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P06899

- H2B1J_HUMAN

UniProt

P06899 - H2B1J_HUMAN

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Protein

Histone H2B type 1-J

Gene

HIST1H2BJ

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

Functioni

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.
Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB

GO - Biological processi

  1. antibacterial humoral response Source: UniProt
  2. chromatin organization Source: Reactome
  3. defense response to Gram-positive bacterium Source: UniProt
  4. innate immune response in mucosa Source: UniProt
  5. nucleosome assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial

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_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-J
Alternative name(s):
Histone H2B.1
Histone H2B.r
Short name:
H2B/r
Gene namesi
Name:HIST1H2BJ
Synonyms:H2BFR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:4761. HIST1H2BJ.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProt
  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

PharmGKBiPA29136.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 126125Histone H2B type 1-JPRO_0000071836Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylprolineBy similarity
Modified residuei6 – 61N6-acetyllysine; alternate2 Publications
Modified residuei6 – 61N6-crotonyllysine; alternate1 Publication
Modified residuei12 – 121N6-acetyllysine; alternate1 Publication
Modified residuei12 – 121N6-crotonyllysine; alternate1 Publication
Modified residuei13 – 131N6-acetyllysine; alternate2 Publications
Modified residuei13 – 131N6-crotonyllysine; alternate1 Publication
Modified residuei15 – 151Phosphoserine; by STK4/MST11 Publication
Modified residuei16 – 161N6-acetyllysine; alternate2 Publications
Modified residuei16 – 161N6-crotonyllysine; alternate1 Publication
Modified residuei17 – 171N6-acetyllysine; alternate1 Publication
Modified residuei17 – 171N6-crotonyllysine; alternate1 Publication
Modified residuei21 – 211N6-acetyllysine; alternate2 Publications
Modified residuei21 – 211N6-crotonyllysine; alternate1 Publication
Modified residuei24 – 241N6-acetyllysine; alternateBy similarity
Modified residuei24 – 241N6-crotonyllysine; alternate1 Publication
Modified residuei35 – 351N6-crotonyllysine; alternate1 Publication
Cross-linki35 – 35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei37 – 371Phosphoserine; by AMPKBy similarity
Modified residuei47 – 471N6-methyllysine1 Publication
Modified residuei58 – 581N6,N6-dimethyllysine1 Publication
Modified residuei80 – 801Dimethylated arginineBy similarity
Modified residuei86 – 861N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei86 – 861N6-acetyllysine; alternateBy similarity
Modified residuei87 – 871Omega-N-methylarginineBy similarity
Modified residuei93 – 931Omega-N-methylarginineBy similarity
Modified residuei109 – 1091N6-methyllysine1 Publication
Glycosylationi113 – 1131O-linked (GlcNAc)By similarity
Modified residuei116 – 1161PhosphothreonineBy similarity
Modified residuei117 – 1171N6-methylated lysineBy similarity
Cross-linki121 – 121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)3 Publications

Post-translational modificationi

Monoubiquitination at Lys-35 (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-121 (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.2 Publications
Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity). Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination.By similarity1 Publication
GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity).By similarity
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

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP06899.
PRIDEiP06899.

PTM databases

PhosphoSiteiP06899.

Expressioni

Gene expression databases

BgeeiP06899.
CleanExiHS_HIST1H2BJ.
ExpressionAtlasiP06899. differential.
GenevestigatoriP06899.

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.1 Publication

Protein-protein interaction databases

BioGridi114460. 17 interactions.
DIPiDIP-421N.
IntActiP06899. 6 interactions.
MINTiMINT-4822927.
STRINGi9606.ENSP00000244601.

Structurei

Secondary structure

1
126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi39 – 4911
Beta strandi54 – 563
Helixi57 – 8327
Turni84 – 863
Beta strandi88 – 903
Helixi92 – 10211
Helixi105 – 12420

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A6NX-ray2.70D/H1-126[»]
3AFAX-ray2.50D/H1-126[»]
3AN2X-ray3.60D/H1-126[»]
3AV1X-ray2.50D/H1-126[»]
3AV2X-ray2.80D/H1-126[»]
3AYWX-ray2.90D/H1-126[»]
3AZEX-ray3.00D/H1-126[»]
3AZFX-ray2.70D/H1-126[»]
3AZGX-ray2.40D/H1-126[»]
3AZHX-ray3.49D/H1-126[»]
3AZIX-ray2.70D/H1-126[»]
3AZJX-ray2.89D/H1-126[»]
3AZKX-ray3.20D/H1-126[»]
3AZLX-ray2.70D/H1-126[»]
3AZMX-ray2.89D/H1-126[»]
3AZNX-ray3.00D/H1-126[»]
3W96X-ray3.00D/H1-126[»]
3W97X-ray3.20D/H26-126[»]
3W98X-ray3.42D/H1-126[»]
3W99X-ray3.00D/H1-126[»]
3WA9X-ray3.07D/H1-126[»]
3WAAX-ray3.20D/H1-126[»]
4CAYX-ray1.48B31-126[»]
ProteinModelPortaliP06899.
SMRiP06899. Positions 5-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06899.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Phylogenomic databases

eggNOGiNOG315146.
GeneTreeiENSGT00760000118976.
HOGENOMiHOG000231213.
HOVERGENiHBG007774.
InParanoidiP06899.
KOiK11252.
OMAiSANIACN.
OrthoDBiEOG72VH8J.
PhylomeDBiP06899.
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.

P06899-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSI YVYKVLKQVH
60 70 80 90 100
PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR
110 120
LLLPGELAKH AVSEGTKAVT KYTSAK
Length:126
Mass (Da):13,904
Last modified:January 23, 2007 - v3
Checksum:i0408C881ABBE6647
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 335KRKRS → SAAH in CAA24950. (PubMed:6647026)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00088 Genomic DNA. Translation: CAA24950.1.
AF531293 Genomic DNA. Translation: AAN06693.1.
AK311849 mRNA. Translation: BAG34791.1.
AL021807 Genomic DNA. Translation: CAA16949.1.
CH471081 Genomic DNA. Translation: EAX03080.1.
CCDSiCCDS4618.1.
PIRiA26318. HSHUB1.
S65409.
RefSeqiNP_066402.2. NM_021058.3.
UniGeneiHs.591807.
Hs.656567.

Genome annotation databases

EnsembliENST00000339812; ENSP00000342886; ENSG00000124635.
ENST00000607124; ENSP00000476136; ENSG00000124635.
GeneIDi8970.
KEGGihsa:8970.
UCSCiuc003niv.3. human.

Polymorphism databases

DMDMi7404367.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00088 Genomic DNA. Translation: CAA24950.1 .
AF531293 Genomic DNA. Translation: AAN06693.1 .
AK311849 mRNA. Translation: BAG34791.1 .
AL021807 Genomic DNA. Translation: CAA16949.1 .
CH471081 Genomic DNA. Translation: EAX03080.1 .
CCDSi CCDS4618.1.
PIRi A26318. HSHUB1.
S65409.
RefSeqi NP_066402.2. NM_021058.3.
UniGenei Hs.591807.
Hs.656567.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3A6N X-ray 2.70 D/H 1-126 [» ]
3AFA X-ray 2.50 D/H 1-126 [» ]
3AN2 X-ray 3.60 D/H 1-126 [» ]
3AV1 X-ray 2.50 D/H 1-126 [» ]
3AV2 X-ray 2.80 D/H 1-126 [» ]
3AYW X-ray 2.90 D/H 1-126 [» ]
3AZE X-ray 3.00 D/H 1-126 [» ]
3AZF X-ray 2.70 D/H 1-126 [» ]
3AZG X-ray 2.40 D/H 1-126 [» ]
3AZH X-ray 3.49 D/H 1-126 [» ]
3AZI X-ray 2.70 D/H 1-126 [» ]
3AZJ X-ray 2.89 D/H 1-126 [» ]
3AZK X-ray 3.20 D/H 1-126 [» ]
3AZL X-ray 2.70 D/H 1-126 [» ]
3AZM X-ray 2.89 D/H 1-126 [» ]
3AZN X-ray 3.00 D/H 1-126 [» ]
3W96 X-ray 3.00 D/H 1-126 [» ]
3W97 X-ray 3.20 D/H 26-126 [» ]
3W98 X-ray 3.42 D/H 1-126 [» ]
3W99 X-ray 3.00 D/H 1-126 [» ]
3WA9 X-ray 3.07 D/H 1-126 [» ]
3WAA X-ray 3.20 D/H 1-126 [» ]
4CAY X-ray 1.48 B 31-126 [» ]
ProteinModelPortali P06899.
SMRi P06899. Positions 5-126.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114460. 17 interactions.
DIPi DIP-421N.
IntActi P06899. 6 interactions.
MINTi MINT-4822927.
STRINGi 9606.ENSP00000244601.

PTM databases

PhosphoSitei P06899.

Polymorphism databases

DMDMi 7404367.

Proteomic databases

PaxDbi P06899.
PRIDEi P06899.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000339812 ; ENSP00000342886 ; ENSG00000124635 .
ENST00000607124 ; ENSP00000476136 ; ENSG00000124635 .
GeneIDi 8970.
KEGGi hsa:8970.
UCSCi uc003niv.3. human.

Organism-specific databases

CTDi 8970.
GeneCardsi GC06M027096.
HGNCi HGNC:4761. HIST1H2BJ.
MIMi 615044. gene.
neXtProti NX_P06899.
PharmGKBi PA29136.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG315146.
GeneTreei ENSGT00760000118976.
HOGENOMi HOG000231213.
HOVERGENi HBG007774.
InParanoidi P06899.
KOi K11252.
OMAi SANIACN.
OrthoDBi EOG72VH8J.
PhylomeDBi P06899.
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_27271. Meiotic recombination.
REACT_75792. Meiotic synapsis.
REACT_75925. Amyloids.
REACT_7963. Packaging Of Telomere Ends.

Miscellaneous databases

EvolutionaryTracei P06899.
GeneWikii HIST1H2BJ.
GenomeRNAii 8970.
NextBioi 33659.
PROi P06899.
SOURCEi Search...

Gene expression databases

Bgeei P06899.
CleanExi HS_HIST1H2BJ.
ExpressionAtlasi P06899. differential.
Genevestigatori P06899.

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. "The primary structure and expression of four cloned human histone genes."
    Zhong R., Roeder R.G., Heintz N.
    Nucleic Acids Res. 11:7409-7425(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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: Hippocampus.
  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. "Glucocorticoid-induced lymphocytolysis is not mediated by an induced endonuclease."
    Alnemri E.S., Litwack G.
    J. Biol. Chem. 264:4104-4111(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-27.
  7. "Endotoxin-neutralizing antimicrobial proteins of the human placenta."
    Kim H.S., Cho J.H., Park H.W., Yoon H., Kim M.S., Kim S.C.
    J. Immunol. 168:2356-2364(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION.
  8. "Biochemical and antibacterial analysis of human wound and blister fluid."
    Frohm M., Gunne H., Bergman A.-C., Agerberth B., Bergman T., Boman A., Liden S., Joernvall H., Boman H.G.
    Eur. J. Biochem. 237:86-92(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
  9. "Antimicrobial peptides in the first line defence of human colon mucosa."
    Tollin M., Bergman P., Svenberg T., Joernvall H., Gudmundsson G.H., Agerberth B.
    Peptides 24:523-530(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13, FUNCTION.
  10. "Antimicrobial polypeptides of the human colonic epithelium."
    Howell S.J., Wilk D., Yadav S.P., Bevins C.L.
    Peptides 24:1763-1770(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13, FUNCTION.
  11. "Quantitative proteomic analysis of post-translational modifications of human histones."
    Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M., Finn P., Grauslund M., Hansen A.M., Jensen O.N.
    Mol. Cell. Proteomics 5:1314-1325(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 7-24, ACETYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17 AND LYS-21, METHYLATION AT LYS-47; LYS-58 AND LYS-109, UBIQUITINATION AT LYS-121, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "Global regulation of post-translational modifications on core histones."
    Galasinski S.C., Louie D.F., Gloor K.K., Resing K.A., Ahn N.G.
    J. Biol. Chem. 277:2579-2588(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, METHYLATION.
  13. "Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile twenty kinase."
    Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A., Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D.
    Cell 113:507-517(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-15.
  14. "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-121.
  15. "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-6; LYS-13; LYS-16 AND LYS-21.
  16. "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-121.
  17. "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-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-21; LYS-24 AND LYS-35.
  18. "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-35.
  19. "USP49 deubiquitinates histone H2B and regulates cotranscriptional pre-mRNA splicing."
    Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S., Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M., Giles K.E., Ma L., Wang H.
    Genes Dev. 27:1581-1595(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP49.
  20. Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 31-126 IN COMPLEX WITH H2AFZ AND ANP32E.

Entry informationi

Entry nameiH2B1J_HUMAN
AccessioniPrimary (citable) accession number: P06899
Secondary accession number(s): B2R4J4, O60816
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 144 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, Direct protein sequencing, 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