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Q8X132

- H2A_NEUCR

UniProt

Q8X132 - H2A_NEUCR

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Protein

Histone H2A

Gene

hh2a

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei121 – 1211Not ubiquitinatedCurated

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

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

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A
Gene namesi
Name:hh2a
Synonyms:hta-1
ORF Names:NCU02437
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805: Chromosome 7, Linkage Group VII

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 134133Histone H2APRO_0000055323Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61N6-acetyllysineBy similarity
Modified residuei10 – 101N6-acetyllysineBy similarity
Modified residuei107 – 1071N5-methylglutamineBy similarity
Modified residuei131 – 1311PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases mec-1/ATR and tel-1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint (By similarity).By similarity
Acetylated by esa-1 to form H2AK4ac and H2AK7ac.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PRIDEiQ8X132.

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

DIPiDIP-59935N.
STRINGi5141.NCU02437.1.

Structurei

3D structure databases

ProteinModelPortaliQ8X132.
SMRiQ8X132. Positions 18-125.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi131 – 1322[ST]-Q motif

Domaini

The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGiCOG5262.
HOGENOMiHOG000234652.
InParanoidiQ8X132.
KOiK11251.
OMAiTKNAQSR.
OrthoDBiEOG7GN30N.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00046. HISTONE_H2A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8X132-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTGGGKSGGK ASGSKNAQSR SSKAGLAFPV GRVHRLLRKG NYAQRVGAGA
60 70 80 90 100
PVYLAAVLEY LAAEILELAG NAARDNKKTR IIPRHLQLAI RNDEELNKLL
110 120 130
GHVTIAQGGV LPNIHQNLLP KKTGKTGKNA SQEL
Length:134
Mass (Da):14,154
Last modified:January 23, 2007 - v3
Checksum:iEE093088EC4850F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY062171 Genomic DNA. Translation: AAL38970.1.
CM002242 Genomic DNA. Translation: EAA30206.1.
RefSeqiXP_959442.1. XM_954349.2.

Genome annotation databases

EnsemblFungiiEFNCRT00000003190; EFNCRP00000003190; EFNCRG00000003187.
GeneIDi3875589.
KEGGincr:NCU02437.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY062171 Genomic DNA. Translation: AAL38970.1 .
CM002242 Genomic DNA. Translation: EAA30206.1 .
RefSeqi XP_959442.1. XM_954349.2.

3D structure databases

ProteinModelPortali Q8X132.
SMRi Q8X132. Positions 18-125.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-59935N.
STRINGi 5141.NCU02437.1.

Proteomic databases

PRIDEi Q8X132.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii EFNCRT00000003190 ; EFNCRP00000003190 ; EFNCRG00000003187 .
GeneIDi 3875589.
KEGGi ncr:NCU02437.

Phylogenomic databases

eggNOGi COG5262.
HOGENOMi HOG000234652.
InParanoidi Q8X132.
KOi K11251.
OMAi TKNAQSR.
OrthoDBi EOG7GN30N.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view ]
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00620. HISTONEH2A.
SMARTi SM00414. H2A. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00046. HISTONE_H2A. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiH2A_NEUCR
AccessioniPrimary (citable) accession number: Q8X132
Secondary accession number(s): Q7S3Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 93 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

In contrast to vertebrates and insects, its C-terminus is not monoubiquitinated.Curated

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: H2AK4ac = acetylated Lys-6; H2AK7ac = acetylated Lys-10; H2AS128ph = phosphorylated Ser-131.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3