UniProt ID | H31_MOUSE | |
---|---|---|
UniProt AC | P68433 | |
Protein Name | Histone H3.1 | |
Gene Name | Hist1h3a | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 136 | |
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.. | |
Protein Sequence | MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | |
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 | 15339660 | |
3 | Methylation | -----MARTKQTARK -----CCCCCHHHHH | 40.95 | - | |
3 | Phosphorylation | -----MARTKQTARK -----CCCCCHHHHH | 40.95 | - | |
4 | Phosphorylation | ----MARTKQTARKS ----CCCCCHHHHHC | 20.26 | 14987995 | |
5 | Allysine | ---MARTKQTARKST ---CCCCCHHHHHCC | 39.85 | - | |
5 | Acetylation | ---MARTKQTARKST ---CCCCCHHHHHCC | 39.85 | 17194708 | |
5 | Crotonylation | ---MARTKQTARKST ---CCCCCHHHHHCC | 39.85 | 21925322 | |
5 | Deamination | ---MARTKQTARKST ---CCCCCHHHHHCC | 39.85 | - | |
5 | Methylation | ---MARTKQTARKST ---CCCCCHHHHHCC | 39.85 | 17194708 | |
5 | Other | ---MARTKQTARKST ---CCCCCHHHHHCC | 39.85 | 27105115 | |
6 | Formation of an isopeptide bond | --MARTKQTARKSTG --CCCCCHHHHHCCC | 39.52 | - | |
6 | Serotonylation | --MARTKQTARKSTG --CCCCCHHHHHCCC | 39.52 | 30867594 | |
7 | Phosphorylation | -MARTKQTARKSTGG -CCCCCHHHHHCCCC | 29.95 | - | |
9 | Citrullination | ARTKQTARKSTGGKA CCCCHHHHHCCCCCC | 36.52 | - | |
9 | Citrullination | ARTKQTARKSTGGKA CCCCHHHHHCCCCCC | 36.52 | 15339660 | |
9 | Methylation | ARTKQTARKSTGGKA CCCCHHHHHCCCCCC | 36.52 | 15485929 | |
10 | "N6,N6,N6-trimethyllysine" | RTKQTARKSTGGKAP CCCHHHHHCCCCCCC | 50.32 | - | |
10 | Acetylation | RTKQTARKSTGGKAP CCCHHHHHCCCCCCC | 50.32 | 17194708 | |
10 | Crotonylation | RTKQTARKSTGGKAP CCCHHHHHCCCCCCC | 50.32 | 21925322 | |
10 | Lactoylation | RTKQTARKSTGGKAP CCCHHHHHCCCCCCC | 50.32 | - | |
10 | Methylation | RTKQTARKSTGGKAP CCCHHHHHCCCCCCC | 50.32 | 17194708 | |
10 | Other | RTKQTARKSTGGKAP CCCHHHHHCCCCCCC | 50.32 | 27105115 | |
11 | ADP-ribosylation | TKQTARKSTGGKAPR CCHHHHHCCCCCCCH | 27.08 | - | |
11 | Phosphorylation | TKQTARKSTGGKAPR CCHHHHHCCCCCCCH | 27.08 | 18936171 | |
12 | Phosphorylation | KQTARKSTGGKAPRK CHHHHHCCCCCCCHH | 53.65 | 18243098 | |
15 | Acetylation | ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH | 57.47 | 12498683 | |
15 | Glutarylation | ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH | 57.47 | - | |
15 | Lactoylation | ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH | 57.47 | 31645732 | |
15 | Methylation | ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH | 57.47 | - | |
15 | Other | ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH | 57.47 | 27105115 | |
15 | Succinylation | ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH | 57.47 | - | |
18 | Asymmetric dimethylarginine | STGGKAPRKQLATKA CCCCCCCHHHHHHHH | 44.18 | - | |
18 | Citrullination | STGGKAPRKQLATKA CCCCCCCHHHHHHHH | 44.18 | 15339660 | |
18 | Methylation | STGGKAPRKQLATKA CCCCCCCHHHHHHHH | 44.18 | 11751582 | |
19 | N6-crotonyl-L-lysine | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | - | |
19 | Acetylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | 12498683 | |
19 | Butyrylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | 27105113 | |
19 | Crotonylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | 21925322 | |
19 | Glutarylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | - | |
19 | Hydroxylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | 24681537 | |
19 | Lactoylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | 31645732 | |
19 | Malonylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | 26320211 | |
19 | Methylation | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | 17194708 | |
19 | Other | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | 27105115 | |
19 | Ubiquitination | TGGKAPRKQLATKAA CCCCCCHHHHHHHHH | 48.91 | 27667366 | |
24 | N6-crotonyl-L-lysine | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | - | |
24 | Acetylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | 12498683 | |
24 | Butyrylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | 27105113 | |
24 | Crotonylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | 21925322 | |
24 | Glutarylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | - | |
24 | Hydroxylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | 24681537 | |
24 | Lactoylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | 31645732 | |
24 | Malonylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | 26320211 | |
24 | Methylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | 17194708 | |
24 | Other | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | 27105115 | |
24 | Succinylation | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | 23806337 | |
24 | Ubiquitination | PRKQLATKAARKSAP CHHHHHHHHHHHHCC | 34.15 | 27667366 | |
27 | Citrullination | QLATKAARKSAPATG HHHHHHHHHHCCCCC | 38.02 | - | |
27 | Citrullination | QLATKAARKSAPATG HHHHHHHHHHCCCCC | 38.02 | 15339660 | |
27 | Methylation | QLATKAARKSAPATG HHHHHHHHHHCCCCC | 38.02 | - | |
28 | "N6,N6,N6-trimethyllysine" | LATKAARKSAPATGG HHHHHHHHHCCCCCC | 46.36 | - | |
28 | Acetylation | LATKAARKSAPATGG HHHHHHHHHCCCCCC | 46.36 | 17194708 | |
28 | Butyrylation | LATKAARKSAPATGG HHHHHHHHHCCCCCC | 46.36 | 27105113 | |
28 | Crotonylation | LATKAARKSAPATGG HHHHHHHHHCCCCCC | 46.36 | 21925322 | |
28 | Glutarylation | LATKAARKSAPATGG HHHHHHHHHCCCCCC | 46.36 | - | |
28 | Hydroxylation | LATKAARKSAPATGG HHHHHHHHHCCCCCC | 46.36 | 24681537 | |
28 | Lactoylation | LATKAARKSAPATGG HHHHHHHHHCCCCCC | 46.36 | 31645732 | |
28 | Methylation | LATKAARKSAPATGG HHHHHHHHHCCCCCC | 46.36 | 17194708 | |
28 | Other | LATKAARKSAPATGG HHHHHHHHHCCCCCC | 46.36 | 24681537 | |
28 | Succinylation | LATKAARKSAPATGG HHHHHHHHHCCCCCC | 46.36 | 23806337 | |
29 | ADP-ribosylation | ATKAARKSAPATGGV HHHHHHHHCCCCCCC | 33.65 | - | |
29 | Phosphorylation | ATKAARKSAPATGGV HHHHHHHHCCCCCCC | 33.65 | 20129940 | |
37 | "N6,N6,N6-trimethyllysine" | APATGGVKKPHRYRP CCCCCCCCCCCCCCC | 64.95 | - | |
37 | Acetylation | APATGGVKKPHRYRP CCCCCCCCCCCCCCC | 64.95 | 17189264 | |
37 | Butyrylation | APATGGVKKPHRYRP CCCCCCCCCCCCCCC | 64.95 | 27105113 | |
37 | Hydroxylation | APATGGVKKPHRYRP CCCCCCCCCCCCCCC | 64.95 | 24681537 | |
37 | Methylation | APATGGVKKPHRYRP CCCCCCCCCCCCCCC | 64.95 | 17194708 | |
37 | Other | APATGGVKKPHRYRP CCCCCCCCCCCCCCC | 64.95 | 24681537 | |
38 | Acetylation | PATGGVKKPHRYRPG CCCCCCCCCCCCCCC | 43.58 | 22826441 | |
38 | Butyrylation | PATGGVKKPHRYRPG CCCCCCCCCCCCCCC | 43.58 | 27105113 | |
38 | Methylation | PATGGVKKPHRYRPG CCCCCCCCCCCCCCC | 43.58 | - | |
41 | Dimethylation | GGVKKPHRYRPGTVA CCCCCCCCCCCCCHH | 37.37 | - | |
42 | Phosphorylation | GVKKPHRYRPGTVAL CCCCCCCCCCCCHHH | 20.37 | 28066266 | |
46 | Phosphorylation | PHRYRPGTVALREIR CCCCCCCCHHHHHHH | 12.80 | 14729942 | |
55 | Phosphorylation | ALREIRRYQKSTELL HHHHHHHHHHCHHHH | 15.50 | 25159016 | |
57 | "N6,N6,N6-trimethyllysine" | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
57 | Acetylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
57 | Crotonylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | 21925322 | |
57 | Glutarylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
57 | Lactoylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | 31645732 | |
57 | Malonylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | 26320211 | |
57 | Methylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | - | |
57 | Other | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | 27105115 | |
57 | Succinylation | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | 22389435 | |
57 | Ubiquitination | REIRRYQKSTELLIR HHHHHHHHCHHHHHH | 50.87 | 27667366 | |
58 | Phosphorylation | EIRRYQKSTELLIRK HHHHHHHCHHHHHHH | 16.16 | 26824392 | |
59 | Phosphorylation | IRRYQKSTELLIRKL HHHHHHCHHHHHHHC | 37.37 | 25521595 | |
65 | Acetylation | STELLIRKLPFQRLV CHHHHHHHCCHHHHH | 54.22 | - | |
65 | Methylation | STELLIRKLPFQRLV CHHHHHHHCCHHHHH | 54.22 | - | |
65 | Other | STELLIRKLPFQRLV CHHHHHHHCCHHHHH | 54.22 | 24681537 | |
80 | "N6,N6,N6-trimethyllysine" | REIAQDFKTDLRFQS HHHHHHHCCCHHHHH | 49.79 | - | |
80 | Acetylation | REIAQDFKTDLRFQS HHHHHHHCCCHHHHH | 49.79 | - | |
80 | Butyrylation | REIAQDFKTDLRFQS HHHHHHHCCCHHHHH | 49.79 | 27105113 | |
80 | Glutarylation | REIAQDFKTDLRFQS HHHHHHHCCCHHHHH | 49.79 | - | |
80 | Lactoylation | REIAQDFKTDLRFQS HHHHHHHCCCHHHHH | 49.79 | - | |
80 | Malonylation | REIAQDFKTDLRFQS HHHHHHHCCCHHHHH | 49.79 | 26320211 | |
80 | Methylation | REIAQDFKTDLRFQS HHHHHHHCCCHHHHH | 49.79 | 17194708 | |
80 | Other | REIAQDFKTDLRFQS HHHHHHHCCCHHHHH | 49.79 | 24681537 | |
80 | Succinylation | REIAQDFKTDLRFQS HHHHHHHCCCHHHHH | 49.79 | 22389435 | |
80 | Ubiquitination | REIAQDFKTDLRFQS HHHHHHHCCCHHHHH | 49.79 | 27667366 | |
81 | Phosphorylation | EIAQDFKTDLRFQSS HHHHHHCCCHHHHHH | 40.01 | 25521595 | |
87 | Phosphorylation | KTDLRFQSSAVMALQ CCCHHHHHHHHHHHH | 19.97 | - | |
100 | Phosphorylation | LQEACEAYLVGLFED HHHHHHHHHHHHHCC | 4.61 | 26239621 | |
108 | Phosphorylation | LVGLFEDTNLCAIHA HHHHHCCCCEEEEEE | 23.93 | 26239621 | |
116 | Acetylation | NLCAIHAKRVTIMPK CEEEEEEEECEECHH | 32.99 | - | |
116 | Glutarylation | NLCAIHAKRVTIMPK CEEEEEEEECEECHH | 32.99 | - | |
119 | Phosphorylation | AIHAKRVTIMPKDIQ EEEEEECEECHHHHH | 18.65 | 29109428 | |
121 | Sulfoxidation | HAKRVTIMPKDIQLA EEEECEECHHHHHHH | 2.17 | 21406390 | |
123 | Acetylation | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | - | |
123 | Butyrylation | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | 27105113 | |
123 | Glutarylation | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | - | |
123 | Malonylation | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | 26320211 | |
123 | Methylation | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | 13678296 | |
123 | Other | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | 24681537 | |
123 | Succinylation | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | - | |
123 | Ubiquitination | KRVTIMPKDIQLARR EECEECHHHHHHHHH | 50.51 | 27667366 | |
129 | Methylation | PKDIQLARRIRGERA HHHHHHHHHHHCCCC | 43.05 | - | |
129 | Phosphorylation | PKDIQLARRIRGERA HHHHHHHHHHHCCCC | 43.05 | - | |
130 | Methylation | KDIQLARRIRGERA- HHHHHHHHHHCCCC- | 19.83 | - | |
130 | Phosphorylation | KDIQLARRIRGERA- HHHHHHHHHHCCCC- | 19.83 | - | |
132 | Phosphorylation | IQLARRIRGERA--- HHHHHHHHCCCC--- | 38.82 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
4 | T | Phosphorylation | Kinase | GSG2 | Q9Z0R0 | GPS |
7 | T | Phosphorylation | Kinase | PKC | - | Uniprot |
10 | S | Phosphorylation | Kinase | AURB | Q96GD4 | PSP |
10 | S | Phosphorylation | Kinase | AURB | O70126 | PSP |
10 | S | Phosphorylation | Kinase | MSK1 | Q8C050 | PSP |
10 | S | Phosphorylation | Kinase | ERK2 | P63085 | PSP |
10 | S | Phosphorylation | Kinase | AURC | O88445 | PSP |
10 | S | Phosphorylation | Kinase | MST2 | Q13188 | PSP |
10 | S | Phosphorylation | Kinase | MSK1 | O75582 | PSP |
10 | S | Phosphorylation | Kinase | CHK1 | O14757 | PSP |
10 | S | Phosphorylation | Kinase | MSK2 | O75676 | PSP |
10 | S | Phosphorylation | Kinase | P38A | Q16539 | PSP |
10 | S | Phosphorylation | Kinase | RSK2 | P18654 | PSP |
11 | S | Phosphorylation | Kinase | RPS6KA5 | Q8C050 | GPS |
11 | S | Phosphorylation | Kinase | RPS6KA4 | Q9Z2B9 | GPS |
11 | S | Phosphorylation | Kinase | RPS6KA3 | P18654 | GPS |
11 | S | Phosphorylation | Kinase | CHEK1 | O14757 | GPS |
11 | T | Phosphorylation | Kinase | CHK1 | O14757 | PSP |
11 | S | Phosphorylation | Kinase | AURKC | O88445 | GPS |
11 | S | Phosphorylation | Kinase | AURKB | O70126 | GPS |
11 | S | Phosphorylation | Kinase | ALTERNATE | - | Uniprot |
12 | T | Phosphorylation | Kinase | PKC | - | Uniprot |
12 | T | Phosphorylation | Kinase | CHEK1 | O35280 | Uniprot |
28 | S | Phosphorylation | Kinase | MSK1 | Q8C050 | PSP |
28 | S | Phosphorylation | Kinase | MSK1 | O75582 | PSP |
28 | S | Phosphorylation | Kinase | MST2 | Q13188 | PSP |
28 | S | Phosphorylation | Kinase | AURB | O70126 | PSP |
28 | S | Phosphorylation | Kinase | AURB | Q96GD4 | PSP |
29 | S | Phosphorylation | Kinase | RPS6KA5 | Q8C050 | GPS |
29 | S | Phosphorylation | Kinase | AURKC | O88445 | GPS |
29 | S | Phosphorylation | Kinase | AURKB | O70126 | GPS |
29 | S | Phosphorylation | Kinase | ALTERNATE | - | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
3 | R | Methylation |
| 15339660 |
4 | T | Phosphorylation |
| 15681610 |
5 | K | Acetylation |
| 11747826 |
5 | K | Methylation |
| 11747826 |
5 | K | ubiquitylation |
| 11747826 |
5 | K | Methylation |
| 11747826 |
5 | K | Methylation |
| 11747826 |
5 | K | Methylation |
| 11747826 |
5 | K | Methylation |
| 11747826 |
5 | K | Methylation |
| 11747826 |
5 | K | Phosphorylation |
| 11747826 |
7 | T | Phosphorylation |
| 13678296 |
7 | T | Methylation |
| 13678296 |
9 | R | Methylation |
| 15339660 |
9 | R | Methylation |
| 15339660 |
9 | R | Methylation |
| 15339660 |
9 | R | Citrullination |
| 15339660 |
9 | R | Acetylation |
| 15339660 |
10 | K | Phosphorylation |
| 13678296 |
10 | K | Phosphorylation |
| 13678296 |
10 | K | Phosphorylation |
| 13678296 |
10 | K | Phosphorylation |
| 13678296 |
10 | K | Methylation |
| 13678296 |
10 | K | Methylation |
| 13678296 |
10 | K | Methylation |
| 13678296 |
10 | K | Methylation |
| 13678296 |
10 | K | Acetylation |
| 13678296 |
10 | K | Acetylation |
| 13678296 |
10 | K | Acetylation |
| 13678296 |
10 | K | Acetylation |
| 13678296 |
10 | K | Acetylation |
| 13678296 |
10 | K | Phosphorylation |
| 13678296 |
10 | K | Methylation |
| 13678296 |
10 | K | Methylation |
| 13678296 |
11 | S | Methylation |
| 10464286 |
11 | S | Methylation |
| 10464286 |
11 | S | Acetylation |
| 10464286 |
11 | S | Acetylation |
| 10464286 |
11 | S | Acetylation |
| 10464286 |
11 | S | Phosphorylation |
| 10464286 |
11 | S | Phosphorylation |
| 10464286 |
11 | S | Phosphorylation |
| 10464286 |
11 | S | Phosphorylation |
| 10464286 |
11 | S | Phosphorylation |
| 10464286 |
11 | S | Phosphorylation |
| 10464286 |
11 | S | Phosphorylation |
| 10464286 |
12 | T | Phosphorylation |
| 18243098 |
12 | T | Acetylation |
| 18243098 |
12 | T | Methylation |
| 18243098 |
12 | T | Phosphorylation |
| 18243098 |
12 | T | Phosphorylation |
| 18243098 |
18 | R | Citrullination |
| 11747826 |
18 | R | Acetylation |
| 11747826 |
18 | R | Methylation |
| 11747826 |
18 | R | Methylation |
| 11747826 |
18 | R | Methylation |
| 11747826 |
19 | K | Methylation |
| 12498683 |
19 | K | Acetylation |
| 12498683 |
24 | K | Methylation |
| 12498683 |
24 | K | Acetylation |
| 12498683 |
28 | K | Methylation |
| 13678296 |
28 | K | Methylation |
| 13678296 |
29 | S | Phosphorylation |
| 10464286 |
37 | K | Methylation |
| 13678296 |
57 | K | Methylation |
| 21925322 |
80 | K | ubiquitylation |
| 13678296 |
80 | K | Methylation |
| 13678296 |
80 | K | Methylation |
| 13678296 |
80 | K | Methylation |
| 13678296 |
80 | K | Succinylation |
| 13678296 |
120 | K | ubiquitylation |
| 13678296 |
120 | K | Methylation |
| 13678296 |
123 | K | Succinylation |
| 13678296 |
123 | K | Acetylation |
| 13678296 |
* 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 H31_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of H31_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Identification of histone H3 lysine 36 acetylation as a highlyconserved histone modification."; Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L.,Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.; J. Biol. Chem. 282:7632-7640(2007). Cited for: ACETYLATION AT LYS-37. | |
"Organismal differences in post-translational modifications inhistones H3 and H4."; Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J.,Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.; J. Biol. Chem. 282:7641-7655(2007). Cited for: ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28,METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37 ANDLYS-80, AND MASS SPECTROMETRY. | |
"Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 andnegatively regulates expression of ST7 and NM23 tumor suppressorgenes."; Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.; Mol. Cell. Biol. 24:9630-9645(2004). Cited for: METHYLATION AT ARG-9, AND ACETYLATION AT LYS-10. | |
"Identification of methylation and acetylation sites on mouse histoneH3 using matrix-assisted laser desorption/ionization time-of-flightand nanoelectrospray ionization tandem mass spectrometry."; Cocklin R.R., Wang M.; J. Protein Chem. 22:327-334(2003). Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-10;LYS-28; LYS-37; LYS-80 AND LYS-123, AND MASS SPECTROMETRY. | |
"Crosstalk between CARM1 methylation and CBP acetylation on histoneH3."; Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T.; Curr. Biol. 12:2090-2097(2002). Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, AND METHYLATION AT ARG-18. | |
Methylation | |
Reference | PubMed |
"Arginine methyltransferase CARM1 is a promoter-specific regulator ofNF-kappaB-dependent gene expression."; Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C.,Imhof R., Bedford M.T., Natoli G., Hottiger M.O.; EMBO J. 24:85-96(2005). Cited for: METHYLATION AT ARG-18. | |
"Methylation at arginine 17 of histone H3 is linked to geneactivation."; Bauer U.-M., Daujat S., Nielsen S.J., Nightingale K., Kouzarides T.; EMBO Rep. 3:39-44(2002). Cited for: METHYLATION AT ARG-18. | |
"Crosstalk between CARM1 methylation and CBP acetylation on histoneH3."; Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T.; Curr. Biol. 12:2090-2097(2002). Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, AND METHYLATION AT ARG-18. | |
"Hormone-dependent, CARM1-directed, arginine-specific methylation ofhistone H3 on a steroid-regulated promoter."; Ma H., Baumann C.T., Li H., Strahl B.D., Rice R., Jelinek M.A.,Aswad D.W., Allis C.D., Hager G.L., Stallcup M.R.; Curr. Biol. 11:1981-1985(2001). Cited for: METHYLATION AT LYS-5 AND ARG-18. | |
"Organismal differences in post-translational modifications inhistones H3 and H4."; Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J.,Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.; J. Biol. Chem. 282:7641-7655(2007). Cited for: ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28,METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37 ANDLYS-80, AND MASS SPECTROMETRY. | |
"Identification of methylation and acetylation sites on mouse histoneH3 using matrix-assisted laser desorption/ionization time-of-flightand nanoelectrospray ionization tandem mass spectrometry."; Cocklin R.R., Wang M.; J. Protein Chem. 22:327-334(2003). Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-10;LYS-28; LYS-37; LYS-80 AND LYS-123, AND MASS SPECTROMETRY. | |
"Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 andnegatively regulates expression of ST7 and NM23 tumor suppressorgenes."; Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.; Mol. Cell. Biol. 24:9630-9645(2004). Cited for: METHYLATION AT ARG-9, AND ACETYLATION AT LYS-10. | |
Phosphorylation | |
Reference | PubMed |
"Stimulation of the Ras-MAPK pathway leads to independentphosphorylation of histone H3 on serine 10 and 28."; Dunn K.L., Davie J.R.; Oncogene 24:3492-3502(2005). Cited for: PHOSPHORYLATION AT SER-11 AND SER-29. | |
"MAP kinase-mediated phosphorylation of distinct pools of histone H3at S10 or S28 via mitogen- and stress-activated kinase 1/2."; Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J.,Nightingale K., Iborra F.J., Mahadevan L.C.; J. Cell Sci. 118:2247-2259(2005). Cited for: PHOSPHORYLATION AT SER-11 AND SER-29. | |
"Phosphorylation of Ser28 in histone H3 mediated by mixed lineagekinase-like mitogen-activated protein triple kinase alpha."; Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.; J. Biol. Chem. 280:13545-13553(2005). Cited for: PHOSPHORYLATION AT SER-29. | |
"The kinase haspin is required for mitotic histone H3 Thr 3phosphorylation and normal metaphase chromosome alignment."; Dai J., Sultan S., Taylor S.S., Higgins J.M.G.; Genes Dev. 19:472-488(2005). Cited for: PHOSPHORYLATION AT THR-4 AND SER-11. | |
"Aurora-B phosphorylates Histone H3 at serine28 with regard to themitotic chromosome condensation."; Goto H., Yasui Y., Nigg E.A., Inagaki M.; Genes Cells 7:11-17(2002). Cited for: PHOSPHORYLATION AT SER-11 AND SER-29. | |
"Ultraviolet B-induced phosphorylation of histone H3 at serine 28 ismediated by MSK1."; Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M.,Ma W.-Y., Dong Z.; J. Biol. Chem. 276:33213-33219(2001). Cited for: PHOSPHORYLATION AT SER-29. | |
"Identification of a novel phosphorylation site on histone H3 coupledwith mitotic chromosome condensation."; Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M.,Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.; J. Biol. Chem. 274:25543-25549(1999). Cited for: PHOSPHORYLATION AT SER-11 AND SER-29. |