H3_NEUCR
ID H3_NEUCR Reviewed; 136 AA.
AC P07041; Q7RV46; Q8WZD9;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Histone H3;
GN Name=hh3; ORFNames=B7K22.030, NCU01635;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6310494; DOI=10.1093/nar/11.16.5347;
RA Woudt L.P., Pastink A., Kempers-Veenstra A.E., Jansen A.E.M., Mager W.H.,
RA Planta R.J.;
RT "The genes coding for histone H3 and H4 in Neurospora crassa are unique and
RT contain intervening sequences.";
RL Nucleic Acids Res. 11:5347-5360(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11901114; DOI=10.1093/genetics/160.3.961;
RA Hays S.M., Swanson J., Selker E.U.;
RT "Identification and characterization of the genes encoding the core
RT histones and histone variants of Neurospora crassa.";
RL Genetics 160:961-973(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [5]
RP METHYLATION AT LYS-10.
RX PubMed=12679815; DOI=10.1038/ng1143;
RA Tamaru H., Zhang X., McMillen D., Singh P.B., Nakayama J., Grewal S.I.,
RA Allis C.D., Cheng X., Selker E.U.;
RT "Trimethylated lysine 9 of histone H3 is a mark for DNA methylation in
RT Neurospora crassa.";
RL Nat. Genet. 34:75-79(2003).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC DNA into chromatin, limiting DNA accessibility to the cellular
CC machineries which require DNA as a template. Histones thereby play a
CC central role in transcription regulation, DNA repair, DNA replication
CC and chromosomal stability. DNA accessibility is regulated via a complex
CC set of post-translational modifications of histones, also called
CC histone code, and nucleosome remodeling.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC DNA.
CC -!- INTERACTION:
CC P07041; Q8X225: dim-5; NbExp=2; IntAct=EBI-1270655, EBI-1268994;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- PTM: Phosphorylated to form H3S10ph. H3S10ph promotes subsequent
CC H3K14ac formation and is required for transcriptional activation
CC through TBP recruitment to the promoters (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Mono-, di- and trimethylated by the COMPASS complex to form
CC H3K4me1/2/3. H3K4me activates gene expression by regulating
CC transcription elongation and plays a role in telomere length
CC maintenance. H3K4me enrichment correlates with transcription levels,
CC and occurs in a 5' to 3' gradient with H3K4me3 enrichment at the 5'-end
CC of genes, shifting to H3K4me2 and then H3K4me1. Trimethylated by
CC methyltransferase dim-5 to form H3K9me3. H3K9me3, but not H3K9me2,
CC marks chromatin regions for cytosine methylation. Methylated by set-2
CC to form H3K36me. H3K36me represses gene expression. Methylated by dot-1
CC to form H3K79me. H3K79me is required for association of SIR proteins
CC with telomeric regions and for telomeric silencing. The COMPASS-
CC mediated formation of H3K4me2/3 and the dot-1-mediated formation of
CC H3K79me require H2BK123ub1 (By similarity). {ECO:0000250}.
CC -!- PTM: Acetylation of histone H3 leads to transcriptional activation.
CC H3K14ac formation by gcn-5 is promoted by H3S10ph. H3K14ac can also be
CC formed by esa-1. H3K56ac formation occurs predominantly in newly
CC synthesized H3 molecules during G1, S and G2/M of the cell cycle and
CC may be involved in DNA repair (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC -!- CAUTION: To ensure consistency between histone entries, we follow the
CC 'Brno' nomenclature for histone modifications, with positions referring
CC to those used in the literature for the 'closest' model organism. Due
CC to slight variations in histone sequences between organisms and to the
CC presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC actual positions of modified amino acids in the sequence generally
CC differ. In this entry the following conventions are used: H3K4me1/2/3 =
CC mono-, di- and trimethylated Lys-5; H3K9ac = acetylated Lys-10; H3K9me3
CC = trimethylated Lys-10; H3S10ph = phosphorylated Ser-11; H3K14ac =
CC acetylated Lys-15; H3K14me2 = dimethylated Lys-15; H3K18ac = acetylated
CC Lys-19; H3K18me1 = monomethylated Lys-19; H3K23ac = acetylated Lys-24;
CC H3K23me1 = monomethylated Lys-24; H3K27ac = acetylated Lys-28;
CC H3K27me1/2/3 = mono-, di- and trimethylated Lys-28; H3K36ac =
CC acetylated Lys-37; H3K36me1/2/3 = mono-, di- and trimethylated Lys-37;
CC H3K56ac = acetylated Lys-57; H3K64ac = acetylated Lys-65; H3K79me1/2/3
CC = mono-, di- and trimethylated Lys-80. {ECO:0000305}.
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DR EMBL; X01612; CAA25761.1; -; Genomic_DNA.
DR EMBL; AY062173; AAL38973.1; -; Genomic_DNA.
DR EMBL; AL670543; CAD21510.1; -; Genomic_DNA.
DR EMBL; CM002237; EAA26767.1; -; Genomic_DNA.
DR PIR; S07350; S07350.
DR RefSeq; XP_956003.1; XM_950910.3.
DR AlphaFoldDB; P07041; -.
DR SMR; P07041; -.
DR DIP; DIP-39601N; -.
DR IntAct; P07041; 2.
DR STRING; 5141.EFNCRP00000001782; -.
DR EnsemblFungi; EAA26767; EAA26767; NCU01635.
DR GeneID; 3872150; -.
DR KEGG; ncr:NCU01635; -.
DR VEuPathDB; FungiDB:NCU01635; -.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; P07041; -.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0009303; P:rRNA transcription; IBA:GO_Central.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00322; HISTONE_H3_1; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; DNA-binding; Methylation; Nucleosome core;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..136
FT /note="Histone H3"
FT /id="PRO_0000221364"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:12679815"
FT MOD_RES 10
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 24
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 65
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 80
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 80
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 80
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250"
FT CONFLICT 92
FT /note="A -> L (in Ref. 1; CAA25761)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 136 AA; 15392 MW; 9AF51E808E698349 CRC64;
MARTKQTARK STGGKAPRKQ LASKAARKSA PSTGGVKKPH RYKPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK SDLRFQSSAI GALQESVESY LVSLFEDTNL CAIHAKRVTI
QSKDIQLARR LRGERN
