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Reviewed, UniProtKB/Swiss-Prot P62807 (H2B1C_HUMAN)

Last modified February 9, 2010. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Histone H2B type 1-C/E/F/G/I
Alternative name(s):
    Histone H2B.a
      Short name=H2B/a
    Histone H2B.g
      Short name=H2B/g
    Histone H2B.h
      Short name=H2B/h
    Histone H2B.k
      Short name=H2B/k
    Histone H2B.l
      Short name=H2B/l
    Histone H2B.1 A
Gene names
Name: HIST1H2BC
Synonyms: H2BFL
AND
Name: HIST1H2BE
Synonyms: H2BFH
AND
Name: HIST1H2BF
Synonyms: H2BFG
AND
Name: HIST1H2BG
Synonyms: H2BFA
AND
Name: HIST1H2BI
Synonyms: H2BFK
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length125 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.8 Ref.10 Ref.11

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. Ref.8 Ref.10 Ref.11

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.

Post-translational modification

Monoubiquitination of Lys-121 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.

Phosphorylated on Ser-15 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. Ref.13 Ref.19

Sequence similarities

Belongs to the histone H2B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.10 Ref.11 Ref.6 Ref.7 Ref.9
Chain2 – 125124Histone H2B type 1-C/E/F/G/I
PRO_0000071826

Amino acid modifications

Modified residue61N6-acetyllysine Ref.12 Ref.15 Ref.18
Modified residue71Phosphoserine Ref.19
Modified residue121N6-acetyllysine Ref.12 Ref.18
Modified residue131N6-acetyllysine Ref.7 Ref.12 Ref.15 Ref.18
Modified residue151Phosphoserine; by STK4 Ref.13
Modified residue161N6-acetyllysine Ref.7 Ref.12 Ref.15 Ref.18
Modified residue171N6-acetyllysine Ref.12 Ref.18
Modified residue211N6-acetyllysine Ref.7 Ref.12 Ref.15 Ref.18
Modified residue241N6-acetyllysine Ref.18
Modified residue471N6-methyllysine Ref.12
Modified residue581N6,N6-dimethyllysine Ref.12
Modified residue1091N6-acetyllysine; alternate Ref.18
Modified residue1091N6-methyllysine; alternate Ref.12
Cross-link121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12 Ref.14 Ref.16

Natural variations

Natural variant271G → S: dbSNP rs7766641. Ref.2
VAR_055887

Experimental info

Sequence conflict51A → S in CAB02545. Ref.2
Sequence conflict331S → T in CAB02545. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P62807-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A7C79F44BE703DF0

FASTA12513,819
        10         20         30         40         50         60 
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM 

        70         80         90        100        110        120 
GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT 


KYTSK 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of two human H1 histone genes within clusters of core histone genes."
Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.
Genomics 10:940-948(1991) [PubMed: 1916825] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2BG).
[2]"Human histone gene organization: nonregular arrangement within a large cluster."
Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D.
Genomics 40:314-322(1997) [PubMed: 9119399] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2BC; HIST1H2BE; HIST1H2BF AND HIST1H2BI), VARIANT SER-27.
[3]"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: 12408966] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2BC; HIST1H2BE; HIST1H2BF; HIST1H2BG AND HIST1H2BI).
[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: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIST1H2BC; HIST1H2BE; HIST1H2BF; HIST1H2BG AND HIST1H2BI).
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Ovary.
[6]"Human spleen histone H2B. Isolation and amino acid sequence."
Ohe Y., Hayashi H., Iwai K.
J. Biochem. 85:615-624(1979) [PubMed: 422550] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-125.
Tissue: Spleen.
[7]"Characterization of histones H2A and H2B variants and their post-translational modifications by mass spectrometry."
Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J.
Mol. Cell. Proteomics 5:541-552(2006) [PubMed: 16319397] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-26, ACETYLATION AT LYS-13; LYS-16 AND LYS-21, MASS SPECTROMETRY.
[8]"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: 11859126] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION.
[9]"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: 8620898] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13.
[10]"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: 12860195] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13, FUNCTION.
[11]"Antimicrobial polypeptides of the human colonic epithelium."
Howell S.J., Wilk D., Yadav S.P., Bevins C.L.
Peptides 24:1763-1770(2003) [PubMed: 15019208] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13, FUNCTION.
[12]"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: 16627869] [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, MASS SPECTROMETRY.
[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: 12757711] [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: 16307923] [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: 16283522] [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: 16713563] [Abstract]
Cited for: UBIQUITINATION AT LYS-121.
[17]"Gene-specific characterization of human histone H2B by electron capture dissociation."
Siuti N., Roth M.J., Mizzen C.A., Kelleher N.L., Pesavento J.J.
J. Proteome Res. 5:233-239(2006) [PubMed: 16457587] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[18]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-21; LYS-24 AND LYS-109, MASS SPECTROMETRY.
Tissue: Epithelium.
[19]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60750 Genomic DNA. Translation: AAA63189.1.
Z80782 Genomic DNA. Translation: CAB02544.1.
Z80779 Genomic DNA. Translation: CAB02541.1.
Z80780 Genomic DNA. Translation: CAB02542.1.
Z80783 Genomic DNA. Translation: CAB02545.1.
AF531286 Genomic DNA. Translation: AAN06686.1.
AF531288 Genomic DNA. Translation: AAN06688.1.
AF531289 Genomic DNA. Translation: AAN06689.1.
AF531290 Genomic DNA. Translation: AAN06690.1.
AF531292 Genomic DNA. Translation: AAN06692.1.
AL031777 Genomic DNA. Translation: CAC03411.1.
AL031777 Genomic DNA. Translation: CAC03417.1.
AL031777 Genomic DNA. Translation: CAC03420.1.
AL353759 Genomic DNA. Translation: CAC04130.1.
BC001131 mRNA. No translation available.
BC009612 mRNA. No translation available.
BC096120 mRNA. Translation: AAH96120.1.
BC096122 mRNA. Translation: AAH96122.1.
BC096123 mRNA. Translation: AAH96123.1.
BC101653 mRNA. Translation: AAI01654.1.
BC101655 mRNA. Translation: AAI01656.1.
BC101748 mRNA. Translation: AAI01749.1.
BC101750 mRNA. Translation: AAI01751.1.
BC106899 mRNA. Translation: AAI06900.1.
IPIIPI00020101.
PIRHSHUB2. E40335.
S65409.
RefSeqNP_003509.1.
NP_003513.1.
NP_003514.2.
NP_003516.1.
NP_003517.2.
UniGeneHs.182137
Hs.534369
Hs.553506
Hs.591797
Hs.591809
Hs.658713

3D structure databases

SMRP62807. Positions 5-124.
ModBaseSearch...

Protein-protein interaction databases

IntActP62807. 17 interactions.
STRINGP62807.

PTM databases

PhosphoSiteP62807.

Proteomic databases

PRIDEP62807.

Genome annotation databases

EnsemblENST00000314332; ENSP00000321744; ENSG00000180596; Homo sapiens. [Genome view]
ENST00000339812; ENSP00000342886; ENSG00000187990; Homo sapiens. [Genome view]
ENST00000356530; ENSP00000348924; ENSG00000197697; Homo sapiens. [Genome view]
ENST00000356950; ENSP00000349430; ENSG00000197903; Homo sapiens. [Genome view]
ENST00000359985; ENSP00000353074; ENSG00000197846; Homo sapiens. [Genome view]
ENST00000377733; ENSP00000366962; ENSG00000168242; Homo sapiens. [Genome view]
ENST00000396891; ENSP00000380100; ENSG00000197903; Homo sapiens. [Genome view]
ENST00000396984; ENSP00000380180; ENSG00000180596; Homo sapiens. [Genome view]
GeneID8339.
8343.
8344.
8346.
8347.
KEGGhsa:8339.
hsa:8343.
hsa:8344.
hsa:8346.
hsa:8347.

Organism-specific databases

CTD8339.
8343.
8344.
8346.
8347.
GeneCardsGC06M026222.
GC06M026324.
GC06P026292.
GC06P026307.
GC06P026381.
H-InvDBHIX0005638.
HIX0023198.
HIX0032906.
HIX0032990.
HIX0033006.
HGNCHGNC:4757. HIST1H2BC.
HGNC:4753. HIST1H2BE.
HGNC:4752. HIST1H2BF.
HGNC:4746. HIST1H2BG.
HGNC:4756. HIST1H2BI.
MIM602798. gene.
602804. gene.
602805. gene.
602807. gene.
602847. gene.
PharmGKBPA29132.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP62807.
InParanoidP62807.
PhylomeDBP62807.

Enzyme and pathway databases

ReactomeREACT_7970. Telomere Maintenance.

Gene expression databases

ArrayExpressP62807.
BgeeP62807.
CleanExHS_HIST1H2BC.
HS_HIST1H2BE.
HS_HIST1H2BF.
HS_HIST1H2BG.
HS_HIST1H2BI.
GenevestigatorP62807.
GermOnlineENSG00000168242. Homo sapiens.
ENSG00000180596. Homo sapiens.
ENSG00000187990. Homo sapiens.
ENSG00000197697. Homo sapiens.
ENSG00000197846. Homo sapiens.
ENSG00000197903. Homo sapiens.

Family and domain databases

InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000558. Histone_H2B.
[Graphical view]
Gene3DG3DSA:1.10.20.10. Histone-fold. 1 hit.
PANTHERPTHR23428. Histone_H2B. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00621. HISTONEH2B.
SMARTSM00427. H2B. 1 hit.
[Graphical view]
PROSITEPS00357. HISTONE_H2B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameH2B1C_HUMAN
AccessionPrimary (citable) accession number: P62807
Secondary accession number(s): P02278 expand/collapse secondary AC list , Q3B872, Q4VB69, Q93078, Q93080
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 6

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents