H2B1_RAT - dbPTM
H2B1_RAT - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MPEPAKSRP
------CCCCCCCCC
57.17-
6Acetylation--MPEPAKSRPAPKK
--CCCCCCCCCCCCC
58.6816283522
6N6-crotonyl-L-lysine--MPEPAKSRPAPKK
--CCCCCCCCCCCCC
58.68-
6Butyrylation--MPEPAKSRPAPKK
--CCCCCCCCCCCCC
58.68-
6Lactoylation--MPEPAKSRPAPKK
--CCCCCCCCCCCCC
58.68-
6Other--MPEPAKSRPAPKK
--CCCCCCCCCCCCC
58.68-
6Crotonylation--MPEPAKSRPAPKK
--CCCCCCCCCCCCC
58.68-
12CrotonylationAKSRPAPKKGSKKAV
CCCCCCCCCCCHHHH
72.39-
12OtherAKSRPAPKKGSKKAV
CCCCCCCCCCCHHHH
72.39-
12LactoylationAKSRPAPKKGSKKAV
CCCCCCCCCCCHHHH
72.39-
12N6-crotonyl-L-lysineAKSRPAPKKGSKKAV
CCCCCCCCCCCHHHH
72.39-
12AcetylationAKSRPAPKKGSKKAV
CCCCCCCCCCCHHHH
72.3925786129
13OtherKSRPAPKKGSKKAVT
CCCCCCCCCCHHHHH
68.32-
13CrotonylationKSRPAPKKGSKKAVT
CCCCCCCCCCHHHHH
68.32-
13N6-crotonyl-L-lysineKSRPAPKKGSKKAVT
CCCCCCCCCCHHHHH
68.32-
13AcetylationKSRPAPKKGSKKAVT
CCCCCCCCCCHHHHH
68.3216283522
15PhosphorylationRPAPKKGSKKAVTKA
CCCCCCCCHHHHHHH
39.60-
16N6-crotonyl-L-lysinePAPKKGSKKAVTKAQ
CCCCCCCHHHHHHHH
54.11-
16AcetylationPAPKKGSKKAVTKAQ
CCCCCCCHHHHHHHH
54.1116283522
16CrotonylationPAPKKGSKKAVTKAQ
CCCCCCCHHHHHHHH
54.11-
16LactoylationPAPKKGSKKAVTKAQ
CCCCCCCHHHHHHHH
54.11-
17GlutarylationAPKKGSKKAVTKAQK
CCCCCCHHHHHHHHH
50.19-
17CrotonylationAPKKGSKKAVTKAQK
CCCCCCHHHHHHHHH
50.19-
17AcetylationAPKKGSKKAVTKAQK
CCCCCCHHHHHHHHH
50.1925786129
17N6-crotonyl-L-lysineAPKKGSKKAVTKAQK
CCCCCCHHHHHHHHH
50.19-
17LactoylationAPKKGSKKAVTKAQK
CCCCCCHHHHHHHHH
50.19-
21LactoylationGSKKAVTKAQKKDGK
CCHHHHHHHHHHCCH
42.07-
21ButyrylationGSKKAVTKAQKKDGK
CCHHHHHHHHHHCCH
42.07-
21OtherGSKKAVTKAQKKDGK
CCHHHHHHHHHHCCH
42.07-
21AcetylationGSKKAVTKAQKKDGK
CCHHHHHHHHHHCCH
42.0716283522
21N6-crotonyl-L-lysineGSKKAVTKAQKKDGK
CCHHHHHHHHHHCCH
42.07-
21CrotonylationGSKKAVTKAQKKDGK
CCHHHHHHHHHHCCH
42.07-
24AcetylationKAVTKAQKKDGKERK
HHHHHHHHHCCHHHH
58.6625786129
24LactoylationKAVTKAQKKDGKERK
HHHHHHHHHCCHHHH
58.66-
24N6-crotonyl-L-lysineKAVTKAQKKDGKERK
HHHHHHHHHCCHHHH
58.66-
24CrotonylationKAVTKAQKKDGKERK
HHHHHHHHHCCHHHH
58.66-
24OtherKAVTKAQKKDGKERK
HHHHHHHHHCCHHHH
58.66-
25OtherAVTKAQKKDGKERKR
HHHHHHHHCCHHHHH
60.68-
25AcetylationAVTKAQKKDGKERKR
HHHHHHHHCCHHHHH
60.6826302492
33PhosphorylationDGKERKRSRKESYSV
CCHHHHHHHHHHHHH
51.2223984901
35AcetylationKERKRSRKESYSVYV
HHHHHHHHHHHHHHH
52.8672631205
35N6-crotonyl-L-lysineKERKRSRKESYSVYV
HHHHHHHHHHHHHHH
52.86-
35GlutarylationKERKRSRKESYSVYV
HHHHHHHHHHHHHHH
52.86-
35CrotonylationKERKRSRKESYSVYV
HHHHHHHHHHHHHHH
52.86-
35SuccinylationKERKRSRKESYSVYV
HHHHHHHHHHHHHHH
52.8626843850
35OtherKERKRSRKESYSVYV
HHHHHHHHHHHHHHH
52.86-
37PhosphorylationRKRSRKESYSVYVYK
HHHHHHHHHHHHHHH
26.2427097102
38PhosphorylationKRSRKESYSVYVYKV
HHHHHHHHHHHHHHH
11.8427097102
39PhosphorylationRSRKESYSVYVYKVL
HHHHHHHHHHHHHHH
19.0927097102
41PhosphorylationRKESYSVYVYKVLKQ
HHHHHHHHHHHHHHH
7.6627097102
43PhosphorylationESYSVYVYKVLKQVH
HHHHHHHHHHHHHHC
4.25-
44GlutarylationSYSVYVYKVLKQVHP
HHHHHHHHHHHHHCC
30.92-
44OtherSYSVYVYKVLKQVHP
HHHHHHHHHHHHHCC
30.92-
44LactoylationSYSVYVYKVLKQVHP
HHHHHHHHHHHHHCC
30.92-
44AcetylationSYSVYVYKVLKQVHP
HHHHHHHHHHHHHCC
30.9225786129
47OtherVYVYKVLKQVHPDTG
HHHHHHHHHHCCCCC
53.94-
47GlutarylationVYVYKVLKQVHPDTG
HHHHHHHHHHCCCCC
53.94-
47AcetylationVYVYKVLKQVHPDTG
HHHHHHHHHHCCCCC
53.9425786129
47MethylationVYVYKVLKQVHPDTG
HHHHHHHHHHCCCCC
53.94-
47UbiquitinationVYVYKVLKQVHPDTG
HHHHHHHHHHCCCCC
53.94-
53PhosphorylationLKQVHPDTGISSKAM
HHHHCCCCCCCHHHH
40.6522673903
56PhosphorylationVHPDTGISSKAMGIM
HCCCCCCCHHHHHHH
27.4227097102
57PhosphorylationHPDTGISSKAMGIMN
CCCCCCCHHHHHHHH
23.6327097102
58"N6,N6-dimethyllysine"PDTGISSKAMGIMNS
CCCCCCHHHHHHHHH
35.29-
58MethylationPDTGISSKAMGIMNS
CCCCCCHHHHHHHHH
35.29-
58OtherPDTGISSKAMGIMNS
CCCCCCHHHHHHHHH
35.29-
65PhosphorylationKAMGIMNSFVNDIFE
HHHHHHHHHHHHHHH
17.1222108457
79MethylationERIAGERRLAHYNKR
HHHHCHHHHHHCCCC
31.74-
85OtherRRLAHYNKRSTITSR
HHHHHCCCCCCCCHH
40.33-
85LactoylationRRLAHYNKRSTITSR
HHHHHCCCCCCCCHH
40.33-
85MethylationRRLAHYNKRSTITSR
HHHHHCCCCCCCCHH
40.33-
85AcetylationRRLAHYNKRSTITSR
HHHHHCCCCCCCCHH
40.3325786129
85"N6,N6,N6-trimethyllysine"RRLAHYNKRSTITSR
HHHHHCCCCCCCCHH
40.33-
86MethylationRLAHYNKRSTITSRE
HHHHCCCCCCCCHHH
35.08-
92MethylationKRSTITSREIQTAVR
CCCCCCHHHHHHHHH
36.07-
108GlutarylationLLPGELAKHAVSEGT
HCCHHHHHHHHHHHH
44.73-
108LactoylationLLPGELAKHAVSEGT
HCCHHHHHHHHHHHH
44.73-
108OtherLLPGELAKHAVSEGT
HCCHHHHHHHHHHHH
44.73-
108UbiquitinationLLPGELAKHAVSEGT
HCCHHHHHHHHHHHH
44.73-
108MethylationLLPGELAKHAVSEGT
HCCHHHHHHHHHHHH
44.73-
108AcetylationLLPGELAKHAVSEGT
HCCHHHHHHHHHHHH
44.7325786129
112PhosphorylationELAKHAVSEGTKAVT
HHHHHHHHHHHHHHH
30.9629779826
112O-linked_GlycosylationELAKHAVSEGTKAVT
HHHHHHHHHHHHHHH
30.96-
115PhosphorylationKHAVSEGTKAVTKYT
HHHHHHHHHHHHHHC
16.2719346237
116OtherHAVSEGTKAVTKYTS
HHHHHHHHHHHHHCC
52.28-
116AcetylationHAVSEGTKAVTKYTS
HHHHHHHHHHHHHCC
52.2822902405
116SuccinylationHAVSEGTKAVTKYTS
HHHHHHHHHHHHHCC
52.28-
116GlutarylationHAVSEGTKAVTKYTS
HHHHHHHHHHHHHCC
52.28-
116LactoylationHAVSEGTKAVTKYTS
HHHHHHHHHHHHHCC
52.28-
116UbiquitinationHAVSEGTKAVTKYTS
HHHHHHHHHHHHHCC
52.28-
116MethylationHAVSEGTKAVTKYTS
HHHHHHHHHHHHHCC
52.28-
119PhosphorylationSEGTKAVTKYTSSK-
HHHHHHHHHHCCCC-
24.1625575281
120OtherEGTKAVTKYTSSK--
HHHHHHHHHCCCC--
39.67-
120GlutarylationEGTKAVTKYTSSK--
HHHHHHHHHCCCC--
39.67-
120LactoylationEGTKAVTKYTSSK--
HHHHHHHHHCCCC--
39.67-
120AcetylationEGTKAVTKYTSSK--
HHHHHHHHHCCCC--
39.6725786129
120SuccinylationEGTKAVTKYTSSK--
HHHHHHHHHCCCC--
39.67-
120UbiquitinationEGTKAVTKYTSSK--
HHHHHHHHHCCCC--
39.67-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
15SPhosphorylationKinaseMST1-Uniprot
37SPhosphorylationKinaseAMPKQ09137
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
4KMethylation

-
4KMethylation

-
4Kubiquitylation

-
4Kubiquitylation

-
15SPhosphorylation

-
15SPhosphorylation

-
35KMethylation

-
35Kubiquitylation

-
37SPhosphorylation

-
79KMethylation

-
79KMethylation

-
79Kubiquitylation

-
79Kubiquitylation

-
112Subiquitylation

-
120Kubiquitylation

-
120Kubiquitylation

-
120KMethylation

-

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of H2B1_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of H2B1_RAT

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Inhibition of core histones acetylation by carcinogenic nickel(II).";
Golebiowski F., Kasprzak K.S.;
Mol. Cell. Biochem. 279:133-139(2005).
Cited for: ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21.

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