Q6NXT2 (H3C_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 72.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Histone H3.3C | ||
| 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 | 135 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 | Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me) By similarity. Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription By similarity. Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters By similarity. Methylation at Lys-5 (H3K4me) is linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) requires preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin By similarity. Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Tyr-41 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin By similarity. Ref.4 |
| Sequence similarities | Belongs to the histone H3 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Chromosome Nucleosome core Nucleus |
| Ligand | DNA-binding |
| PTM | Acetylation Citrullination Methylation Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | nucleosome assembly Inferred from electronic annotation. Source: InterPro |
| Cellular component | nucleosome Inferred from electronic annotation. Source: UniProtKB-KW nucleusInferred from direct assay. Source: HPA |
| Molecular function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW |
| 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 – 135 | 134 | Histone H3.3C | PRO_0000253960 | |||||
Amino acid modifications | |||||||||
| Modified residue | 3 | 1 | Asymmetric dimethylarginine; by PRMT6 By similarity | ||||||
| Modified residue | 4 | 1 | Phosphothreonine; by GSG2 By similarity | ||||||
| Modified residue | 5 | 1 | N6-methylated lysine By similarity | ||||||
| Modified residue | 7 | 1 | Phosphothreonine; by PKC By similarity | ||||||
| Modified residue | 9 | 1 | Citrulline; alternate By similarity | ||||||
| Modified residue | 9 | 1 | Symmetric dimethylarginine; by PRMT5; alternate By similarity | ||||||
| Modified residue | 10 | 1 | N6-acetyllysine; alternate By similarity | ||||||
| Modified residue | 10 | 1 | N6-methylated lysine; alternate By similarity | ||||||
| Modified residue | 11 | 1 | Phosphoserine; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 By similarity | ||||||
| Modified residue | 12 | 1 | Phosphothreonine; by PKC By similarity | ||||||
| Modified residue | 15 | 1 | N6-acetyllysine Ref.3 | ||||||
| Modified residue | 18 | 1 | Asymmetric dimethylarginine; by CARM1; alternate By similarity | ||||||
| Modified residue | 18 | 1 | Citrulline; alternate By similarity | ||||||
| Modified residue | 19 | 1 | N6-acetyllysine; alternate By similarity | ||||||
| Modified residue | 19 | 1 | N6-methylated lysine; alternate By similarity | ||||||
| Modified residue | 24 | 1 | N6-acetyllysine Ref.3 | ||||||
| Modified residue | 28 | 1 | N6-acetyllysine; alternate By similarity | ||||||
| Modified residue | 28 | 1 | N6-methylated lysine; alternate By similarity | ||||||
| Modified residue | 29 | 1 | Phosphoserine; by AURKB, AURKC and RPS6KA5 By similarity | ||||||
| Modified residue | 32 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 41 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 56 | 1 | N6-acetyllysine Ref.3 | ||||||
| Modified residue | 57 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 80 | 1 | Phosphothreonine Ref.4 | ||||||
| Modified residue | 122 | 1 | N6-acetyllysine Ref.3 | ||||||
| Modified residue | 122 | 1 | N6-methylated lysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 88 | 1 | A → V in AAH66906. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. Gibbs R.A.Nature 440:346-351(2006) [PubMed: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | "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: Testis. |
| [3] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-15; LYS-19; LYS-24; LYS-56 AND LYS-122, MASS SPECTROMETRY. |
| [4] | "Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers." Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M. Cell 142:967-980(2010) [PubMed: 20850016] [Abstract] Cited for: PHOSPHORYLATION AT SER-57 AND THR-80. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AC023050 Genomic DNA. No translation available. BC066906 mRNA. Translation: AAH66906.1. | ||||||||||||
| IPI | IPI00419884. | ||||||||||||
| RefSeq | NP_001013721.2. NM_001013699.2. | ||||||||||||
| UniGene | Hs.448697. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q6NXT2. | ||||||||||||
| SMR | Q6NXT2. Positions 2-135. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q6NXT2. 1 interaction. | ||||||||||||
| STRING | Q6NXT2. | ||||||||||||
Polymorphism databases | |||||||||||||
| DMDM | 116248097. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | Q6NXT2. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000340398; ENSP00000339835; ENSG00000188375. | ||||||||||||
| GeneID | 440093. | ||||||||||||
| KEGG | hsa:440093. | ||||||||||||
| NMPDR | fig|9606.3.peg.7374. | ||||||||||||
| UCSC | uc001rkr.1. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 440093. | ||||||||||||
| GeneCards | GC12M031944. | ||||||||||||
| HGNC | HGNC:33164. H3F3C. | ||||||||||||
| neXtProt | NX_Q6NXT2. | ||||||||||||
| PharmGKB | PA165512903. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | prNOG04423. | ||||||||||||
| GeneTree | ENSGT00560000076889. | ||||||||||||
| HOGENOM | HBG715487. | ||||||||||||
| HOVERGEN | HBG001172. | ||||||||||||
| InParanoid | Q6NXT2. | ||||||||||||
| OMA | HRIRGEC. | ||||||||||||
| PhylomeDB | Q6NXT2. | ||||||||||||
Gene expression databases | |||||||||||||
| Genevestigator | Q6NXT2. | ||||||||||||
| GermOnline | ENSG00000188375. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR000164. Histone_H3. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:1.10.20.10. Histone-fold. 1 hit. | ||||||||||||
| KO | K11253. | ||||||||||||
| PANTHER | PTHR11426. Histone_H3. 1 hit. | ||||||||||||
| Pfam | PF00125. Histone. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00622. HISTONEH3. | ||||||||||||
| SMART | SM00428. H3. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF47113. Histone-fold. 1 hit. | ||||||||||||
| PROSITE | PS00322. HISTONE_H3_1. 1 hit. PS00959. HISTONE_H3_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| NextBio | 108939. | ||||||||||||
Entry information
| Entry name | H3C_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q6NXT2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 12 Human chromosome 12: entries, gene names and cross-references to MIM |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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