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Q96A08 (H2B1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H2B type 1-A
Alternative name(s):
Histone H2B, testis
Short name=TSH2B.1
Testis-specific histone H2B
Gene names
Name:HIST1H2BA
Synonyms:TSH2B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length127 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. Also expressed maternally and is present in the female pronucleus, suggesting a similar role in protamine replacement by nucleosomes at fertilization By similarity. Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear. 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. 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. The octamer wraps approximately 147 bp of DNA.

Subcellular location

Nucleus. Chromosome.

Tissue specificity

Mainly expressed in testis, and the corresponding protein is also present in mature sperm (at protein level). Also found in some fat cells. Ref.1 Ref.12

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. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons.

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

Acetylated during spermatogenesis. Acetylated form is most abundant in spermatogonia compared to spermatocytes and round spermatids By similarity. Ref.8 Ref.12

Phosphorylated at Thr-117 in spermatogonia, spermatocytes and round spermatids By similarity. Ref.12

Methylated at Lys-118 in spermatogonia, spermatocytes and round spermatids By similarity. Ref.12

Sequence similarities

Belongs to the histone H2B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 127126Histone H2B type 1-A
PRO_0000071842

Amino acid modifications

Modified residue21N-acetylproline By similarity
Modified residue71N6-acetyllysine; alternate Ref.8
Modified residue71N6-crotonyllysine; alternate Ref.10
Modified residue131N6-acetyllysine; alternate By similarity
Modified residue131N6-crotonyllysine; alternate Ref.10
Modified residue141N6-acetyllysine; alternate Ref.8
Modified residue141N6-crotonyllysine; alternate Ref.10
Modified residue171N6-acetyllysine; alternate Ref.8
Modified residue171N6-crotonyllysine; alternate Ref.10
Modified residue181N6-acetyllysine; alternate By similarity
Modified residue181N6-crotonyllysine; alternate Ref.10
Modified residue221N6-acetyllysine; alternate Ref.8
Modified residue221N6-crotonyllysine; alternate Ref.10
Modified residue251N6-acetyllysine; alternate By similarity
Modified residue251N6-crotonyllysine; alternate Ref.10
Modified residue361N6-crotonyllysine; alternate Ref.10
Modified residue381Phosphoserine By similarity
Modified residue481N6-methyllysine By similarity
Modified residue591N6,N6-dimethyllysine By similarity
Modified residue811Dimethylated arginine Ref.12
Modified residue861Phosphoserine Ref.12
Modified residue871N6,N6,N6-trimethyllysine; alternate Ref.12
Modified residue871N6-acetyllysine; alternate Ref.12
Modified residue881Omega-N-methylarginine Ref.12
Modified residue941Omega-N-methylarginine Ref.12
Modified residue1101N6-methyllysine By similarity
Modified residue1171Phosphothreonine By similarity
Modified residue1181N6-methylated lysine By similarity
Cross-link36Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Cross-link122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7 Ref.9

Experimental info

Sequence conflict21P → A in AAH66243. Ref.6
Sequence conflict221K → E in AAH66241. Ref.6
Sequence conflict801S → P in AAH66240. Ref.6

Secondary structure

........... 127
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96A08 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3EE4124DA9B3C3E8

FASTA12714,167
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. 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 (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-22; 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.
[12]"Histone variants and their post-translational modifications in primary human fat cells."
Jufvas A., Stralfors P., Vener A.V.
PLoS ONE 6:E15960-E15960(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-87, METHYLATION AT ARG-81; LYS-87; ARG-88 AND ARG-94, PHOSPHORYLATION AT SER-86, FUNCTION, TISSUE SPECIFICITY.
+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.
CCDSCCDS4563.1.
RefSeqNP_733759.1. NM_170610.2.
UniGeneHs.591786.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3WKJX-ray2.80D/H1-127[»]
ProteinModelPortalQ96A08.
SMRQ96A08. Positions 6-127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid129111. 17 interactions.
IntActQ96A08. 4 interactions.
MINTMINT-2813617.
STRING9606.ENSP00000274764.

PTM databases

PhosphoSiteQ96A08.

Polymorphism databases

DMDM51316070.

Proteomic databases

MaxQBQ96A08.
PaxDbQ96A08.
PRIDEQ96A08.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000274764; ENSP00000274764; ENSG00000146047.
GeneID255626.
KEGGhsa:255626.
UCSCuc003nfd.3. human.

Organism-specific databases

CTD255626.
GeneCardsGC06P025727.
HGNCHGNC:18730. HIST1H2BA.
HPACAB011603.
MIM609904. gene.
neXtProtNX_Q96A08.
PharmGKBPA134937673.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG291964.
HOGENOMHOG000231213.
HOVERGENHBG007774.
InParanoidQ96A08.
KOK11252.
OMAERVSCEA.
OrthoDBEOG72VH8J.
PhylomeDBQ96A08.
TreeFamTF300212.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_172623. Chromatin organization.
REACT_21300. Mitotic M-M/G1 phases.
REACT_71. Gene Expression.

Gene expression databases

BgeeQ96A08.
CleanExHS_HIST1H2BA.
GenevestigatorQ96A08.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000558. Histone_H2B.
[Graphical view]
PANTHERPTHR23428. PTHR23428. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00621. HISTONEH2B.
SMARTSM00427. H2B. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00357. HISTONE_H2B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiHIST1H2BA.
GenomeRNAi255626.
NextBio92610.
PROQ96A08.
SOURCESearch...

Entry information

Entry nameH2B1A_HUMAN
AccessionPrimary (citable) accession number: Q96A08
Secondary accession number(s): B2R544 expand/collapse secondary AC list , Q6NZ98, Q6NZA0, Q6NZA1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 101 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM