UniProt ID | H32_ARATH | |
---|---|---|
UniProt AC | P59226 | |
Protein Name | Histone H3.2 | |
Gene Name | HTR2 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 136 | |
Subcellular Localization | Nucleus . Chromosome . Localized at chromocenters. | |
Protein Description | 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.. | |
Protein Sequence | MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRFRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVAALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
5 | "N6,N6,N6-trimethyllysine" | ---MARTKQTARKST ---CCCCCHHHHHCC | 39.85 | - | |
5 | Methylation | ---MARTKQTARKST ---CCCCCHHHHHCC | 39.85 | 14712277 | |
10 | "N6,N6,N6-trimethyllysine" | RTKQTARKSTGGKAP CCCHHHHHCCCCCCC | 50.32 | - | |
10 | Methylation | RTKQTARKSTGGKAP CCCHHHHHCCCCCCC | 50.32 | 12456661 | |
10 | Acetylation | RTKQTARKSTGGKAP CCCHHHHHCCCCCCC | 50.32 | 12581305 | |
11 | Phosphorylation | TKQTARKSTGGKAPR CCHHHHHCCCCCCCH | 27.08 | 14610360 | |
12 | Phosphorylation | KQTARKSTGGKAPRK CHHHHHCCCCCCCHH | 53.65 | 15753571 | |
15 | Acetylation | ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH | 57.47 | 17363895 | |
19 | Acetylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | 12581305 | |
19 | Methylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | 15598823 | |
24 | Acetylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | 15598823 | |
24 | Methylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | 15598823 | |
28 | Acetylation | LATKAARKSAPATGG HHHHHHHHHCCCCCC | 46.36 | 21311030 | |
28 | "N6,N6,N6-trimethyllysine" | LATKAARKSAPATGG HHHHHHHHHCCCCCC | 46.36 | - | |
28 | Methylation | LATKAARKSAPATGG HHHHHHHHHCCCCCC | 46.36 | 24626927 | |
29 | Phosphorylation | ATKAARKSAPATGGV HHHHHHHHCCCCCCC | 33.65 | 14610360 | |
37 | "N6,N6,N6-trimethyllysine" | APATGGVKKPHRFRP CCCCCCCCCCCCCCC | 64.95 | - | |
37 | Methylation | APATGGVKKPHRFRP CCCCCCCCCCCCCCC | 64.95 | 16299497 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of H32_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of H32_ARATH !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of H32_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of H32_ARATH !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"SKB1-mediated symmetric dimethylation of histone H4R3 controlsflowering time in Arabidopsis."; Wang X., Zhang Y., Ma Q., Zhang Z., Xue Y., Bao S., Chong K.; EMBO J. 26:1934-1941(2007). Cited for: ACETYLATION AT LYS-15. | |
"Erasure of histone acetylation by Arabidopsis HDA6 mediates large-scale gene silencing in nucleolar dominance."; Earley K., Lawrence R.J., Pontes O., Reuther R., Enciso A.J.,Silva M., Neves N., Gross M., Viegas W., Pikaard C.S.; Genes Dev. 20:1283-1293(2006). Cited for: ACETYLATION AT LYS-15 BY HAG1, AND DEACETYLATION BY HDA6. | |
"Mass spectrometry analysis of Arabidopsis histone H3 reveals distinctcombinations of post-translational modifications."; Johnson L., Mollah S., Garcia B.A., Muratore T.L., Shabanowitz J.,Hunt D.F., Jacobsen S.E.; Nucleic Acids Res. 32:6511-6518(2004). Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19 AND LYS-24, ABSENCE OFACETYLATION AT LYS-28 AND LYS-37, METHYLATION AT LYS-5; LYS-10;LYS-19; LYS-24; LYS-28 AND LYS-37, ABSENCE OF METHYLATION AT LYS-15,AND MASS SPECTROMETRY. | |
"Histone modifications in Arabidopsis -- high methylation of H3 lysine9 is dispensable for constitutive heterochromatin."; Jasencakova Z., Soppe W.J.J., Meister A., Gernand D., Turner B.M.,Schubert I.; Plant J. 33:471-480(2003). Cited for: ACETYLATION AT LYS-10 AND LYS-19, AND METHYLATION AT LYS-5 AND LYS-10. | |
Methylation | |
Reference | PubMed |
"Whole-genome analysis of histone H3 lysine 27 trimethylation inArabidopsis."; Zhang X., Clarenz O., Cokus S., Bernatavichute Y.V., Pellegrini M.,Goodrich J., Jacobsen S.E.; PLoS Biol. 5:1026-1035(2007). Cited for: METHYLATION AT LYS-28, AND SUBCELLULAR LOCATION. | |
"The PHD finger protein VRN5 functions in the epigenetic silencing ofArabidopsis FLC."; Greb T., Mylne J.S., Crevillen P., Geraldo N., An H., Gendall A.R.,Dean C.; Curr. Biol. 17:73-78(2007). Cited for: ACETYLATION, AND METHYLATION AT LYS-28. | |
"Prevention of early flowering by expression of FLOWERING LOCUS Crequires methylation of histone H3 K36."; Zhao Z., Yu Y., Meyer D., Wu C., Shen W.-H.; Nat. Cell Biol. 7:1256-1260(2005). Cited for: METHYLATION AT LYS-37. | |
"Establishment of the vernalization-responsive, winter-annual habit inArabidopsis requires a putative histone H3 methyl transferase."; Kim S.Y., He Y., Jacob Y., Noh Y.-S., Michaels S., Amasino R.; Plant Cell 17:3301-3310(2005). Cited for: METHYLATION AT LYS-5. | |
"Vernalization requires epigenetic silencing of FLC by histonemethylation."; Bastow R., Mylne J.S., Lister C., Lippman Z., Martienssen R.A.,Dean C.; Nature 427:164-167(2004). Cited for: METHYLATION AT LYS-5; LYS-10 AND LYS-28. | |
"Mass spectrometry analysis of Arabidopsis histone H3 reveals distinctcombinations of post-translational modifications."; Johnson L., Mollah S., Garcia B.A., Muratore T.L., Shabanowitz J.,Hunt D.F., Jacobsen S.E.; Nucleic Acids Res. 32:6511-6518(2004). Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19 AND LYS-24, ABSENCE OFACETYLATION AT LYS-28 AND LYS-37, METHYLATION AT LYS-5; LYS-10;LYS-19; LYS-24; LYS-28 AND LYS-37, ABSENCE OF METHYLATION AT LYS-15,AND MASS SPECTROMETRY. | |
"Dimethylation of histone H3 lysine 9 is a critical mark for DNAmethylation and gene silencing in Arabidopsis thaliana."; Jackson J.P., Johnson L., Jasencakova Z., Zhang X., PerezBurgos L.,Singh P.B., Cheng X., Schubert I., Jenuwein T., Jacobsen S.E.; Chromosoma 112:308-315(2004). Cited for: METHYLATION AT LYS-10. | |
"Histone modifications in Arabidopsis -- high methylation of H3 lysine9 is dispensable for constitutive heterochromatin."; Jasencakova Z., Soppe W.J.J., Meister A., Gernand D., Turner B.M.,Schubert I.; Plant J. 33:471-480(2003). Cited for: ACETYLATION AT LYS-10 AND LYS-19, AND METHYLATION AT LYS-5 AND LYS-10. | |
"DNA methylation controls histone H3 lysine 9 methylation andheterochromatin assembly in Arabidopsis."; Soppe W.J.J., Jasencakova Z., Houben A., Kakutani T., Meister A.,Huang M.S., Jacobsen S.E., Schubert I., Fransz P.F.; EMBO J. 21:6549-6559(2002). Cited for: METHYLATION AT LYS-10. | |
Phosphorylation | |
Reference | PubMed |
"Novel phosphorylation of histone H3 at threonine 11 that temporallycorrelates with condensation of mitotic and meiotic chromosomes inplant cells."; Houben A., Demidov D., Rutten T., Scheidtmann K.H.; Cytogenet. Genome Res. 109:148-155(2005). Cited for: PHOSPHORYLATION AT SER-11; THR-12 AND SER-29. | |
"The temporal and spatial pattern of histone H3 phosphorylation atserine 28 and serine 10 is similar in plants but differs between mono-and polycentric chromosomes."; Gernand D., Demidov D., Houben A.; Cytogenet. Genome Res. 101:172-176(2003). Cited for: PHOSPHORYLATION AT SER-11 AND SER-29. |