{ "uniprot_canonical_ac": "Q8CGP7-1", "uniprot_ac": "Q8CGP7", "uniprot_id": "H2A1K_MOUSE", "mass": { "chemical_mass": 14150.0, "monoisotopic_mass": 14150.0 }, "refseq": { "ac": "NP_835490", "name": "histone H2A type 1-K", "summary": "Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a replication-dependent histone that is a member of the histone H2A family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. [provided by RefSeq, Aug 2015].", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_835490" }, "gene_names": [ { "name": "H2ac15", "resource": "UniProtKB", "type": "recommended", "url": "https://www.uniprot.org/uniprot/Q8CGP7", "id": "Q8CGP7" }, { "name": "H2ac15", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_835490", "id": "NP_835490" }, { "name": "Hist1h2ak", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_835490", "id": "NP_835490" }, { "name": "Hist1h2ak", "resource": "UniProtKB", "type": "synonym", "url": "https://www.uniprot.org/uniprot/Q8CGP7", "id": "Q8CGP7" } ], "protein_names": [ { "name": "Histone H2A type 1-K", "resource": "UniProtKB", "type": "recommended", "url": "", "id": "Q8CGP7" }, { "name": "histone 1, H2ak; histone cluster 1, H2ak", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_835490", "id": "NP_835490" }, { "name": "histone H2A type 1-K", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_835490", "id": "NP_835490" } ], "function": [ { "annotation": "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.", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7#function" } ] }, { "annotation": "Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene is intronless and encodes a replication-dependent histone that is a member of the histone H2A family. Transcripts from this gene lack polyA tails but instead contain a palindromic termination element. [provided by RefSeq, Aug 2015].", "evidence": [ { "database": "RefSeq", "id": "NP_835490", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_835490" } ] } ], "disease": [], "snv": [], "mutagenesis": [], "expression_tissue": [], "expression_disease": [], "species": [ { "name": "Mus musculus", "taxid": 10090, "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" } ], "common_name": "Mouse" } ], "gene": [ { "name": "H2ac15", "url": "https://www.uniprot.org/uniprot/Q8CGP7", "locus": { "chromosome": "13", "start_pos": 21937605, "end_pos": 21937997, "strand": "+", "evidence": [ { "database": "Ensembl Gene", "id": "ENSMUSG00000063021", "url": "https://www.ensembl.org/id/ENSMUSG00000063021" } ] } } ], "crossref": [ { "id": "ENSMUSG00000063021", "url": "https://bgee.org/?page=gene&gene_id=ENSMUSG00000063021", "database": "Bgee", "categories": [ "Gene Expression" ] }, { "id": "cd00074", "url": "https://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00074", "database": "CDD", "categories": [ "Protein Classification" ] }, { "id": "319169", "url": "https://www.ncbi.nlm.nih.gov/gene/319169", "database": "GeneID", "categories": [ "Genome Annotation" ] }, { "id": "Q8CGP7", "url": "https://www.ebi.ac.uk/intact/interactors/id:Q8CGP7*", "database": "IntAct", "categories": [ "Other" ] }, { "id": "IPR002119", "url": "https://www.ebi.ac.uk/interpro/entry/IPR002119", "database": "InterPro", "categories": [ "Protein Classification" ] }, { "id": "IPR007125", "url": "https://www.ebi.ac.uk/interpro/entry/IPR007125", "database": "InterPro", "categories": [ "Protein Classification" ] }, { "id": "IPR009072", "url": "https://www.ebi.ac.uk/interpro/entry/IPR009072", "database": "InterPro", "categories": [ "Protein Classification" ] }, { "id": "IPR032454", "url": "https://www.ebi.ac.uk/interpro/entry/IPR032454", "database": "InterPro", "categories": [ "Protein Classification" ] }, { "id": "IPR032458", "url": "https://www.ebi.ac.uk/interpro/entry/IPR032458", "database": "InterPro", "categories": [ "Protein Classification" ] }, { "id": "mmu:319169", "url": "https://www.genome.jp/dbget-bin/get_linkdb?-t+pathway+mmu:319169", "database": "KEGG Pathway", "categories": [ "Enzyme and Pathway" ] }, { "id": "2448297", "url": "http://www.informatics.jax.org/marker/MGI:2448297", "database": "MGI", "categories": [ "Organism-specific" ] }, { "id": "Q8CGP7", "url": "https://www.oglcnac.mcw.edu/search/?query_protein=Q8CGP7", "database": "O-GlcNAc Database", "categories": [ "Glycoproteomics" ] }, { "id": "SAXTRSA", "url": "https://omabrowser.org/oma/group/SAXTRSA/", "database": "OMA", "categories": [ "Protein Classification" ] }, { "id": "4732793at2759", "url": "http://www.orthodb.org/?query=4732793at2759", "database": "OrthoDB", "categories": [ "Protein Classification" ] }, { "id": "PTHR23430", "url": "http://www.pantherdb.org/panther/family.do?clsAccession=PTHR23430", "database": "PANTHER", "categories": [ "Protein Classification" ] }, { "id": "PTHR23430:SF56", "url": "http://www.pantherdb.org/panther/family.do?clsAccession=PTHR23430:SF56", "database": "PANTHER", "categories": [ "Protein Classification" ] }, { "id": "8OTT", "url": "https://www.rcsb.org/structure/8OTT", "database": "PDB", "categories": [ "3D Structure" ] }, { "id": "PF00125", "url": "http://pfam.xfam.org/family/PF00125", "database": "Pfam", "categories": [ "Protein Classification" ] }, { "id": "PF16211", "url": "http://pfam.xfam.org/family/PF16211", "database": "Pfam", "categories": [ "Protein Classification" ] }, { "id": "PR_Q8CGP7", "url": "http://purl.obolibrary.org/obo/PR_Q8CGP7", "database": "PRO", "categories": [ "Protein" ] }, { "id": "R-MMU-212300", "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-212300", "database": "Reactome", "categories": [ "Protein Classification" ] }, { "id": "R-MMU-2299718", "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-2299718", "database": "Reactome", "categories": [ "Protein Classification" ] }, { "id": "R-MMU-3214858", "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-3214858", "database": "Reactome", "categories": [ "Protein Classification" ] }, { "id": "R-MMU-5689603", "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-5689603", "database": "Reactome", "categories": [ "Protein Classification" ] }, { "id": "R-MMU-5689880", "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-5689880", "database": "Reactome", "categories": [ "Protein Classification" ] }, { "id": "R-MMU-5689901", "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-5689901", "database": "Reactome", "categories": [ "Protein Classification" ] }, { "id": "R-MMU-606279", "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-606279", "database": "Reactome", "categories": [ "Protein Classification" ] }, { "id": "R-MMU-8936459", "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-8936459", "database": "Reactome", "categories": [ "Protein Classification" ] }, { "id": "NP_835490", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_835490", "database": "RefSeq", "categories": [ "Protein" ] }, { "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "Q8CGP7-1", "url": "https://www.uniprot.org/uniprot/Q8CGP7-1", "database": "UniProtKB", "categories": [ "Protein" ] } ], "sequence": { "sequence": "MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK", "length": 130, "header": "sp|Q8CGP7-1|H2A1K_MOUSE Isoform 1 of Histone H2A type 1-K OS=Mus musculus OX=10090 GN=H2ac15 PE=1 SV=3 CANONICAL=Q8CGP7-1" }, "isoforms": [ { "isoform_ac": "Q8CGP7-1", "url": "", "sequence": { "sequence": "MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK", "length": 130, "header": "sp|Q8CGP7-1|H2A1K_MOUSE Isoform 1 of Histone H2A type 1-K OS=Mus musculus OX=10090 GN=H2ac15 PE=1 SV=3 CANONICAL=Q8CGP7-1" }, "locus": { "chromosome": "13", "start_pos": 21937997, "end_pos": 21937608, "strand": "+", "evidence": [ { "database": "Ensembl Transcript", "id": "ENSMUST00000074752", "url": "https://www.ensembl.org/id/ENSMUST00000074752" }, { "database": "Ensembl Peptide", "id": "ENSMUSP00000074310", "url": "https://www.ensembl.org/id/ENSMUSP00000074310" } ] } } ], "glycosylation": [ { "glytoucan_ac": "G49108TO", "type": "O-linked", "subtype": "O-GlcNAcylation", "site_category": "reported_with_glycan", "site_seq": "", "relation": "attached", "comment": "O-GlcNAcylation", "evidence": [ { "id": "Q8CGP7", "database": "O-GlcNAc Database", "url": "https://www.oglcnac.mcw.edu/search/?query_protein=Q8CGP7" }, { "id": "36288343", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/36288343" }, { "id": "33300544", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/33300544" } ] } ], "phosphorylation": [ { "start_pos": 121, "end_pos": 121, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Thr", "comment": "Phosphothreonine; by DCAF1", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" } ], "site_lbl": "Thr121" }, { "start_pos": 2, "end_pos": 2, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Ser", "comment": "Phosphoserine; by RPS6KA5", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" } ], "site_lbl": "Ser2" } ], "glycation": [], "keywords": [ "glycoprotein", "glycoprotein_reported_with_glycan" ], "publication": [ { "title": "The human and mouse replication-dependent histone genes.", "journal": "Genomics", "date": "2002", "authors": "Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" } ], "reference": [ { "type": "PubMed", "id": "12408966", "url": "https://glygen.org/publication/PubMed/12408966" } ] }, { "title": "Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes and is involved in initiation of X inactivation.", "journal": "J. Biol. Chem.", "date": "2004", "authors": "Fang J, Chen T, Chadwick B, Li E, Zhang Y", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" } ], "reference": [ { "type": "PubMed", "id": "15509584", "url": "https://glygen.org/publication/PubMed/15509584" } ] }, { "title": "Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation.", "journal": "Dev. Cell", "date": "2004", "authors": "de Napoles M, Mermoud JE, Wakao R, Tang YA, Endoh M, Appanah R, Nesterova TB, Silva J, Otte AP, Vidal M, Koseki H, Brockdorff N", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" } ], "reference": [ { "type": "PubMed", "id": "15525528", "url": "https://glygen.org/publication/PubMed/15525528" } ] }, { "title": "Blimp1 associates with Prmt5 and directs histone arginine methylation in mouse germ cells.", "journal": "Nat. Cell Biol.", "date": "2006", "authors": "Ancelin K, Lange UC, Hajkova P, Schneider R, Bannister AJ, Kouzarides T, Surani MA", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" } ], "reference": [ { "type": "PubMed", "id": "16699504", "url": "https://glygen.org/publication/PubMed/16699504" } ] }, { "title": "Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification.", "journal": "Cell", "date": "2011", "authors": "Tan M, Luo H, Lee S, Jin F, Yang JS, Montellier E, Buchou T, Cheng Z, Rousseaux S, Rajagopal N, Lu Z, Ye Z, Zhu Q, Wysocka J, Ye Y, Khochbin S, Ren B, Zhao Y", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" } ], "reference": [ { "type": "PubMed", "id": "21925322", "url": "https://glygen.org/publication/PubMed/21925322" } ] }, { "title": "Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification.", "journal": "Nature", "date": "2014", "authors": "Tessarz P, Santos-Rosa H, Robson SC, Sylvestersen KB, Nelson CJ, Nielsen ML, Kouzarides T", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" } ], "reference": [ { "type": "PubMed", "id": "24352239", "url": "https://glygen.org/publication/PubMed/24352239" } ] }, { "title": "Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark.", "journal": "Nat. Chem. Biol.", "date": "2014", "authors": "Dai L, Peng C, Montellier E, Lu Z, Chen Y, Ishii H, Debernardi A, Buchou T, Rousseaux S, Jin F, Sabari BR, Deng Z, Allis CD, Ren B, Khochbin S, Zhao Y", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" } ], "reference": [ { "type": "PubMed", "id": "24681537", "url": "https://glygen.org/publication/PubMed/24681537" } ] }, { "title": "Metabolic regulation of gene expression by histone lysine beta-hydroxybutyrylation.", "journal": "Mol. Cell", "date": "2016", "authors": "Xie Z, Zhang D, Chung D, Tang Z, Huang H, Dai L, Qi S, Li J, Colak G, Chen Y, Xia C, Peng C, Ruan H, Kirkey M, Wang D, Jensen LM, Kwon OK, Lee S, Pletcher SD, Tan M, Lombard DB, White KP, Zhao H, Li J, Roeder RG, Yang X, Zhao Y", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" } ], "reference": [ { "type": "PubMed", "id": "27105115", "url": "https://glygen.org/publication/PubMed/27105115" } ] }, { "title": "O-GlcNAcylation regulates dopamine neuron function, survival and degeneration in Parkinson disease.", "journal": "Brain : a journal of neurology", "date": "2020", "authors": "Lee BE, Kim HY, Kim HJ, Jeong H, Kim BG, Lee HE, Lee J, Kim HB, Lee SE, Yang YR, Yi EC, Hanover JA, Myung K, Suh PG, Kwon T, Kim JI", "evidence": [ { "database": "O-GlcNAc Database", "id": "Q8CGP7", "url": "https://www.oglcnac.mcw.edu/search/?query_protein=Q8CGP7" } ], "reference": [ { "type": "PubMed", "id": "33300544", "url": "https://glygen.org/publication/PubMed/33300544" } ] }, { "title": "First comprehensive identification of cardiac proteins with putative increased O-GlcNAc levels during pressure overload hypertrophy.", "journal": "PloS one", "date": "2022", "authors": "Zhu Wei Zhong, Palazzo Teresa, Zhou Mowei, Ledee Dolena, Olson Heather M, Pa\u0161a-Toli\u0107 Ljiljana, Olson Aaron K", "evidence": [ { "database": "O-GlcNAc Database", "id": "Q8CGP7", "url": "https://www.oglcnac.mcw.edu/search/?query_protein=Q8CGP7" } ], "reference": [ { "type": "PubMed", "id": "36288343", "url": "https://glygen.org/publication/PubMed/36288343" } ] } ], "pathway": [ { "id": "mmu:319169", "name": "", "url": "https://www.genome.jp/dbget-bin/get_linkdb?-t+pathway+mmu:319169", "resource": "KEGG Pathway" }, { "id": "R-MMU-212300", "name": "PRC2 methylates histones and DNA", "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-212300", "resource": "Reactome", "description": "PRC2 methylates histones and DNA" }, { 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}, { "id": "R-MMU-606279", "name": "Deposition of new CENPA-containing nucleosomes at the centromere", "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-606279", "resource": "Reactome", "description": "Deposition of new CENPA-containing nucleosomes at the centromere" }, { "id": "R-MMU-8936459", "name": "RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function", "url": "https://www.reactome.org/PathwayBrowser/#R-MMU-8936459", "resource": "Reactome", "description": "RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function" } ], "orthologs": [ { "uniprot_canonical_ac": "P0C170-1", "protein_name": "Histone H2A type 1-E", "gene_name": "", "tax_id": 10116, "organism": "Rattus norvegicus", "sequence": { "sequence": "MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK", "length": 130 }, "evidence": [ { "id": "45230124", "url": 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"end_pos": 41, "annotation": "n_glycosylation_sequon" } ], "ptm_annotation": [ { "annotation": "Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" }, { "database": "PubMed", "id": "21925322", "url": "https://glygen.org/publication/PubMed/21925322" } ] }, { "annotation": "Deiminated on Arg-4 in granulocytes upon calcium entry.", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" }, { "database": "PubMed", "id": "P0C0S8", "url": "https://glygen.org/publication/PubMed/P0C0S8" } ] }, { "annotation": "Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex.", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" }, { "database": "PubMed", "id": "24352239", "url": "https://glygen.org/publication/PubMed/24352239" } ] }, { "annotation": "Hydroxybutyrylation of histones is induced by starvation.", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" }, { "database": "PubMed", "id": "27105115", "url": "https://glygen.org/publication/PubMed/27105115" } ] }, { "annotation": "Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription.", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" }, { "database": "PubMed", "id": "P0C0S5", "url": "https://glygen.org/publication/PubMed/P0C0S5" } ] }, { "annotation": "Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" }, { "database": "PubMed", "id": "P0C0S8", "url": "https://glygen.org/publication/PubMed/P0C0S8" }, { "database": "PubMed", "id": "15525528", "url": "https://glygen.org/publication/PubMed/15525528" }, { "database": "PubMed", "id": "24352239", "url": "https://glygen.org/publication/PubMed/24352239" }, { "database": "PubMed", "id": "15509584", "url": "https://glygen.org/publication/PubMed/15509584" } ] }, { "annotation": "Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription.", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" }, { "database": "PubMed", "id": "P0C0S8", "url": "https://glygen.org/publication/PubMed/P0C0S8" } ] }, { "annotation": "Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.", "evidence": [ { "database": "UniProtKB", "id": "Q8CGP7", "url": "https://www.uniprot.org/uniprot/Q8CGP7" }, { "database": "PubMed", "id": "16699504", "url": "https://glygen.org/publication/PubMed/16699504" } ] } ], "interactions": [], "reactions": [], "reaction_participants": [], "reaction_enzymes": [], "biomarkers": [], "synthesized_glycans": [], "cluster_types": [ { "name": "homologset.mgi", "label": "MGI Homologs" } ], "section_stats": [ { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 1 }, { "field": "total_sites", "count": 1 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycans", "count": 1 }, { "field": "o_linked_glycan_sites", "count": 1 } ], "sort_fields": [ "glytoucan_ac", "type", "subtype", "site_category", "site_seq", "relation", "comment" ] }, { "table_id": "glycosylation_reported", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycans", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_reported_with_glycan", "table_stats": [ { "field": "total", "count": 1 }, { "field": "total_sites", "count": 1 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycans", "count": 1 }, { "field": "o_linked_glycan_sites", "count": 1 } ], "sort_fields": [ "glytoucan_ac", "type", "subtype", "site_category", "site_seq", "relation", "comment" ] }, { "table_id": "glycosylation_predicted", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycans", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "glycosylation_automatic_literature_mining", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycans", "count": 0 }, { "field": "o_linked_glycan_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "phosphorylation", "table_stats": [ { "field": "total", "count": 2 }, { "field": "total_sites", "count": 2 } ], "sort_fields": [ "start_pos", "end_pos", "kinase_uniprot_canonical_ac", "kinase_gene_name", "residue", "comment", "site_lbl" ] }, { "table_id": "snv", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "snv_disease", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "snv_non_disease", "table_stats": [ { "field": "total", "count": 0 }, { "field": "total_sites", "count": 0 } ], "sort_fields": [] }, { "table_id": "publication", "table_stats": [ { "field": "total", "count": 10 } ], "sort_fields": [ "title", "journal", "date", "authors" ] } ] }