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Q9BTM1

- H2AJ_HUMAN

UniProt

Q9BTM1 - H2AJ_HUMAN

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Protein

Histone H2A.J

Gene

H2AFJ

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

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
Complete GO annotation...

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: UniProtKB
  2. nucleosome Source: UniProtKB-KW
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

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

BgeeiQ9BTM1.
CleanExiHS_H2AFJ.
ExpressionAtlasiQ9BTM1. baseline and differential.
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.
GeneTreeiENSGT00760000118934.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiQ9BTM1.
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

        10         20         30         40         50
MSGRGKQGGK VRAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV
60 70 80 90 100
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK
110 120
VTIAQGGVLP NIQAVLLPKK TESQKTKSK
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.
GeneTreei ENSGT00760000118934.
HOGENOMi HOG000234652.
HOVERGENi HBG009342.
InParanoidi Q9BTM1.
KOi K11251.
OMAi ANEMFIN.
OrthoDBi EOG7M0NTR.
PhylomeDBi Q9BTM1.
TreeFami TF300137.

Miscellaneous databases

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

Gene expression databases

Bgeei Q9BTM1.
CleanExi HS_H2AFJ.
ExpressionAtlasi Q9BTM1. baseline and differential.
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 29, 2014
This is version 102 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