[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1007/s004390050078; PubMed=8834248 [NCBI, ExPASy, EBI, Israel, Japan]
Albig W.,
Ebentheuer J.,
Klobeck H.,
Kunz J.,
Doenecke D.;
"A solitary human H3 histone gene on chromosome 1.";
Hum. Genet. 97:486-491(1996).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/S0888-7543(02)96850-3; PubMed=12408966 [NCBI, ExPASy, EBI, Israel, Japan]
Marzluff W.F.,
Gongidi P.,
Woods K.R.,
Jin J.,
Maltais L.J.;
"The human and mouse replication-dependent histone genes.";
Genomics 80:487-498(2002).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L.,
Schick M.,
Neubert P.,
Schatten R.,
Henze S.,
Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G.,
Barlow K.F.,
McLay K.E.,
Kaul R.,
Swarbreck D.,
Dunham A.,
Scott C.E.,
Howe K.L.,
Woodfine K.,
Spencer C.C.A.,
Jones M.C.,
Gillson C.,
Searle S.,
Zhou Y.,
Kokocinski F.,
McDonald L.,
Evans R.,
Phillips K.,
Atkinson A.,
Cooper R.,
Jones C.,
Hall R.E.,
Andrews T.D.,
Lloyd C.,
Ainscough R.,
Almeida J.P.,
Ambrose K.D.,
Anderson F.,
Andrew R.W.,
Ashwell R.I.S.,
Aubin K.,
Babbage A.K.,
Bagguley C.L.,
Bailey J.,
Beasley H.,
Bethel G.,
Bird C.P.,
Bray-Allen S.,
Brown J.Y.,
Brown A.J.,
Buckley D.,
Burton J.,
Bye J.,
Carder C.,
Chapman J.C.,
Clark S.Y.,
Clarke G.,
Clee C.,
Cobley V.,
Collier R.E.,
Corby N.,
Coville G.J.,
Davies J.,
Deadman R.,
Dunn M.,
Earthrowl M.,
Ellington A.G.,
Errington H.,
Frankish A.,
Frankland J.,
French L.,
Garner P.,
Garnett J.,
Gay L.,
Ghori M.R.J.,
Gibson R.,
Gilby L.M.,
Gillett W.,
Glithero R.J.,
Grafham D.V.,
Griffiths C.,
Griffiths-Jones S.,
Grocock R.,
Hammond S.,
Harrison E.S.I.,
Hart E.,
Haugen E.,
Heath P.D.,
Holmes S.,
Holt K.,
Howden P.J.,
Hunt A.R.,
Hunt S.E.,
Hunter G.,
Isherwood J.,
James R.,
Johnson C.,
Johnson D.,
Joy A.,
Kay M.,
Kershaw J.K.,
Kibukawa M.,
Kimberley A.M.,
King A.,
Knights A.J.,
Lad H.,
Laird G.,
Lawlor S.,
Leongamornlert D.A.,
Lloyd D.M.,
Loveland J.,
Lovell J.,
Lush M.J.,
Lyne R.,
Martin S.,
Mashreghi-Mohammadi M.,
Matthews L.,
Matthews N.S.W.,
McLaren S.,
Milne S.,
Mistry S.,
Moore M.J.F.,
Nickerson T.,
O'Dell C.N.,
Oliver K.,
Palmeiri A.,
Palmer S.A.,
Parker A.,
Patel D.,
Pearce A.V.,
Peck A.I.,
Pelan S.,
Phelps K.,
Phillimore B.J.,
Plumb R.,
Rajan J.,
Raymond C.,
Rouse G.,
Saenphimmachak C.,
Sehra H.K.,
Sheridan E.,
Shownkeen R.,
Sims S.,
Skuce C.D.,
Smith M.,
Steward C.,
Subramanian S.,
Sycamore N.,
Tracey A.,
Tromans A.,
Van Helmond Z.,
Wall M.,
Wallis J.M.,
White S.,
Whitehead S.L.,
Wilkinson J.E.,
Willey D.L.,
Williams H.,
Wilming L.,
Wray P.W.,
Wu Z.,
Coulson A.,
Vaudin M.,
Sulston J.E.,
Durbin R.M.,
Hubbard T.,
Wooster R.,
Dunham I.,
Carter N.P.,
McVean G.,
Ross M.T.,
Harrow J.,
Olson M.V.,
Beck S.,
Rogers J.,
Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
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[5]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[6]
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METHYLATION [LARGE SCALE ANALYSIS] AT LYS-28, AND MASS SPECTROMETRY.
DOI=10.1038/nmeth715; PubMed=15782174 [NCBI, ExPASy, EBI, Israel, Japan]
Ong S.E.,
Mittler G.,
Mann M.;
"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC.";
Nat. Methods 1:119-126(2004).
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[7]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H.,
Olsen J.V.,
Bairlein M.,
Gnad F.,
Oppermann F.S.,
Korner R.,
Greff Z.,
Keri G.,
Stemmann O.,
Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
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- 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: 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.
- INTERACTION:
O60341:AOF2; NbExp=1; IntAct=EBI-358900, EBI-710124;
O75164:JMJD2A; NbExp=3; IntAct=EBI-358900, EBI-936709;
- SUBCELLULAR LOCATION: Nucleus.
- TISSUE SPECIFICITY: Expressed in testicular cells.
- DEVELOPMENTAL STAGE: Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation.
- PTM: Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8sme2). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me) (By similarity).
- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription (By similarity).
- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8sme2) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters (By similarity).
- PTM: Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin (By similarity).
- PTM: Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during prophase and dephosphorylated during anaphase. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase. Phosphorylated at Ser-11 during the whole mitosis. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation (By similarity).
- PTM: Phosphorylation at Ser-11 (H3S10ph) is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) is important during interphase because it enables the transcription of genes following external stimulation, like stress or growth factors. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylation at Ser-11 (H3S10ph) by AURKB/Aurora-B mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin.
- PTM: Ubiquitinated (By similarity).
- SIMILARITY: Belongs to the histone H3 family.
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