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P0C5Z0 (H2AB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H2A-Bbd type 2/3
Alternative name(s):
H2A Barr body-deficient
Short name=H2A.Bbd
Gene names
Name:H2AFB2
AND
Name:H2AFB3
Synonyms:H2ABBD, H2AFB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length115 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12

Subunit structure

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.

Subcellular location

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. Ref.1 Ref.11 Ref.12

Tissue specificity

Present in mature sperm. Ref.11

Domain

The docking domain is responsible for the weaker heterodimerization with H2B. Ref.5

Miscellaneous

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

Sequence similarities

Belongs to the histone H2A family.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentChromosome
Nucleosome core
Nucleus
   LigandDNA-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmRNA processing

Inferred from mutant phenotype Ref.12. Source: UniProtKB

nucleosome assembly

Inferred from direct assay Ref.12. Source: UniProtKB

   Cellular_componentnuclear nucleosome

Inferred from direct assay Ref.12. Source: UniProtKB

transcriptionally active chromatin

Inferred from direct assay Ref.12. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 115115Histone H2A-Bbd type 2/3
PRO_0000055321

Regions

Region87 – 11529Docking domain

Sequences

Sequence LengthMass (Da)Tools
P0C5Z0 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: F7CA7588C2F57451

FASTA11512,713
        10         20         30         40         50         60 
MPRRRRRRGS SGAGGRGRTC SRTVRAELSF SVSQVERSLR EGHYAQRLSR TAPVYLAAVI 

        70         80         90        100        110 
EYLTAKVLEL AGNEAQNSGE RNITPLLLDM VVHNDRLLST LFNTTTISQV APGED 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.

Web resources

Wikipedia

Histone H2A entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001017991.1. NM_001017991.2.
NP_542451.1. NM_080720.1.
UniGeneHs.534498.
Hs.632841.

3D structure databases

ProteinModelPortalP0C5Z0.
SMRP0C5Z0. Positions 25-109.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-6630756.
STRING9606.ENSP00000346509.

PTM databases

PhosphoSiteP0C5Z0.

Polymorphism databases

DMDM161784333.

Proteomic databases

PaxDbP0C5Z0.
PRIDEP0C5Z0.

Protocols and materials databases

DNASU474381.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354514; ENSP00000346509; ENSG00000198307.
ENST00000369444; ENSP00000358452; ENSG00000185978.
ENST00000596716; ENSP00000472471; ENSG00000272571.
ENST00000599985; ENSP00000469402; ENSG00000273440.
GeneID474381.
83740.
KEGGhsa:474381.
hsa:83740.
UCSCuc004fmu.3. human.

Organism-specific databases

CTD474381.
83740.
GeneCardsGC0XM154689.
GC0XP154610.
HGNCHGNC:18298. H2AFB2.
HGNC:14455. H2AFB3.
MIM300445. gene.
neXtProtNX_P0C5Z0.
PharmGKBPA29101.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5262.
HOGENOMHOG000234652.
HOVERGENHBG009342.
InParanoidP0C5Z0.
KOK11251.
OMAVDMAVHN.
OrthoDBEOG7Z0JZT.
PhylomeDBP0C5Z0.
TreeFamTF300137.

Gene expression databases

BgeeP0C5Z0.
CleanExHS_H2AFB2.
HS_H2AFB3.
GenevestigatorP0C5Z0.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view]
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00620. HISTONEH2A.
SMARTSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
ProtoNetSearch...

Other

GeneWikiH2AFB2.
H2AFB3.
NextBio111701.
PROP0C5Z0.
SOURCESearch...

Entry information

Entry nameH2AB2_HUMAN
AccessionPrimary (citable) accession number: P0C5Z0
Secondary accession number(s): A1L4E4 expand/collapse secondary AC list , P98176, Q5TZB2, Q6FG78, Q96PR7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 4, 2007
Last modified: April 16, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM