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P0C5Z0

- H2AB2_HUMAN

UniProt

P0C5Z0 - H2AB2_HUMAN

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Protein

Histone H2A-Bbd type 2/3

Gene
H2AFB2
H2AFB3, H2ABBD, H2AFB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Atypical histone H2A which can replace conventional H2A in some nucleosomes and is associated with active transcription and mRNA processing. 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. Nucleosomes containing this histone are less rigid and organize less DNA than canonical nucleosomes in vivo. They are enriched in actively transcribed genes and associate with the elongating form of RNA polymerase. They associate with spliceosome components and are required for mRNA splicing. May participate in spermatogenesis.7 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. mRNA processing Source: UniProtKB
  2. nucleosome assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Organism-specific databases

Protein namesi
Recommended name:
Histone H2A-Bbd type 2/3
Alternative name(s):
H2A Barr body-deficient
Short name:
H2A.Bbd
Gene namesi
Name:H2AFB2
AND
Name:H2AFB3
Synonyms:H2ABBD, H2AFB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X
HGNCiHGNC:18298. H2AFB2.
HGNC:14455. H2AFB3.

Subcellular locationi

Nucleus. Chromosome
Note: Associated with the active X chromosome and with autosomes, while it is absent from the inactive X chromosome and excluded from Barr bodies.3 Publications

GO - Cellular componenti

  1. nuclear nucleosome Source: UniProtKB
  2. nucleus Source: UniProt
  3. transcriptionally active chromatin Source: UniProtKB

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29101.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 115115Histone H2A-Bbd type 2/3PRO_0000055321Add
BLAST

Proteomic databases

PaxDbiP0C5Z0.
PRIDEiP0C5Z0.

PTM databases

PhosphoSiteiP0C5Z0.

Expressioni

Tissue specificityi

Present in mature sperm.1 Publication

Gene expression databases

BgeeiP0C5Z0.
CleanExiHS_H2AFB2.
HS_H2AFB3.
GenevestigatoriP0C5Z0.

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. May be incorporated into a proportion of nucleosomes, replacing one or more H2A molecules.

Protein-protein interaction databases

MINTiMINT-6630756.
STRINGi9606.ENSP00000346509.

Structurei

3D structure databases

ProteinModelPortaliP0C5Z0.
SMRiP0C5Z0. Positions 25-109.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni87 – 11529Docking domainAdd
BLAST

Domaini

The docking domain is responsible for the weaker heterodimerization with H2B.1 Publication

Sequence similaritiesi

Belongs to the histone H2A family.

Phylogenomic databases

eggNOGiCOG5262.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP0C5Z0.
KOiK11251.
OMAiHTHAMTR.
OrthoDBiEOG7Z0JZT.
PhylomeDBiP0C5Z0.
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.

Sequencei

Sequence statusi: Complete.

P0C5Z0-1 [UniParc]FASTAAdd to Basket

« Hide

MPRRRRRRGS SGAGGRGRTC SRTVRAELSF SVSQVERSLR EGHYAQRLSR    50
TAPVYLAAVI EYLTAKVLEL AGNEAQNSGE RNITPLLLDM VVHNDRLLST 100
LFNTTTISQV APGED 115
Length:115
Mass (Da):12,713
Last modified:December 4, 2007 - v1
Checksum:iF7CA7588C2F57451
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF254576 mRNA. Translation: AAL01652.1.
BX276110 Genomic DNA. Translation: CAH71440.1.
BX682237 Genomic DNA. Translation: CAI41332.1.
CH471172 Genomic DNA. Translation: EAW72649.1.
BC101409 mRNA. Translation: AAI01410.1.
BC101415 mRNA. Translation: AAI01416.1.
BC101417 mRNA. Translation: AAI01418.1.
BC101418 mRNA. Translation: AAI01419.1.
BC130510 mRNA. Translation: AAI30511.1.
BC130512 mRNA. Translation: AAI30513.1.
BC134365 mRNA. Translation: AAI34366.1.
CCDSiCCDS35461.1.
CCDS35464.1.
RefSeqiNP_001017991.1. NM_001017991.2.
NP_542451.1. NM_080720.1.
UniGeneiHs.534498.
Hs.632841.

Genome annotation databases

EnsembliENST00000354514; ENSP00000346509; ENSG00000198307.
ENST00000369444; ENSP00000358452; ENSG00000185978.
ENST00000596716; ENSP00000472471; ENSG00000272571.
ENST00000599985; ENSP00000469402; ENSG00000273440.
GeneIDi474381.
83740.
KEGGihsa:474381.
hsa:83740.
UCSCiuc004fmu.3. human.

Polymorphism databases

DMDMi161784333.

Cross-referencesi

Web resourcesi

Wikipedia

Histone H2A entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF254576 mRNA. Translation: AAL01652.1 .
BX276110 Genomic DNA. Translation: CAH71440.1 .
BX682237 Genomic DNA. Translation: CAI41332.1 .
CH471172 Genomic DNA. Translation: EAW72649.1 .
BC101409 mRNA. Translation: AAI01410.1 .
BC101415 mRNA. Translation: AAI01416.1 .
BC101417 mRNA. Translation: AAI01418.1 .
BC101418 mRNA. Translation: AAI01419.1 .
BC130510 mRNA. Translation: AAI30511.1 .
BC130512 mRNA. Translation: AAI30513.1 .
BC134365 mRNA. Translation: AAI34366.1 .
CCDSi CCDS35461.1.
CCDS35464.1.
RefSeqi NP_001017991.1. NM_001017991.2.
NP_542451.1. NM_080720.1.
UniGenei Hs.534498.
Hs.632841.

3D structure databases

ProteinModelPortali P0C5Z0.
SMRi P0C5Z0. Positions 25-109.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-6630756.
STRINGi 9606.ENSP00000346509.

PTM databases

PhosphoSitei P0C5Z0.

Polymorphism databases

DMDMi 161784333.

Proteomic databases

PaxDbi P0C5Z0.
PRIDEi P0C5Z0.

Protocols and materials databases

DNASUi 474381.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000354514 ; ENSP00000346509 ; ENSG00000198307 .
ENST00000369444 ; ENSP00000358452 ; ENSG00000185978 .
ENST00000596716 ; ENSP00000472471 ; ENSG00000272571 .
ENST00000599985 ; ENSP00000469402 ; ENSG00000273440 .
GeneIDi 474381.
83740.
KEGGi hsa:474381.
hsa:83740.
UCSCi uc004fmu.3. human.

Organism-specific databases

CTDi 474381.
83740.
GeneCardsi GC0XM154689.
GC0XP154610.
HGNCi HGNC:18298. H2AFB2.
HGNC:14455. H2AFB3.
MIMi 300445. gene.
neXtProti NX_P0C5Z0.
PharmGKBi PA29101.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5262.
HOGENOMi HOG000234652.
HOVERGENi HBG009342.
InParanoidi P0C5Z0.
KOi K11251.
OMAi HTHAMTR.
OrthoDBi EOG7Z0JZT.
PhylomeDBi P0C5Z0.
TreeFami TF300137.

Miscellaneous databases

GeneWikii H2AFB2.
H2AFB3.
NextBioi 111701.
PROi P0C5Z0.
SOURCEi Search...

Gene expression databases

Bgeei P0C5Z0.
CleanExi HS_H2AFB2.
HS_H2AFB3.
Genevestigatori P0C5Z0.

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.
ProtoNeti Search...

Publicationsi

  1. "A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome."
    Chadwick B.P., Willard H.F.
    J. Cell Biol. 152:375-384(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
  5. "Nucleosomes containing the histone variant H2A.Bbd organize only 118 base pairs of DNA."
    Bao Y., Konesky K., Park Y.-J., Rosu S., Dyer P.N., Rangasamy D., Tremethick D.J., Laybourn P.J., Luger K.
    EMBO J. 23:3314-3324(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN.
  6. "Assembly and disassembly of nucleosome core particles containing histone variants by human nucleosome assembly protein I."
    Okuwaki M., Kato K., Shimahara H., Tate S., Nagata K.
    Mol. Cell. Biol. 25:10639-10651(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome."
    Doyen C.M., Montel F., Gautier T., Menoni H., Claudet C., Delacour-Larose M., Angelov D., Hamiche A., Bednar J., Faivre-Moskalenko C., Bouvet P., Dimitrov S.
    EMBO J. 25:4234-4244(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "ATP-dependent chromatin remodeling is required for base excision repair in conventional but not in variant H2A.Bbd nucleosomes."
    Menoni H., Gasparutto D., Hamiche A., Cadet J., Dimitrov S., Bouvet P., Angelov D.
    Mol. Cell. Biol. 27:5949-5956(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "H2A.Bbd: a quickly evolving hypervariable mammalian histone that destabilizes nucleosomes in an acetylation-independent way."
    Eirin-Lopez J.M., Ishibashi T., Ausio J.
    FASEB J. 22:316-326(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Quickly evolving histones, nucleosome stability and chromatin folding: all about histone H2A.Bbd."
    Gonzalez-Romero R., Mendez J., Ausio J., Eirin-Lopez J.M.
    Gene 413:1-7(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "H2A.Bbd: an X-chromosome-encoded histone involved in mammalian spermiogenesis."
    Ishibashi T., Li A., Eirin-Lopez J.M., Zhao M., Missiaen K., Abbott D.W., Meistrich M., Hendzel M.J., Ausio J.
    Nucleic Acids Res. 38:1780-1789(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  12. "Histone variant H2A.Bbd is associated with active transcription and mRNA processing in human cells."
    Tolstorukov M.Y., Goldman J.A., Gilbert C., Ogryzko V., Kingston R.E., Park P.J.
    Mol. Cell 47:596-607(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiH2AB2_HUMAN
AccessioniPrimary (citable) accession number: P0C5Z0
Secondary accession number(s): A1L4E4
, P98176, Q5TZB2, Q6FG78, Q96PR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 4, 2007
Last modified: July 9, 2014
This is version 56 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

Miscellaneous

In contrast to other H2A histones, it does not contain the conserved residues that are the target of post-translational modifications.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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