Moon J.J., Gombert W.M., Nelson B.H., Krumm A. J. Biol. Chem. 280:25298-25303(2005) [PubMed: 15878876] [Abstract] Cited for: FUNCTION.
[10]	"Precise characterization of human histones in the H2A gene family by top down mass spectrometry." Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L. J. Proteome Res. 5:248-253(2006) [PubMed: 16457589] [Abstract] Cited for: MASS SPECTROMETRY.
[11]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-8; LYS-12 AND LYS-14, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Characterization of histones H2A and H2B variants and their post-translational modifications by mass spectrometry." Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J. Mol. Cell. Proteomics 5:541-552(2006) [PubMed: 16319397] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, ACETYLATION AT LYS-5 AND LYS-8.
[13]	"Quantitative proteomic analysis of post-translational modifications of human histones." Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M., Finn P., Grauslund M., Hansen A.M., Jensen O.N. Mol. Cell. Proteomics 5:1314-1325(2006) [PubMed: 16627869] [Abstract] Cited for: ACETYLATION AT LYS-5; LYS-8 AND LYS-12, MASS SPECTROMETRY.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-8; LYS-12 AND LYS-14, MASS SPECTROMETRY.
[15]	"Crystal structure of a nucleosome core particle containing the variant histone H2A.Z." Suto R.K., Clarkson M.J., Tremethick D.J., Luger K. Nat. Struct. Biol. 7:1121-1124(2000) [PubMed: 11101893] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH THE NUCLEOSOME.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X52317 mRNA. Translation: CAA36553.1.
M37583 mRNA. Translation: AAA35984.1.
L10138 Genomic DNA. Translation: AAC61625.1.
CR457415 mRNA. Translation: CAG33696.1.
AK315413 mRNA. Translation: BAG37803.1.
AC097460 Genomic DNA. Translation: AAY41013.1.
CH471057 Genomic DNA. Translation: EAX06118.1.
BC018002 mRNA. Translation: AAH18002.1.
BC020936 mRNA. Translation: AAH20936.1.
BC103743 mRNA. Translation: AAI03744.1.

IPI

IPI00218448.

PIR

A35881.

RefSeq

NP_002097.1. NM_002106.3.

UniGene

Hs.119192.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F66	X-ray	2.60	C/G	1-128	[»]

ProteinModelPortal

P0C0S5.

SMR

P0C0S5. Positions 17-123.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38593N.

IntAct

P0C0S5. 2 interactions.

STRING

P0C0S5.

PTM databases

PhosphoSite

P0C0S5.

Polymorphism databases

DMDM

83288408.

Proteomic databases

PRIDE

P0C0S5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000296417; ENSP00000296417; ENSG00000164032.

GeneID

3015.

KEGG

hsa:3015.

UCSC

uc003hvo.1. human.

Organism-specific databases

CTD

3015.

GeneCards

GC04M100869.

H-InvDB

HIX0004404.

HGNC

HGNC:4741. H2AFZ.

HPA

CAB022549.

MIM

142763. gene.

neXtProt

NX_P0C0S5.

PharmGKB

PA29119.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20613.

GeneTree

ENSGT00540000069960.

HOGENOM

HBG610736.

HOVERGEN

HBG009342.

InParanoid

P0C0S5.

OMA

FGGVLPH.

OrthoDB

EOG4MW87G.

PhylomeDB

P0C0S5.

Enzyme and pathway databases

Reactome

REACT_111183. Meiosis.
REACT_22172. Chromosome Maintenance.
REACT_75925. Amyloids.

Gene expression databases

ArrayExpress

P0C0S5.

Bgee

P0C0S5.

CleanEx

HS_H2AFZ.

Genevestigator

P0C0S5.

GermOnline

ENSG00000164032. Homo sapiens.

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

11952.

PMAP-CutDB

P0C0S5.

SOURCE

Search...

Entry information

Entry name

H2AZ_HUMAN

Accession

Primary (citable) accession number: P0C0S5
Secondary accession number(s): B2RD56, P17317, Q6I9U0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.