P37210 (H2B_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H2B

Gene names

Name:	hh2b
ORF Names:	NCU02435

Organism

Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]

Taxonomic identifier

367110 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora › Neurospora crassa

Protein attributes

Sequence length	137 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.
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	Monoubiquitinated by the ubc-2-bre-1 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. Phosphorylated by ste-20 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation By similarity. Acetylated by gcn-5 to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by esa-1. 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; H2BS10ph = phosphorylated Ser-12; H2BK11ac = acetylated Lys-13; H2BK16ac = acetylated Lys-24; H2BK16su = sumoylated Lys-24; H2BK17su = sumoylated Lys-25; H2BK123ub1 = monoubiquitinated Lys-131.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference 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 – 137	136	Histone H2B		PRO_0000071935
Amino acid modifications
	Modified residue	8	1	N6-acetyllysine; alternate By similarity
	Modified residue	9	1	N6-acetyllysine; alternate By similarity
	Modified residue	12	1	Phosphoserine By similarity
	Modified residue	13	1	N6-acetyllysine By similarity
	Modified residue	24	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	24		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) By similarity
	Cross-link	131		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Experimental info
	Sequence conflict	68 – 69	2	RA → KS AA sequence Ref.3
	Sequence conflict	133	1	S → T AA sequence Ref.3
	Sequence conflict	136	1	Missing AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P37210 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 324E2D13B1FF9D50	FASTA	137	14,841
	10 20 30 40 50 60 MPPKPADKKP ASKAPATASK APEKKDAGKK TAASGDKKKR TKARKETYSS YIYKVLKQVH 70 80 90 100 110 120 PDTGISNRAM SILNSFVNDI FERVATEASK LAAYNKKSTI SSREIQTSVR LILPGELAKH 130 AVSEGTKAVT KYSSSTK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of the genes encoding the core histones and histone variants of Neurospora crassa." Hays S.M., Swanson J., Selker E.U. Genetics 160:961-973(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome sequence of the filamentous fungus Neurospora crassa." Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D. , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W. Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]	"Some peculiarities of primary structure of histone H2b of the mould fungus Neurospora crassa." Karpova O.I., Ananyeva N.M., Ermokhina T.M., Krasheninnikov I.A. Biokhimiia 51:788-800(1986) Cited for: PROTEIN SEQUENCE OF 43-137. Strain: ATCC 32313 / FGSC 327.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY062171 Genomic DNA. Translation: AAL38971.1. AABX02000010 Genomic DNA. Translation: EAA30204.1.
PIR	PN0142.
RefSeq	XP_959440.1. XM_954347.2.
UniGene	Ncr.22778.
3D structure databases
ProteinModelPortal	P37210.
SMR	P37210. Positions 18-135.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-59936N.
STRING	5141.NCU02435.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	EFNCRT00000003257; EFNCRP00000003257; EFNCRG00000003253.
GeneID	3875587.
KEGG	ncr:NCU02435.
Phylogenomic databases
eggNOG	NOG289161.
HOGENOM	HOG000231213.
KO	K11252.
OMA	TQKKEGR.
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_NEUCR

Accession

Primary (citable) accession number: P37210
Secondary accession number(s): Q7S3Y6, Q8X131

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 105 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program