UniProt ID | H33_RAT | |
---|---|---|
UniProt AC | P84245 | |
Protein Name | Histone H3.3 | |
Gene Name | H3f3b | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 136 | |
Subcellular Localization | Nucleus. Chromosome. | |
Protein Description | Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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.. | |
Protein Sequence | MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | |
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 ----CCCCCHHHHHC | 20.26 | 11498542 | |
5 | Allysine | ---MARTKQTARKST ---CCCCCHHHHHCC | 39.85 | - | |
5 | Acetylation | ---MARTKQTARKST ---CCCCCHHHHHCC | 39.85 | 1001435 | |
5 | Crotonylation | ---MARTKQTARKST ---CCCCCHHHHHCC | 39.85 | - | |
5 | Deamination | ---MARTKQTARKST ---CCCCCHHHHHCC | 39.85 | - | |
5 | Methylation | ---MARTKQTARKST ---CCCCCHHHHHCC | 39.85 | - | |
5 | Other | ---MARTKQTARKST ---CCCCCHHHHHCC | 39.85 | - | |
6 | Formation of an isopeptide bond | --MARTKQTARKSTG --CCCCCHHHHHCCC | 39.52 | 32273471 | |
6 | Serotonylation | --MARTKQTARKSTG --CCCCCHHHHHCCC | 39.52 | - | |
7 | Phosphorylation | -MARTKQTARKSTGG -CCCCCHHHHHCCCC | 29.95 | - | |
9 | Citrullination | ARTKQTARKSTGGKA CCCCHHHHHCCCCCC | 36.52 | - | |
9 | Citrullination | ARTKQTARKSTGGKA CCCCHHHHHCCCCCC | 36.52 | - | |
9 | Methylation | ARTKQTARKSTGGKA CCCCHHHHHCCCCCC | 36.52 | - | |
10 | "N6,N6,N6-trimethyllysine" | RTKQTARKSTGGKAP CCCHHHHHCCCCCCC | 50.32 | - | |
10 | Acetylation | RTKQTARKSTGGKAP CCCHHHHHCCCCCCC | 50.32 | 25786129 | |
10 | Crotonylation | RTKQTARKSTGGKAP CCCHHHHHCCCCCCC | 50.32 | - | |
10 | Lactoylation | RTKQTARKSTGGKAP CCCHHHHHCCCCCCC | 50.32 | - | |
10 | Methylation | RTKQTARKSTGGKAP CCCHHHHHCCCCCCC | 50.32 | - | |
10 | Other | RTKQTARKSTGGKAP CCCHHHHHCCCCCCC | 50.32 | - | |
11 | ADP-ribosylation | TKQTARKSTGGKAPR CCHHHHHCCCCCCCH | 27.08 | - | |
11 | Phosphorylation | TKQTARKSTGGKAPR CCHHHHHCCCCCCCH | 27.08 | 10911986 | |
12 | Phosphorylation | KQTARKSTGGKAPRK CHHHHHCCCCCCCHH | 53.65 | 12560483 | |
15 | Acetylation | ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH | 57.47 | 25786129 | |
15 | Glutarylation | ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH | 57.47 | - | |
15 | Lactoylation | ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH | 57.47 | - | |
15 | Other | ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH | 57.47 | - | |
15 | Succinylation | ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH | 57.47 | - | |
18 | Asymmetric dimethylarginine | STGGKAPRKQLATKA CCCCCCCHHHHHHHH | 44.18 | - | |
18 | Citrullination | STGGKAPRKQLATKA CCCCCCCHHHHHHHH | 44.18 | - | |
18 | Methylation | STGGKAPRKQLATKA CCCCCCCHHHHHHHH | 44.18 | - | |
19 | N6-crotonyl-L-lysine | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | - | |
19 | Acetylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | 25786129 | |
19 | Butyrylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | - | |
19 | Crotonylation | 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 | - | |
24 | N6-crotonyl-L-lysine | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | - | |
24 | Acetylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | 25786129 | |
24 | Butyrylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | - | |
24 | Crotonylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | - | |
24 | Glutarylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | - | |
24 | Lactoylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | - | |
24 | Methylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | - | |
24 | Other | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | - | |
27 | Citrullination | QLATKAARKSAPSTG HHHHHHHHHHCCCCC | 38.02 | - | |
27 | Citrullination | QLATKAARKSAPSTG HHHHHHHHHHCCCCC | 38.02 | - | |
28 | "N6,N6,N6-trimethyllysine" | LATKAARKSAPSTGG HHHHHHHHHCCCCCC | 46.36 | - | |
28 | Acetylation | LATKAARKSAPSTGG HHHHHHHHHCCCCCC | 46.36 | 25786129 | |
28 | Crotonylation | LATKAARKSAPSTGG HHHHHHHHHCCCCCC | 46.36 | - | |
28 | Glutarylation | LATKAARKSAPSTGG HHHHHHHHHCCCCCC | 46.36 | - | |
28 | Lactoylation | LATKAARKSAPSTGG HHHHHHHHHCCCCCC | 46.36 | - | |
28 | Methylation | LATKAARKSAPSTGG HHHHHHHHHCCCCCC | 46.36 | - | |
28 | Other | LATKAARKSAPSTGG HHHHHHHHHCCCCCC | 46.36 | - | |
29 | ADP-ribosylation | ATKAARKSAPSTGGV HHHHHHHHCCCCCCC | 39.60 | - | |
29 | Phosphorylation | ATKAARKSAPSTGGV HHHHHHHHCCCCCCC | 39.60 | 28432305 | |
32 | Phosphorylation | AARKSAPSTGGVKKP HHHHHCCCCCCCCCC | 39.13 | - | |
37 | "N6,N6,N6-trimethyllysine" | APSTGGVKKPHRYRP CCCCCCCCCCCCCCC | 64.95 | - | |
37 | Acetylation | APSTGGVKKPHRYRP CCCCCCCCCCCCCCC | 64.95 | 19343714 | |
37 | Methylation | APSTGGVKKPHRYRP CCCCCCCCCCCCCCC | 64.95 | - | |
37 | Other | APSTGGVKKPHRYRP CCCCCCCCCCCCCCC | 64.95 | - | |
38 | Acetylation | PSTGGVKKPHRYRPG CCCCCCCCCCCCCCC | 43.58 | 25786129 | |
38 | Methylation | PSTGGVKKPHRYRPG CCCCCCCCCCCCCCC | 43.58 | - | |
42 | Phosphorylation | GVKKPHRYRPGTVAL CCCCCCCCCCCCHHH | 20.37 | - | |
46 | Phosphorylation | PHRYRPGTVALREIR CCCCCCCCHHHHHHH | 12.80 | 23984901 | |
57 | "N6,N6,N6-trimethyllysine" | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
57 | Acetylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | 22902405 | |
57 | Crotonylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
57 | Glutarylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
57 | Lactoylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
57 | Methylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
57 | Other | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
57 | Succinylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
58 | Phosphorylation | EIRRYQKSTELLIRK HHHHHHHCHHHHHHH | 16.16 | 27097102 | |
59 | Phosphorylation | IRRYQKSTELLIRKL HHHHHHCHHHHHHHC | 37.37 | 27097102 | |
65 | Methylation | STELLIRKLPFQRLV CHHHHHHHCCHHHHH | 54.22 | - | |
65 | Other | STELLIRKLPFQRLV CHHHHHHHCCHHHHH | 54.22 | - | |
65 | Succinylation | STELLIRKLPFQRLV CHHHHHHHCCHHHHH | 54.22 | 26843850 | |
80 | "N6,N6,N6-trimethyllysine" | REIAQDFKTDLRFQS HHHHHHHHHCHHHHH | 49.79 | - | |
80 | Acetylation | REIAQDFKTDLRFQS HHHHHHHHHCHHHHH | 49.79 | 22902405 | |
80 | Glutarylation | REIAQDFKTDLRFQS HHHHHHHHHCHHHHH | 49.79 | - | |
80 | Lactoylation | REIAQDFKTDLRFQS HHHHHHHHHCHHHHH | 49.79 | - | |
80 | Methylation | REIAQDFKTDLRFQS HHHHHHHHHCHHHHH | 49.79 | - | |
80 | Other | REIAQDFKTDLRFQS HHHHHHHHHCHHHHH | 49.79 | - | |
80 | Succinylation | REIAQDFKTDLRFQS HHHHHHHHHCHHHHH | 49.79 | - | |
80 | Ubiquitination | REIAQDFKTDLRFQS HHHHHHHHHCHHHHH | 49.79 | - | |
81 | Phosphorylation | EIAQDFKTDLRFQSA HHHHHHHHCHHHHHH | 40.01 | 29779826 | |
87 | Phosphorylation | KTDLRFQSAAIGALQ HHCHHHHHHHHHHHH | 19.56 | 16641100 | |
97 | Phosphorylation | IGALQEASEAYLVGL HHHHHHHHHHHHHHH | 23.23 | 17683130 | |
108 | Phosphorylation | LVGLFEDTNLCAIHA HHHHHCCCCEEEEEE | 23.93 | - | |
116 | Acetylation | NLCAIHAKRVTIMPK CEEEEEEEECEECHH | 32.99 | 25786129 | |
116 | Glutarylation | NLCAIHAKRVTIMPK CEEEEEEEECEECHH | 32.99 | - | |
123 | Acetylation | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | - | |
123 | Glutarylation | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | - | |
123 | Methylation | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | - | |
123 | Other | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | - | |
123 | Succinylation | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | - |
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 | - | Uniprot |
7 | T | Phosphorylation | Kinase | PKC | - | Uniprot |
11 | S | Phosphorylation | Kinase | RPS6KA5 | A0A0G2K366 | GPS |
11 | S | Phosphorylation | Kinase | AURKB | O55099 | GPS |
11 | S | Phosphorylation | Kinase | RPS6KA3 | D3Z8E0 | GPS |
11 | S | Phosphorylation | Kinase | RPS6KA4 | D3ZSB7 | GPS |
11 | S | Phosphorylation | Kinase | AURKC | D4AD76 | GPS |
11 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
11 | S | Phosphorylation | Kinase | ALTERNATE | - | Uniprot |
12 | T | Phosphorylation | Kinase | DAPK3 | O88764 | GPS |
12 | T | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
12 | T | Phosphorylation | Kinase | PKC | - | Uniprot |
29 | S | Phosphorylation | Kinase | MAPK8 | P49185 | GPS |
29 | S | Phosphorylation | Kinase | MAPK9 | P49186 | GPS |
29 | S | Phosphorylation | Kinase | ALTERNATE | - | Uniprot |
46 | T | Phosphorylation | Kinase | DYRK1A | Q63470 | GPS |
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 |
| - |
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 |
| - |
10 | K | Phosphorylation |
| - |
10 | K | Methylation |
| - |
10 | K | Methylation |
| - |
10 | K | Phosphorylation |
| - |
10 | K | Acetylation |
| - |
10 | K | Acetylation |
| - |
10 | K | Acetylation |
| - |
10 | K | Acetylation |
| - |
10 | K | Methylation |
| - |
10 | K | Methylation |
| - |
10 | K | Methylation |
| - |
10 | K | Methylation |
| - |
11 | S | Acetylation |
| 12560483 |
11 | S | Acetylation |
| 12560483 |
11 | S | Acetylation |
| 12560483 |
11 | S | Methylation |
| 12560483 |
11 | S | Methylation |
| 12560483 |
11 | S | Phosphorylation |
| 12560483 |
11 | S | Phosphorylation |
| 12560483 |
11 | S | Phosphorylation |
| 12560483 |
11 | S | Phosphorylation |
| 12560483 |
11 | S | Phosphorylation |
| 12560483 |
11 | S | Phosphorylation |
| 12560483 |
11 | S | Phosphorylation |
| 12560483 |
12 | T | Phosphorylation |
| 12560483 |
12 | T | Methylation |
| 12560483 |
12 | T | Phosphorylation |
| 12560483 |
18 | R | Citrullination |
| - |
18 | R | Acetylation |
| - |
18 | R | Methylation |
| - |
18 | R | Methylation |
| - |
18 | R | Methylation |
| - |
19 | K | Methylation |
| - |
19 | K | Acetylation |
| - |
24 | K | Methylation |
| - |
24 | K | Acetylation |
| - |
28 | K | Methylation |
| - |
28 | K | Methylation |
| - |
29 | S | Phosphorylation |
| - |
32 | S | Phosphorylation |
| - |
37 | K | Methylation |
| 19343714 |
57 | K | Methylation |
| - |
80 | K | Succinylation |
| - |
80 | K | ubiquitylation |
| - |
80 | K | Methylation |
| - |
80 | K | Methylation |
| - |
80 | K | Methylation |
| - |
120 | K | Methylation |
| - |
120 | K | ubiquitylation |
| - |
123 | K | Acetylation |
| - |
123 | K | Succinylation |
| - |
* 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 H33_RAT !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Acetylation | |
Reference | PubMed |
"Mass spectrometry-compatible silver staining of histones resolved onacetic acid-urea-Triton PAGE."; Pramod K.S., Bharat K., Sanjay G.; Proteomics 9:2589-2592(2009). Cited for: IDENTIFICATION BY MASS SPECTROMETRY, AND ACETYLATION AT LYS-37. | |
Phosphorylation | |
Reference | PubMed |
"Novel mitosis-specific phosphorylation of histone H3 at Thr11mediated by Dlk/ZIP kinase."; Preuss U., Landsberg G., Scheidtmann K.H.; Nucleic Acids Res. 31:878-885(2003). Cited for: PHOSPHORYLATION AT SER-11 AND THR-12. |