Linked Annotation External Source PAT ID Label Synonyms Similar Term Definition Equivalent Term Annotation Term owl:Thing http://localhost/plosthes.2017-1#2007 http://purl.obolibrary.org/obo/GO_0006304 http://www.bootstrep.eu/ontology/GRO#DNAModification P00000032 DNA Modification modifed DNA [GO Definition]: The covalent alteration of one or more nucleotide sites in DNA, resulting in a change in its properties. P00000032 http://localhost/plosthes.2017-1#2309 http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C17961 http://purl.bioontology.org/ontology/CSP/2101-9974 http://purl.bioontology.org/ontology/MESH/D019175 http://purl.obolibrary.org/obo/GO_0006306 P00000033 DNA Methylation DNA Methylation Process DNA Methylations Methylation, DNA Methylations, DNA [NCIt Definition]: The process by which methyl groups are added to nucleotides in genomic DNA. P00000033 http://purl.obolibrary.org/obo/GO_0044028 P00000034 DNA Hypomethylation [GO Definition]: An decrease in the epigenetic methylation of cytosine and adenosine residues in DNA. P00000034 http://purl.obolibrary.org/obo/GO_0044026 P00000036 DNA Hypermethylation Promoter Hypermethylation [GO Definition]: An increase in the epigenetic methylation of cytosine and adenosine residues in DNA. P00000036 P00000039 Maternal DNA Methylation maternal DNA methylation maternal derived methylation Maternally inherited DNA methylation P00000039 P00000040 Paternal DNA Methylation Paternally inherited DNA methylation P00000040 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2892089/ P00000041 Allelic Methylation allele-specific methylation allelic methylation allelic-methylation allelically methylated In addition to DNA methylation pattern differences between cell lines, DNA methylation can also be allele-specific within a cell line and is thus linked to allele-specific gene expression (ASE). P00000041 P00000042 Gene-specific Methylation P00000042 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5485512/ P00000043 CpG Methylation DNA methylation was found to occur predominantly on cytosines followed by guanine residues (CpG). This type of methylation is referred to as CpG methylation, and cytosine methylated at the fifth carbon of the pyrimidine ring is called 5-methylcytosine (5mC). P00000043 P00000044 Differential DNA Methylation P00000044 P00000045 Tissue-Specific Differential DNA Methylation P00000045 https://www-sciencedirect-com.proxy1.library.jhu.edu/science/article/pii/S0168952511001582 P00000046 De Novo DNA Methylation De novo DNA methylation takes place in distinct cellular contexts in male and female germ cells and this is an important notion to consider from a mechanistic point of view P00000046 http://nathansheffield.com/wordpress/what-is-hemimethylated-dna/ P00000047 DNA Hemimethylation DNA-hemimethylation DNA-hemimethylation is when only one of two (complementary) strands is methylated. A hemi-methylated site is a single CpG that is methylated on one strand, but not on the other. P00000047 http://purl.obolibrary.org/obo/GO_0044729 P00000048 Hemimethylated DNA Binding double-stranded hemi-methylated DNA binding hemi-methylated DNA binding hemi-methylated DNA-binding [GO Definition]: Interacting selectively and non-covalently with double-stranded hemi-methylated DNA at replication foci (one strand methylated, while the other strand is unmethylated). Methylation of cytosine or adenine in DNA is an important mechanism for establishing stable heritable epigenetic marks. P00000048 http://purl.bioontology.org/ontology/MESH/D000073399 http://purl.obolibrary.org/obo/GO_0080111 P00000049 DNA Demethylation DNA Demethylations Demethylation, DNA Demethylations, DNA [GO Definition]: The removal of a methyl group from one or more nucleotides within an DNA molecule. P00000049 http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C106316 P00000050 DNA Hydroxmethylation [NCIt Definition]: A DNA modification process where a hydrogen at the C5-position of a cytosine residue is replaced with a hydroxmethyl group. P00000050 http://purl.obolibrary.org/obo/GO_0006325 P00000051 Chromatin Organization chromatin modification chromatin organisation chromatin organization establishment or maintenance of chromatin architecture [GO Definition]: Any process that results in the specification, formation or maintenance of the physical structure of eukaryotic chromatin. P00000051 http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C19797 http://purl.obolibrary.org/obo/GO_0006338 P00000052 Chromatin Remodeling Chromatin Remodeling Cofactor chromatin modeling chromatin modelling chromatin remodelling [NCIt Definition]: Chromatin Remodeling involves alterations of the content or activity of DNA-binding and chromatin-associated proteins that affect the function and higher order conformational state of chromatin, as well as the activity of specific genes or functional DNA regions. P00000052 http://purl.obolibrary.org/obo/GO_0042393 P00000054 Histone Binding histone-specific chaperone activity [GO Definition]: Interacting selectively and non-covalently with a histone, any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in nonspecific suppression of gene activity. P00000054 http://purl.obolibrary.org/obo/GO_0035064 P00000055 Methylated Histone Binding [GO Definition]: Interacting selectively and non-covalently with a histone in which a residue has been modified by methylation. Histones are any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. P00000055 http://purl.obolibrary.org/obo/GO_0006342 http://www.bootstrep.eu/ontology/GRO#ChromatinSilencing P00000056 Chromatin Silencing TGS chromatin-mediated maintenance of transcriptional inactivation chromatin-mediated silencing heterochromatic silencing transcriptional gene silencing [GO Definition]: Note that this process is the opposite of chromatin-mediated maintenance of transcription. This regulation is exemplified by members of the Polycomb group, which maintain the inactive state of homeotic gene transcription. Repression of transcription by altering the structure of chromatin, e.g. by conversion of large regions of DNA into an inaccessible state often called heterochromatin. P00000056 http://purl.obolibrary.org/obo/GO_0000183 P00000057 Chromatin Silencing at rDNA chromatin silencing at ribosomal DNA heterochromatic silencing at rDNA rDNA chromatin silencing [GO Definition]: Repression of transcription of ribosomal DNA by altering the structure of chromatin. P00000057 http://purl.obolibrary.org/obo/GO_0006348 P00000058 Chromatin Silencing at Telomere Telomere Position Effect heterochromatic silencing at telomere telomere chromatin silencing telomeric silencing [GO Definition]: Repression of transcription of telomeric DNA by altering the structure of chromatin. P00000058 http://purl.obolibrary.org/obo/GO_0031048 P00000059 Chromatin Silencing by Small RNA RNA interference-like chromatin silencing RNA-mediated TGS RNA-mediated chromatin silencing RNA-mediated transcriptional silencing RNAi-directed chromatin silencing RNAi-like chromatin silencing small RNA-mediated heterochromatic silencing [GO Definition]: Repression of transcription by conversion of large regions of DNA into heterochromatin, directed by small RNAs sharing sequence identity to the repressed region. P00000059 http://purl.obolibrary.org/obo/GO_0006346 P00000060 Methylation-Dependent Chromatin Silencing methylation dependent chromatin silencing methylation-dependent heterochromatic silencing [GO Definition]: Repression of transcription by methylation of DNA, leading to the formation of heterochromatin. P00000060 P00000061 Chromosomal Positioning Effect P00000061 http://purl.obolibrary.org/obo/GO_0016584 P00000062 Nucleosome Positioning nucleosome spacing [GO Definition]: Ordering of successions of nucleosomes into regular arrays so that nucleosomes are positioned at defined distances from one another. P00000062 P00000063 Nucleosome Process P00000063 http://purl.obolibrary.org/obo/GO_0034728 P00000064 Nucleosome Organization nucleosome organisation [GO Definition]: A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of one or more nucleosomes. P00000064 http://purl.obolibrary.org/obo/GO_0006334 http://purl.obolibrary.org/obo/HINO_0017710 http://scai.fraunhofer.de/PWDICT#ID1595 P00000065 Nucleosome Assembly [GO Definition]: The aggregation, arrangement and bonding together of a nucleosome, the beadlike structural units of eukaryotic chromatin composed of histones and DNA. P00000065 http://purl.obolibrary.org/obo/GO_0006337 P00000066 Nucleosome Disassembly [GO Definition]: The controlled breakdown of nucleosomes, the beadlike structural units of eukaryotic chromatin composed of histones and DNA. P00000066 http://purl.obolibrary.org/obo/GO_0031491 P00000067 Nucleosome Binding [GO Definition]: Interacting selectively and non-covalently with a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures. P00000067 http://purl.obolibrary.org/obo/GO_0016584 http://purl.obolibrary.org/obo/VariO_0158 P00000068 Nucleosome Sliding nucleosome spacing [GO Definition]: Ordering of successions of nucleosomes into regular arrays so that nucleosomes are positioned at defined distances from one another. P00000068 http://localhost/plosthes.2017-1#1628 http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C129422 http://purl.jp/bio/4/id/200906074118403576 http://purl.obolibrary.org/obo/GO_0016570 http://purl.obolibrary.org/obo/VariO_0453 P00000069 Histone Modification Histone Modification Post-Translational Histone Modification modified histone modified histones [NCIt Definition]: Post-translational processing of amino acids within a histone protein. P00000069 http://purl.obolibrary.org/obo/GO_0043486 P00000070 Histone Exchange histone chaperone histone replacement [GO Definition]: The replacement, within chromatin, of resident histones or histone subunits with alternative, sometimes variant, histones or subunits. Note that this term also includes the exchange of sperm-specific histones or protamines with histones, occurring during spermatogenesis and fertilization. P00000070 http://purl.obolibrary.org/obo/GO_0016571 http://purl.obolibrary.org/obo/SO_0001701 P00000071 Histone Methylation Histone Glutamine Methylation histone methylation histone methylation site [SO Definition]: A histone modification site where the modification is the methylation of the residue. P00000071 http://purl.obolibrary.org/obo/GO_0016577 P00000080 Histone Demethylation [GO Definition]: The modification of histones by removal of methyl groups. P00000080 http://localhost/plosthes.2017-1#9263 http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C20740 http://purl.obolibrary.org/obo/GO_0016573 http://www.bootstrep.eu/ontology/GRO#HistoneAcetylation P00000081 Histone Acetylation [NCIt Definition]: Histone Acetylation involves covalent linkage of acetyl groups to highly basic histone proteins associated with DNA, particularly in active chromatin, and may be involved in regulation of gene expression. P00000081 http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C40580 http://purl.obolibrary.org/obo/GO_0016575 P00000089 Histone Deacetylation [NCIt Definition]: Histone Deacetylation is the covalent post-translational enzymatic addition of an acetyl group(s) to a histone protein. By exposing cationic sites on the protein that promote ionic interaction with the negatively charged DNA backbone, Histone Deacetylation induces DNA condensation and regulates genetic functions, such as transcription. (NCI) P00000089 P00000090 Histone Butyrylation The modification of histones by addition of butyryl groups. P00000090 http://purl.obolibrary.org/obo/GO_0071110 P00000091 Histone Biotinylation [GO Definition]: The modification of a histone by the addition of a biotinyl group. [ http://www.ncbi.nlm.nih.gov/pubmed/19019041 http://www.ncbi.nlm.nih.gov/pubmed/14613969 GOC:rph ] P00000091 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4501262/ P00000092 Histone Crotonylation The modification of a lysine residue on a histone by crotonylation. P00000092 http://purl.obolibrary.org/obo/GO_0036414 P00000093 Histone Citrullination histone deimination [GO Definition]: The hydrolysis of peptidyl-arginine to form peptidyl-citrulline on a histone protein. [ http://www.ncbi.nlm.nih.gov/pubmed/22853951 GOC:als http://www.ncbi.nlm.nih.gov/pubmed/23175390 ] P00000093 http://www.iiserpune.ac.in/~coee/histome/ptm.php?mod_type=lysine_ribosylation P00000094 Histone ADP-Ribosylation histone ADP ribosylation Histone proteins often undergo ribosylation (ar) i.e. the addition of poly (ADP-ribose) units specifically at the lysine residues. This modification is mediated by Poly [ADP-ribose] polymerase (PARP) enzymes. In this case, the NAD+ acts as the ADP-ribose donor. These are big units and each ADP-ribose moiety adds ~560 Da to the histone protein. ADP-ribosylation causes disruption of the nucleosome structure by loss of histone-DNA interaction on account of charge modification. ADP ribosylation plays an important role in DNA break repair mechanisms. P00000094 P00000095 Histone Glycosylation The modification of histones by addition of carbohydrate groups. P00000095 P00000096 Histone Malonylation The addition of a malonyl group to a histone lysine residue which serves a yet-to-be-determined function. P00000096 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4176146/ P00000097 O-GlcNAcylated histone Histone O-GlcNAcylation histone O-GlcNAc glycosylation A histone modification where the modification is the covalent linkage of N-acetylglucosamine (GlcNAc) to the histone residue. P00000097 https://www.ncbi.nlm.nih.gov/pubmed/14578449 P00000098 Histone Sumoylation The modification of histones by addition of small Ubiquitin-like Modifier (SUMO) groups. P00000098 P00000099 Histone Propionylation The modification of histones by addition of propionyl groups. P00000099 http://purl.obolibrary.org/obo/GO_0016572 P00000100 Histone Phosphorylation histone-serine phosphorylation histone-threonine phosphorylation histone-tyrosine phosphorylation [GO Definition]: The modification of histones by addition of phosphate groups. [ GOC:ai ] P00000100 http://purl.obolibrary.org/obo/GO_0016576 P00000102 Histone Dephosphorylation [GO Definition]: The modification of histones by removal of phosphate groups. P00000102 http://purl.obolibrary.org/obo/GO_0016574 http://purl.obolibrary.org/obo/SO_0001716 P00000103 Histone Ubiquitination histone ubiquitination site histone ubiquitinylation histone ubiquitylation [GO Definition]: The modification of histones by addition of ubiquitin groups. [ GOC:ai ] P00000103 http://purl.obolibrary.org/obo/GO_0033522 P00000104 Histone H2A Ubiquitination [GO Definition]: The modification of histone H2A by addition of one or more ubiquitin groups. [ GOC:mah http://www.ncbi.nlm.nih.gov/pubmed/15509584 GOC:bf http://www.ncbi.nlm.nih.gov/pubmed/16473935 http://www.ncbi.nlm.nih.gov/pubmed/18430235 ] P00000104 http://purl.obolibrary.org/obo/GO_0016578 P00000105 Histone Deubiquitination histone deubiquitinylation histone deubiquitylation [GO Definition]: The modification of histones by removal of ubiquitin groups. [ GOC:ai ] P00000105 http://purl.obolibrary.org/obo/GO_0070537 P00000106 Histone H2AK63-Linked Deubiquitination [GO Definition]: A protein deubiquitination process in which a K63-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 63 of the ubiquitin monomers, is removed from a lysine residue in histone H2A or the variant H2AX. [ http://www.ncbi.nlm.nih.gov/pubmed/19214193 GOC:mah http://www.ncbi.nlm.nih.gov/pubmed/19202061 ] P00000106 http://localhost/plosthes.2017-1#782 http://purl.bioontology.org/ontology/MESH/D004303 http://purl.bioontology.org/ontology/SNOMEDCT/14915001 http://purl.obolibrary.org/obo/GENO_0000923 http://purl.obolibrary.org/obo/GO_0007549 http://www.bootstrep.eu/ontology/GRO#DosageCompensation P00000108 Genetic Dosage Compensation Compensation, Dosage (Genetics) Compensation, Gene Dosage Compensation, Genetic Dosage Dosage Compensation (Genetics) Dosage Compensation, Gene Dosage compensation Gene Dosage Compensation Gene Dosage Compensations Genetic Dosage Compensation Genetic Dosage Compensations Hypertranscription, X Chromosome Hypertranscription, X-Chromosome X Chromosome Hypertranscription X-Chromosome Hypertranscription [GO Definition]: Compensating for the variation in the unpaired sex chromosome:autosome chromosome ratios between sexes by activation or inactivation of genes on one or both of the sex chromosomes. P00000108 http://localhost/plosthes.2017-1#10656 http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C20674 http://purl.obolibrary.org/obo/GO_0060816 P00000109 X Chromosome Inactivation X Chromosome Inactivation X Inactivation X-Chromosome Inactivation [NCIt Definition]: A human early embryonic event in which in any given cell one of a female's two X chromosomes becomes inactivated and converted into a Barr body. After inactivation has occurred, all descendants of that cell have the same inactivated X chromosome. Thus, X-inactivation creates cell clones with differing effective gene content. An organism whose cells vary in effective gene content and hence in the expression of a trait, is called a genetic mosaic. P00000109 http://localhost/plosthes.2017-1#1696 http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C17743 http://purl.bioontology.org/ontology/CSP/4003-0019 http://purl.bioontology.org/ontology/MESH/D018392 P00000110 Genomic Imprinting Genetic Imprinting Imprinting, Genetic Imprinting, Genomic Imprinting, Parental Parental Imprinting [NCIt Definition]: Parent-specific expression or repression of genes or chromosomes in offspring. P00000110 P00000112 Tissue-Specific Imprinting tissue specific imprinting The variable phenotypic expression of a tissue-specific GENE depending on whether it is of paternal or maternal origin, which is a function of the DNA METHYLATION pattern. Imprinted regions are observed to be more methylated and less transcriptionally active. P00000112 P00000113 Mosaic Imprinting P00000113 https://www.abcam.com/epigenetics/epigenetics-glossary P00000114 Loss of Imprinting LOI loss of imprinting Alteration of imprinted gene expression caused by aberrant DNA methylation or deletion of regulatory DNA sequences. P00000114 P00000115 Imprinted Expression Pattern P00000115 P00000116 Extra-Embryonic Lineage Imprinted Expression P00000116 P00000117 Multi-Lineage Imprinted Expression P00000117 http://ncicb.nci.nih.gov/xml/owl/EVS/Thesaurus.owl#C48186 P00000118 Epigenetic Silencing [NCIt Definition]: This process is initiated by the formation of heterochromatin which ultimately leads to transcriptional inactivation or silencing. Once formed, heterochromatin can be inherited through many cell divisions, including meiosis. Inappropriate gain of heterochromatin structure, such as the inactivation of tumor suppressor genes by DNA hyper-methylation at their promoter regions, can be directly linked to carcinogenesis. P00000118 http://localhost/plosthes.2017-1#9955 http://purl.bioontology.org/ontology/MESH/D020868 http://purl.obolibrary.org/obo/GO_0016458 http://www.bootstrep.eu/ontology/GRO#GeneSilencing P00000119 Gene Silencing long-term maintenance of gene inactivation [GO Definition]: This is a rather broad grouping term. While it was originally defined for long-term, heritable, epigenetic effects, short term effects on expression mediated by RNA are also frequently referred to as gene silencing, and are grouped under this class. Any process carried out at the cellular level that results in either long-term transcriptional repression via action on chromatin structure or RNA mediated, post-transcriptional repression of gene expression. P00000119 http://purl.obolibrary.org/obo/GO_0016441 P00000120 Post-Transcriptional Gene Silencing PTGS cosuppression post-transcriptional gene silencing quelling [GO Definition]: The inactivation of gene expression by a posttranscriptional mechanism. P00000120 P00000121 Position Effect Variegation position-effect variegation P00000121 http://purl.obolibrary.org/obo/GO_0044027 P00000369 Hypermethylation of CpG Island DNA hypermethylation of CpG island [GO Definition]: An increase in the epigenetic methylation of cytosine and adenosine residues in a CpG island in DNA. CpG islands are genomic regions that contain a high frequency of the CG dinucleotide and are often associated with the transcription start site of genes. P00000369 http://purl.obolibrary.org/obo/GO_0044029 P00000370 Hypomethylation of CpG Island DNA hypomethylation of CpG island [GO Definition]: An decrease in the epigenetic methylation of cytosine and adenosine residues in a CpG island in DNA. CpG islands are genomic regions that contain a high frequency of the CG dinucleotide and are often associated with the transcription start site of genes. P00000370 http://purl.obolibrary.org/obo/GO_0043968 http://purl.obolibrary.org/obo/SO_0002142 P00000372 Histone H2A Acetylation H2A Acetylation H2Aac histone 2A acetylation site [GO Definition]: The modification of histone H2A by the addition of an acetyl group. P00000372 http://purl.obolibrary.org/obo/GO_0043969 http://purl.obolibrary.org/obo/SO_0002143 P00000373 Histone H2B Acetylation H2Bac histone 2B acetylation site [SO Definition]: A histone 2B modification where the modification is the acetylation of the residue. P00000373 http://purl.obolibrary.org/obo/GO_0043966 http://purl.obolibrary.org/obo/SO_0001973 P00000374 AcH3 Histone H3 Acetylation H3ac histone 3 acetylation site [SO Definition]: A histone 3 modification where the modification is the acetylation of the residue. P00000374 http://purl.obolibrary.org/obo/GO_0043967 http://purl.obolibrary.org/obo/SO_0001972 P00000375 Histone H4 Acetylation H4ac histone 4 acetylation site [SO Definition]: A histone 4 modification where the modification is the acetylation of the residue. P00000375 http://purl.obolibrary.org/obo/GO_0070577 P00000376 Lysine-Acetylated Histone Binding [GO Definition]: Interacting selectively and non-covalently with a histone in which a lysine residue has been modified by acetylation. [ GOC:rl http://www.ncbi.nlm.nih.gov/pubmed/17582821 GOC:BHF GOC:mah ] P00000376 http://purl.obolibrary.org/obo/GO_0043977 http://purl.obolibrary.org/obo/SO_0001938 P00000377 H2AK5 Acetylation H2AK5 acetylation site H2AK5ac histone H2A acetylation at K5 histone H2A-K5 acetylation [GO Definition]: The modification of histone H2A by the addition of an acetyl group to a lysine residue at position 5 of the histone. Source: GOC:jl P00000377 http://purl.obolibrary.org/obo/GO_0043978 http://purl.obolibrary.org/obo/SO_0001944 P00000378 H2AK9 Acetylation H2AK9 acetylation site H2AK9ac histone H2A acetylation at K9 histone H2A-K9 acetylation [GO Definition]: The modification of histone H2A by the addition of an acetyl group to a lysine residue at position 9 of the histone. [ GOC:jl ] P00000378 P00000379 Histone H2A.X Acetylation H2A.Xac H2AXac Histone H2A.X acetylation histone 2AX acetylation site A histone 2AX modification where the modification is the acetylation of the residue. P00000379 http://purl.obolibrary.org/obo/SO_0002144 P00000380 Histone H2A.Z Acetylation H2A.Zac H2AZac histone 2AZ acetylation site [SO Definition]: A histone 2AZ modification where the modification is the acetylation of the residue. P00000380 P00000381 H2A.XK5 Acetylation H2A.XK5ac H2AXK5 acetylation site H2AXK5ac histone H2A.X acetylation at K5 histone H2A.X-K5 acetylation histone H2AX acetylation at K5 histone H2AX-K5 acetylation A kind of histone modification site, whereby the 5th residue (a lysine), from the start of the H2AX histone protein is acetylated. P00000381 http://purl.obolibrary.org/obo/SO_0002145 P00000382 H2A.ZK4 Acetylation H2A.ZK4ac H2AZK4 acetylation site H2AZK4ac [SO Definition]: A kind of histone modification site, whereby the 4th residue (a lysine), from the start of the H2AZ histone protein is acetylated. P00000382 http://purl.obolibrary.org/obo/SO_0002146 P00000383 H2A.ZK7 Acetylation H2A.ZK7ac H2AZK7 acetylation site H2AZK7ac [SO Definition]: A kind of histone modification site, whereby the 7th residue (a lysine), from the start of the H2AZ histone protein is acetylated. P00000383 http://purl.obolibrary.org/obo/SO_0002147 P00000384 H2A.ZK11 Acetylation H2A.ZK11ac H2AZK11 acetylation site H2AZK11ac histone H2AZ acetylation at K11 histone H2AZ-K11 acetylation [SO Definition]: A kind of histone modification site, whereby the 11th residue (a lysine), from the start of the H2AZ histone protein is acetylated. P00000384 http://purl.obolibrary.org/obo/SO_0002148 P00000385 H2A.ZK13 Acetylation H2A.ZK13ac H2AZK13 acetylation site H2AZK13ac [SO Definition]: A kind of histone modification site, whereby the 13th residue (a lysine), from the start of the H2AZ histone protein is acetylated. P00000385 http://purl.obolibrary.org/obo/SO_0002149 P00000386 H2A.ZK15 Acetylation H2A.ZK15ac H2AZK15 acetylation site H2AZK15ac [SO Definition]: A kind of histone modification site, whereby the 15th residue (a lysine), from the start of the H2AZ histone protein is acetylated. P00000386 http://purl.obolibrary.org/obo/GO_0043979 http://purl.obolibrary.org/obo/SO_0002164 P00000387 H2BK5 Acetylation H2BK5 acetylation site H2BK5ac histone H2B acetylation at K5 histone H2B-K5 acetylation [SO Definition]: A kind of histone modification site, whereby the 5th residue (a lysine), from the start of the H2B histone protein is acetylated. P00000387 http://purl.obolibrary.org/obo/GO_0043980 http://purl.obolibrary.org/obo/SO_0001937 P00000388 H2BK12 Acetylation H2BK12 acetylation site H2BK12ac histone H2B acetylation at K12 histone H2B-K12 acetylation [SO Definition]: A kind of histone modification site, whereby the 12th residue (a lysine), from the start of the H2B protein is acetylated. P00000388 http://purl.obolibrary.org/obo/SO_0001946 P00000389 H2BK15 Acetylation H2BK15 acetylation site H2BK15ac [SO Definition]: A kind of histone modification site, whereby the 15th residue (a lysine), from the start of the H2B histone protein is acetylated. P00000389 http://purl.obolibrary.org/obo/SO_0001942 P00000390 H2BK20 Acetylation H2BK20 acetylation site H2BK20ac A kind of histone modification site, whereby the 20th residue (a lysine), from the start of the H2B histone protein is acetylated. P00000390 http://purl.obolibrary.org/obo/SO_0001940 P00000391 H2BK120 Acetylation H2BK120 acetylation site H2BK120ac [SO Definition]: A kind of histone modification site, whereby the 120th residue (a lysine), from the start of the H2B histone protein is acetylated. P00000391 http://purl.obolibrary.org/obo/GO_0043973 http://purl.obolibrary.org/obo/SO_0001943 P00000392 H3K4 Acetylation H3K4 acetylation site H3K4ac histone H3 acetylation at K4 histone H3-K4 acetylation histone H3K4 acetylation [SO Definition]: A kind of histone modification site, whereby the 4th residue (a lysine), from the start of the H3 histone protein is acetylated. P00000392 http://purl.obolibrary.org/obo/GO_0043970 http://purl.obolibrary.org/obo/SO_0001703 P00000393 H3K9 Acetylation H3K9 acetylation site H3K9ac histone H3 acetylation at K9 histone H3-K9 acetylation histone H3K9 acetylation [SO Definition]: A kind of histone modification site, whereby the 9th residue (a lysine), from the start of the H3 histone protein is acetylated. P00000393 http://purl.obolibrary.org/obo/GO_0044154 http://purl.obolibrary.org/obo/SO_0001704 P00000394 H3K14 Acetylation H3K14 acetylation site H3K14ac histone H3 acetylation at K14 histone H3-K14 acetylation histone H3K14 acetylation [SO Definition]: A kind of histone modification site, whereby the 14th residue (a lysine), from the start of the H3 histone protein is acetylated. P00000394 http://purl.obolibrary.org/obo/GO_0043971 http://purl.obolibrary.org/obo/SO_0001718 P00000395 H3K18 Acetylation H3K18 acetylation site H3K18ac histone H3 acetylation at K18 histone H3-K18 acetylation histone H3K18 acetylation [SO Definition]: A kind of histone modification site, whereby the 18th residue (a lysine), from the start of the H3 histone protein is acetylated. P00000395 http://purl.obolibrary.org/obo/GO_0043972 http://purl.obolibrary.org/obo/SO_0001719 P00000396 H3K23 Acetylation H3K23 acetylation site H3K23ac histone H3 acetylation at K23 histone H3-K23 acetylation histone H3K23 acetylation [SO Definition]: A kind of histone modification, whereby the 23rd residue (a lysine), from the start of the H3 histone protein is acetylated. P00000396 http://purl.obolibrary.org/obo/GO_0043974 http://purl.obolibrary.org/obo/SO_0002049 P00000397 H3K27 Acetylation H3K27 acetylation site H3K27ac histone H3 acetylation at K27 histone H3-K27 acetylation histone H3K27 acetylation [SO Definition]: A kind of histone modification site, whereby the 27th residue (a lysine), from the start of the H3 histone protein is acetylated. P00000397 http://purl.obolibrary.org/obo/GO_0043975 http://purl.obolibrary.org/obo/SO_0001936 P00000398 H3K36 Acetylation H3K36 acetylation site H3K36ac histone H3 acetylation at K36 histone H3-K36 acetylation histone H3K36 acetylation [SO Definition]: A kind of histone modification site, whereby the 36th residue (a lysine), from the start of the H3 histone protein is acetylated. P00000398 http://purl.obolibrary.org/obo/GO_0097043 http://purl.obolibrary.org/obo/SO_0001945 P00000399 H3K56 Acetylation H3K56 acetylation site H3K56ac histone H3 acetylation at K56 histone H3-K56 acetylation histone H3K56 acetylation [SO Definition]: A kind of histone modification site, whereby the 56th residue (a lysine), from the start of the H3 histone protein is acetylated. P00000399 P00000400 H3K72 Acetylation H3K72 acetylation site H3K72ac histone H3 acetylation at K72 histone H3-K72 acetylation histone H3K72 acetylation A kind of histone modification site, whereby the 72nd residue (a lysine), from the start of the H3 histone protein is acetylated. P00000400 http://purl.obolibrary.org/obo/GO_0043976 P00000401 H3K79 Acetylation histone H3 acetylation at K79 histone H3-K79 acetylation histone H3K79 acetylation [GO Definition]: The modification of histone H3 by the addition of an acetyl group to a lysine residue at position 79 of the histone. [ GOC:jl ] P00000401 P00000402 H3R18 Acetylation H3R18 acetylation site H3R18ac histone H3 acetylation at R18 histone H3-R18 acetylation histone H3R18 acetylation A kind of histone modification site, whereby the 18th residue (an arginine), from the start of the H3 histone protein is acetylated." P00000402 http://purl.obolibrary.org/obo/GO_0043981 http://purl.obolibrary.org/obo/SO_0001730 P00000403 H4K5 Acetylation H4K5 acetylation site H4K5ac histone H4 acetylation at K5 histone H4-K5 acetylation [SO Definition]: A kind of histone modification site, whereby the 5th residue (a lysine), from the start of the H4 histone protein is acetylated. P00000403 http://purl.obolibrary.org/obo/GO_0043982 http://purl.obolibrary.org/obo/SO_0001731 P00000404 H4K8 Acetylation H4K8 acetylation site H4K8ac histone H4 acetylation at K8 histone H4-K8 acetylation [SO Definition]: A kind of histone modification site, whereby the 8th residue (a lysine), from the start of the H4 histone protein is acetylated. P00000404 http://purl.obolibrary.org/obo/GO_0043983 http://purl.obolibrary.org/obo/SO_0001939 P00000405 H4K12 Acetylation H4K12 acetylation site H4K12ac histone H4 acetylation at K12 histone H4-K12 acetylation [SO Definition]: A kind of histone modification site, whereby the 12th residue (a lysine), from the start of the H4 histone protein is acetylated. P00000405 http://purl.obolibrary.org/obo/GO_0043984 http://purl.obolibrary.org/obo/SO_0001729 P00000406 H4K16 Acetylation H4K16 acetylation site H4K16ac histone H4 acetylation at K16 histone H4-K16 acetylation [SO Definition]: A kind of histone modification site, whereby the 16th residue (a lysine), from the start of the H4 histone protein is acetylated. P00000406 P00000407 H4K20 Acetylation H4K20 acetylation site H4K20ac histone H4 acetylation at K20 histone H4-K20 acetylation A kind of histone modification site, whereby the 20th residue (a lysine), from the start of the H4 histone protein is acetylated. P00000407 http://purl.obolibrary.org/obo/SO_0001941 P00000408 H4K91 Acetylation H4K91 acetylation site H4K91ac [SO Definition]: A kind of histone modification site, whereby the 91st residue (a lysine), from the start of the H4 histone protein is acetylated. P00000408 P00000409 Histone H2A ADP-Ribosylation A histone H2A modification where the modification is the ADP-ribosylation of the residue. P00000409 P00000410 Histone H2B ADP-Ribosylation A histone H2B modification where the modification is the ADP-ribosylation of the residue. P00000410 P00000411 Histone H3 ADP-Ribosylation A histone H3 modification where the modification is the ADP-ribosylation of the residue. P00000411 P00000412 Histone H4 ADP-Ribosylation A histone H4 modification where the modification is the ADP-ribosylation of the residue. P00000412 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2AK13ar P00000413 H2AK13 ADP-Ribosylation H2AK13ar PARP1 is shown to mediate H2A K13 ADP-ribosylation in in vitro conditions. This site is also confirmed by mass spectrometry (PMID: 20525793). P00000413 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2BK30ar P00000414 H2BK30 ADP-Ribosylation H2BK30ar PARP1 is shown to mediate H2B K30 ADP-ribosylation in in vitro conditions. This site is also confirmed by mass spectrometry (PMID: 20525793). P00000414 P00000415 H3K27 ADP-Ribosylation H3K27ar A kind of histone modification, whereby the 27th residue (a lysine), from the start of the H3 histone protein is ADP-ribosylated. P00000415 P00000416 H3K37 ADP-Ribosylation K3H37ar A kind of histone modification, whereby the 37th residue (a lysine), from the start of the H3 histone protein is ADP-ribosylated. P00000416 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H4K16ar P00000417 H4K16 ADP-Ribosylation H4K16ar Different acetylation patterns on histone H4 are subjected to binding of different number of ADP-ribosyl units. Poly ADP ribosylation of histone H4 plays an important role during chromatin replication (PMID: 2387872). Important in shuttling of histones in and out of DNA (PMID: 1326536). It s also implicated in DNA excision repair (PMID: 1429884). P00000417 P00000418 Histone H2A Biotinylation The modification of histone H2A by the addition of a biotinyl group. P00000418 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2AK9bio P00000419 H2AK9 Biotinylation H2AK9bio Biotinidase is shown to mediate H2A K9 biotinylation in in vitro conditions. This site is also confirmed by mass spectrometry (PMID: 16772434). P00000419 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2AK13bio P00000420 H2AK13 Biotinylation H2AK13bio Biotinidase is shown to mediate H2A K13 biotinylation in in vitro conditions. This site is also confirmed by mass spectrometry (PMID: 16772434). P00000420 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2AK125bio P00000421 H2AK125 Biotinylation H2AK125bio Substitution of neighbouring lysines eg: K127 and K129 causes a considerable decrease in the biotinylation at K125 (PMID: 16109483). Site also confirmed by Mass Spectrometry (PMID: 16772434). P00000421 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2AK127bio P00000422 H2AK127 Biotinylation H2AK127bio Substitution of neighbouring lysines eg: K125 and K129 causes a considerable decrease in the biotinylation at K127 (PMID: 16109483). Site also confirmed by Mass Spectrometry (PMID: 16772434). P00000422 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2AK129bio P00000423 H2AK129 Biotinylation H2AK129bio K129 is a sturdy site for biotinylation since substitution of neighbouring lysines e.g. K125 and K127 did not significantly affect biotinylation at his site (PMID: 16109483). Site also confirmed by Mass Spectrometry (PMID: 16772434). P00000423 P00000424 Histone H3 Biotinylation The modification of histone H3 by the addition of a biotinyl group. P00000424 P00000425 H3K4 Biotinylation H3K4bio The modification of histone H3 by the addition of an biotinyl group to a lysine residue at position 4 of the histone. P00000425 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H3K9bio P00000426 H3K9 Biotinylation H3K9bio Holocarboxylase synthetase (HCS) catalyses the biotinylation of H3K9 (PMID: 20688500). P00000426 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H3K18bio P00000427 H3K18 Biotinylation H3K18bio Holocarboxylase synthetase (HCS) catalyses the biotinylation of H3K18 (PMID: 20688500). P00000427 P00000428 H3K23 Biotinylation H3K23bio The modification of histone H3 by the addition of an biotinyl group to a lysine residue at position 23 of the histone. P00000428 P00000429 Histone H4 Biotinylation The modification of histone H4 by the addition of a biotinyl group. P00000429 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H4K8bio P00000430 H4K8 Biotinylation H4K8bio H4K8 is a preferred site for biotinylation (PMID: 15153116). Biotinylated histone H4 is enriched in pericentromeric heterochromatin and it participates in gene silencing, mitotic condensation of chromatin, and the cellular response to DNA damage(PMID: 16772434). P00000430 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H4K12bio P00000431 H4K12 Biotinylation H4K12bio H4K12 is a preferred site for biotinylation (PMID: 15153116). Biotinylated histone H4 is enriched in pericentromeric heterochromatin, and that biotinylation of histone H4 participates in gene silencing, mitotic condensation of chromatin, and the cellular response to DNA damage(PMID: 16772434). P00000431 P00000432 Histone H2A Citrullination The modification of histone H2A by the hydrolysis of peptidyl-arginine to form peptidyl-citrulline. P00000432 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2AR3ci P00000433 H2AR3 Citrullination H2AR3ci The modification of histone H2A by the hydrolysis of peptidyl-arginine to form peptidyl-citrulline at position 3 of the histone. P00000433 P00000434 Histone H3 Citrullination The modification of histone H3 by the hydrolysis of peptidyl-arginine to form peptidyl-citrulline. P00000434 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H3R2ci P00000435 H3R2 Citrullination H3R2ci PADI4 catalyses deimination at R2 position on H3. This activity inhibits the methylation of these residues by CARM1 thus causing transcriptional repression of target genes (PMID: 15339660). P00000435 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H3R8ci P00000436 H3R8 Citrullination H3R8ci H3 arginine 8 citrullination by PADI4 helps in reversing the transcriptional activation brought about by the combined efforts of nuclear hormone receptor coactivators, histone arginine methyltransferases and histone deacetylases (PMID: 15345777). H3 deimination increases rapidly in response to neutrophile activation stimuli like LPS, TNF, lipoteichoic acid, f-MLP, or hydrogen peroxide and is released to the extracellular space as part of the neutrophil response to infections (PMID: 18209087). R8 deimination prevents methylation by CARM1 thus causing transcriptional repression of target genes (PMID: 15339660). P00000436 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H3R17ci P00000437 H3R17 Citrullination H3R17ci H3 arginine 17 citrullination by PADI4 helps in reversing the transcriptional activation brought about by nuclear hormone receptor coactivators and histone arginine methyltransferases and histone deacetylases.(PMID: 15345777). H3 deimination increases rapidly in response to neutrophile acivation stimuli like LPS, TNF, lipoteichoic acid, f-MLP, or hydrogen peroxide and is released to the extracellular space as part of the neutrophil response to infections. (PMID: 18209087) . R17 deimination prevents methylation by CARM1 thus causing transcriptional repression of target genes (PMID: 15339660). P00000437 http://purl.obolibrary.org/obo/GO_0036413 P00000438 H3R26 Citrullination H3R26ci histone H3 arginine 26 citrullination histone H3-R26 citrullination [GO Definition]: The hydrolysis of peptidyl-arginine to form peptidyl-citrulline at position 26 in histone H3. [ GOC:als http://www.ncbi.nlm.nih.gov/pubmed/22853951 ] P00000438 P00000439 Histone H4 Citrullination The modification of histone H4 by the hydrolysis of peptidyl-arginine to form peptidyl-citrulline. P00000439 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H4R3ci P00000440 H4R3 Citrullination H4R3ci H4R3 methylation is converted to citrulline by PADI4 (PMID: 15345777). P00000440 http://purl.obolibrary.org/obo/GO_0033169 P00000441 Histone H3K9 Demethylation [GO Definition]: The modification of histone H3 by the removal of a methyl group from lysine at position 9 of the histone. P00000441 http://purl.obolibrary.org/obo/GO_0000412 P00000442 Histone Peptidyl-Prolyl Isomerization histone proline isomerization [GO Definition]: The modification of a histone by cis-trans isomerization of a proline residue. [ GOC:krc ] P00000442 P00000443 Histone 3 Peptidyl-Prolyl Isomerization The modification of a histone H3 by cis-trans isomerization of a proline residue. P00000443 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3764789/ P00000444 H3P30 Peptidyl-Prolyl Isomerization The modification of a histone H3 by cis-trans isomerization of a proline residue at position 30. P00000444 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3764789/ P00000445 H3P38 Peptidyl-Prolyl Isomerization The modification of a histone H3 by cis-trans isomerization of a proline residue at position 38. P00000445 P00000446 Histone H1 Methylation The modification of histone H1 by the addition of methyl groups. P00000446 P00000447 Histone H2A Methylation The modification of histone H2A by the addition of methyl groups. P00000447 P00000448 Histone H2B Methylation The modification of histone H2B by the addition of methyl groups. P00000448 P00000449 Histone H3 Methylation The modification of histone H3 by the addition of methyl groups. P00000449 P00000450 Histone H4 Methylation The modification of histone H4 by the addition of methyl groups. P00000450 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H1K25me1 P00000451 H1K26 Methylation H1K25 Methylation H1K25me H1K25me1 H1K26me H1K26me1 H1.4 K25 (reported as H1K26) methylation is mediated by Ezh2 of the Polycomb repressive complex (PRC2) which is associated with transcriptional repression and might play a role in the formation of chromatin fibre (PMID: 15099518). H1.4K26 is specifically required for the binding of Heterochromatin protein 1 (HP1), whereas simultaneous phosphorylation at S27 blocks HP1 binding (PMID: 16127177). P00000451 http://purl.obolibrary.org/obo/GO_0070612 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2AR3me2 P00000452 H2AR3 Methylation histone methylase activity (H2A-R3 specific) histone methyltransferase activity (H2A-R3 specific) histone-arginine N-methyltransferase activity (H2A-R3 specific) H2AR3 is a preferred site for PRMT methylation activity (PMID: 18079182). P00000452 P00000453 H2AR11 Methylation The modification of histone H2A by addition of one or more methyl groups to arginine at position 11 of the histone. P00000453 P00000454 H2AR29 Methylation The modification of histone H2A by addition of one or more methyl groups to arginine at position 29 of the histone. P00000454 http://purl.obolibrary.org/obo/SO_0001714 P00000455 H2BK5 Monomethylation H2BK5 mono-methylation site H2BK5 monomethylation site [SO Definition]: A kind of histone modification site, whereby the 5th residue (a lysine), from the start of the H2B protein is methylated. P00000455 http://purl.obolibrary.org/obo/GO_0051568 http://purl.obolibrary.org/obo/SO_0001734 P00000456 H3K4 Methylation H3K4 methylation site histone H3 K4 methylation histone H3-K4 methylation histone H3K4me histone lysine H3 K4 methylation [SO Definition]: A kind of histone modification, whereby the 4th residue (a lysine), from the start of the H3 protein is methylated. P00000456 http://purl.obolibrary.org/obo/GO_0097692 http://purl.obolibrary.org/obo/SO_0001705 P00000457 H3K4 Monomethylation H3K4 mono-methylation site H3K4me1 histone H3-K4 monomethylation [SO Definition]: A kind of histone modification, whereby the 4th residue (a lysine), from the start of the H3 protein is mono-methylated. P00000457 http://purl.obolibrary.org/obo/GO_0044648 http://purl.obolibrary.org/obo/SO_0001725 P00000458 H3K4 Dimethylation H3K4 di-methylation site H3K4Me2 histone H3-K4 dimethylation [SO Definition]: A kind of histone modification site, whereby the 4th residue (a lysine), from the start of the H3 histone protein is di-methylated. P00000458 http://purl.obolibrary.org/obo/GO_0080182 http://purl.obolibrary.org/obo/SO_0001706 P00000459 H3K4 Trimethylation H3K4 tri-methylation H3K4me3 histone H3-K4 trimethylation [SO Definition]: A kind of histone modification site, whereby the 4th residue (a lysine), from the start of the H3 protein is tri-methylated. P00000459 http://purl.obolibrary.org/obo/GO_0051567 http://purl.obolibrary.org/obo/SO_0001736 P00000460 H3K9 Methylation H3K9 methylation site histone H3 K9 methylation histone H3-K9 methylation histone H3K9me histone lysine H3 K9 methylation [SO Definition]: A kind of histone modification site, whereby the 9th residue (a lysine), from the start of the H3 histone protein is methylated. P00000460 http://purl.obolibrary.org/obo/SO_0001727 P00000461 H3K9 Monomethylation H3K9 mono-methylation site H3K9Me1 [SO Definition]: A kind of histone modification site, whereby the 9th residue (a lysine), from the start of the H3 histone protein is mono-methylated. P00000461 http://purl.obolibrary.org/obo/GO_0036123 http://purl.obolibrary.org/obo/SO_0001728 P00000462 H3K9 Dimethylation H3K9 di-methylation site H3K9Me2 histone H3 K9 dimethylation histone H3-K9 dimethylation histone lysine H3 K9 dimethylation [SO Definition]: A kind of histone modification site, whereby the 9th residue (a lysine), from the start of the H3 histone protein may be dimethylated. P00000462 http://purl.obolibrary.org/obo/GO_0036124 http://purl.obolibrary.org/obo/SO_0001707 P00000463 H3K9 Trimethylation H3K9 tri-methylation site H3K9Me3 histone H3-K9 trimethylation [SO Definition]: A kind of histone modification site, whereby the 9th residue (a lysine), from the start of the H3 histone protein is tri-methylated. P00000463 P00000464 H3K20 Methylation The modification of histone H3 by addition of one or more methyl groups to lysine at position 20 of the histone. P00000464 http://purl.obolibrary.org/obo/SO_0001935 P00000465 H3K20 Trimethylation H3K20 trimethylation site [SO Definition]: A kind of histone modification site, whereby the 20th residue (a lysine), from the start of the H3 protein is tri-methylated. P00000465 P00000466 H3K23 Methylation The modification of histone H3 by addition of one or more methyl groups to lysine at position 23 of the histone. P00000466 http://purl.obolibrary.org/obo/SO_0001951 P00000467 H3K23 Dimethylation H3K23 dimethylation site H3K23me2 [SO Definition]: A kind of histone modification site, whereby the 23rd residue (a lysine), from the start of the H3 protein is di-methylated. P00000467 http://purl.obolibrary.org/obo/GO_0070734 http://purl.obolibrary.org/obo/SO_0001732 P00000468 H3K27 Methylation H3K27 methylation site histone H3 K27 methylation histone H3-K27 methylation histone H3K27me histone lysine H3 K27 methylation [GO Definition]: The modification of histone H3 by addition of one or more methyl groups to lysine at position 27 of the histone. [ GOC:pr GOC:mah ] P00000468 http://purl.obolibrary.org/obo/SO_0001708 P00000469 H3K27 Monomethylation H2K27 mono-methylation site H2K27 monomethylation site H2K27Me1 [SO Definition]: A kind of histone modification site, whereby the 27th residue (a lysine), from the start of the H3 histone protein is mono-methylated. P00000469 http://purl.obolibrary.org/obo/SO_0001726 P00000470 H3K27 Dimethylation H3K27 di-methylation site H3K27 dimethylation site H3K27Me2 [SO Definition]: A kind of histone modification site, whereby the 27th residue (a lysine), from the start of the H3 histone protein is di-methylated. P00000470 http://purl.obolibrary.org/obo/GO_0098532 http://purl.obolibrary.org/obo/SO_0001709 P00000471 histone H3 lysine 27 trimethylation H3K27 Trimethylation H3K27 tri-methylation site H3K27 trimethylation site H3K27Me3 histone H3-K27 trimethylation [SO Definition]: A kind of histone modification site, whereby the 27th residue (a lysine), from the start of the H3 histone protein is tri-methylated. P00000471 http://purl.obolibrary.org/obo/GO_0010452 http://purl.obolibrary.org/obo/SO_0001733 P00000472 H3K36 Methylation H3K36 methylation site histone H3 K36 methylation histone H3K36me histone lysine H3 K36 methylation [SO Definition]: A kind of histone modification site, whereby the 36th residue (a lysine), from the start of the H3 histone protein is methylated. P00000472 http://purl.obolibrary.org/obo/SO_0001722 P00000473 H3K36 Monomethylation H3K36 mono-methylation site H3K36 monomethylation site H3K36<Me1 [SO Definition]: A kind of histone modification site, whereby the 36th residue (a lysine), from the start of the H3 histone protein is mono-methylated. P00000473 http://purl.obolibrary.org/obo/GO_0097676 http://purl.obolibrary.org/obo/SO_0001723 P00000474 H3K36 Dimethylation H3K36 di-methylation site H3K36Me2 histone H3-K36 dimethylation [SO Definition]: A kind of histone modification site, whereby the 36th residue (a lysine), from the start of the H3 histone protein is dimethylated. P00000474 http://purl.obolibrary.org/obo/GO_0097198 http://purl.obolibrary.org/obo/SO_0001724 P00000475 H3K36 Trimethylation H3K36 tri-methylation site H3K36Me3 histone H3-K36 trimethylation [SO Definition]: A kind of histone modification site, whereby the 36th residue (a lysine), from the start of the H3 histone protein is tri-methylated. P00000475 http://purl.obolibrary.org/obo/GO_0034729 http://purl.obolibrary.org/obo/SO_0001735 P00000476 H3K79 Methylation H3K79 methylation site histone H3 K79 methylation histone H3-K79 methylation histone H3K79me histone lysine H3 K79 methylation [SO Definition]: A kind of histone modification site, whereby the 79th residue (a lysine), from the start of the H3 histone protein is methylated. P00000476 http://purl.obolibrary.org/obo/SO_0001710 P00000477 H3K79 Monomethylation H3K79 mono-methylation site H3K79 monomethylation site H3K79me1 [SO Definition]: A kind of histone modification site, whereby the 79th residue (a lysine), from the start of the H3 histone protein is mono- methylated. P00000477 http://purl.obolibrary.org/obo/GO_0097725 http://purl.obolibrary.org/obo/SO_0001711 P00000478 H3K79 Dimethylation H3K79 di-methylation site H3K79 dimethylation site H3K79Me2 histone H3 K79 dimethylation histone H3-K79 dimethylation histone lysine H3 K79 dimethylation [SO Definition]: A kind of histone modification site, whereby the 79th residue (a lysine), from the start of the H3 histone protein is di-methylated. P00000478 http://purl.obolibrary.org/obo/SO_0001712 P00000479 H3K79 Trimethylation H3K79 tri-methylation site H3K79 trimethylation site H3K79Me3 [SO Definition]: A kind of histone modification site, whereby the 79th residue (a lysine), from the start of the H3 histone protein is tri-methylated. P00000479 http://purl.obolibrary.org/obo/GO_0034970 P00000480 H3R2 Methylation histone H3 R2 methylation histone H3-R2 methylation histone H3R2me histone lysine H3 R2 methylation [GO Definition]: The modification of histone H3 by addition of a methyl group to arginine at position 2 of the histone. [ GOC:mah ] P00000480 http://purl.obolibrary.org/obo/SO_0001947 P00000481 H3R2 Monomethylation H3R2 monomethylation site H3R2me1 [SO Definition]: A kind of histone modification site, whereby the 2nd residue (an arginine), from the start of the H3 protein is mono-methylated. P00000481 http://purl.obolibrary.org/obo/SO_0001948 P00000482 H3R2 Dimethylation H3R2 dimethylation site H3R2me2 [SO Definition]: A kind of histone modification site, whereby the 2nd residue (an arginine), from the start of the H3 protein is di-methylated. P00000482 P00000484 H3R8 Methylation The modification of histone H3 by addition of a methyl group to arginine at position 8 of the histone. P00000484 http://purl.obolibrary.org/obo/GO_0034971 P00000485 H3R17 Methylation histone H3 R17 methylation histone H3-R17 methylation histone H3R17me histone lysine H3 R17 methylation [GO Definition]: The modification of histone H3 by addition of a methyl group to arginine at position 17 of the histone. [ GOC:mah ] P00000485 http://purl.obolibrary.org/obo/GO_0034972 P00000486 H3R26 Methylation H3R26me1 histone H3 R26 methylation histone H3-R26 methylation histone H3R26me histone lysine H3 R26 methylation [GO Definition]: The modification of histone H3 by addition of a methyl group to arginine at position 26 of the histone. [ GOC:mah ] P00000486 P00000487 H4K4 Methylation The modification of histone H4 by addition of one or more methyl groups to lysine at position 4 of the histone. P00000487 http://purl.obolibrary.org/obo/SO_0001950 P00000488 H4K4 Trimethylation H4K4 trimethylation site H4K4me3 [SO Definition]: A kind of histone modification site, whereby the 4th residue (a lysine), from the start of the H4 protein is tri-methylated. P00000488 http://purl.obolibrary.org/obo/GO_0034770 P00000489 H4K20 Methylation histone H4 K20 methylation histone H4-K20 methylation histone H4K20me histone lysine H4 K20 methylation [GO Definition]: The modification of histone H4 by addition of one or more methyl groups to lysine at position 20 of the histone. [ GOC:mah ] P00000489 http://purl.obolibrary.org/obo/GO_0034771 http://purl.obolibrary.org/obo/SO_0001713 P00000490 H4K20 Monomethylation H4K20 mono-methylation site H4K20Me1 histone H4 K20 monomethylation histone H4-K20 monomethylation histone lysine H4 K20 monomethylation [SO Definition]: A kind of histone modification site, whereby the 20th residue (a lysine), from the start of the H4histone protein is mono-methylated. P00000490 P00000492 H4K59 Methylation The modification of histone H4 by addition of one or more methyl groups to lysine at position 59 of the histone. P00000492 http://purl.obolibrary.org/obo/GO_0043985 P00000493 H4R3 Methylation histone H4 R3 methylation histone H4 methylation at R3 histone H4-R3 methylation histone H4R3me [GO Definition]: The modification of histone H4 by addition of a methyl group to arginine at position 3 of the histone. [ GOC:mah ] P00000493 http://purl.obolibrary.org/obo/SO_0001949 P00000494 H4R3 Dimethylation H4R3 dimethylation site H4R3me2 [SO Definition]: A kind of histone modification site, whereby the 3nd residue (an arginine), from the start of the H4 protein is di-methylated. P00000494 P00000495 Histone Palmitoylation The modification of histones by O-palmitoylation. P00000495 https://www.ncbi.nlm.nih.gov/pubmed/21685381 P00000496 Histone H4 Palmitoylation The modification of histone H4 by O-palmitoylation. P00000496 https://www.ncbi.nlm.nih.gov/pubmed/21685381 P00000497 H4S47 Palmitoylation The modification of histone H4 by O-palmitoylation at position 47 of the histone. P00000497 P00000498 Histone H1 Phosphorylation H1 Phosphorlyation Histone 1 Phosphorylation The modification of histone H1 by addition of phosphate groups. P00000498 http://purl.obolibrary.org/obo/GO_1990164 P00000499 Histone H2A Phosphorylation h2a phosphorylation histone 2a phosphorylation [GO Definition]: The modification of histone H2A by the addition of a phosphate group. [ http://www.ncbi.nlm.nih.gov/pubmed/23080121 GOC:mah ] P00000499 P00000500 Histone H2B Phosphorylation The modification of histone H2B by the addition of a phosphate group. P00000500 P00000501 Histone H3 Phosphorylation The modification of histone H3 by the addition of a phosphate group. P00000501 P00000502 Histone H4 Phosphorylation The modification of histone H4 by the addition of a phosphate group. P00000502 P00000503 H1S27 Phosphorylation H1S27p histone H1 phosphorylation at S27 histone H1-S27 phosphorylation histone H1S27 phosphorylation The modification of histone H1 by the addition of an phosphate group to a serine residue at position 27 of the histone. P00000503 http://purl.obolibrary.org/obo/GO_0043990 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2AS1ph P00000504 H2AS1 Phosphorylation H2AS1p H2AS1ph histone H2A phosphorylation at S1 histone H2A-S1 phosphorylation histone H2AS1 phosphorylation [GO Definition]: The modification of histone H2A by the addition of an phosphate group to a serine residue at position 1 of the histone. [ GOC:jl ] P00000504 http://purl.obolibrary.org/obo/GO_0072370 P00000505 H2AS121 Phosphorylation histone H2A phosphorylation at S121 histone H2A-S121 phosphorylation histone H2AS121 phosphorylation [GO Definition]: The modification of histone H2A by the addition of an phosphate group to a serine residue at position 121 of the histone. [ GOC:mah http://www.ncbi.nlm.nih.gov/pubmed/19965387 ] P00000505 P00000506 H2AS122 Phosphorylation histone H2A phosphorylation at S122 histone H2A-S122 phosphorylation histone H2AS122 phosphorylation The modification of histone H2A by the addition of an phosphate group to a serine residue at position 122 of the histone. P00000506 http://purl.obolibrary.org/obo/GO_0035978 P00000507 H2AS139 Phosphorylation H2AS139p H2AS139ph [GO Definition]: The modification of histone H2A by the addition of an phosphate group to a serine residue at position 139 of the histone. [ GOC:yaf http://www.ncbi.nlm.nih.gov/pubmed/16061642 ] P00000507 http://purl.obolibrary.org/obo/GO_1990245 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2AT120ph P00000508 H2AT120 Phosphorylation H2AT120p H2AT120ph histone H2A phosphorylation at T120 histone H2A-T120 phosphorylation histone H2AT120 phosphorylation [GO Definition]: The modification of histone H2A by the addition of a phosphate group to a threonine residue at position 120 of the histone. [ http://www.ncbi.nlm.nih.gov/pubmed/24140421 ] P00000508 P00000509 Histone H2A.X Phosphorylation The modification of histone H2A.X by the addition of a phosphate group. P00000509 P00000510 H2A.XS139 Phosphorylation H2AXS139p" H2AXS139ph histone H2AX phosphorylation at S139 histone H2AX-S139 phosphorylation histone H2AXS139 phosphorylation The modification of histone H2A.X by the addition of an phosphate group to a serine residue at position 139 of the histone. P00000510 P00000511 H2A.XY142 Phosphorylation H2AXY142p H2AXY142ph histone H2AX phosphorylation at Y142 histone H2AX-Y142 phosphorylation histone H2AXY142 phosphorylation The modification of histone H2A.X by the addition of an phosphate group to a tyrosine residue at position 142 of the histone. P00000511 http://purl.obolibrary.org/obo/GO_0034772 P00000526 H4K20 Dimethylation histone H4 K20 dimethylation histone H4-K20 dimethylation histone lysine H4 K20 dimethylation [GO Definition]: The modification of histone H4 by addition of two methyl groups to lysine at position 20 of the histone. [ GOC:mah ] P00000526 http://purl.obolibrary.org/obo/GO_0034773 P00000527 H4K20 Trimethylation histone H4 K20 trimethylation histone H4-K20 trimethylation histone lysine H4 K20 trimethylation [GO Definition]: The modification of histone H4 by addition of three methyl groups to lysine at position 20 of the histone. [ GOC:mah ] P00000527 P00000528 H2BK14 Phosphorylation H2BK14p H2BK14ph histone H2B phosphorylation at K14 histone H2B-K14 phosphorylation histone H2BK14 phosphorylation The modification of histone H2B by the addition of an phosphate group to a lysine residue at position 14 of the histone. P00000528 http://purl.obolibrary.org/obo/GO_0043991 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2BS14ph P00000529 H2BS14 Phosphorylation h2bs14p h2bs14ph histone H2B phosphorylation at S14 histone H2B-S14 phosphorylation histone H2BS14 phosphorylation [GO Definition]: The modification of histone H2B by the addition of an phosphate group to a serine residue at position 14 of the histone. [ GOC:jl ] P00000529 http://purl.obolibrary.org/obo/GO_0043987 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H3S10ph P00000530 H3S10 Phosphorylation H3S10p H3S10ph histone H3 phosphorylation at S10 histone H3-S10 phosphorylation histone H3S10 phosphorylation [GO Definition]: The modification of histone H3 by the addition of an phosphate group to a serine residue at position 10 of the histone. [ GOC:jl ] P00000530 http://purl.obolibrary.org/obo/GO_0043988 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H3S28ph P00000531 H3S28 Phosphorylation H3S28p H3S28ph histone H3 phosphorylation at S28 histone H3-S28 phosphorylation histone H3S28 phosphorylation [GO Definition]: The modification of histone H3 by the addition of an phosphate group to a serine residue at position 28 of the histone. [ GOC:jl ] P00000531 http://purl.obolibrary.org/obo/GO_0072355 P00000532 H3T3 Phosphorylation H3T3p H3T3ph [GO Definition]: The modification of histone H3 by the addition of an phosphate group to a threonine residue at position 3 of the histone. [ GOC:mah ] P00000532 http://purl.obolibrary.org/obo/GO_0035408 P00000533 H3T6 Phosphorylation H3T6p H3T6ph [GO Definition]: The modification of histone H3 by the addition of an phosphate group to a threonine residue at position 6 of the histone. [ GOC:bf ] P00000533 http://purl.obolibrary.org/obo/GO_0035407 P00000534 H3T11 Phosphorylation H3T11p H3T11ph [GO Definition]: The modification of histone H3 by the addition of an phosphate group to a threonine residue at position 11 of the histone. [ GOC:bf ] P00000534 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H3T45ph P00000535 H3T45 Phosphorylation H3T45p H3T45ph H3T45 phosphorylation induces structural change within the nucleosome to facilitate DNA nicking and/or fragmentation linking its role to apoptosis (PMID: 19363025). P00000535 http://purl.obolibrary.org/obo/GO_0035409 P00000536 H3Y41 Phosphorylation H3Y41p H3Y41ph [GO Definition]: The modification of histone H3 by the addition of a phosphate group to a tyrosine residue at position 41 of the histone. [ GOC:bf ] P00000536 http://purl.obolibrary.org/obo/GO_0043989 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H4S1ph P00000537 H4S1 Phosphorylation H4S1p H4S1ph histone H4 phosphorylation at S1 histone H4-S1 phosphorylation histone H4S1 phosphorylation [GO Definition]: The modification of histone H4 by the addition of an phosphate group to a serine residue at position 1 of the histone. [ GOC:jl ] P00000537 http://purl.obolibrary.org/obo/GO_0036351 P00000538 H2AK13 Ubiquitination histone H2A ubiquitination (H2A-K13) histone H2A-K13 ubiquitination [GO Definition]: The modification of histone H2A by addition of ubiquitin group at lysine 13 (H2A-K13) in metazoans, and at the equivalent residue in other organisms. Monoubiquitin is first attached to H2A-K13 and K63-linked ubiquitin chains are then extended from this monoubiquitin. [ http://www.ncbi.nlm.nih.gov/pubmed/22713238 http://www.ncbi.nlm.nih.gov/pubmed/22980979 GOC:sp ] P00000538 http://purl.obolibrary.org/obo/GO_0036352 P00000539 H2AK15 Ubiquitination histone H2A ubiquitination (H2A-K15) histone H2A-K15 ubiquitination [GO Definition]: The modification of histone H2A by addition of ubiquitin group at lysine 15 (H2A-K15) in metazoans, and at the equivalent residue in other organisms. Monoubiquitin is first attached to H2A-K15 and K63-linked ubiquitin chains are then extended from this monoubiquitin. [ GOC:sp http://www.ncbi.nlm.nih.gov/pubmed/22713238 http://www.ncbi.nlm.nih.gov/pubmed/22980979 ] P00000539 http://purl.obolibrary.org/obo/GO_0070535 P00000540 H2AK63-Linked Ubiquitination histone H2A K63-linked ubiquitination [GO Definition]: A histone ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 63 of the ubiquitin monomers, is added to a lysine residue in histone H2A or the variant H2AX. [ GOC:mah http://www.ncbi.nlm.nih.gov/pubmed/18430235 ] P00000540 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2AK119ub P00000541 H2AK119 Ubiquitination H2AK119ub H2AK119 ubiquitination is linked to Polycomb mediated gene silencing (PMID: 15386022). P00000541 P00000542 H2A.X Ubiquitination The modification of histone H2A.X by addition of one or more ubiquitin groups. P00000542 http://purl.obolibrary.org/obo/GO_0036353 P00000543 H2AK119 Monoubiquitination histone H2A monoubiquitination (H2A-K119) histone H2A-K119 monoubiquitination [GO Definition]: The modification of histone H2A by addition of a single ubiquitin group to lysine-119 (H2A- K119) in metazoans, and at the equivalent residue in other organisms. [ http://www.ncbi.nlm.nih.gov/pubmed/15386022 GOC:sp ] P00000543 P00000544 H2A.XK119 Ubiquitination H2A.XK119ub H2AXK119 Ubiquitination The modification of histone H2A.X by addition of ubiquitin group at lysine 119. P00000544 http://purl.obolibrary.org/obo/GO_0033523 http://purl.obolibrary.org/obo/SO_0001717 P00000545 Histone H2B Ubiquitination H2B ubiquitination site H2BUbiq [GO Definition]: The modification of histone H2B by addition of ubiquitin groups. [ GOC:mah ] P00000545 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2BK120ub P00000546 H2BK120 Ubiquitination H2BK120ub H2B-K120 monoubiquitination is essential for subsequent H3-K4 and H3-K79 methylation and these modifications are marks for active gene transcription (PMID: 16307923). H2BK120ub1 stimulates elongation by RNA polymerase II through chromatin (PMID: 16713563). H2B specific ubiquitin ligase RNF20/hBRE1 which mediates H2BK120ub acts as a putative tumour suppressor through selective regulation of gene expression (PMID: 18832071). CDK9 is reported to regulate gene expression by controlling H2BK120ub1 mark at a global level (PMID: 19575011). P00000546 P00000547 Histone H4 Ubiquitination The modification of histone H2B by addition of ubiquitin groups. P00000547 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H4K91ub P00000548 H4K91 Ubiquitination H4K91ub H4K91 monoubiquitination is essential for protection against DNA damage. Mutation at the H4K91 residue exhibits defective chromatin assembly and increased sensitivity to DNA-damaging agents (PMID: 19818714). P00000548 P00000602 H2AR3 Dimethylation H2AR3me2 The modification of histone H2A by addition of three methyl groups to arginine at position 3 of the histone. P00000602 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H3R17me1 P00000603 H3R17 Monomethylation H3R17me1 Methylation of H3R17 is catalysed by CARM1 and this in turn coactivates nuclear hormone receptor-mediated transcription suggesting that the H3R17 methylation may be involved in transcriptional activation (PMID: 15186775). P00000603 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H3R17me2 P00000604 H3R17 Dimethylation H3R17me2 CARM1 dependent methylation of H3R17 leads to the activation of E2F1 promoter indicating its role in gene activation (PMID: 18172323). H3R17me2 is important for transcriptional activation of MHC II HLA-DRA genes (PMID: 17478518). P00000604 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H3R8me2 P00000605 H3R8 Dimethylation H3R8me2 PRMT5-dependent dimethylation of H3R8 plays a role in regulating rRNA promoter activity (PMID: 19998411). P00000605 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H4R3me1 P00000606 H4R3 Monomethylation H3R4me1 H4 R3 methylation plays a major role in transcriptional activation by nuclear hormone receptors. Methylation of arginine 3 by PRMT1 facilitates subsequent acetylation of H4 tails by p300 (PMID: 11387442). H4R3 methylation stimulates subsequent acetylation of H3 and H4 resulting in gene activation (PMID: 16103216). P00000606 P00000612 Histone H1 Acetylation H1 Acetylation H1ac The modification of histone H1 by the addition of an acetyl group. P00000612 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H1K25ac P00000613 H1K25 Acetylation H1K25ac histone H1 acetylation at K25 histone H1-K25 acetylation Deacetylation of H1 K25 (reported as H1K26) by SirT1 is involved in formation of repressive heterochromatin (PMID: 15469825). P00000613 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2BK16ac P00000614 H2BK16 Acetylation H2BK16ac H2BK16 acetylation is found at differentially methylated regions of imprinted genes (PMID: 20693536). P00000614 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2BK46ac P00000615 H2BK46 Acetylation H2BK46ac H2BK46 acetylation is found at differentially methylated regions of imprinted genes (PMID: 20693536). P00000615 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H1K186me1 P00000619 H1K187 Methylation H1k186me1 Histone H1.2 K186 methylation (reported as H1K187) is cell cycle-independent (PMID: 20334638). P00000619 P00000621 H2A.Z Ubiquitination The modification of histone H2A.Z by addition of one or more ubiquitin groups. P00000621 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2AK121ub P00000622 H2A.ZK121 Ubiquitination K2AK121ub Monoubiquitylated H2A.Z is enriched on the inactive X chromosome in females. H2A.Z preferentially associates with H3K4me2 and H3K4me3 in the nucleosome context. H2A.Z is associated with facultative heterochromatin, and this modification marks the fraction of H2A.Z associated with gene silencing.(PMID: 17636032). P00000622 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H1S171ph P00000623 H1S171 Phosphorylation H1S171p H1S171ph histone H1 phosphorylation at S171 histone H1S-171 phosphorylation histone H1S171 phosphorylation Phosphorylated on H1.4 during interphase and mitosis (PMID: 20439994). P00000623 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H1S172ph P00000624 H1S17 Phosphorylation H1S17p H1S17ph histone H1 phosphorylation at S17 histone H1S-17 phosphorylation" histone H1S17 phosphorylation Interphase specific phosphorylation in H1.5 (PMID: 16377619, PMID: 16083285). P00000624 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H1S186ph P00000625 H1S186 Phosphorylation H1S186p H1S186ph H1.4 serine 186 (reported as H1S187) phosphorylation is preferentially associated with active rDNA promoters and enriched at hormone response element (PMID: 20439994). P00000625 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H1S188ph P00000626 H1S188 Phosphorylation H1S188p H1S188ph Interphase specific phosphorylation in H1.5 (PMID: 16377619). P00000626 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H1S26ph P00000627 H1S26 Phosphorylation H1S26p H1S26ph Histone H1.4 serine 26 (reported as H1S27) is phosphorylated exclusively during mitosis (PMID: 20439994). Inhibits the binding of Heterochromatin protein 1 (HP1) (PMID: 16127177). P00000627 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H1T10ph P00000628 H1T10 Phosphorylation H1T10p H1T10ph Mitosis-specific phosphorylation in H1.5 (PMID: 16377619, PMID: 19136008). P00000628 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H1T137ph P00000629 H1T137 Phosphorylation H1T137p H1T137ph Mitosis-specific phosphorylation in H1.5 (PMID: 16377619, PMID: 19007248). P00000629 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H1T145ph P00000630 H1T145 Phosphorylation H1T145p H1T145ph Histone H1 T145 (reported as H1T146) is phosphorylated exclusively during mitosis (PMID: 20439994). P00000630 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H1T153ph P00000631 H1T153 Phosphorylation H1T153p H1T153ph This site is phosphorylated exclusively during mitosis (PMID: 20439994). P00000631 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H1T154ph P00000632 H1T154 Phosphorylation H1T154p H1T154ph Mitosis-specific phosphorylation in H1.5 (PMID: 16377619). P00000632 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H1T17ph P00000633 H1T17 Phosphorylation H1T17p H1T17ph This site is phosphorylated exclusively during mitosis (PMID: 20439994). P00000633 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H1T30ph P00000634 H1T30 Phosphorylation H1T30p H1T30ph This site is phosphorylated exclusively during mitosis (PMID: 20439994). P00000634 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H1S172ph P00000635 H1S172 Phosphorylation H1S172p H1S172ph Phosphorylated on H1.2 during interphase and mitosis (PMID: 20439994). Exclusively phosphorylated on H1.5 during interphase (PMID: 16377619). P00000635 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2AS137ph P00000636 H2AS137 Phosphorylation H2AS137p H2AS137ph Macro H2A is found to be enriched on inactive X chromosome but its phosphorylation at S137 leads to the exclusion of this variant from the heterochromatic region, suggesting its unique role in chromatin regulation beyond X inactivation. S137 phosphorylation is enriched during mitosis phase. Thus suggesting its role in normal cell cycle progression (PMID: 18227505). P00000636 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H2AY142ph P00000637 H2AY142 Phosphorylation H2AY142p H2AY142ph Tyrosine 142 phosphorylation is mediated by WSTF tyrosine kinase which has no homology to any known kinase fold. This represents a separate mechanism for DNA damage response other than S139 phosphorylation of H2A.X.(PMID: 19092802). P00000637 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H3S31ph P00000638 H3S31 Phosphorylation H3S31p H3S31ph H3.3 S31 phosphorylation is observed only in late prometaphase and metaphase and is absent in anaphase. H3.3 S31ph is localized in distinct chromosomal regions immediately adjacent to centromeres (PMID: 15851689). P00000638 http://www.iiserpune.ac.in/~coee/histome/ptm_sp.php?ptm_sp=H3S6ph P00000639 H3S6 Phosphorylation H3S6p H3S6ph CENP-A Serine 6 mutant cells show delay in cytokinesis. CENP-A is an essential histone H3-like kinetochore protein incorporated specifically at active centromeres. Thus phosphorylated S6 in kinetochore plays an important role in regulation of cytokinesis (PMID: 11756469). The initial phosphorylation of CENP-A on Ser-6 during prophase is mediated by Aurora-A, but the maintenance of this residue in the phosphorylated state during prometaphase is dependent on Aurora-B and seems to require prior phosphorylation of CENP-A by Aurora-A (PMID: 14667408). P00000639 P00000719 Histone H2A O-GlcNAcylation A histone modification site where the modification is the covalent linkage of N-acetylglucosamine (GlcNAc) to a residue on histone H2A. P00000719 https://www.ncbi.nlm.nih.gov/pubmed/27615797 P00000720 H2AS40 O-GlcNAcylation H2A-S40Gc H2AS40 O-GlcNAcylation Site H2AS40Gc O-linked-N-acetylglucosamine (O-GlcNAc) modification of histone H2A at Ser(40) A histone modification where the modification is the covalent linkage of N-acetylglucosamine (GlcNAc) to a serine 40 on histone H2A. P00000720 Sub Class Of