A1D8G9 (H2B_NEOFI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H2B

Gene names

Name:	htb1
ORF Names:	NFIA_071840

Organism

Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus) [Complete proteome]

Taxonomic identifier

331117 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Neosartorya › Neosartorya fischeri group › Neosartorya fischeri

Protein attributes

Sequence length	140 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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.
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 By similarity. Chromosome By similarity.
Post-translational modification	Monoubiquitinated by the ubc2-bre1 complex to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation. H2BK123ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damage checkpoint activation By similarity. Acetylated by gcn5 to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by esa1. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription By similarity. Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription By similarity.
Sequence similarities	Belongs to the histone H2B family.
Caution	To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H2BK6ac = acetylated Lys-8; H2BK6su = sumoylated Lys-8; H2BK7ac = acetylated Lys-9; H2BK7su = sumoylated Lys-9; H2BK11ac = acetylated Lys-15; H2BK16ac = acetylated Lys-25; H2BK16su = sumoylated Lys-25; H2BK17su = sumoylated Lys-26; H2BK123ub1 = monoubiquitinated Lys-134.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Isopeptide bond Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleosome Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 140	139	Histone H2B		PRO_0000297850
Amino acid modifications
	Modified residue	8	1	N6-acetyllysine; alternate By similarity
	Modified residue	9	1	N6-acetyllysine; alternate By similarity
	Modified residue	15	1	N6-acetyllysine By similarity
	Modified residue	25	1	N6-acetyllysine; alternate By similarity
	Cross-link	8		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
	Cross-link	9		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
	Cross-link	25		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
	Cross-link	26		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	134		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1D8G9 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: 1F162438ADAF4872	FASTA	140	14,955
	10 20 30 40 50 60 MPPKAAEKKP STGGKAPAGK APAEKKEAGK KTAAAATGDK KKRGKTRKET YSSYIYKVLK 70 80 90 100 110 120 QVHPDTGIST RAMSILNSFV NDIFERVATE ASKLAAYNKK STISSREIQT SVRLILPGEL 130 140 AKHAVSEGTK AVTKYSSSAK

References

[1]

"Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. , Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., Jiang B., Denning D.W., Nierman W.C. PLoS Genet. 4:E1000046-E1000046(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS027690 Genomic DNA. Translation: EAW22013.1.
RefSeq	XP_001263910.1. XM_001263909.1.
3D structure databases
ProteinModelPortal	A1D8G9.
SMR	A1D8G9. Positions 18-138.
ModBase	Search...
Protein-protein interaction databases
STRING	36630.CADNFIAP00005834.
Proteomic databases
PRIDE	A1D8G9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADNFIAT00005991; CADNFIAP00005834; CADNFIAG00005991.
GeneID	4590556.
KEGG	nfi:NFIA_071840.
Phylogenomic databases
eggNOG	NOG289161.
HOGENOM	HOG000231213.
KO	K11252.
OrthoDB	EOG4MKRS0.
Family and domain databases
Gene3D	1.10.20.10. 1 hit.
InterPro	IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR000558. Histone_H2B. [Graphical view]
PANTHER	PTHR23428. PTHR23428. 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...

Entry information

Entry name

H2B_NEOFI

Accession

Primary (citable) accession number: A1D8G9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 21, 2007
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program