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Protein

Histone H2A.Z

Gene

H2AFZ

Organism
Homo sapiens (Human)
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.1 Publication

GO - Molecular functioni

  • chromatin DNA binding Source: UniProtKB
  • nucleosomal DNA binding Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: UniProtKB
  • RNA polymerase II core promoter sequence-specific DNA binding Source: UniProtKB
  • RNA polymerase II distal enhancer sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • cellular response to estradiol stimulus Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_2232. RNA Polymerase I Promoter Opening.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_264242. formation of the beta-catenin:TCF transactivating complex.
REACT_264303. Condensation of Prophase Chromosomes.
REACT_264352. PRC2 methylates histones and DNA.
REACT_264541. SIRT1 negatively regulates rRNA Expression.
REACT_264545. RMTs methylate histone arginines.
REACT_268237. DNA methylation.
REACT_268530. Transcriptional regulation by small RNAs.
REACT_27271. Meiotic recombination.
REACT_355391. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
REACT_75792. Meiotic synapsis.
REACT_75925. Amyloids.
REACT_7963. Packaging Of Telomere Ends.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A.Z
Short name:
H2A/z
Gene namesi
Name:H2AFZ
Synonyms:H2AZ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:4741. H2AFZ.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29119.

Polymorphism and mutation databases

BioMutaiH2AFZ.
DMDMi83288408.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 128127Histone H2A.ZPRO_0000055297Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei5 – 51N6-acetyllysine2 Publications
Modified residuei8 – 81N6-acetyllysine3 Publications
Modified residuei12 – 121N6-acetyllysine2 Publications
Modified residuei14 – 141N6-acetyllysine1 Publication
Cross-linki122 – 122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

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).By similarity
Not phosphorylated.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP0C0S5.
PaxDbiP0C0S5.
PRIDEiP0C0S5.

PTM databases

PhosphoSiteiP0C0S5.

Miscellaneous databases

PMAP-CutDBP0C0S5.

Expressioni

Gene expression databases

BgeeiP0C0S5.
CleanExiHS_H2AFZ.
GenevisibleiP0C0S5. HS.

Organism-specific databases

HPAiCAB022549.
HPA045242.

Interactioni

Subunit structurei

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 similarity). Interacts (via M6 cassette) with ANP32E; leading to removal of H2A.Z/H2AFZ from the nucleosome.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ZNHIT1O432573EBI-1199859,EBI-347522

Protein-protein interaction databases

BioGridi109269. 60 interactions.
DIPiDIP-38593N.
IntActiP0C0S5. 4 interactions.
MINTiMINT-1605675.
STRINGi9606.ENSP00000296417.

Structurei

Secondary structure

1
128
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 234Combined sources
Helixi30 – 3910Combined sources
Beta strandi42 – 443Combined sources
Helixi49 – 7628Combined sources
Beta strandi80 – 823Combined sources
Helixi84 – 929Combined sources
Helixi95 – 10612Combined sources
Helixi116 – 1183Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F66X-ray2.60C/G1-128[»]
3WA9X-ray3.07C/G1-128[»]
4CAYX-ray1.48A19-128[»]
4NFTX-ray2.61A/B/C/D16-114[»]
ProteinModelPortaliP0C0S5.
SMRiP0C0S5. Positions 17-123.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0S5.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGiCOG5262.
GeneTreeiENSGT00710000106735.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP0C0S5.
KOiK11251.
OMAiIHRYLMN.
OrthoDBiEOG7M0NTR.
PhylomeDBiP0C0S5.
TreeFamiTF354232.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view]
PfamiPF00125. Histone. 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.

P0C0S5-1 [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

Mass spectrometryi

Molecular mass is 13413.4 Da from positions 2 - 128. Determined by ESI. Monoisotopic, not modified.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3654.1.
PIRiA35881.
RefSeqiNP_002097.1. NM_002106.3.
UniGeneiHs.119192.

Genome annotation databases

EnsembliENST00000296417; ENSP00000296417; ENSG00000164032.
GeneIDi3015.
KEGGihsa:3015.
UCSCiuc003hvo.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3654.1.
PIRiA35881.
RefSeqiNP_002097.1. NM_002106.3.
UniGeneiHs.119192.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F66X-ray2.60C/G1-128[»]
3WA9X-ray3.07C/G1-128[»]
4CAYX-ray1.48A19-128[»]
4NFTX-ray2.61A/B/C/D16-114[»]
ProteinModelPortaliP0C0S5.
SMRiP0C0S5. Positions 17-123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109269. 60 interactions.
DIPiDIP-38593N.
IntActiP0C0S5. 4 interactions.
MINTiMINT-1605675.
STRINGi9606.ENSP00000296417.

PTM databases

PhosphoSiteiP0C0S5.

Polymorphism and mutation databases

BioMutaiH2AFZ.
DMDMi83288408.

Proteomic databases

MaxQBiP0C0S5.
PaxDbiP0C0S5.
PRIDEiP0C0S5.

Protocols and materials databases

DNASUi3015.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296417; ENSP00000296417; ENSG00000164032.
GeneIDi3015.
KEGGihsa:3015.
UCSCiuc003hvo.1. human.

Organism-specific databases

CTDi3015.
GeneCardsiGC04M100869.
HGNCiHGNC:4741. H2AFZ.
HPAiCAB022549.
HPA045242.
MIMi142763. gene.
neXtProtiNX_P0C0S5.
PharmGKBiPA29119.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5262.
GeneTreeiENSGT00710000106735.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP0C0S5.
KOiK11251.
OMAiIHRYLMN.
OrthoDBiEOG7M0NTR.
PhylomeDBiP0C0S5.
TreeFamiTF354232.

Enzyme and pathway databases

ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_2232. RNA Polymerase I Promoter Opening.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_264242. formation of the beta-catenin:TCF transactivating complex.
REACT_264303. Condensation of Prophase Chromosomes.
REACT_264352. PRC2 methylates histones and DNA.
REACT_264541. SIRT1 negatively regulates rRNA Expression.
REACT_264545. RMTs methylate histone arginines.
REACT_268237. DNA methylation.
REACT_268530. Transcriptional regulation by small RNAs.
REACT_27271. Meiotic recombination.
REACT_355391. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
REACT_75792. Meiotic synapsis.
REACT_75925. Amyloids.
REACT_7963. Packaging Of Telomere Ends.

Miscellaneous databases

ChiTaRSiH2AFZ. human.
EvolutionaryTraceiP0C0S5.
GeneWikiiH2AFZ.
GenomeRNAii3015.
NextBioi11952.
PMAP-CutDBP0C0S5.
PROiP0C0S5.
SOURCEiSearch...

Gene expression databases

BgeeiP0C0S5.
CleanExiHS_H2AFZ.
GenevisibleiP0C0S5. HS.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view]
PfamiPF00125. Histone. 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. "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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain, Skeletal muscle and Uterus.
  8. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
  11. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-5; LYS-8 AND LYS-12, IDENTIFICATION BY MASS SPECTROMETRY.
  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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5 AND LYS-8, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-8; LYS-12 AND LYS-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH THE NUCLEOSOME.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 19-128 IN COMPLEX WITH ANP32E AND HISTONE H2B, INTERACTION WITH ANP32E.

Entry informationi

Entry nameiH2AZ_HUMAN
AccessioniPrimary (citable) accession number: P0C0S5
Secondary accession number(s): B2RD56, P17317, Q6I9U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.