H32_ARATH - dbPTM
H32_ARATH - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
5"N6,N6,N6-trimethyllysine"---MARTKQTARKST
---CCCCCHHHHHCC
39.85-
5Methylation---MARTKQTARKST
---CCCCCHHHHHCC
39.8514712277
10"N6,N6,N6-trimethyllysine"RTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.32-
10MethylationRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.3212456661
10AcetylationRTKQTARKSTGGKAP
CCCHHHHHCCCCCCC
50.3212581305
11PhosphorylationTKQTARKSTGGKAPR
CCHHHHHCCCCCCCH
27.0814610360
12PhosphorylationKQTARKSTGGKAPRK
CHHHHHCCCCCCCHH
53.6515753571
15AcetylationARKSTGGKAPRKQLA
HHHCCCCCCCHHHHH
57.4717363895
19AcetylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.9112581305
19MethylationTGGKAPRKQLATKAA
CCCCCCHHHHHHHHH
48.9115598823
24AcetylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.1515598823
24MethylationPRKQLATKAARKSAP
CHHHHHHHHHHHHCC
34.1515598823
28AcetylationLATKAARKSAPATGG
HHHHHHHHHCCCCCC
46.3621311030
28"N6,N6,N6-trimethyllysine"LATKAARKSAPATGG
HHHHHHHHHCCCCCC
46.36-
28MethylationLATKAARKSAPATGG
HHHHHHHHHCCCCCC
46.3624626927
29PhosphorylationATKAARKSAPATGGV
HHHHHHHHCCCCCCC
33.6514610360
37"N6,N6,N6-trimethyllysine"APATGGVKKPHRFRP
CCCCCCCCCCCCCCC
64.95-
37MethylationAPATGGVKKPHRFRP
CCCCCCCCCCCCCCC
64.9516299497

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of H32_ARATH !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of H32_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of H32_ARATH

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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
ReferencePubMed
"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
ReferencePubMed
"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.

TOP