H2A2B_MOUSE - dbPTM
H2A2B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H2A2B_MOUSE
UniProt AC Q64522
Protein Name Histone H2A type 2-B
Gene Name Hist2h2ab
Organism Mus musculus (Mouse).
Sequence Length 130
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 MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTESHKPGKNK
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
2Phosphorylation------MSGRGKQGG
------CCCCCCCCH
36.887217105
2Acetylation------MSGRGKQGG
------CCCCCCCCH
36.88-
4Citrullination----MSGRGKQGGKA
----CCCCCCCCHHH
41.66-
4Methylation----MSGRGKQGGKA
----CCCCCCCCHHH
41.6616699504
4Citrullination----MSGRGKQGGKA
----CCCCCCCCHHH
41.66-
6Acetylation--MSGRGKQGGKARA
--CCCCCCCCHHHHH
44.3920612055
6Other--MSGRGKQGGKARA
--CCCCCCCCHHHHH
44.3927105115
10AcetylationGRGKQGGKARAKAKS
CCCCCCHHHHHHHHH
41.3422693562
10MethylationGRGKQGGKARAKAKS
CCCCCCHHHHHHHHH
41.3422693562
10LactoylationGRGKQGGKARAKAKS
CCCCCCHHHHHHHHH
41.34-
10SuccinylationGRGKQGGKARAKAKS
CCCCCCHHHHHHHHH
41.34-
10OtherGRGKQGGKARAKAKS
CCCCCCHHHHHHHHH
41.3424681537
37HydroxylationRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC
52.0224681537
37CrotonylationRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC
52.02-
37OtherRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC
52.0227105115
37N6-crotonyl-L-lysineRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC
52.02-
37UbiquitinationRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC
52.02-
75OtherGNAARDNKKTRIIPR
CHHHHCCCCCCEEHH
60.8724681537
76OtherNAARDNKKTRIIPRH
HHHHCCCCCCEEHHH
49.6524681537
96UbiquitinationRNDEELNKLLGGVTI
CCHHHHHHHHCCEEE
58.68-
96GlutarylationRNDEELNKLLGGVTI
CCHHHHHHHHCCEEE
58.68-
96SuccinylationRNDEELNKLLGGVTI
CCHHHHHHHHCCEEE
58.68-
96OtherRNDEELNKLLGGVTI
CCHHHHHHHHCCEEE
58.6824681537
102PhosphorylationNKLLGGVTIAQGGVL
HHHHCCEEEECCCCC
17.5527180971
105MethylationLGGVTIAQGGVLPNI
HCCEEEECCCCCCCE
45.3724352239
119N6-crotonyl-L-lysineIQAVLLPKKTESHKP
EEEEECCCCCCCCCC
72.76-
119UbiquitinationIQAVLLPKKTESHKP
EEEEECCCCCCCCCC
72.76-
119AcetylationIQAVLLPKKTESHKP
EEEEECCCCCCCCCC
72.7622650733
119CrotonylationIQAVLLPKKTESHKP
EEEEECCCCCCCCCC
72.76-
119OtherIQAVLLPKKTESHKP
EEEEECCCCCCCCCC
72.7624681537
119GlutarylationIQAVLLPKKTESHKP
EEEEECCCCCCCCCC
72.76-
120OtherQAVLLPKKTESHKPG
EEEECCCCCCCCCCC
56.4327105115
120AcetylationQAVLLPKKTESHKPG
EEEECCCCCCCCCCC
56.4330589207
120N6-crotonyl-L-lysineQAVLLPKKTESHKPG
EEEECCCCCCCCCCC
56.43-
120GlutarylationQAVLLPKKTESHKPG
EEEECCCCCCCCCCC
56.43-
120CrotonylationQAVLLPKKTESHKPG
EEEECCCCCCCCCCC
56.4315509584
120UbiquitinationQAVLLPKKTESHKPG
EEEECCCCCCCCCCC
56.4315509584
121PhosphorylationAVLLPKKTESHKPGK
EEECCCCCCCCCCCC
49.1727600695
125UbiquitinationPKKTESHKPGKNK--
CCCCCCCCCCCCC--
65.82-

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
2SPhosphorylationKinaseRPS6KA5Q8C050
Uniprot
121TPhosphorylationKinaseDCAF1Q80TR8
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
2SAcetylation

-
2SPhosphorylation

-
2SPhosphorylation

-
2SPhosphorylation

-
4RMethylation

16699504
14Kubiquitylation

15509584
14Kubiquitylation

15509584
16Kubiquitylation

15509584
16Kubiquitylation

15509584
27KMethylation

15509584
27Kubiquitylation

15509584
63Kubiquitylation

15509584
105QMethylation

24352239
120Kubiquitylation

15525528
121TPhosphorylation

-

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 H2A2B_MOUSE !!

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

Oops, there are no PPI records of H2A2B_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of H2A2B_MOUSE

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Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"Ring1b-mediated H2A ubiquitination associates with inactive Xchromosomes and is involved in initiation of X inactivation.";
Fang J., Chen T., Chadwick B., Li E., Zhang Y.;
J. Biol. Chem. 279:52812-52815(2004).
Cited for: UBIQUITINATION AT LYS-120.
"Polycomb group proteins Ring1A/B link ubiquitylation of histone H2Ato heritable gene silencing and X inactivation.";
de Napoles M., Mermoud J.E., Wakao R., Tang Y.A., Endoh M.,Appanah R., Nesterova T.B., Silva J., Otte A.P., Vidal M., Koseki H.,Brockdorff N.;
Dev. Cell 7:663-676(2004).
Cited for: UBIQUITINATION AT LYS-120.

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