Q93077 · H2A1C_HUMAN
- ProteinHistone H2A type 1-C
- GeneH2AC6
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids130 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular exosome | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleosome | |
Cellular Component | nucleus | |
Molecular Function | nucleosomal DNA binding | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | structural constituent of chromatin | |
Biological Process | heterochromatin formation | |
Biological Process | negative regulation of cell population proliferation |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone H2A type 1-C
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ93077
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 2 | Blocks the inhibition of transcription by RPS6KA5/MSK1. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 268 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Modified residue | 2 | UniProt | Phosphoserine; by RPS6KA5 | ||||
Sequence: S | |||||||
Chain | PRO_0000055236 | 2-130 | UniProt | Histone H2A type 1-C | |||
Sequence: SGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | |||||||
Modified residue | 4 | UniProt | Citrulline; alternate | ||||
Sequence: R | |||||||
Modified residue | 4 | UniProt | Symmetric dimethylarginine; by PRMT5; alternate | ||||
Sequence: R | |||||||
Modified residue | 6 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 6 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 10 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 10 | UniProt | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 10 | UniProt | N6-lactoyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 10 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 14 | UniProt | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 14 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | |||||||
Cross-link | 16 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 19 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 37 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 37 | UniProt | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 37 | UniProt | N6-crotonyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 75 | UniProt | N6-(2-hydroxyisobutyryl)lysine | ||||
Sequence: K | |||||||
Modified residue | 76 | UniProt | N6-(2-hydroxyisobutyryl)lysine | ||||
Sequence: K | |||||||
Modified residue | 96 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 96 | UniProt | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 96 | UniProt | N6-glutaryllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 96 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 102 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 105 | UniProt | N5-methylglutamine | ||||
Sequence: Q | |||||||
Modified residue | 119 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 119 | UniProt | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 119 | UniProt | N6-crotonyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 119 | UniProt | N6-glutaryllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 120 | UniProt | N6-crotonyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 120 | UniProt | N6-glutaryllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 120 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | |||||||
Modified residue | 121 | UniProt | Phosphothreonine; by DCAF1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 121 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 123 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 126 | UniProt | N6-crotonyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 126 | UniProt | N6-glutaryllysine; alternate | ||||
Sequence: K |
Post-translational modification
Deiminated on Arg-4 in granulocytes upon calcium entry.
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. Monoubiquitination of Lys-120 (H2AK119Ub) by TRIM37 may promote transformation of cells in a number of breast cancers (PubMed:25470042).
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 (PubMed:27083998).
H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.
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 (PubMed:27083998).
H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.
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.
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 (PubMed:24352239).
Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.
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.
Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q93077 | BAG6 P46379-2 | 3 | EBI-725259, EBI-10988864 | |
BINARY | Q93077 | KLF11 O14901 | 3 | EBI-725259, EBI-948266 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-22 | Disordered | ||||
Sequence: MSGRGKQGGKARAKAKSRSSRA |
Sequence similarities
Belongs to the histone H2A family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length130
- Mass (Da)14,105
- Last updated2007-01-23 v3
- ChecksumECEF06C793FE9AC2
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U90551 EMBL· GenBank· DDBJ | AAB53429.1 EMBL· GenBank· DDBJ | mRNA | ||
U91328 EMBL· GenBank· DDBJ | AAB82086.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z80778 EMBL· GenBank· DDBJ | CAB02540.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY131984 EMBL· GenBank· DDBJ | AAN59965.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK311811 EMBL· GenBank· DDBJ | BAG34754.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471087 EMBL· GenBank· DDBJ | EAW55532.1 EMBL· GenBank· DDBJ | Genomic DNA |