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P0C0S5

- H2AZ_HUMAN

UniProt

P0C0S5 - H2AZ_HUMAN

Protein

Histone H2A.Z

Gene

H2AFZ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    1. chromatin DNA binding Source: UniProt
    2. nucleosomal DNA binding Source: UniProt
    3. protein binding Source: IntAct
    4. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: UniProt
    5. RNA polymerase II core promoter sequence-specific DNA binding Source: UniProt
    6. RNA polymerase II distal enhancer sequence-specific DNA binding Source: UniProt

    GO - Biological processi

    1. cellular response to estradiol stimulus Source: UniProt
    2. nucleosome assembly Source: InterPro
    3. positive regulation of transcription from RNA polymerase II promoter Source: UniProt

    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_172744. Condensation of Prophase Chromosomes.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    REACT_200808. PRC2 methylates histones and DNA.
    REACT_200827. SIRT1 negatively regulates rRNA Expression.
    REACT_200856. NoRC negatively regulates rRNA expression.
    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_27271. Meiotic recombination.
    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: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:4741. H2AFZ.

    Subcellular locationi

    GO - Cellular componenti

    1. nuclear euchromatin Source: UniProt
    2. nuclear heterochromatin Source: UniProt
    3. nucleosome Source: UniProtKB-KW
    4. nucleus Source: UniProt

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29119.

    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.
    GenevestigatoriP0C0S5.

    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. 57 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 – 234
    Helixi30 – 3910
    Beta strandi42 – 443
    Helixi49 – 7628
    Beta strandi80 – 823
    Helixi84 – 929
    Helixi95 – 10612
    Helixi116 – 1183

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000234652.
    HOVERGENiHBG009342.
    InParanoidiP0C0S5.
    KOiK11251.
    OMAiDPQRKGN.
    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

    MAGGKAGKDS GKAKTKAVSR SQRAGLQFPV GRIHRHLKSR TTSHGRVGAT    50
    AAVYSAAILE YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL 100
    IKATIAGGGV IPHIHKSLIG KKGQQKTV 128
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi83288408.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS3654.1.
    PIRi A35881.
    RefSeqi NP_002097.1. NM_002106.3.
    UniGenei Hs.119192.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F66 X-ray 2.60 C/G 1-128 [» ]
    3WA9 X-ray 3.07 C/G 1-128 [» ]
    4CAY X-ray 1.48 A 19-128 [» ]
    4NFT X-ray 2.61 A/B/C/D 16-114 [» ]
    ProteinModelPortali P0C0S5.
    SMRi P0C0S5. Positions 17-123.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109269. 57 interactions.
    DIPi DIP-38593N.
    IntActi P0C0S5. 4 interactions.
    MINTi MINT-1605675.
    STRINGi 9606.ENSP00000296417.

    PTM databases

    PhosphoSitei P0C0S5.

    Polymorphism databases

    DMDMi 83288408.

    Proteomic databases

    MaxQBi P0C0S5.
    PaxDbi P0C0S5.
    PRIDEi P0C0S5.

    Protocols and materials databases

    DNASUi 3015.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296417 ; ENSP00000296417 ; ENSG00000164032 .
    GeneIDi 3015.
    KEGGi hsa:3015.
    UCSCi uc003hvo.1. human.

    Organism-specific databases

    CTDi 3015.
    GeneCardsi GC04M100869.
    HGNCi HGNC:4741. H2AFZ.
    HPAi CAB022549.
    HPA045242.
    MIMi 142763. gene.
    neXtProti NX_P0C0S5.
    PharmGKBi PA29119.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5262.
    HOGENOMi HOG000234652.
    HOVERGENi HBG009342.
    InParanoidi P0C0S5.
    KOi K11251.
    OMAi DPQRKGN.
    OrthoDBi EOG7M0NTR.
    PhylomeDBi P0C0S5.
    TreeFami TF354232.

    Enzyme and pathway databases

    Reactomei REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_172744. Condensation of Prophase Chromosomes.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    REACT_200808. PRC2 methylates histones and DNA.
    REACT_200827. SIRT1 negatively regulates rRNA Expression.
    REACT_200856. NoRC negatively regulates rRNA expression.
    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_27271. Meiotic recombination.
    REACT_75792. Meiotic synapsis.
    REACT_75925. Amyloids.
    REACT_7963. Packaging Of Telomere Ends.

    Miscellaneous databases

    ChiTaRSi H2AFZ. human.
    EvolutionaryTracei P0C0S5.
    GeneWikii H2AFZ.
    GenomeRNAii 3015.
    NextBioi 11952.
    PMAP-CutDB P0C0S5.
    PROi P0C0S5.
    SOURCEi Search...

    Gene expression databases

    Bgeei P0C0S5.
    CleanExi HS_H2AFZ.
    Genevestigatori P0C0S5.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR002119. Histone_H2A.
    [Graphical view ]
    Pfami PF00125. Histone. 1 hit.
    [Graphical view ]
    PRINTSi PR00620. HISTONEH2A.
    SMARTi SM00414. H2A. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    PROSITEi PS00046. HISTONE_H2A. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 96 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