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O75367

- H2AY_HUMAN

UniProt

O75367 - H2AY_HUMAN

Protein

Core histone macro-H2A.1

Gene

H2AFY

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. 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. Involved in stable X chromosome inactivation. Inhibits the binding of transcription factors and interferes with the activity of remodeling SWI/SNF complexes. Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin. In addition, isoform 1, but not isoform 2, binds ADP-ribose and O-acetyl-ADP-ribose, and may be involved in ADP-ribose-mediated chromatin modulation.5 Publications

    GO - Molecular functioni

    1. chromatin DNA binding Source: UniProt
    2. DNA binding Source: UniProtKB
    3. double-stranded methylated DNA binding Source: UniProt
    4. protein binding Source: IntAct
    5. protein kinase binding Source: UniProt
    6. protein serine/threonine kinase inhibitor activity Source: UniProt
    7. rDNA binding Source: UniProt
    8. transcription regulatory region DNA binding Source: UniProt

    GO - Biological processi

    1. chromatin modification Source: UniProtKB-KW
    2. dosage compensation Source: MGI
    3. establishment of protein localization to chromatin Source: UniProt
    4. negative regulation of cell cycle G2/M phase transition Source: UniProt
    5. negative regulation of gene expression, epigenetic Source: UniProt
    6. negative regulation of histone phosphorylation Source: UniProt
    7. negative regulation of protein serine/threonine kinase activity Source: UniProt
    8. negative regulation of transcription from RNA polymerase II promoter Source: UniProt
    9. negative regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter Source: UniProt
    10. nucleosome assembly Source: UniProtKB

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Core histone macro-H2A.1
    Short name:
    Histone macroH2A1
    Short name:
    mH2A1
    Alternative name(s):
    Histone H2A.y
    Short name:
    H2A/y
    Medulloblastoma antigen MU-MB-50.205
    Gene namesi
    Name:H2AFY
    Synonyms:MACROH2A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:4740. H2AFY.

    Subcellular locationi

    Nucleus. Chromosome
    Note: Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin.

    GO - Cellular componenti

    1. Barr body Source: MGI
    2. condensed chromosome Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. nuclear chromatin Source: UniProt
    5. nucleolus Source: UniProt
    6. nucleosome Source: UniProtKB
    7. nucleus Source: UniProt
    8. sex chromatin Source: BHF-UCL

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29117.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 372372Core histone macro-H2A.1PRO_0000055318Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei18 – 181N6-methyllysine1 Publication
    Modified residuei116 – 1161N6-acetyllysine; alternateBy similarity
    Cross-linki116 – 116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
    Cross-linki117 – 117Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei123 – 1231N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei123 – 1231N6-acetyllysine; alternateBy similarity
    Modified residuei129 – 1291Phosphothreonine6 Publications
    Modified residuei170 – 1701Phosphoserine3 Publications
    Modified residuei173 – 1731Phosphoserine1 Publication
    Modified residuei178 – 1781Phosphothreonine4 Publications

    Post-translational modificationi

    Monoubiquitinated at either Lys-116 or Lys-117. May also be polyubiquitinated. Ubiquitination is mediated by the CUL3/SPOP E3 complex and does not promote proteasomal degradation. Instead, it is required for enrichment in inactive X chromosome chromatin.3 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO75367.
    PaxDbiO75367.
    PRIDEiO75367.

    2D gel databases

    SWISS-2DPAGEO75367.

    PTM databases

    PhosphoSiteiO75367.

    Miscellaneous databases

    PMAP-CutDBO75367.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiO75367.
    BgeeiO75367.
    CleanExiHS_H2AFY.
    GenevestigatoriO75367.

    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. Interacts with HDAC1 and HDAC2 By similarity. Interacts with SPOP. Part of a complex consisting of H2AFY, CUL3 and SPOP.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERBB2P046266EBI-2868511,EBI-641062

    Protein-protein interaction databases

    BioGridi114927. 37 interactions.
    DIPiDIP-44283N.
    IntActiO75367. 6 interactions.
    MINTiMINT-2866965.
    STRINGi9606.ENSP00000353806.

    Structurei

    Secondary structure

    1
    372
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 195
    Helixi25 – 3511
    Beta strandi36 – 383
    Beta strandi39 – 413
    Helixi44 – 7027
    Beta strandi74 – 763
    Helixi78 – 869
    Helixi89 – 946
    Turni95 – 973
    Beta strandi98 – 1003
    Helixi111 – 1133
    Beta strandi174 – 1774
    Beta strandi185 – 1906
    Beta strandi196 – 2027
    Helixi204 – 2063
    Beta strandi213 – 2197
    Helixi227 – 25226
    Beta strandi260 – 2645
    Beta strandi268 – 27710
    Helixi286 – 30318
    Beta strandi307 – 3115
    Beta strandi315 – 3195
    Helixi323 – 34018
    Beta strandi341 – 3433
    Beta strandi348 – 3558
    Helixi356 – 36712

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U35X-ray3.00C/G1-120[»]
    1ZR3X-ray1.66A/B/C/D162-372[»]
    1ZR5X-ray2.92A/B161-372[»]
    2F8NX-ray2.90G1-120[»]
    2FXKX-ray2.54A/B162-372[»]
    3HQHX-ray2.30M167-181[»]
    3HSVX-ray1.43M172-186[»]
    3IIDX-ray1.90A162-372[»]
    3IIFX-ray2.10A/B/C162-372[»]
    3IVBX-ray1.75M167-181[»]
    ProteinModelPortaliO75367.
    SMRiO75367. Positions 10-117, 181-369.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75367.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 117116Histone H2AAdd
    BLAST
    Domaini184 – 370187MacroPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi118 – 16245Lys-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 histone H2A domain.Curated
    Contains 1 Macro domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2110.
    HOVERGENiHBG009342.
    InParanoidiO75367.
    KOiK11251.
    OMAiQVVQADI.
    OrthoDBiEOG71G9VP.
    PhylomeDBiO75367.
    TreeFamiTF332276.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR021171. Core_histone_macro-H2A.
    IPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR002119. Histone_H2A.
    IPR002589. Macro_dom.
    [Graphical view]
    PfamiPF00125. Histone. 1 hit.
    PF01661. Macro. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037942. Core_histone_macro-H2A. 1 hit.
    PRINTSiPR00620. HISTONEH2A.
    SMARTiSM00506. A1pp. 1 hit.
    SM00414. H2A. 1 hit.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.
    PROSITEiPS51154. MACRO. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: O75367-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA    50
    AVLEYLTAEI LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI 100
    ASGGVLPNIH PELLAKKRGS KGKLEAIITP PPAKKAKSPS QKKPVSKKAG 150
    GKKGARKSKK KQGEVSKAAS ADSTTEGTPA DGFTVLSTKS LFLGQKLNLI 200
    HSEISNLAGF EVEAIINPTN ADIDLKDDLG NTLEKKGGKE FVEAVLELRK 250
    KNGPLEVAGA AVSAGHGLPA KFVIHCNSPV WGADKCEELL EKTVKNCLAL 300
    ADDKKLKSIA FPSIGSGRNG FPKQTAAQLI LKAISSYFVS TMSSSIKTVY 350
    FVLFDSESIG IYVQEMAKLD AN 372
    Length:372
    Mass (Da):39,617
    Last modified:January 23, 2007 - v4
    Checksum:i37DED989EF7E69DC
    GO
    Isoform 1 (identifier: O75367-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         198-229: NLIHSEISNLAGFEVEAIINPTNADIDLKDDL → QVVQADIASIDSDAVVHPTNTDFYIGGEV

    Note: Specifically binds ADP-ribose and O-acetyl-ADP-ribose. Important residues for binding are Asp-203, Gly-224, Gly-314 and Phe-348.

    Show »
    Length:369
    Mass (Da):39,184
    Checksum:iD21A4CE6C7AA3BB1
    GO
    Isoform 3 (identifier: O75367-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         159-159: Missing.

    Show »
    Length:371
    Mass (Da):39,489
    Checksum:i54320BFD118454D1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti186 – 1861L → F in BAB14565. (PubMed:14702039)Curated
    Sequence conflicti210 – 2101F → S in BAB14565. (PubMed:14702039)Curated
    Sequence conflicti225 – 2251L → P in AAC33433. (PubMed:9714746)Curated
    Sequence conflicti291 – 2911E → G in AAH95406. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei159 – 1591Missing in isoform 3. 2 PublicationsVSP_038379
    Alternative sequencei198 – 22932NLIHS…LKDDL → QVVQADIASIDSDAVVHPTN TDFYIGGEV in isoform 1. 1 PublicationVSP_002056Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF041483 mRNA. Translation: AAC33433.1.
    AF044286 mRNA. Translation: AAC33434.1.
    AF054174 mRNA. Translation: AAC39908.1.
    AK023409 mRNA. Translation: BAB14565.1.
    AC026691 Genomic DNA. No translation available.
    BC013331 mRNA. Translation: AAH13331.1.
    BC095406 mRNA. Translation: AAH95406.1.
    AY134746 mRNA. Translation: AAN08620.1.
    CCDSiCCDS4183.1. [O75367-3]
    CCDS4184.1. [O75367-2]
    CCDS4185.1. [O75367-1]
    RefSeqiNP_001035248.1. NM_001040158.1. [O75367-3]
    NP_004884.1. NM_004893.2. [O75367-3]
    NP_613075.1. NM_138609.2. [O75367-2]
    NP_613258.2. NM_138610.2. [O75367-1]
    UniGeneiHs.420272.
    Hs.599225.

    Genome annotation databases

    EnsembliENST00000304332; ENSP00000302572; ENSG00000113648. [O75367-3]
    ENST00000312469; ENSP00000310169; ENSG00000113648. [O75367-2]
    ENST00000510038; ENSP00000424971; ENSG00000113648. [O75367-1]
    ENST00000511689; ENSP00000423563; ENSG00000113648. [O75367-1]
    GeneIDi9555.
    KEGGihsa:9555.
    UCSCiuc003lam.1. human. [O75367-1]
    uc003lan.1. human. [O75367-2]
    uc003lao.1. human. [O75367-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF041483 mRNA. Translation: AAC33433.1 .
    AF044286 mRNA. Translation: AAC33434.1 .
    AF054174 mRNA. Translation: AAC39908.1 .
    AK023409 mRNA. Translation: BAB14565.1 .
    AC026691 Genomic DNA. No translation available.
    BC013331 mRNA. Translation: AAH13331.1 .
    BC095406 mRNA. Translation: AAH95406.1 .
    AY134746 mRNA. Translation: AAN08620.1 .
    CCDSi CCDS4183.1. [O75367-3 ]
    CCDS4184.1. [O75367-2 ]
    CCDS4185.1. [O75367-1 ]
    RefSeqi NP_001035248.1. NM_001040158.1. [O75367-3 ]
    NP_004884.1. NM_004893.2. [O75367-3 ]
    NP_613075.1. NM_138609.2. [O75367-2 ]
    NP_613258.2. NM_138610.2. [O75367-1 ]
    UniGenei Hs.420272.
    Hs.599225.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U35 X-ray 3.00 C/G 1-120 [» ]
    1ZR3 X-ray 1.66 A/B/C/D 162-372 [» ]
    1ZR5 X-ray 2.92 A/B 161-372 [» ]
    2F8N X-ray 2.90 G 1-120 [» ]
    2FXK X-ray 2.54 A/B 162-372 [» ]
    3HQH X-ray 2.30 M 167-181 [» ]
    3HSV X-ray 1.43 M 172-186 [» ]
    3IID X-ray 1.90 A 162-372 [» ]
    3IIF X-ray 2.10 A/B/C 162-372 [» ]
    3IVB X-ray 1.75 M 167-181 [» ]
    ProteinModelPortali O75367.
    SMRi O75367. Positions 10-117, 181-369.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114927. 37 interactions.
    DIPi DIP-44283N.
    IntActi O75367. 6 interactions.
    MINTi MINT-2866965.
    STRINGi 9606.ENSP00000353806.

    PTM databases

    PhosphoSitei O75367.

    2D gel databases

    SWISS-2DPAGE O75367.

    Proteomic databases

    MaxQBi O75367.
    PaxDbi O75367.
    PRIDEi O75367.

    Protocols and materials databases

    DNASUi 9555.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000304332 ; ENSP00000302572 ; ENSG00000113648 . [O75367-3 ]
    ENST00000312469 ; ENSP00000310169 ; ENSG00000113648 . [O75367-2 ]
    ENST00000510038 ; ENSP00000424971 ; ENSG00000113648 . [O75367-1 ]
    ENST00000511689 ; ENSP00000423563 ; ENSG00000113648 . [O75367-1 ]
    GeneIDi 9555.
    KEGGi hsa:9555.
    UCSCi uc003lam.1. human. [O75367-1 ]
    uc003lan.1. human. [O75367-2 ]
    uc003lao.1. human. [O75367-3 ]

    Organism-specific databases

    CTDi 9555.
    GeneCardsi GC05M134669.
    HGNCi HGNC:4740. H2AFY.
    MIMi 610054. gene.
    neXtProti NX_O75367.
    PharmGKBi PA29117.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2110.
    HOVERGENi HBG009342.
    InParanoidi O75367.
    KOi K11251.
    OMAi QVVQADI.
    OrthoDBi EOG71G9VP.
    PhylomeDBi O75367.
    TreeFami TF332276.

    Miscellaneous databases

    ChiTaRSi H2AFY. human.
    EvolutionaryTracei O75367.
    GeneWikii H2AFY.
    GenomeRNAii 9555.
    NextBioi 35835.
    PMAP-CutDB O75367.
    PROi O75367.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75367.
    Bgeei O75367.
    CleanExi HS_H2AFY.
    Genevestigatori O75367.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR021171. Core_histone_macro-H2A.
    IPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR002119. Histone_H2A.
    IPR002589. Macro_dom.
    [Graphical view ]
    Pfami PF00125. Histone. 1 hit.
    PF01661. Macro. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037942. Core_histone_macro-H2A. 1 hit.
    PRINTSi PR00620. HISTONEH2A.
    SMARTi SM00506. A1pp. 1 hit.
    SM00414. H2A. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    PROSITEi PS51154. MACRO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of cDNA clones encoding human histone macroH2A1 subtypes."
      Lee Y., Hong M., Kim J.W., Hong Y.M., Choe Y.-K., Chang S.Y., Lee K.S., Choe I.S.
      Biochim. Biophys. Acta 1399:73-77(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
      Tissue: Liver.
    2. "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
      Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
      Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
      Tissue: Umbilical cord blood.
    3. "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] (ISOFORM 2).
      Tissue: Ovary.
    4. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 2).
      Tissue: Bone marrow and Placenta.
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-372 (ISOFORM 3).
      Tissue: Medulloblastoma.
    7. "Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals."
      Costanzi C., Pehrson J.R.
      Nature 393:599-601(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. "The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling."
      Angelov D., Molla A., Perche P.-Y., Hans F., Cote J., Khochbin S., Bouvet P., Dimitrov S.
      Mol. Cell 11:1033-1041(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Histone variant macroH2A1.2 is mono-ubiquitinated at its histone domain."
      Ogawa Y., Ono T., Wakata Y., Okawa K., Tagami H., Shibahara K.
      Biochem. Biophys. Res. Commun. 336:204-209(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-116 AND LYS-117, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "Formation of MacroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA."
      Zhang R., Poustovoitov M.V., Ye X., Santos H.A., Chen W., Daganzo S.M., Erzberger J.P., Serebriiskii I.G., Canutescu A.A., Dunbrack R.L., Pehrson J.R., Berger J.M., Kaufman P.D., Adams P.D.
      Dev. Cell 8:19-30(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. Cited for: BINDING TO ADP-RIBOSE (ISOFORM 1).
    12. "Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase."
      Hernandez-Munoz I., Lund A.H., van der Stoop P., Boutsma E., Muijrers I., Verhoeven E., Nusinow D.A., Panning B., Marahrens Y., van Lohuizen M.
      Proc. Natl. Acad. Sci. U.S.A. 102:7635-7640(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH CULLIN3 AND SPOP, UBIQUITINATION, SUBCELLULAR LOCATION, FUNCTION.
    13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Mechanism of polymerase II transcription repression by the histone variant macroH2A."
      Doyen C.-M., An W., Angelov D., Bondarenko V., Mietton F., Studitsky V.M., Hamiche A., Roeder R.G., Bouvet P., Dimitrov S.
      Mol. Cell. Biol. 26:1156-1164(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Mapping post-translational modifications of the histone variant MacroH2A1 using tandem mass spectrometry."
      Chu F., Nusinow D.A., Chalkley R.J., Plath K., Panning B., Burlingame A.L.
      Mol. Cell. Proteomics 5:194-203(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-18 AND LYS-123, PHOSPHORYLATION AT THR-129, IDENTIFICATION BY MASS SPECTROMETRY.
    16. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; SER-170; SER-173 AND THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-120 IN COMPLEX WITH THE NUCLEOSOME CORE PARTICLE, FUNCTION.
    23. Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 162-372 (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 161-372 (ISOFORM 2), BINDING TO ADP-RIBOSE AND O-ACETYL-ADP-RIBOSE (ISOFORM 1).
    24. "Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases."
      Zhuang M., Calabrese M.F., Liu J., Waddell M.B., Nourse A., Hammel M., Miller D.J., Walden H., Duda D.M., Seyedin S.N., Hoggard T., Harper J.W., White K.P., Schulman B.A.
      Mol. Cell 36:39-50(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 172-186 IN COMPLEXES WITH SPOP, SUBUNIT, UBIQUITINATION.

    Entry informationi

    Entry nameiH2AY_HUMAN
    AccessioniPrimary (citable) accession number: O75367
    Secondary accession number(s): O75377
    , Q503A8, Q7Z5E3, Q96D41, Q9H8P3, Q9UP96
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 149 of the entry and version 4 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

    Miscellaneous

    The number of individuals with antibodies against this antigen is 2-fold higher in pediatric patients with cancer compared to healthy controls.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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