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Q96A08

- H2B1A_HUMAN

UniProt

Q96A08 - H2B1A_HUMAN

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Protein

Histone H2B type 1-A

Gene

HIST1H2BA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. cellular response to acid chemical Source: Ensembl
  2. chromatin organization Source: Reactome
  3. inflammatory response Source: Ensembl
  4. mononuclear cell migration Source: Ensembl
  5. nucleosome assembly Source: UniProtKB
  6. nucleosome disassembly Source: UniProtKB
  7. plasminogen activation Source: Ensembl
  8. positive regulation of binding Source: Ensembl
  9. spermatogenesis, exchange of chromosomal proteins Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_172610. HATs acetylate histones.
REACT_172744. Condensation of Prophase Chromosomes.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_200808. PRC2 methylates histones and DNA.
REACT_200827. SIRT1 negatively regulates rRNA Expression.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_2232. RNA Polymerase I Promoter Opening.
REACT_228222. HDACs deacetylate histones.
REACT_267652. DNA methylation.
REACT_267668. Transcriptional regulation by small RNAs.
REACT_27271. Meiotic recombination.
REACT_75792. Meiotic synapsis.
REACT_75925. Amyloids.
REACT_7963. Packaging Of Telomere Ends.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2B type 1-A
Alternative name(s):
Histone H2B, testis
Short name:
TSH2B.1
Testis-specific histone H2B
Gene namesi
Name:HIST1H2BA
Synonyms:TSH2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:18730. HIST1H2BA.

Subcellular locationi

GO - Cellular componenti

  1. extrinsic component of plasma membrane Source: Ensembl
  2. nucleoplasm Source: Reactome
  3. nucleosome Source: UniProtKB
  4. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134937673.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 127126Histone H2B type 1-APRO_0000071842Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylprolineBy similarity
Modified residuei7 – 71N6-acetyllysine; alternate1 Publication
Modified residuei7 – 71N6-crotonyllysine; alternate1 Publication
Modified residuei13 – 131N6-acetyllysine; alternateBy similarity
Modified residuei13 – 131N6-crotonyllysine; alternate1 Publication
Modified residuei14 – 141N6-acetyllysine; alternate1 Publication
Modified residuei14 – 141N6-crotonyllysine; alternate1 Publication
Modified residuei17 – 171N6-acetyllysine; alternate1 Publication
Modified residuei17 – 171N6-crotonyllysine; alternate1 Publication
Modified residuei18 – 181N6-acetyllysine; alternateBy similarity
Modified residuei18 – 181N6-crotonyllysine; alternate1 Publication
Modified residuei22 – 221N6-acetyllysine; alternate1 Publication
Modified residuei22 – 221N6-crotonyllysine; alternate1 Publication
Modified residuei25 – 251N6-acetyllysine; alternateBy similarity
Modified residuei25 – 251N6-crotonyllysine; alternate1 Publication
Modified residuei36 – 361N6-crotonyllysine; alternate1 Publication
Cross-linki36 – 36Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei38 – 381PhosphoserineBy similarity
Modified residuei48 – 481N6-methyllysineBy similarity
Modified residuei59 – 591N6,N6-dimethyllysineBy similarity
Modified residuei81 – 811Dimethylated arginine1 Publication
Modified residuei86 – 861Phosphoserine1 Publication
Modified residuei87 – 871N6,N6,N6-trimethyllysine; alternate1 Publication
Modified residuei87 – 871N6-acetyllysine; alternate1 Publication
Modified residuei88 – 881Omega-N-methylarginine1 Publication
Modified residuei94 – 941Omega-N-methylarginine1 Publication
Modified residuei110 – 1101N6-methyllysineBy similarity
Modified residuei117 – 1171PhosphothreonineBy similarity
Modified residuei118 – 1181N6-methylated lysineBy similarity
Cross-linki122 – 122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications

Post-translational modificationi

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.1 Publication
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.1 Publication
Acetylated during spermatogenesis. Acetylated form is most abundant in spermatogonia compared to spermatocytes and round spermatids (By similarity).By similarity
Phosphorylated at Thr-117 in spermatogonia, spermatocytes and round spermatids.By similarity
Methylated at Lys-118 in spermatogonia, spermatocytes and round spermatids.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ96A08.
PaxDbiQ96A08.
PRIDEiQ96A08.

PTM databases

PhosphoSiteiQ96A08.

Expressioni

Tissue specificityi

Mainly expressed in testis, and the corresponding protein is also present in mature sperm (at protein level). Also found in some fat cells.2 Publications

Gene expression databases

BgeeiQ96A08.
CleanExiHS_HIST1H2BA.
GenevestigatoriQ96A08.

Organism-specific databases

HPAiCAB011603.

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. The octamer wraps approximately 147 bp of DNA.

Protein-protein interaction databases

BioGridi129111. 88 interactions.
IntActiQ96A08. 4 interactions.
MINTiMINT-2813617.
STRINGi9606.ENSP00000274764.

Structurei

Secondary structure

1
127
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 5011Combined sources
Helixi58 – 8528Combined sources
Beta strandi89 – 913Combined sources
Helixi93 – 10311Combined sources
Helixi108 – 12417Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WKJX-ray2.80D/H1-127[»]
ProteinModelPortaliQ96A08.
SMRiQ96A08. Positions 6-127.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Phylogenomic databases

eggNOGiNOG291964.
GeneTreeiENSGT00730000110319.
HOGENOMiHOG000231213.
HOVERGENiHBG007774.
InParanoidiQ96A08.
KOiK11252.
OMAiERVSCEA.
OrthoDBiEOG72VH8J.
PhylomeDBiQ96A08.
TreeFamiTF300212.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000558. Histone_H2B.
[Graphical view]
PANTHERiPTHR23428. PTHR23428. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00621. HISTONEH2B.
SMARTiSM00427. H2B. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00357. HISTONE_H2B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q96A08-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPEVSSKGAT ISKKGFKKAV VKTQKKEGKK RKRTRKESYS IYIYKVLKQV
60 70 80 90 100
HPDTGISSKA MSIMNSFVTD IFERIASEAS RLAHYSKRST ISSREIQTAV
110 120
RLLLPGELAK HAVSEGTKAV TKYTSSK
Length:127
Mass (Da):14,167
Last modified:January 23, 2007 - v3
Checksum:i3EE4124DA9B3C3E8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21P → A in AAH66243. (PubMed:15489334)Curated
Sequence conflicti22 – 221K → E in AAH66241. (PubMed:15489334)Curated
Sequence conflicti80 – 801S → P in AAH66240. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4563.1.
RefSeqiNP_733759.1. NM_170610.2.
UniGeneiHs.591786.

Genome annotation databases

EnsembliENST00000274764; ENSP00000274764; ENSG00000146047.
GeneIDi255626.
KEGGihsa:255626.
UCSCiuc003nfd.3. human.

Polymorphism databases

DMDMi51316070.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS4563.1.
RefSeqi NP_733759.1. NM_170610.2.
UniGenei Hs.591786.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3WKJ X-ray 2.80 D/H 1-127 [» ]
ProteinModelPortali Q96A08.
SMRi Q96A08. Positions 6-127.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 129111. 88 interactions.
IntActi Q96A08. 4 interactions.
MINTi MINT-2813617.
STRINGi 9606.ENSP00000274764.

PTM databases

PhosphoSitei Q96A08.

Polymorphism databases

DMDMi 51316070.

Proteomic databases

MaxQBi Q96A08.
PaxDbi Q96A08.
PRIDEi Q96A08.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000274764 ; ENSP00000274764 ; ENSG00000146047 .
GeneIDi 255626.
KEGGi hsa:255626.
UCSCi uc003nfd.3. human.

Organism-specific databases

CTDi 255626.
GeneCardsi GC06P025727.
HGNCi HGNC:18730. HIST1H2BA.
HPAi CAB011603.
MIMi 609904. gene.
neXtProti NX_Q96A08.
PharmGKBi PA134937673.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG291964.
GeneTreei ENSGT00730000110319.
HOGENOMi HOG000231213.
HOVERGENi HBG007774.
InParanoidi Q96A08.
KOi K11252.
OMAi ERVSCEA.
OrthoDBi EOG72VH8J.
PhylomeDBi Q96A08.
TreeFami TF300212.

Enzyme and pathway databases

Reactomei REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_172610. HATs acetylate histones.
REACT_172744. Condensation of Prophase Chromosomes.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_200808. PRC2 methylates histones and DNA.
REACT_200827. SIRT1 negatively regulates rRNA Expression.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_2232. RNA Polymerase I Promoter Opening.
REACT_228222. HDACs deacetylate histones.
REACT_267652. DNA methylation.
REACT_267668. Transcriptional regulation by small RNAs.
REACT_27271. Meiotic recombination.
REACT_75792. Meiotic synapsis.
REACT_75925. Amyloids.
REACT_7963. Packaging Of Telomere Ends.

Miscellaneous databases

GeneWikii HIST1H2BA.
GenomeRNAii 255626.
NextBioi 92610.
PROi Q96A08.
SOURCEi Search...

Gene expression databases

Bgeei Q96A08.
CleanExi HS_HIST1H2BA.
Genevestigatori Q96A08.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000558. Histone_H2B.
[Graphical view ]
PANTHERi PTHR23428. PTHR23428. 1 hit.
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00621. HISTONEH2B.
SMARTi SM00427. H2B. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00357. HISTONE_H2B. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiH2B1A_HUMAN
AccessioniPrimary (citable) accession number: Q96A08
Secondary accession number(s): B2R544
, Q6NZ98, Q6NZA0, Q6NZA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 105 of the entry and version 3 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3