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A2QY49

- H2B_ASPNC

UniProt

A2QY49 - H2B_ASPNC

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Protein
Histone H2B
Gene
htb1, An11g11310
Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

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.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. nucleosome assembly Source: InterPro
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2B
Gene namesi
Name:htb1
ORF Names:An11g11310
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 7R

Subcellular locationi

Nucleus By similarity. Chromosome By similarity

GO - Cellular componenti

  1. nucleosome Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 141140Histone H2B
PRO_0000297846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81N6-acetyllysine; alternate By similarity
Cross-linki8 – 8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Modified residuei9 – 91N6-acetyllysine; alternate By similarity
Cross-linki9 – 9Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Modified residuei15 – 151N6-acetyllysine By similarity
Modified residuei26 – 261N6-acetyllysine; alternate By similarity
Cross-linki26 – 26Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Cross-linki27 – 27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-linki135 – 135Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

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

STRINGi5061.CADANGAP00009270.

Structurei

3D structure databases

ProteinModelPortaliA2QY49.
SMRiA2QY49. Positions 22-139.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.

Phylogenomic databases

eggNOGiNOG289161.
HOGENOMiHOG000231213.
KOiK11252.
OrthoDBiEOG7WHHPK.

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.

A2QY49-1 [UniParc]FASTAAdd to Basket

« Hide

MPPKAAEKKP STGGKAPAGG KAPAEKKEAG KKTAAAASGD KKKRGKTRKE    50
TYSSYIYKVL KQVHPDTGIS TRAMSILNSF VNDIFERVAT EASKLAAYNK 100
KSTISSREIQ TSVRLILPGE LAKHAVSEGT KAVTKYSSSA K 141
Length:141
Mass (Da):14,998
Last modified:March 6, 2007 - v1
Checksum:iB0CC2518858D47B2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270257 Genomic DNA. Translation: CAK40929.1.
RefSeqiXP_001395088.1. XM_001395051.2.

Genome annotation databases

EnsemblFungiiCADANGAT00009448; CADANGAP00009270; CADANGAG00009448.
GeneIDi4985348.
KEGGiang:ANI_1_1488094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270257 Genomic DNA. Translation: CAK40929.1 .
RefSeqi XP_001395088.1. XM_001395051.2.

3D structure databases

ProteinModelPortali A2QY49.
SMRi A2QY49. Positions 22-139.
ModBasei Search...

Protein-protein interaction databases

STRINGi 5061.CADANGAP00009270.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANGAT00009448 ; CADANGAP00009270 ; CADANGAG00009448 .
GeneIDi 4985348.
KEGGi ang:ANI_1_1488094.

Phylogenomic databases

eggNOGi NOG289161.
HOGENOMi HOG000231213.
KOi K11252.
OrthoDBi EOG7WHHPK.

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

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiH2B_ASPNC
AccessioniPrimary (citable) accession number: A2QY49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: March 6, 2007
Last modified: November 13, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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-26; H2BK16su = sumoylated Lys-26; H2BK17su = sumoylated Lys-27; H2BK123ub1 = monoubiquitinated Lys-135.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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