Reviewed,
UniProtKB/Swiss-Prot Q93077 (H2A1C_HUMAN)
Last modified
June 16, 2009.
Version 97.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Histone H2A type 1-C Alternative name(s): H2A/l | ||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 130 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| 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. |
| Subunit structure | 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. |
| Subcellular location | |
| Post-translational modification | The chromatin-associated form is phosphorylated on Thr-121 during mitosis Probable. Deiminated on Arg-4 in granulocytes upon calcium entry. Monoubiquitination of Lys-120 by RING1 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. Monoubiquitination of Lys-120 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. Monoubiquitination and ionizing radiation-induced 'Lys-63'-linked ubiquitination are distinct events. Ref.7 Ref.9 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16 Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage By similarity. |
| Sequence similarities | Belongs to the histone H2A family. |
| Mass spectrometry | Molecular mass is 14007.8 Da from positions 2 - 130. Determined by ESI. Monoisotopic with N-acetylserine. Ref.12 |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Chromosomal protein Nucleosome core Nucleus |
| Ligand | DNA-binding |
| PTM | Acetylation Citrullination Isopeptide bond Methylation Phosphoprotein Ubl conjugation |
| Gene Ontology (GO) | |
| Biological process | nucleosome assembly Non-traceable author statement. Source: UniProtKB |
| Cellular component | nucleosome Non-traceable author statement. Source: UniProtKB nucleusInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | DNA binding Non-traceable author statement. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 130 | 129 | Histone H2A type 1-C | PRO_0000055236 | |||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine Ref.8 Ref.12 | ||||||
| Modified residue | 2 | 1 | Phosphoserine Ref.11 Ref.6 | ||||||
| Modified residue | 4 | 1 | Citrulline; alternate | ||||||
| Modified residue | 4 | 1 | Symmetric dimethylarginine; alternate By similarity | ||||||
| Modified residue | 6 | 1 | N6-acetyllysine Ref.11 | ||||||
| Modified residue | 121 | 1 | Phosphothreonine Probable | ||||||
| Cross-link | 120 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7 Ref.9 Ref.10 | |||||||
Experimental info | |||||||||
| Mutagenesis | 2 | 1 | S → A: Blocks the inhibition of transcription by RPS6KA5/MSK1. Ref.6 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Human histone gene organization: nonregular arrangement within a large cluster." Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D. Genomics 40:314-322(1997) [PubMed: 9119399] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "A 1.1-Mb transcript map of the hereditary hemochromatosis locus." Ruddy D.A., Kronmal G.S., Lee V.K., Mintier G.A., Quintana L., Domingo R. Jr., Meyer N.C., Irrinki A., McClelland E.E., Fullan A., Mapa F.A., Moore T., Thomas W., Loeb D.B., Harmon C., Tsuchihashi Z., Wolff R.K., Schatzman R.C., Feder J.N. Genome Res. 7:441-456(1997) [PubMed: 9149941] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "The human and mouse replication-dependent histone genes." Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J. Genomics 80:487-498(2002) [PubMed: 12408966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [4] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Blood, Skin and Uterus. |
| [5] | "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo." Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N., Takio K., Kaneko M., Takeshima Y., Muramatsu M., Ito T. Genes Dev. 18:877-888(2004) [PubMed: 15078818] [Abstract] Cited for: PHOSPHORYLATION AT THR-121. |
| [6] | "Phosphorylation of histone H2A inhibits transcription on chromatin templates." Zhang Y., Griffin K., Mondal N., Parvin J.D. J. Biol. Chem. 279:21866-21872(2004) [PubMed: 15010469] [Abstract] Cited for: PHOSPHORYLATION AT SER-2, MUTAGENESIS OF SER-2. |
| [7] | "Role of histone H2A ubiquitination in Polycomb silencing." Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S., Zhang Y. Nature 431:873-878(2004) [PubMed: 15386022] [Abstract] Cited for: UBIQUITINATION AT LYS-120. |
| [8] | "Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes." Hagiwara T., Hidaka Y., Yamada M. Biochemistry 44:5827-5834(2005) [PubMed: 15823041] [Abstract] Cited for: ACETYLATION AT SER-2, CITRULLINATION AT ARG-4, MASS SPECTROMETRY. |
| [9] | "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing." Cao R., Tsukada Y., Zhang Y. Mol. Cell 20:845-854(2005) [PubMed: 16359901] [Abstract] Cited for: UBIQUITINATION AT LYS-120. |
| [10] | "DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A." Bergink S., Salomons F.A., Hoogstraten D., Groothuis T.A.M., de Waard H., Wu J., Yuan L., Citterio E., Houtsmuller A.B., Neefjes J., Hoeijmakers J.H.J., Vermeulen W., Dantuma N.P. Genes Dev. 20:1343-1352(2006) [PubMed: 16702407] [Abstract] Cited for: UBIQUITINATION AT LYS-120. |
| [11] | "Characterization of histones H2A and H2B variants and their post-translational modifications by mass spectrometry." Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J. Mol. Cell. Proteomics 5:541-552(2006) [PubMed: 16319397] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, ACETYLATION AT LYS-6, PHOSPHORYLATION AT SER-2. |
| [12] | "Precise characterization of human histones in the H2A gene family by top down mass spectrometry." Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L. J. Proteome Res. 5:248-253(2006) [PubMed: 16457589] [Abstract] Cited for: MASS SPECTROMETRY, ACETYLATION AT SER-2. |
| [13] | "RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins." Mailand N., Bekker-Jensen S., Faustrup H., Melander F., Bartek J., Lukas C., Lukas J. Cell 131:887-900(2007) [PubMed: 18001824] [Abstract] Cited for: UBIQUITINATION. |
| [14] | "RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly." Huen M.S.Y., Grant R., Manke I., Minn K., Yu X., Yaffe M.B., Chen J. Cell 131:901-914(2007) [PubMed: 18001825] [Abstract] Cited for: UBIQUITINATION. |
| [15] | "The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage." Stewart G.S., Panier S., Townsend K., Al-Hakim A.K., Kolas N.K., Miller E.S., Nakada S., Ylanko J., Olivarius S., Mendez M., Oldreive C., Wildenhain J., Tagliaferro A., Pelletier L., Taubenheim N., Durandy A., Byrd P.J., Stankovic T., Taylor A.M.R., Durocher D. Cell 136:420-434(2009) [PubMed: 19203578] [Abstract] Cited for: UBIQUITINATION. |
| [16] | "RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins." Doil C., Mailand N., Bekker-Jensen S., Menard P., Larsen D.H., Pepperkok R., Ellenberg J., Panier S., Durocher D., Bartek J., Lukas J., Lukas C. Cell 136:435-446(2009) [PubMed: 19203579] [Abstract] Cited for: UBIQUITINATION. |
Cross-references
Sequence databases | |
|---|---|
| Z80778 Genomic DNA. Translation: CAB02540.1. U91328 Genomic DNA. Translation: AAB82086.1. U90551 mRNA. Translation: AAB53429.1. AY131984 Genomic DNA. Translation: AAN59965.1. BC017379 mRNA. Translation: AAH17379.1. BC050602 mRNA. Translation: AAH50602.1. BC085010 mRNA. Translation: AAH85010.1. | |
| IPI | IPI00216456. |
| RefSeq | NP_003503.1. |
| UniGene | Hs.484950 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1AOI based on UniProtKB P06897. |
| SMR | Q93077. Positions 2-124. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q93077. 1 interaction. |
PTM databases | |
| PhosphoSite | Q93077. |
Proteomic databases | |
| PRIDE | Q93077. |
Genome annotation databases | |
| Ensembl | ENSG00000180573. Homo sapiens. [Contig view] |
| GeneID | 8334. |
| KEGG | hsa:8334. |
Organism-specific databases | |
| GeneCards | GC06P026232. |
| H-InvDB | HIX0005639. |
| HGNC | HGNC:4733. HIST1H2AC. |
| MIM | 602794. gene. |
| PharmGKB | PA29110. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOGENOM | Q93077. |
| HOVERGEN | Q93077. |
| OMA | Q93077. EYLAVEI. |
Enzyme and pathway databases | |
| Reactome | REACT_7970. Telomere Maintenance. |
Gene expression databases | |
| ArrayExpress | Q93077. |
| Bgee | Q93077. |
| CleanEx | HS_HIST1H2AC. |
| GermOnline | ENSG00000180573. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR007125. Histone_core_D. IPR002119. Histone_H2A. [Graphical view] |
| PANTHER | PTHR23430. Histone_H2A. 1 hit. |
| Pfam | PF00125. Histone. 1 hit. [Graphical view] |
| PRINTS | PR00620. HISTONEH2A. |
| ProDom | PD000522. Histone_H2A. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00414. H2A. 1 hit. [Graphical view] |
| PROSITE | PS00046. HISTONE_H2A. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 31208. |
| SOURCE | Search... |
Entry information
| Entry name | H2A1C_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q93077 Secondary accession number(s): O00775 Q540R1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 6 Human chromosome 6: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


