UniProt ID | H3C_HUMAN | |
---|---|---|
UniProt AC | Q6NXT2 | |
Protein Name | Histone H3.3C | |
Gene Name | H3F3C | |
Organism | Homo sapiens (Human). | |
Sequence Length | 135 | |
Subcellular Localization | Nucleus. Chromosome. | |
Protein Description | 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. Hominid-specific H3.5/H3F3C preferentially colocalizes with euchromatin, and it is associated with actively transcribed genes.. | |
Protein Sequence | MARTKQTARKSTGGKAPRKQLATKAARKSTPSTCGVKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFNTDLRFQSAAVGALQEASEAYLVGLLEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
3 | Asymmetric dimethylarginine | -----MARTKQTARK -----CCCCCHHHHH | 40.95 | - | |
3 | Citrullination | -----MARTKQTARK -----CCCCCHHHHH | 40.95 | - | |
3 | Methylation | -----MARTKQTARK -----CCCCCHHHHH | 40.95 | - | |
4 | Phosphorylation | ----MARTKQTARKS ----CCCCCHHHHHH | 20.26 | 17938195 | |
5 | Allysine | ---MARTKQTARKST ---CCCCCHHHHHHC | 39.85 | - | |
5 | Acetylation | ---MARTKQTARKST ---CCCCCHHHHHHC | 39.85 | - | |
5 | Deamination | ---MARTKQTARKST ---CCCCCHHHHHHC | 39.85 | - | |
5 | Methylation | ---MARTKQTARKST ---CCCCCHHHHHHC | 39.85 | - | |
5 | Other | ---MARTKQTARKST ---CCCCCHHHHHHC | 39.85 | - | |
6 | Formation of an isopeptide bond | --MARTKQTARKSTG --CCCCCHHHHHHCC | 39.52 | - | |
6 | Serotonylation | --MARTKQTARKSTG --CCCCCHHHHHHCC | 39.52 | - | |
7 | Phosphorylation | -MARTKQTARKSTGG -CCCCCHHHHHHCCC | 29.95 | 20228790 | |
9 | Citrullination | ARTKQTARKSTGGKA CCCCHHHHHHCCCCC | 36.52 | - | |
9 | Citrullination | ARTKQTARKSTGGKA CCCCHHHHHHCCCCC | 36.52 | - | |
9 | Methylation | ARTKQTARKSTGGKA CCCCHHHHHHCCCCC | 36.52 | - | |
10 | "N6,N6,N6-trimethyllysine" | RTKQTARKSTGGKAP CCCHHHHHHCCCCCC | 50.32 | - | |
10 | Acetylation | RTKQTARKSTGGKAP CCCHHHHHHCCCCCC | 50.32 | 54236075 | |
10 | Lactoylation | RTKQTARKSTGGKAP CCCHHHHHHCCCCCC | 50.32 | - | |
10 | Methylation | RTKQTARKSTGGKAP CCCHHHHHHCCCCCC | 50.32 | - | |
10 | Other | RTKQTARKSTGGKAP CCCHHHHHHCCCCCC | 50.32 | - | |
10 | Ubiquitination | RTKQTARKSTGGKAP CCCHHHHHHCCCCCC | 50.32 | 22817900 | |
11 | ADP-ribosylation | TKQTARKSTGGKAPR CCHHHHHHCCCCCCH | 27.08 | - | |
11 | Phosphorylation | TKQTARKSTGGKAPR CCHHHHHHCCCCCCH | 27.08 | 10469656 | |
12 | Phosphorylation | KQTARKSTGGKAPRK CHHHHHHCCCCCCHH | 53.65 | 26074081 | |
15 | Sumoylation | ARKSTGGKAPRKQLA HHHHCCCCCCHHHHH | 57.47 | - | |
15 | Acetylation | ARKSTGGKAPRKQLA HHHHCCCCCCHHHHH | 57.47 | 54236071 | |
15 | Glutarylation | ARKSTGGKAPRKQLA HHHHCCCCCCHHHHH | 57.47 | - | |
15 | Lactoylation | ARKSTGGKAPRKQLA HHHHCCCCCCHHHHH | 57.47 | - | |
15 | Other | ARKSTGGKAPRKQLA HHHHCCCCCCHHHHH | 57.47 | - | |
15 | Succinylation | ARKSTGGKAPRKQLA HHHHCCCCCCHHHHH | 57.47 | 21890473 | |
15 | Sumoylation | ARKSTGGKAPRKQLA HHHHCCCCCCHHHHH | 57.47 | - | |
15 | Ubiquitination | ARKSTGGKAPRKQLA HHHHCCCCCCHHHHH | 57.47 | 23000965 | |
18 | Asymmetric dimethylarginine | STGGKAPRKQLATKA HCCCCCCHHHHHHHH | 44.18 | - | |
18 | Citrullination | STGGKAPRKQLATKA HCCCCCCHHHHHHHH | 44.18 | - | |
18 | Methylation | STGGKAPRKQLATKA HCCCCCCHHHHHHHH | 44.18 | - | |
19 | Sumoylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | - | |
19 | Acetylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | 66741851 | |
19 | Butyrylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | - | |
19 | Glutarylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | - | |
19 | Lactoylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | - | |
19 | Methylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | - | |
19 | Other | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | - | |
19 | Sumoylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | - | |
19 | Ubiquitination | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | 23000965 | |
24 | Sumoylation | PRKQLATKAARKSTP CHHHHHHHHHHHCCC | 34.15 | - | |
24 | Acetylation | PRKQLATKAARKSTP CHHHHHHHHHHHCCC | 34.15 | 66724869 | |
24 | Butyrylation | PRKQLATKAARKSTP CHHHHHHHHHHHCCC | 34.15 | - | |
24 | Glutarylation | PRKQLATKAARKSTP CHHHHHHHHHHHCCC | 34.15 | - | |
24 | Lactoylation | PRKQLATKAARKSTP CHHHHHHHHHHHCCC | 34.15 | - | |
24 | Methylation | PRKQLATKAARKSTP CHHHHHHHHHHHCCC | 34.15 | - | |
24 | Other | PRKQLATKAARKSTP CHHHHHHHHHHHCCC | 34.15 | - | |
24 | Sumoylation | PRKQLATKAARKSTP CHHHHHHHHHHHCCC | 34.15 | - | |
24 | Ubiquitination | PRKQLATKAARKSTP CHHHHHHHHHHHCCC | 34.15 | 23000965 | |
27 | Citrullination | QLATKAARKSTPSTC HHHHHHHHHCCCCCC | 38.01 | - | |
27 | Citrullination | QLATKAARKSTPSTC HHHHHHHHHCCCCCC | 38.01 | - | |
28 | "N6,N6,N6-trimethyllysine" | LATKAARKSTPSTCG HHHHHHHHCCCCCCC | 54.69 | - | |
28 | Acetylation | LATKAARKSTPSTCG HHHHHHHHCCCCCCC | 54.69 | - | |
28 | Glutarylation | LATKAARKSTPSTCG HHHHHHHHCCCCCCC | 54.69 | - | |
28 | Lactoylation | LATKAARKSTPSTCG HHHHHHHHCCCCCCC | 54.69 | - | |
28 | Methylation | LATKAARKSTPSTCG HHHHHHHHCCCCCCC | 54.69 | - | |
28 | Other | LATKAARKSTPSTCG HHHHHHHHCCCCCCC | 54.69 | - | |
28 | Ubiquitination | LATKAARKSTPSTCG HHHHHHHHCCCCCCC | 54.69 | 22817900 | |
29 | ADP-ribosylation | ATKAARKSTPSTCGV HHHHHHHCCCCCCCC | 39.74 | - | |
29 | Phosphorylation | ATKAARKSTPSTCGV HHHHHHHCCCCCCCC | 39.74 | - | |
32 | Phosphorylation | AARKSTPSTCGVKPH HHHHCCCCCCCCCCC | 36.10 | - | |
37 | Methylation | TPSTCGVKPHRYRPG CCCCCCCCCCCCCCC | 22.01 | - | |
41 | Phosphorylation | CGVKPHRYRPGTVAL CCCCCCCCCCCCHHH | 20.37 | 28152594 | |
42 | Methylation | GVKPHRYRPGTVALR CCCCCCCCCCCHHHH | 24.11 | - | |
45 | Phosphorylation | PHRYRPGTVALREIR CCCCCCCCHHHHHHH | 12.80 | 30266825 | |
49 | Methylation | RPGTVALREIRRYQK CCCCHHHHHHHHHHH | 27.79 | - | |
54 | Phosphorylation | ALREIRRYQKSTELL HHHHHHHHHHCHHHH | 15.50 | 22817900 | |
56 | "N6,N6,N6-trimethyllysine" | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
56 | Acetylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | 66739507 | |
56 | Glutarylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
56 | Lactoylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
56 | Methylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
56 | Other | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
56 | Succinylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | 21890473 | |
56 | Sumoylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
56 | Ubiquitination | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | 23000965 | |
57 | Phosphorylation | EIRRYQKSTELLIRK HHHHHHHCHHHHHHH | 16.16 | 23401153 | |
58 | Phosphorylation | IRRYQKSTELLIRKL HHHHHHCHHHHHHHC | 37.37 | 30266825 | |
63 | Methylation | KSTELLIRKLPFQRL HCHHHHHHHCCHHHH | 34.13 | - | |
64 | Methylation | STELLIRKLPFQRLV CHHHHHHHCCHHHHH | 54.22 | - | |
64 | Other | STELLIRKLPFQRLV CHHHHHHHCCHHHHH | 54.22 | - | |
80 | O-linked_Glycosylation | EIAQDFNTDLRFQSA HHHHHCCCCHHHHHH | 36.08 | 21224338 | |
80 | Phosphorylation | EIAQDFNTDLRFQSA HHHHHCCCCHHHHHH | 36.08 | 20850016 | |
86 | Phosphorylation | NTDLRFQSAAVGALQ CCCHHHHHHHHHHHH | 18.58 | - | |
107 | Phosphorylation | LVGLLEDTNLCAIHA HHHHHCCCCCEEEEE | 22.25 | - | |
115 | Acetylation | NLCAIHAKRVTIMPK CCEEEEEEECEECHH | 32.99 | - | |
115 | Glutarylation | NLCAIHAKRVTIMPK CCEEEEEEECEECHH | 32.99 | - | |
118 | Phosphorylation | AIHAKRVTIMPKDIQ EEEEEECEECHHHHH | 18.65 | 20068231 | |
122 | Sumoylation | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | - | |
122 | Acetylation | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | 54236079 | |
122 | Glutarylation | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | - | |
122 | Methylation | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | - | |
122 | Other | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | - | |
122 | Succinylation | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | 21890473 | |
122 | Sumoylation | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | - | |
122 | Ubiquitination | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | 23000965 | |
128 | Methylation | PKDIQLARRIRGERA HHHHHHHHHHHCCCC | 43.05 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
4 | T | Phosphorylation | Kinase | HASPIN | Q8TF76 | Uniprot |
7 | T | Phosphorylation | Kinase | PKC | - | Uniprot |
11 | S | Phosphorylation | Kinase | ALTERNATE | - | Uniprot |
12 | T | Phosphorylation | Kinase | PKC | - | Uniprot |
29 | S | Phosphorylation | Kinase | ALTERNATE | - | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
3 | R | Methylation |
| - |
4 | T | Phosphorylation |
| - |
5 | K | ubiquitylation |
| - |
5 | K | Acetylation |
| - |
5 | K | Methylation |
| - |
5 | K | Methylation |
| - |
5 | K | Methylation |
| - |
5 | K | Methylation |
| - |
5 | K | Phosphorylation |
| - |
5 | K | Methylation |
| - |
7 | T | Phosphorylation |
| - |
7 | T | Methylation |
| - |
9 | R | Methylation |
| - |
9 | R | Methylation |
| - |
9 | R | Methylation |
| - |
9 | R | Citrullination |
| - |
9 | R | Acetylation |
| - |
10 | K | Phosphorylation |
| - |
10 | K | Phosphorylation |
| 30257210 |
10 | K | Phosphorylation |
| - |
10 | K | Phosphorylation |
| - |
10 | K | Methylation |
| - |
10 | K | Methylation |
| - |
10 | K | Methylation |
| - |
10 | K | Acetylation |
| - |
10 | K | Acetylation |
| - |
10 | K | Acetylation |
| - |
10 | K | Acetylation |
| 30257210 |
10 | K | Methylation |
| - |
10 | K | Methylation |
| - |
10 | K | Methylation |
| - |
11 | S | Acetylation |
| 30257210 |
11 | S | Acetylation |
| - |
11 | S | Acetylation |
| - |
11 | S | Methylation |
| - |
11 | S | Methylation |
| - |
11 | S | Phosphorylation |
| - |
11 | S | Phosphorylation |
| - |
11 | S | Phosphorylation |
| - |
11 | S | Phosphorylation |
| - |
11 | S | Phosphorylation |
| - |
11 | S | Phosphorylation |
| - |
11 | S | Phosphorylation |
| 30257210 |
12 | T | Phosphorylation |
| - |
12 | T | Methylation |
| - |
12 | T | Phosphorylation |
| - |
18 | R | Citrullination |
| - |
18 | R | Methylation |
| - |
18 | R | Methylation |
| - |
18 | R | Methylation |
| - |
18 | R | Acetylation |
| - |
19 | K | Methylation |
| - |
19 | K | Acetylation |
| - |
24 | K | Methylation |
| - |
24 | K | Acetylation |
| - |
28 | K | Methylation |
| - |
28 | K | Methylation |
| - |
29 | S | Phosphorylation |
| - |
56 | K | Methylation |
| - |
120 | K | ubiquitylation |
| - |
120 | K | Methylation |
| - |
122 | K | Succinylation |
| - |
122 | K | Acetylation |
| - |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of H3C_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
KDM1A_HUMAN | KDM1A | physical | 23455924 | |
KDM4B_HUMAN | KDM4B | physical | 23455924 | |
ANM5_HUMAN | PRMT5 | physical | 23455924 | |
ANM6_HUMAN | PRMT6 | physical | 23455924 | |
ANM7_HUMAN | PRMT7 | physical | 23455924 | |
SETMR_HUMAN | SETMAR | physical | 23455924 | |
SMYD1_HUMAN | SMYD1 | physical | 23455924 | |
SMYD3_HUMAN | SMYD3 | physical | 23455924 | |
SUV91_HUMAN | SUV39H1 | physical | 23455924 | |
NSD3_HUMAN | WHSC1L1 | physical | 23455924 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-15; LYS-19; LYS-24;LYS-56 AND LYS-122, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Quantitative interaction proteomics and genome-wide profiling ofepigenetic 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). Cited for: PHOSPHORYLATION AT SER-57 AND THR-80. |