{ "uniprot_canonical_ac": "P0C170-1", "uniprot_ac": "P0C170", "uniprot_id": "H2A1E_RAT", "mass": { "chemical_mass": 14119.0, "monoisotopic_mass": 14119.0 }, "refseq": { "ac": "NP_001302421", "name": "histone H2A type 1-E", "summary": "", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001302421" }, "gene_names": [ { "name": "H2A.1", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001302421", "id": "NP_001302421" }, { "name": "Hist1h2ah", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001302421", "id": "NP_001302421" } ], "protein_names": [ { "name": "Histone H2A type 1-E", "resource": "UniProtKB", "type": "recommended", "url": "", "id": "P0C170" }, { "name": "histone H2A type 1-E", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001302421", "id": "NP_001302421" }, { "name": "histone cluster 1, H2ah", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001302421", "id": "NP_001302421" } ], "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": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170#function" } ] } ], "disease": [], "snv": [], "mutagenesis": [], "expression_tissue": [], "expression_disease": [], "species": [ { "name": "Rattus norvegicus", "taxid": 10116, "evidence": [ { "database": "UniProtKB", "id": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" } ], "common_name": "Rat" } ], "gene": [ { "name": "", "url": "https://www.uniprot.org/uniprot/P0C170", "locus": {} } ], "crossref": [ { "id": "ENSRNOG00000049649", "url": "https://bgee.org/?page=gene&gene_id=ENSRNOG00000049649", "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": "103690190", "url": "https://www.ncbi.nlm.nih.gov/gene/103690190", "database": "GeneID", "categories": [ "Genome Annotation" ] }, { "id": "502125", "url": "https://www.ncbi.nlm.nih.gov/gene/502125", "database": "GeneID", "categories": [ "Genome Annotation" ] }, { "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": "rno:103690190", "url": "https://www.genome.jp/dbget-bin/get_linkdb?-t+pathway+rno:103690190", "database": "KEGG Pathway", "categories": [ "Enzyme and Pathway" ] }, { "id": "rno:502125", "url": "https://www.genome.jp/dbget-bin/get_linkdb?-t+pathway+rno:502125", "database": "KEGG Pathway", "categories": [ "Enzyme and Pathway" ] }, { "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:SF59", "url": "http://www.pantherdb.org/panther/family.do?clsAccession=PTHR23430:SF59", "database": "PANTHER", "categories": [ "Protein Classification" ] }, { "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_P0C170", "url": "http://purl.obolibrary.org/obo/PR_P0C170", "database": "PRO", "categories": [ "Protein" ] }, { "id": "R-RNO-5689901", "url": "https://www.reactome.org/PathwayBrowser/#R-RNO-5689901", "database": "Reactome", "categories": [ "Protein Classification" ] }, { "id": "NP_001302421", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_001302421", "database": "RefSeq", "categories": [ "Protein" ] }, { "id": "1594367", "url": "http://rgd.mcw.edu/tools/genes/genes_view.cgi?id=1594367", "database": "RGD", "categories": [ "Organism-specific" ] }, { "id": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "P0C170-1", "url": "https://www.uniprot.org/uniprot/P0C170-1", "database": "UniProtKB", "categories": [ "Protein" ] } ], "sequence": { "sequence": "MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK", "length": 130, "header": "sp|P0C170-1|H2A1E_RAT Isoform 1 of Histone H2A type 1-E OS=Rattus norvegicus OX=10116 GN= PE=1 SV=2 CANONICAL=P0C170-1" }, "isoforms": [ { "isoform_ac": "P0C170-1", "url": "", "sequence": { "sequence": "MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK", "length": 130, "header": "sp|P0C170-1|H2A1E_RAT Isoform 1 of Histone H2A type 1-E OS=Rattus norvegicus OX=10116 GN= PE=1 SV=2 CANONICAL=P0C170-1" }, "locus": {} } ], "glycosylation": [], "phosphorylation": [ { "start_pos": 121, "end_pos": 121, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Thr", "comment": "Phosphothreonine; by DCAF1", "evidence": [ { "database": "UniProtKB", "id": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" } ], "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": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" } ], "site_lbl": "Ser2" } ], "glycation": [], "keywords": [], "publication": [ { "title": "Primary structure and microheterogeneities of rat chloroleukemia histone H2A (histone ALK, IIbl or F2a2).", "journal": "Biochemistry", "date": "1976", "authors": "Laine B, Sautiere P, Biserte G", "evidence": [ { "database": "UniProtKB", "id": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" } ], "reference": [ { "type": "PubMed", "id": "1268188", "url": "https://glygen.org/publication/PubMed/1268188" } ] }, { "title": "Mass spectrometry-compatible silver staining of histones resolved on acetic acid-urea-Triton PAGE.", "journal": "Proteomics", "date": "2009", "authors": "Pramod KS, Bharat K, Sanjay G", "evidence": [ { "database": "UniProtKB", "id": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" } ], "reference": [ { "type": "PubMed", "id": "19343714", "url": "https://glygen.org/publication/PubMed/19343714" } ] }, { "title": "Overexpression of histone variant H2A.1 and cellular transformation are related in N-nitrosodiethylamine-induced sequential hepatocarcinogenesis.", "journal": "Exp. Biol. Med.", "date": "2011", "authors": "Sharma A., Gupta S., Deodhar K.K., Khare S.P.", "evidence": [ { "database": "UniProtKB", "id": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" } ], "reference": [ { "type": "PubMed", "id": "21239733", "url": "https://glygen.org/publication/PubMed/21239733" } ] } ], "pathway": [ { "id": "rno:103690190", "name": "", "url": "https://www.genome.jp/dbget-bin/get_linkdb?-t+pathway+rno:103690190", "resource": "KEGG Pathway" }, { "id": "rno:502125", "name": "", "url": "https://www.genome.jp/dbget-bin/get_linkdb?-t+pathway+rno:502125", "resource": "KEGG Pathway" }, { "id": "R-RNO-5689901", "name": "Metalloprotease DUBs", "url": "https://www.reactome.org/PathwayBrowser/#R-RNO-5689901", "resource": "Reactome", "description": "Metalloprotease DUBs" } ], "orthologs": [ { "uniprot_canonical_ac": "Q8CGP7-1", "protein_name": "Histone H2A type 1-K", "gene_name": "H2ac15", "tax_id": 10090, "organism": "Mus musculus", "sequence": { "sequence": "MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTETHHKAKGK", "length": 130 }, "evidence": [ { "id": "45230124", "url": "http://www.informatics.jax.org/homology/45230124", "database": "MGI" } ], "common_name": "Mouse" }, { "uniprot_canonical_ac": "Q96QV6-1", "protein_name": "Histone H2A type 1-A", "gene_name": "H2AC1", "tax_id": 9606, "organism": "Homo sapiens", "sequence": { "sequence": "MSGRGKQGGKARAKSKSRSSRAGLQFPVGRIHRLLRKGNYAERIGAGAPVYLAAVLEYLTAEILELAGNASRDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTESHHHKAQSK", "length": 131 }, "evidence": [ { "id": "45230124", "url": "http://www.informatics.jax.org/homology/45230124", "database": "MGI" } ], "common_name": "Human" } ], "go_annotation": { "categories": [ { "name": "Molecular Function", "total": 4, "go_terms": [ { "name": "DNA binding", "id": "GO:0003677", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0003677", "evidence": [ { "database": "UniProtKB", "id": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" } ], "pmid": "" }, { "name": "enzyme binding", "id": "GO:0019899", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019899", "evidence": [ { "database": "UniProtKB", "id": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" } ], "pmid": "" }, { "name": "protein heterodimerization activity", "id": "GO:0046982", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0046982", "evidence": [ { "database": "UniProtKB", "id": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" } ], "pmid": "" }, { "name": "structural constituent of chromatin", "id": "GO:0030527", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030527", "evidence": [ { "database": "UniProtKB", "id": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" } ], "pmid": "" } ] }, { "name": "Cellular Component", "total": 2, "go_terms": [ { "name": "nucleus", "id": "GO:0005634", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005634", "evidence": [ { "database": "UniProtKB", "id": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" } ], "pmid": "" }, { "name": "nucleosome", "id": "GO:0000786", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0000786", "evidence": [ { "database": "UniProtKB", "id": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" } ], "pmid": "" } ] } ] }, "pro_annotation": [], "site_annotation": [], "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": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" }, { "database": "PubMed", "id": "P0C0S8", "url": "https://glygen.org/publication/PubMed/P0C0S8" } ] }, { "annotation": "Deiminated on Arg-4 in granulocytes upon calcium entry.", "evidence": [ { "database": "UniProtKB", "id": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" }, { "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": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" }, { "database": "PubMed", "id": "P0C0S8", "url": "https://glygen.org/publication/PubMed/P0C0S8" } ] }, { "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": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" }, { "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. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.", "evidence": [ { "database": "UniProtKB", "id": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" }, { "database": "PubMed", "id": "P0C0S8", "url": "https://glygen.org/publication/PubMed/P0C0S8" } ] }, { "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": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" }, { "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": "P0C170", "url": "https://www.uniprot.org/uniprot/P0C170" }, { "database": "PubMed", "id": "P22752", "url": "https://glygen.org/publication/PubMed/P22752" } ] } ], "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": 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", "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": 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_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": 3 } ], "sort_fields": [ "title", "journal", "date", "authors" ] } ] }