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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04569; PubMed=16541075 [NCBI, ExPASy, EBI, Israel, Japan]
Scherer S.E.,
Muzny D.M.,
Buhay C.J.,
Chen R.,
Cree A.,
Ding Y.,
Dugan-Rocha S.,
Gill R.,
Gunaratne P.,
Harris R.A.,
Hawes A.C.,
Hernandez J.,
Hodgson A.V.,
Hume J.,
Jackson A.,
Khan Z.M.,
Kovar-Smith C.,
Lewis L.R.,
Lozado R.J., ![]()
Metzker M.L.,
Milosavljevic A.,
Miner G.R.,
Montgomery K.T.,
Morgan M.B.,
Nazareth L.V.,
Scott G.,
Sodergren E.,
Song X.-Z.,
Steffen D.,
Lovering R.C.,
Wheeler D.A.,
Worley K.C.,
Yuan Y.,
Zhang Z.,
Adams C.Q.,
Ansari-Lari M.A.,
Ayele M.,
Brown M.J.,
Chen G.,
Chen Z.,
Clerc-Blankenburg K.P.,
Davis C.,
Delgado O.,
Dinh H.H.,
Draper H.,
Gonzalez-Garay M.L.,
Havlak P.,
Jackson L.R.,
Jacob L.S.,
Kelly S.H.,
Li L.,
Li Z.,
Liu J.,
Liu W.,
Lu J.,
Maheshwari M.,
Nguyen B.-V.,
Okwuonu G.O.,
Pasternak S.,
Perez L.M.,
Plopper F.J.H.,
Santibanez J.,
Shen H.,
Tabor P.E.,
Verduzco D.,
Waldron L.,
Wang Q.,
Williams G.A.,
Zhang J.,
Zhou J.,
Allen C.C.,
Amin A.G.,
Anyalebechi V.,
Bailey M.,
Barbaria J.A.,
Bimage K.E.,
Bryant N.P.,
Burch P.E.,
Burkett C.E.,
Burrell K.L.,
Calderon E.,
Cardenas V.,
Carter K.,
Casias K.,
Cavazos I.,
Cavazos S.R.,
Ceasar H.,
Chacko J.,
Chan S.N.,
Chavez D.,
Christopoulos C.,
Chu J.,
Cockrell R.,
Cox C.D.,
Dang M.,
Dathorne S.R.,
David R.,
Davis C.M.,
Davy-Carroll L.,
Deshazo D.R.,
Donlin J.E.,
D'Souza L.,
Eaves K.A.,
Egan A.,
Emery-Cohen A.J.,
Escotto M.,
Flagg N.,
Forbes L.D.,
Gabisi A.M.,
Garza M.,
Hamilton C.,
Henderson N.,
Hernandez O.,
Hines S.,
Hogues M.E.,
Huang M.,
Idlebird D.G.,
Johnson R.,
Jolivet A.,
Jones S.,
Kagan R.,
King L.M.,
Leal B.,
Lebow H.,
Lee S.,
LeVan J.M.,
Lewis L.C.,
London P.,
Lorensuhewa L.M.,
Loulseged H.,
Lovett D.A.,
Lucier A.,
Lucier R.L.,
Ma J.,
Madu R.C.,
Mapua P.,
Martindale A.D.,
Martinez E.,
Massey E.,
Mawhiney S.,
Meador M.G.,
Mendez S.,
Mercado C.,
Mercado I.C.,
Merritt C.E.,
Miner Z.L.,
Minja E.,
Mitchell T.,
Mohabbat F.,
Mohabbat K.,
Montgomery B.,
Moore N.,
Morris S.,
Munidasa M.,
Ngo R.N.,
Nguyen N.B.,
Nickerson E.,
Nwaokelemeh O.O.,
Nwokenkwo S.,
Obregon M.,
Oguh M.,
Oragunye N.,
Oviedo R.J.,
Parish B.J.,
Parker D.N.,
Parrish J.,
Parks K.L.,
Paul H.A.,
Payton B.A.,
Perez A.,
Perrin W.,
Pickens A.,
Primus E.L.,
Pu L.-L.,
Puazo M.,
Quiles M.M.,
Quiroz J.B.,
Rabata D.,
Reeves K.,
Ruiz S.J.,
Shao H.,
Sisson I.,
Sonaike T.,
Sorelle R.P.,
Sutton A.E.,
Svatek A.F.,
Svetz L.A.,
Tamerisa K.S.,
Taylor T.R.,
Teague B.,
Thomas N.,
Thorn R.D.,
Trejos Z.Y.,
Trevino B.K.,
Ukegbu O.N.,
Urban J.B.,
Vasquez L.I.,
Vera V.A.,
Villasana D.M.,
Wang L.,
Ward-Moore S.,
Warren J.T.,
Wei X.,
White F.,
Williamson A.L.,
Wleczyk R.,
Wooden H.S.,
Wooden S.H.,
Yen J.,
Yoon L.,
Yoon V.,
Zorrilla S.E.,
Nelson D.,
Kucherlapati R.,
Weinstock G.,
Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
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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- 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.
- SUBCELLULAR LOCATION: Nucleus.
- 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) is linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. 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) requires 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, probably by DAPK3. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 by MLTK isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation.
- SIMILARITY: Belongs to the histone H3 family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 135 AA [This is the length of the unprocessed precursor] |
Molecular weight: 15214 Da [This is the MW of the unprocessed precursor] |
CRC64: F2941F8A9BC61BB5 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MARTKQTARK STGGKAPRKQ LATKAARKST PSTCGVKPHR YRPGTVALRE IRRYQKSTEL
70 80 90 100 110 120
LIRKLPFQRL VREIAQDFNT DLRFQSAAVG ALQEASEAYL VGLLEDTNLC AIHAKRVTIM
130
PKDIQLARRI RGERA
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Q6NXT2 in FASTA format |
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