P0C5Z0 (H2AB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	115 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	mRNA processing
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA processing Inferred from mutant phenotype Ref.12. Source: UniProtKB nucleosome assembly Inferred from direct assay Ref.12. Source: UniProtKB
Cellular_component	nuclear nucleosome Inferred from direct assay Ref.12. Source: UniProtKB transcriptionally active chromatin Inferred from direct assay Ref.12. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 115	115	Histone H2A-Bbd type 2/3		PRO_0000055321
Regions
	Region	87 – 115	29	Docking domain

Sequences

	Sequence		Length	Mass (Da)
	P0C5Z0 [UniParc]. Last modified December 4, 2007. Version 1. Checksum: F7CA7588C2F57451	FASTA	115	12,713
	10 20 30 40 50 60 MPRRRRRRGS SGAGGRGRTC SRTVRAELSF SVSQVERSLR EGHYAQRLSR TAPVYLAAVI 70 80 90 100 110 EYLTAKVLEL AGNEAQNSGE RNITPLLLDM VVHNDRLLST LFNTTTISQV APGED

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00044631.
RefSeq	NP_001017991.1. NM_001017991.1. NP_542451.1. NM_080720.1.
UniGene	Hs.534498. Hs.632841.
3D structure databases
ProteinModelPortal	P0C5Z0.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000346509.
PTM databases
PhosphoSite	P0C5Z0.
Proteomic databases
PaxDb	P0C5Z0.
PRIDE	P0C5Z0.
Protocols and materials databases
DNASU	474381.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000354514; ENSP00000346509; ENSG00000198307. ENST00000369444; ENSP00000358452; ENSG00000185978. ENST00000596716; ENSP00000472471; ENSG00000268901. ENST00000599985; ENSP00000469402; ENSG00000267863.
GeneID	474381. 83740.
KEGG	hsa:474381. hsa:83740.
UCSC	uc004fmu.3. human.
Organism-specific databases
CTD	474381. 83740.
GeneCards	GC0XM154689. GC0XP154610.
HGNC	HGNC:18298. H2AFB2. HGNC:14455. H2AFB3.
MIM	300445. gene.
neXtProt	NX_P0C5Z0.
PharmGKB	PA29101.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5262.
HOGENOM	HOG000234652.
HOVERGEN	HBG009342.
InParanoid	P0C5Z0.
KO	K11251.
OMA	VDMAVHN.
OrthoDB	EOG4KWJVH.
PhylomeDB	P0C5Z0.
Gene expression databases
Bgee	P0C5Z0.
CleanEx	HS_H2AFB2. HS_H2AFB3.
Genevestigator	P0C5Z0.
GermOnline	ENSG00000185978. Homo sapiens. ENSG00000198307. Homo sapiens.
Family and domain databases
Gene3D	1.10.20.10. 1 hit.
InterPro	IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR002119. Histone_H2A. [Graphical view]
Pfam	PF00125. Histone. 1 hit. [Graphical view]
PRINTS	PR00620. HISTONEH2A.
SMART	SM00414. H2A. 1 hit. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
PROSITE	PS00046. HISTONE_H2A. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	111701.
SOURCE	Search...

Entry information

Entry name

H2AB2_HUMAN

Accession

Primary (citable) accession number: P0C5Z0
Secondary accession number(s): A1L4E4 , P98176, Q5TZB2, Q6FG78, Q96PR7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 4, 2007
Last sequence update:	December 4, 2007
Last modified:	May 1, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.