P62807 (H2B1C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H2B type 1-C/E/F/G/I

Alternative name(s):
Histone H2B.1 A
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

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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	126 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. 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. Chromosome.
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. 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. Ref.13 Ref.19
Sequence similarities	Belongs to the histone H2B family.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Antibiotic Antimicrobial
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW nucleosome assembly Non-traceable author statement Ref.6Ref.2. Source: UniProtKB
Cellular component	nucleosome Non-traceable author statement Ref.6Ref.2. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Non-traceable author statement Ref.6Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
	Chain	2 – 126	125	Histone H2B type 1-C/E/F/G/I		PRO_0000071826
Amino acid modifications
	Modified residue	6	1	N6-acetyllysine Ref.12 Ref.15 Ref.18
	Modified residue	7	1	Phosphoserine Ref.19
	Modified residue	12	1	N6-acetyllysine Ref.12 Ref.18
	Modified residue	13	1	N6-acetyllysine Ref.7 Ref.12 Ref.15 Ref.18
	Modified residue	15	1	Phosphoserine; by STK4/MST1 Ref.13
	Modified residue	16	1	N6-acetyllysine Ref.7 Ref.12 Ref.15 Ref.18
	Modified residue	17	1	N6-acetyllysine Ref.12 Ref.18
	Modified residue	21	1	N6-acetyllysine Ref.7 Ref.12 Ref.15 Ref.18
	Modified residue	24	1	N6-acetyllysine Ref.18
	Modified residue	37	1	Phosphoserine; by AMPK By similarity
	Modified residue	47	1	N6-methyllysine Ref.12
	Modified residue	58	1	N6,N6-dimethyllysine Ref.12
	Modified residue	109	1	N6-acetyllysine; alternate Ref.18
	Modified residue	109	1	N6-methyllysine; alternate Ref.12
	Cross-link	121		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12 Ref.14 Ref.16
Natural variations
	Natural variant	27	1	G → S. Ref.2 Corresponds to variant rs7766641 [ dbSNP | Ensembl ].		VAR_055887
Experimental info
	Sequence conflict	5	1	A → S in CAB02545. Ref.2
	Sequence conflict	33	1	S → T in CAB02545. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P62807 [UniParc]. Last modified March 2, 2010. Version 4. Checksum: FAE1479F44BE703D	FASTA	126	13,906
	10 20 30 40 50 60 MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM 70 80 90 100 110 120 GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT KYTSSK

References

	« Hide 'large scale' referencesShow '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. , 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 2-126. 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: Cervix carcinoma.
[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. Tissue: Embryonic kidney.
+	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.
IPI	IPI00020101.
PIR	HSHUB2. E40335. S65409.
RefSeq	NP_003509.1. NM_003518.3. NP_003513.1. NM_003522.3. NP_003514.2. NM_003523.2. NP_003516.1. NM_003525.2. NP_003517.2. NM_003526.2. NP_066407.1. NM_021063.3.
UniGene	Hs.182137. Hs.534369. Hs.553506. Hs.591797. Hs.591809. Hs.658713. Hs.726509.
3D structure databases
ProteinModelPortal	P62807.
SMR	P62807. Positions 5-126.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62807. 6 interactions.
MINT	MINT-276222.
STRING	P62807.
PTM databases
PhosphoSite	P62807.
Proteomic databases
PRIDE	P62807.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000024276; ENSRNOP00000024276; ENSRNOG00000018034. ENSRNOT00000028779; ENSRNOP00000028779; ENSRNOG00000021198. ENSRNOT00000047071; ENSRNOP00000049203; ENSRNOG00000029472. ENST00000339812; ENSP00000342886; ENSG00000187990. ENST00000356530; ENSP00000348924; ENSG00000197697. ENST00000359985; ENSP00000353074; ENSG00000197846. ENST00000377733; ENSP00000366962; ENSG00000168242. ENST00000396984; ENSP00000380180; ENSG00000180596.
GeneID	3017. 8339. 8343. 8344. 8346. 8347.
KEGG	hsa:3017. hsa:8339. hsa:8343. hsa:8344. hsa:8346. hsa:8347.
Organism-specific databases
CTD	8339. 8343. 8344. 8346. 8347.
GeneCards	GC06M026066. GC06M026159. GC06P026183. GC06P026199. GC06P026273.
HGNC	HGNC:4757. HIST1H2BC. HGNC:4753. HIST1H2BE. HGNC:4752. HIST1H2BF. HGNC:4746. HIST1H2BG. HGNC:4756. HIST1H2BI.
MIM	602798. gene. 602804. gene. 602805. gene. 602807. gene. 602847. gene.
neXtProt	NX_P62807.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG007774.
InParanoid	P62807.
OMA	TSSKAIY.
OrthoDB	EOG46DM4D. EOG4FN4K9. EOG4HHP3Z.
PhylomeDB	P62807.
Enzyme and pathway databases
Reactome	REACT_111183. Meiosis. REACT_22172. Chromosome Maintenance. REACT_75925. Amyloids.
Gene expression databases
ArrayExpress	P62807.
Bgee	P62807.
CleanEx	HS_HIST1H2BC. HS_HIST1H2BE. HS_HIST1H2BF. HS_HIST1H2BG. HS_HIST1H2BI.
Genevestigator	P62807.
GermOnline	ENSG00000168242. Homo sapiens. ENSG00000180596. Homo sapiens. ENSG00000187990. Homo sapiens. ENSG00000197697. Homo sapiens. ENSG00000197846. Homo sapiens. ENSG00000197903. Homo sapiens.
Family and domain databases
InterPro	IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR000558. Histone_H2B. [Graphical view]
Gene3D	G3DSA:1.10.20.10. Histone-fold. 1 hit.
KO	K11252.
PANTHER	PTHR23428. Histone_H2B. 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
SOURCE	Search...

Entry information

Entry name

H2B1C_HUMAN

Accession

Primary (citable) accession number: P62807
Secondary accession number(s): P02278 , Q3B872, Q4VB69, Q93078, Q93080

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	March 2, 2010
Last modified:	January 25, 2012
This is version 94 of the entry and version 4 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.