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Q9BTM1

- H2AJ_HUMAN

UniProt

Q9BTM1 - H2AJ_HUMAN

Protein

Histone H2A.J

Gene

H2AFJ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Core component of nucleosome. 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.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. nucleosome assembly Source: InterPro

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone H2A.J
    Short name:
    H2a/j
    Gene namesi
    Name:H2AFJ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:14456. H2AFJ.

    Subcellular locationi

    Nucleus By similarity. Chromosome By similarity

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. nucleosome Source: UniProtKB-KW
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29108.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 129128Histone H2A.JPRO_0000344247Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei2 – 21PhosphoserineBy similarity
    Modified residuei6 – 61N6-acetyllysineBy similarity
    Modified residuei10 – 101N6-acetyllysineBy similarity
    Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki16 – 16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei105 – 1051N5-methylglutamineBy similarity
    Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei121 – 1211Phosphothreonine; by VPRBPBy similarity
    Modified residuei123 – 1231PhosphoserineBy similarity

    Post-translational modificationi

    Monoubiquitination of Lys-120 (H2AXK119ub) gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties By similarity.By similarity
    Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by VPRBP is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription By similarity.By similarity
    Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ9BTM1.
    PRIDEiQ9BTM1.

    PTM databases

    PhosphoSiteiQ9BTM1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BTM1.
    BgeeiQ9BTM1.
    CleanExiHS_H2AFJ.
    GenevestigatoriQ9BTM1.

    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.

    Protein-protein interaction databases

    BioGridi120884. 5 interactions.
    IntActiQ9BTM1. 15 interactions.
    MINTiMINT-5001944.
    STRINGi9606.ENSP00000373730.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4EDUX-ray2.58T31-46[»]
    ProteinModelPortaliQ9BTM1.
    SMRiQ9BTM1. Positions 14-119.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histone H2A family.Curated

    Phylogenomic databases

    eggNOGiCOG5262.
    HOGENOMiHOG000234652.
    HOVERGENiHBG009342.
    KOiK11251.
    OMAiANEMFIN.
    OrthoDBiEOG7M0NTR.
    PhylomeDBiQ9BTM1.
    TreeFamiTF300137.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BTM1-1) [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

    MSGRGKQGGK VRAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV    50
    YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK 100
    VTIAQGGVLP NIQAVLLPKK TESQKTKSK 129
    Length:129
    Mass (Da):14,019
    Last modified:June 1, 2001 - v1
    Checksum:iE35049617B456D45
    GO
    Isoform 2 (identifier: Q9BTM1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         119-129: KKTESQKTKSK → VCEHSGPSSGKIPSDRAELGAGSVCGHIFQKVE

    Show »
    Length:151
    Mass (Da):16,110
    Checksum:i5CD96E044A740AB5
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei119 – 12911KKTESQKTKSK → VCEHSGPSSGKIPSDRAELG AGSVCGHIFQKVE in isoform 2. 1 PublicationVSP_034750Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK001765 mRNA. Translation: BAA91894.1.
    CH471094 Genomic DNA. Translation: EAW96326.1.
    BC003602 mRNA. Translation: AAH03602.1.
    CCDSiCCDS31752.1. [Q9BTM1-1]
    RefSeqiNP_808760.1. NM_177925.3. [Q9BTM1-1]
    UniGeneiHs.524280.

    Genome annotation databases

    EnsembliENST00000389078; ENSP00000373730; ENSG00000246705. [Q9BTM1-1]
    ENST00000544848; ENSP00000438553; ENSG00000246705. [Q9BTM1-1]
    GeneIDi55766.
    KEGGihsa:55766.
    UCSCiuc009zia.3. human. [Q9BTM1-1]

    Polymorphism databases

    DMDMi74733131.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK001765 mRNA. Translation: BAA91894.1 .
    CH471094 Genomic DNA. Translation: EAW96326.1 .
    BC003602 mRNA. Translation: AAH03602.1 .
    CCDSi CCDS31752.1. [Q9BTM1-1 ]
    RefSeqi NP_808760.1. NM_177925.3. [Q9BTM1-1 ]
    UniGenei Hs.524280.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4EDU X-ray 2.58 T 31-46 [» ]
    ProteinModelPortali Q9BTM1.
    SMRi Q9BTM1. Positions 14-119.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120884. 5 interactions.
    IntActi Q9BTM1. 15 interactions.
    MINTi MINT-5001944.
    STRINGi 9606.ENSP00000373730.

    PTM databases

    PhosphoSitei Q9BTM1.

    Polymorphism databases

    DMDMi 74733131.

    Proteomic databases

    PaxDbi Q9BTM1.
    PRIDEi Q9BTM1.

    Protocols and materials databases

    DNASUi 55766.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389078 ; ENSP00000373730 ; ENSG00000246705 . [Q9BTM1-1 ]
    ENST00000544848 ; ENSP00000438553 ; ENSG00000246705 . [Q9BTM1-1 ]
    GeneIDi 55766.
    KEGGi hsa:55766.
    UCSCi uc009zia.3. human. [Q9BTM1-1 ]

    Organism-specific databases

    CTDi 55766.
    GeneCardsi GC12P014827.
    HGNCi HGNC:14456. H2AFJ.
    neXtProti NX_Q9BTM1.
    PharmGKBi PA29108.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5262.
    HOGENOMi HOG000234652.
    HOVERGENi HBG009342.
    KOi K11251.
    OMAi ANEMFIN.
    OrthoDBi EOG7M0NTR.
    PhylomeDBi Q9BTM1.
    TreeFami TF300137.

    Miscellaneous databases

    GeneWikii H2AFJ.
    GenomeRNAii 55766.
    NextBioi 60813.
    PROi Q9BTM1.

    Gene expression databases

    ArrayExpressi Q9BTM1.
    Bgeei Q9BTM1.
    CleanExi HS_H2AFJ.
    Genevestigatori Q9BTM1.

    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. "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: Ovarian carcinoma.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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 1).
      Tissue: Eye.

    Entry informationi

    Entry nameiH2AJ_HUMAN
    AccessioniPrimary (citable) accession number: Q9BTM1
    Secondary accession number(s): Q9NV63
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 22, 2008
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 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 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3