Q96A08 (H2B1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H2B type 1-A

Alternative name(s):
Histone H2B, testis
Testis-specific histone H2B

Gene names

Name:	HIST1H2BA
Synonyms:	TSH2B

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	127 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
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. The octamer wraps approximately 147 bp of DNA.
Subcellular location	Nucleus. Chromosome.
Tissue specificity	Transcribed exclusively in testis, and the corresponding protein is also present in mature sperm. Ref.1
Post-translational modification	Monoubiquitination at Lys-36 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-122 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. Ref.10
Sequence similarities	Belongs to the histone H2B family.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to acid Inferred from electronic annotation. Source: Compara inflammatory response Inferred from electronic annotation. Source: Compara mononuclear cell migration Inferred from electronic annotation. Source: Compara nucleosome assembly Inferred from electronic annotation. Source: InterPro plasminogen activation Inferred from electronic annotation. Source: Compara positive regulation of binding Inferred from electronic annotation. Source: Compara
Cellular_component	extrinsic to plasma membrane Inferred from electronic annotation. Source: Compara nucleosome Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 127	126	Histone H2B type 1-A		PRO_0000071842
Amino acid modifications
	Modified residue	2	1	N-acetylproline By similarity
	Modified residue	7	1	N6-acetyllysine; alternate Ref.8
	Modified residue	7	1	N6-crotonyl-L-lysine; alternate Ref.10
	Modified residue	13	1	N6-acetyllysine; alternate By similarity
	Modified residue	13	1	N6-crotonyl-L-lysine; alternate Ref.10
	Modified residue	14	1	N6-acetyllysine; alternate Ref.8
	Modified residue	14	1	N6-crotonyl-L-lysine; alternate Ref.10
	Modified residue	17	1	N6-acetyllysine; alternate Ref.8
	Modified residue	17	1	N6-crotonyl-L-lysine; alternate Ref.10
	Modified residue	18	1	N6-acetyllysine; alternate By similarity
	Modified residue	18	1	N6-crotonyl-L-lysine; alternate Ref.10
	Modified residue	22	1	N6-acetyllysine; alternate Ref.8
	Modified residue	22	1	N6-crotonyl-L-lysine; alternate
	Modified residue	25	1	N6-acetyllysine; alternate By similarity
	Modified residue	25	1	N6-crotonyl-L-lysine; alternate Ref.10
	Modified residue	36	1	N6-acetyllysine; alternate By similarity
	Modified residue	36	1	N6-crotonyl-L-lysine; alternate Ref.10
	Modified residue	38	1	Phosphoserine By similarity
	Modified residue	44	1	Phosphotyrosine By similarity
	Modified residue	48	1	N6-acetyllysine; alternate By similarity
	Modified residue	48	1	N6-methyllysine; alternate By similarity
	Modified residue	59	1	N6,N6-dimethyllysine By similarity
	Modified residue	77	1	Phosphoserine By similarity
	Modified residue	80	1	Phosphoserine By similarity
	Modified residue	87	1	N6-acetyllysine By similarity
	Modified residue	110	1	N6-acetyllysine; alternate By similarity
	Modified residue	110	1	N6-methyllysine; alternate By similarity
	Modified residue	114	1	Phosphoserine By similarity
	Modified residue	118	1	N6-acetyllysine By similarity
	Modified residue	122	1	N6-acetyllysine; alternate By similarity
	Cross-link	36		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
	Cross-link	122		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.7 Ref.9
Experimental info
	Sequence conflict	2	1	P → A in AAH66243. Ref.6
	Sequence conflict	22	1	K → E in AAH66241. Ref.6
	Sequence conflict	80	1	S → P in AAH66240. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q96A08 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 3EE4124DA9B3C3E8	FASTA	127	14,167
	10 20 30 40 50 60 MPEVSSKGAT ISKKGFKKAV VKTQKKEGKK RKRTRKESYS IYIYKVLKQV HPDTGISSKA 70 80 90 100 110 120 MSIMNSFVTD IFERIASEAS RLAHYSKRST ISSREIQTAV RLLLPGELAK HAVSEGTKAV TKYTSSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human testis/sperm-specific histone H2B (hTSH2B). Molecular cloning and characterization." Zalensky A.O., Siino J.S., Gineitis A.A., Zalenskaya I.A., Tomilin N.V., Yau P., Bradbury E.M. J. Biol. Chem. 277:43474-43480(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
[2]	"The human and mouse replication-dependent histone genes." Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J. Genomics 80:487-498(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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]. Tissue: Testis.
[4]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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].
[7]	"Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation." Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D. Mol. Cell 20:601-611(2005) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION AT LYS-122.
[8]	"Inhibition of core histones acetylation by carcinogenic nickel(II)." Golebiowski F., Kasprzak K.S. Mol. Cell. Biochem. 279:133-139(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-7; LYS-14; LYS-17 AND LYS-22.
[9]	"Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II." Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., Reinberg D. Cell 125:703-717(2006) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION AT LYS-122.
[10]	"Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification." Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y. Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract] Cited for: CROTONYLATION AT LYS-7; LYS-13; LYS-14; LYS-17; LYS-18; LYS-25 AND LYS-36.
[11]	"The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation." Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y. Mol. Cell 43:132-144(2011) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION AT LYS-36.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF397301 Genomic DNA. Translation: AAK84040.1. AF531284 Genomic DNA. Translation: AAN06684.1. AK312055 mRNA. Translation: BAG34991.1. AL512384 Genomic DNA. Translation: CAC44615.1. CH471087 Genomic DNA. Translation: EAW55490.1. BC066238 mRNA. Translation: AAH66238.1. BC066239 mRNA. Translation: AAH66239.1. BC066240 mRNA. Translation: AAH66240.1. BC066241 mRNA. Translation: AAH66241.1. BC066242 mRNA. Translation: AAH66242.1. BC066243 mRNA. Translation: AAH66243.1.
IPI	IPI00465363.
RefSeq	NP_733759.1. NM_170610.2.
UniGene	Hs.591786.
3D structure databases
ProteinModelPortal	Q96A08.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96A08. 2 interactions.
MINT	MINT-2813617.
STRING	9606.ENSP00000274764.
PTM databases
PhosphoSite	Q96A08.
Polymorphism databases
DMDM	51316070.
Proteomic databases
PaxDb	Q96A08.
PRIDE	Q96A08.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000274764; ENSP00000274764; ENSG00000146047.
GeneID	255626.
KEGG	hsa:255626.
UCSC	uc003nfd.3. human.
Organism-specific databases
CTD	255626.
GeneCards	GC06P025727.
HGNC	HGNC:18730. HIST1H2BA.
HPA	CAB011603.
MIM	609904. gene.
neXtProt	NX_Q96A08.
PharmGKB	PA134937673.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG291964.
HOGENOM	HOG000231213.
HOVERGEN	HBG007774.
InParanoid	Q96A08.
KO	K11252.
OMA	TQKKEGR.
OrthoDB	EOG4FN4K9.
PhylomeDB	Q96A08.
Enzyme and pathway databases
Pathway_Interaction_DB	foxm1pathway. FOXM1 transcription factor network.
Reactome	REACT_111183. Meiosis. REACT_115566. Cell Cycle. REACT_116125. Disease.
Gene expression databases
Bgee	Q96A08.
CleanEx	HS_HIST1H2BA.
Genevestigator	Q96A08.
GermOnline	ENSG00000146047. Homo sapiens.
Family and domain databases
Gene3D	1.10.20.10. 1 hit.
InterPro	IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR000558. Histone_H2B. [Graphical view]
PANTHER	PTHR23428. PTHR23428. 1 hit.
Pfam	PF00125. Histone. 1 hit. [Graphical view]
PRINTS	PR00621. HISTONEH2B.
SMART	SM00427. H2B. 1 hit. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
PROSITE	PS00357. HISTONE_H2B. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	255626.
NextBio	92610.
SOURCE	Search...

Entry information

Entry name

H2B1A_HUMAN

Accession

Primary (citable) accession number: Q96A08
Secondary accession number(s): B2R544 , Q6NZ98, Q6NZA0, Q6NZA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 90 of the entry and version 3 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.