UniProt ID | H2B1_RAT | |
---|---|---|
UniProt AC | Q00715 | |
Protein Name | Histone H2B type 1 | |
Gene Name | ||
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 125 | |
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.; Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid (By similarity).. | |
Protein Sequence | MPEPAKSRPAPKKGSKKAVTKAQKKDGKERKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGERRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MPEPAKSRP ------CCCCCCCCC | 57.17 | - | |
6 | Acetylation | --MPEPAKSRPAPKK --CCCCCCCCCCCCC | 58.68 | 16283522 | |
6 | N6-crotonyl-L-lysine | --MPEPAKSRPAPKK --CCCCCCCCCCCCC | 58.68 | - | |
6 | Butyrylation | --MPEPAKSRPAPKK --CCCCCCCCCCCCC | 58.68 | - | |
6 | Lactoylation | --MPEPAKSRPAPKK --CCCCCCCCCCCCC | 58.68 | - | |
6 | Other | --MPEPAKSRPAPKK --CCCCCCCCCCCCC | 58.68 | - | |
6 | Crotonylation | --MPEPAKSRPAPKK --CCCCCCCCCCCCC | 58.68 | - | |
12 | Crotonylation | AKSRPAPKKGSKKAV CCCCCCCCCCCHHHH | 72.39 | - | |
12 | Other | AKSRPAPKKGSKKAV CCCCCCCCCCCHHHH | 72.39 | - | |
12 | Lactoylation | AKSRPAPKKGSKKAV CCCCCCCCCCCHHHH | 72.39 | - | |
12 | N6-crotonyl-L-lysine | AKSRPAPKKGSKKAV CCCCCCCCCCCHHHH | 72.39 | - | |
12 | Acetylation | AKSRPAPKKGSKKAV CCCCCCCCCCCHHHH | 72.39 | 25786129 | |
13 | Other | KSRPAPKKGSKKAVT CCCCCCCCCCHHHHH | 68.32 | - | |
13 | Crotonylation | KSRPAPKKGSKKAVT CCCCCCCCCCHHHHH | 68.32 | - | |
13 | N6-crotonyl-L-lysine | KSRPAPKKGSKKAVT CCCCCCCCCCHHHHH | 68.32 | - | |
13 | Acetylation | KSRPAPKKGSKKAVT CCCCCCCCCCHHHHH | 68.32 | 16283522 | |
15 | Phosphorylation | RPAPKKGSKKAVTKA CCCCCCCCHHHHHHH | 39.60 | - | |
16 | N6-crotonyl-L-lysine | PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH | 54.11 | - | |
16 | Acetylation | PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH | 54.11 | 16283522 | |
16 | Crotonylation | PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH | 54.11 | - | |
16 | Lactoylation | PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH | 54.11 | - | |
17 | Glutarylation | APKKGSKKAVTKAQK CCCCCCHHHHHHHHH | 50.19 | - | |
17 | Crotonylation | APKKGSKKAVTKAQK CCCCCCHHHHHHHHH | 50.19 | - | |
17 | Acetylation | APKKGSKKAVTKAQK CCCCCCHHHHHHHHH | 50.19 | 25786129 | |
17 | N6-crotonyl-L-lysine | APKKGSKKAVTKAQK CCCCCCHHHHHHHHH | 50.19 | - | |
17 | Lactoylation | APKKGSKKAVTKAQK CCCCCCHHHHHHHHH | 50.19 | - | |
21 | Lactoylation | GSKKAVTKAQKKDGK CCHHHHHHHHHHCCH | 42.07 | - | |
21 | Butyrylation | GSKKAVTKAQKKDGK CCHHHHHHHHHHCCH | 42.07 | - | |
21 | Other | GSKKAVTKAQKKDGK CCHHHHHHHHHHCCH | 42.07 | - | |
21 | Acetylation | GSKKAVTKAQKKDGK CCHHHHHHHHHHCCH | 42.07 | 16283522 | |
21 | N6-crotonyl-L-lysine | GSKKAVTKAQKKDGK CCHHHHHHHHHHCCH | 42.07 | - | |
21 | Crotonylation | GSKKAVTKAQKKDGK CCHHHHHHHHHHCCH | 42.07 | - | |
24 | Acetylation | KAVTKAQKKDGKERK HHHHHHHHHCCHHHH | 58.66 | 25786129 | |
24 | Lactoylation | KAVTKAQKKDGKERK HHHHHHHHHCCHHHH | 58.66 | - | |
24 | N6-crotonyl-L-lysine | KAVTKAQKKDGKERK HHHHHHHHHCCHHHH | 58.66 | - | |
24 | Crotonylation | KAVTKAQKKDGKERK HHHHHHHHHCCHHHH | 58.66 | - | |
24 | Other | KAVTKAQKKDGKERK HHHHHHHHHCCHHHH | 58.66 | - | |
25 | Other | AVTKAQKKDGKERKR HHHHHHHHCCHHHHH | 60.68 | - | |
25 | Acetylation | AVTKAQKKDGKERKR HHHHHHHHCCHHHHH | 60.68 | 26302492 | |
33 | Phosphorylation | DGKERKRSRKESYSV CCHHHHHHHHHHHHH | 51.22 | 23984901 | |
35 | Acetylation | KERKRSRKESYSVYV HHHHHHHHHHHHHHH | 52.86 | 72631205 | |
35 | N6-crotonyl-L-lysine | KERKRSRKESYSVYV HHHHHHHHHHHHHHH | 52.86 | - | |
35 | Glutarylation | KERKRSRKESYSVYV HHHHHHHHHHHHHHH | 52.86 | - | |
35 | Crotonylation | KERKRSRKESYSVYV HHHHHHHHHHHHHHH | 52.86 | - | |
35 | Succinylation | KERKRSRKESYSVYV HHHHHHHHHHHHHHH | 52.86 | 26843850 | |
35 | Other | KERKRSRKESYSVYV HHHHHHHHHHHHHHH | 52.86 | - | |
37 | Phosphorylation | RKRSRKESYSVYVYK HHHHHHHHHHHHHHH | 26.24 | 27097102 | |
38 | Phosphorylation | KRSRKESYSVYVYKV HHHHHHHHHHHHHHH | 11.84 | 27097102 | |
39 | Phosphorylation | RSRKESYSVYVYKVL HHHHHHHHHHHHHHH | 19.09 | 27097102 | |
41 | Phosphorylation | RKESYSVYVYKVLKQ HHHHHHHHHHHHHHH | 7.66 | 27097102 | |
43 | Phosphorylation | ESYSVYVYKVLKQVH HHHHHHHHHHHHHHC | 4.25 | - | |
44 | Glutarylation | SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC | 30.92 | - | |
44 | Other | SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC | 30.92 | - | |
44 | Lactoylation | SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC | 30.92 | - | |
44 | Acetylation | SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC | 30.92 | 25786129 | |
47 | Other | VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC | 53.94 | - | |
47 | Glutarylation | VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC | 53.94 | - | |
47 | Acetylation | VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC | 53.94 | 25786129 | |
47 | Methylation | VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC | 53.94 | - | |
47 | Ubiquitination | VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC | 53.94 | - | |
53 | Phosphorylation | LKQVHPDTGISSKAM HHHHCCCCCCCHHHH | 40.65 | 22673903 | |
56 | Phosphorylation | VHPDTGISSKAMGIM HCCCCCCCHHHHHHH | 27.42 | 27097102 | |
57 | Phosphorylation | HPDTGISSKAMGIMN CCCCCCCHHHHHHHH | 23.63 | 27097102 | |
58 | "N6,N6-dimethyllysine" | PDTGISSKAMGIMNS CCCCCCHHHHHHHHH | 35.29 | - | |
58 | Methylation | PDTGISSKAMGIMNS CCCCCCHHHHHHHHH | 35.29 | - | |
58 | Other | PDTGISSKAMGIMNS CCCCCCHHHHHHHHH | 35.29 | - | |
65 | Phosphorylation | KAMGIMNSFVNDIFE HHHHHHHHHHHHHHH | 17.12 | 22108457 | |
79 | Methylation | ERIAGERRLAHYNKR HHHHCHHHHHHCCCC | 31.74 | - | |
85 | Other | RRLAHYNKRSTITSR HHHHHCCCCCCCCHH | 40.33 | - | |
85 | Lactoylation | RRLAHYNKRSTITSR HHHHHCCCCCCCCHH | 40.33 | - | |
85 | Methylation | RRLAHYNKRSTITSR HHHHHCCCCCCCCHH | 40.33 | - | |
85 | Acetylation | RRLAHYNKRSTITSR HHHHHCCCCCCCCHH | 40.33 | 25786129 | |
85 | "N6,N6,N6-trimethyllysine" | RRLAHYNKRSTITSR HHHHHCCCCCCCCHH | 40.33 | - | |
86 | Methylation | RLAHYNKRSTITSRE HHHHCCCCCCCCHHH | 35.08 | - | |
92 | Methylation | KRSTITSREIQTAVR CCCCCCHHHHHHHHH | 36.07 | - | |
108 | Glutarylation | LLPGELAKHAVSEGT HCCHHHHHHHHHHHH | 44.73 | - | |
108 | Lactoylation | LLPGELAKHAVSEGT HCCHHHHHHHHHHHH | 44.73 | - | |
108 | Other | LLPGELAKHAVSEGT HCCHHHHHHHHHHHH | 44.73 | - | |
108 | Ubiquitination | LLPGELAKHAVSEGT HCCHHHHHHHHHHHH | 44.73 | - | |
108 | Methylation | LLPGELAKHAVSEGT HCCHHHHHHHHHHHH | 44.73 | - | |
108 | Acetylation | LLPGELAKHAVSEGT HCCHHHHHHHHHHHH | 44.73 | 25786129 | |
112 | Phosphorylation | ELAKHAVSEGTKAVT HHHHHHHHHHHHHHH | 30.96 | 29779826 | |
112 | O-linked_Glycosylation | ELAKHAVSEGTKAVT HHHHHHHHHHHHHHH | 30.96 | - | |
115 | Phosphorylation | KHAVSEGTKAVTKYT HHHHHHHHHHHHHHC | 16.27 | 19346237 | |
116 | Other | HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC | 52.28 | - | |
116 | Acetylation | HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC | 52.28 | 22902405 | |
116 | Succinylation | HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC | 52.28 | - | |
116 | Glutarylation | HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC | 52.28 | - | |
116 | Lactoylation | HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC | 52.28 | - | |
116 | Ubiquitination | HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC | 52.28 | - | |
116 | Methylation | HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC | 52.28 | - | |
119 | Phosphorylation | SEGTKAVTKYTSSK- HHHHHHHHHHCCCC- | 24.16 | 25575281 | |
120 | Other | EGTKAVTKYTSSK-- HHHHHHHHHCCCC-- | 39.67 | - | |
120 | Glutarylation | EGTKAVTKYTSSK-- HHHHHHHHHCCCC-- | 39.67 | - | |
120 | Lactoylation | EGTKAVTKYTSSK-- HHHHHHHHHCCCC-- | 39.67 | - | |
120 | Acetylation | EGTKAVTKYTSSK-- HHHHHHHHHCCCC-- | 39.67 | 25786129 | |
120 | Succinylation | EGTKAVTKYTSSK-- HHHHHHHHHCCCC-- | 39.67 | - | |
120 | Ubiquitination | EGTKAVTKYTSSK-- HHHHHHHHHCCCC-- | 39.67 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
15 | S | Phosphorylation | Kinase | MST1 | - | Uniprot |
37 | S | Phosphorylation | Kinase | AMPK | Q09137 | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
4 | K | Methylation |
| - |
4 | K | Methylation |
| - |
4 | K | ubiquitylation |
| - |
4 | K | ubiquitylation |
| - |
15 | S | Phosphorylation |
| - |
15 | S | Phosphorylation |
| - |
35 | K | Methylation |
| - |
35 | K | ubiquitylation |
| - |
37 | S | Phosphorylation |
| - |
79 | K | Methylation |
| - |
79 | K | Methylation |
| - |
79 | K | ubiquitylation |
| - |
79 | K | ubiquitylation |
| - |
112 | S | ubiquitylation |
| - |
120 | K | ubiquitylation |
| - |
120 | K | ubiquitylation |
| - |
120 | K | Methylation |
| - |
* 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 H2B1_RAT !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of H2B1_RAT !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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