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Protein

Histone H2A.Z

Gene

H2afz

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Essential for early development.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-1221633. Meiotic Synapsis.
R-MMU-573389. NoRC negatively regulates rRNA expression.
R-MMU-912497. Meiotic Recombination.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A.Z
Short name:
H2A/z
Gene namesi
Name:H2afz
Synonyms:H2az
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1888388. H2afz.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • nuclear euchromatin Source: MGI
  • nuclear heterochromatin Source: MGI
  • nucleosome Source: UniProtKB-KW
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 128127Histone H2A.ZPRO_0000055298Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51N6-acetyllysine; alternate1 Publication
Modified residuei5 – 51N6-methyllysine; alternateBy similarity
Modified residuei8 – 81N6-acetyllysine; alternate1 Publication
Modified residuei8 – 81N6-methyllysine; alternateBy similarity
Modified residuei12 – 121N6-acetyllysine1 Publication
Modified residuei14 – 141N6-acetyllysineBy similarity
Cross-linki122 – 122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression.By similarity
Acetylated on Lys-5, Lys-8 and Lys-12 during interphase. Acetylation disappears at mitosis.2 Publications
Not phosphorylated.1 Publication
Monomethylated on Lys-5 and Lys-8 by SETD6. SETD6 predominantly methylates Lys-8, lys-5 being a possible secondary site.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Ubl conjugation

Proteomic databases

EPDiP0C0S6.
MaxQBiP0C0S6.
PaxDbiP0C0S6.
PRIDEiP0C0S6.
TopDownProteomicsiP0C0S6.

PTM databases

iPTMnetiP0C0S6.
PhosphoSiteiP0C0S6.

Expressioni

Gene expression databases

BgeeiP0C0S6.
CleanExiMM_H2AFZ.
ExpressionAtlasiP0C0S6. baseline and differential.
GenevisibleiP0C0S6. MM.

Interactioni

Subunit structurei

Interacts (via M6 cassette) with ANP32E; leading to removal of H2A.Z/H2AFZ from the nucleosome (By similarity). 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 a heterodimer with H2B. H2AFZ interacts with INCENP.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi206173. 4 interactions.
IntActiP0C0S6. 13 interactions.
MINTiMINT-1605699.
STRINGi10090.ENSMUSP00000036907.

Structurei

3D structure databases

ProteinModelPortaliP0C0S6.
SMRiP0C0S6. Positions 17-123.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 1716Required for interaction with INCENPAdd
BLAST
Regioni89 – 10012M6 cassetteBy similarityAdd
BLAST
Regioni93 – 10311Required for interaction with INCENPAdd
BLAST

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGiKOG1757. Eukaryota.
COG5262. LUCA.
GeneTreeiENSGT00710000106735.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP0C0S6.
KOiK11251.
OMAiCAAILEY.
OrthoDBiEOG7M0NTR.
PhylomeDBiP0C0S6.
TreeFamiTF354232.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR002119. Histone_H2A.
IPR007125. Histone_H2A/H2B/H3.
IPR032454. Histone_H2A_C.
IPR032458. Histone_H2A_CS.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
PF16211. Histone_H2A_C. 1 hit.
[Graphical view]
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00046. HISTONE_H2A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0C0S6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGGKAGKDS GKAKTKAVSR SQRAGLQFPV GRIHRHLKSR TTSHGRVGAT
60 70 80 90 100
AAVYSAAILE YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL
110 120
IKATIAGGGV IPHIHKSLIG KKGQQKTV
Length:128
Mass (Da):13,553
Last modified:January 23, 2007 - v2
Checksum:iE024E53818230371
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121K → E in BAE30460 (PubMed:16141072).Curated
Sequence conflicti29 – 291P → A in BAE26959 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70494 mRNA. Translation: AAB09578.1.
AY074806 mRNA. Translation: AAL71864.1.
AK028176 mRNA. Translation: BAC25791.1.
AK088704 mRNA. Translation: BAC40515.1.
AK143572 mRNA. Translation: BAE25443.1.
AK146181 mRNA. Translation: BAE26959.1.
AK150454 mRNA. Translation: BAE29574.1.
AK151052 mRNA. Translation: BAE30069.1.
AK151509 mRNA. Translation: BAE30460.1.
AK151868 mRNA. Translation: BAE30756.1.
AK152398 mRNA. Translation: BAE31186.1.
AK152848 mRNA. Translation: BAE31541.1.
AK168178 mRNA. Translation: BAE40138.1.
BC079903 mRNA. Translation: AAH79903.1.
BC147478 mRNA. Translation: AAI47479.1.
BC158035 mRNA. Translation: AAI58036.1.
BC171999 mRNA. Translation: AAI71999.1.
CCDSiCCDS38647.1.
RefSeqiNP_058030.1. NM_016750.3.
UniGeneiMm.117541.
Mm.372513.
Mm.465508.

Genome annotation databases

EnsembliENSMUST00000041045; ENSMUSP00000036907; ENSMUSG00000037894.
GeneIDi51788.
KEGGimmu:51788.
UCSCiuc008rmo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70494 mRNA. Translation: AAB09578.1.
AY074806 mRNA. Translation: AAL71864.1.
AK028176 mRNA. Translation: BAC25791.1.
AK088704 mRNA. Translation: BAC40515.1.
AK143572 mRNA. Translation: BAE25443.1.
AK146181 mRNA. Translation: BAE26959.1.
AK150454 mRNA. Translation: BAE29574.1.
AK151052 mRNA. Translation: BAE30069.1.
AK151509 mRNA. Translation: BAE30460.1.
AK151868 mRNA. Translation: BAE30756.1.
AK152398 mRNA. Translation: BAE31186.1.
AK152848 mRNA. Translation: BAE31541.1.
AK168178 mRNA. Translation: BAE40138.1.
BC079903 mRNA. Translation: AAH79903.1.
BC147478 mRNA. Translation: AAI47479.1.
BC158035 mRNA. Translation: AAI58036.1.
BC171999 mRNA. Translation: AAI71999.1.
CCDSiCCDS38647.1.
RefSeqiNP_058030.1. NM_016750.3.
UniGeneiMm.117541.
Mm.372513.
Mm.465508.

3D structure databases

ProteinModelPortaliP0C0S6.
SMRiP0C0S6. Positions 17-123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206173. 4 interactions.
IntActiP0C0S6. 13 interactions.
MINTiMINT-1605699.
STRINGi10090.ENSMUSP00000036907.

PTM databases

iPTMnetiP0C0S6.
PhosphoSiteiP0C0S6.

Proteomic databases

EPDiP0C0S6.
MaxQBiP0C0S6.
PaxDbiP0C0S6.
PRIDEiP0C0S6.
TopDownProteomicsiP0C0S6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041045; ENSMUSP00000036907; ENSMUSG00000037894.
GeneIDi51788.
KEGGimmu:51788.
UCSCiuc008rmo.2. mouse.

Organism-specific databases

CTDi3015.
MGIiMGI:1888388. H2afz.

Phylogenomic databases

eggNOGiKOG1757. Eukaryota.
COG5262. LUCA.
GeneTreeiENSGT00710000106735.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP0C0S6.
KOiK11251.
OMAiCAAILEY.
OrthoDBiEOG7M0NTR.
PhylomeDBiP0C0S6.
TreeFamiTF354232.

Enzyme and pathway databases

ReactomeiR-MMU-1221633. Meiotic Synapsis.
R-MMU-573389. NoRC negatively regulates rRNA expression.
R-MMU-912497. Meiotic Recombination.

Miscellaneous databases

NextBioi308012.
PROiP0C0S6.
SOURCEiSearch...

Gene expression databases

BgeeiP0C0S6.
CleanExiMM_H2AFZ.
ExpressionAtlasiP0C0S6. baseline and differential.
GenevisibleiP0C0S6. MM.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR002119. Histone_H2A.
IPR007125. Histone_H2A/H2B/H3.
IPR032454. Histone_H2A_C.
IPR032458. Histone_H2A_CS.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
PF16211. Histone_H2A_C. 1 hit.
[Graphical view]
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00046. HISTONE_H2A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the murine histone H2A.Z cDNA and chromosomal localization of mouse H2A.Z related sequences."
    Rocha D., Carrier A., Anderson E., Botcherby M., Guenet J.-L., Jordan B.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  2. "Histone H2A.Z expression and regulation in mouse mammary gland."
    Le Provost F., Charlier M.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/cJ, C57BL/6J, DBA/2J and NOD.
    Tissue: Bone marrow, Spleen and Thymus.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "Quantitative determination of histone modification. H2A acetylation and phosphorylation."
    Pantazis P., Bonner W.M.
    J. Biol. Chem. 256:4669-4675(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION, LACK OF PHOSPHORYLATION.
  6. Cited for: FUNCTION.
  7. "Pericentric heterochromatin becomes enriched with H2A.Z during early mammalian development."
    Rangasamy D., Berven L., Ridgway P., Tremethick D.J.
    EMBO J. 22:1599-1607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH INCENP.
  8. "H2A.Z alters the nucleosome surface to promote HP1alpha-mediated chromatin fiber folding."
    Fan J.Y., Rangasamy D., Luger K., Tremethick D.J.
    Mol. Cell 16:655-661(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "RNA interference demonstrates a novel role for H2A.Z in chromosome segregation."
    Rangasamy D., Greaves I., Tremethick D.J.
    Nat. Struct. Mol. Biol. 11:650-655(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.
  10. "The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken."
    Bruce K., Myers F.A., Mantouvalou E., Lefevre P., Greaves I., Bonifer C., Tremethick D.J., Thorne A.W., Crane-Robinson C.
    Nucleic Acids Res. 33:5633-5639(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-5; LYS-8 AND LYS-12.

Entry informationi

Entry nameiH2AZ_MOUSE
AccessioniPrimary (citable) accession number: P0C0S6
Secondary accession number(s): B2RXZ3
, P17317, Q3UA55, Q3UK43, Q68FD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Down-regulation of H2afz by RNA interference leads to death at early embryonic stages.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.