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Protein Page:
HIST2H2AB (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
HIST2H2AB 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. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Belongs to the histone H2A family. Note: This description may include information from UniProtKB.
Protein type: DNA binding protein
Cellular Component: nucleosome; nucleus
Molecular Function: DNA binding; protein heterodimerization activity
Biological Process: nucleosome assembly
Reference #:  Q8IUE6 (UniProtKB)
Alt. Names/Synonyms: H2A2B; HIST2H2AB; histone 2, H2ab; histone cluster 2, H2ab; Histone H2A type 2-B
Gene Symbols: HIST2H2AB
Molecular weight: 13,995 Da
Basal Isoelectric point: 10.88  Predict pI for various phosphorylation states
Select Structure to View Below

HIST2H2AB

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 94 K6-ac __MSGRGkQGGkARA
0 93 K10-ac GRGkQGGkARAkAKS
0 1 K14-ac QGGkARAkAKSRSSR
0 14 K37-ub RVHRLLRkGNYAERV
0 3 R89-m1 RHLQLAVrNDEELNk
0 20 K96-ub rNDEELNkLLGGVtI
0 4 T102-p NkLLGGVtIAQGGVL
0 16 K119-ac IQAVLLPkktESHkP
0 147 K119-ub IQAVLLPkktESHkP
0 138 K120-ub QAVLLPkktESHkPG
0 1 K120-m2 QAVLLPkktESHkPG
0 12 K120-ac QAVLLPkktESHkPG
0 2 T121-p AVLLPkktESHkPGk
0 103 K125-ub PkktESHkPGkNk__
0 1 K128-m2 tESHkPGkNk_____
0 34 K128-ub tESHkPGkNk_____
0 2 K130-ub SHkPGkNk_______
  mouse

 
K6-ac __MSGRGkQGGkARA
K10-ac GRGkQGGkARAKAKS
K14 QGGkARAKAKSRSSR
K37-ub RVHRLLRkGNYAERV
R89 RHLQLAVRNDEELNk
K96-ub RNDEELNkLLGGVtI
T102-p NkLLGGVtIAQGGVL
K119-ac IQAVLLPkkTESHkP
K119-ub IQAVLLPkkTESHkP
K120-ub QAVLLPkkTESHkPG
K120 QAVLLPkKTESHkPG
K120-ac QAVLLPkkTESHkPG
T121 AVLLPkkTESHkPGK
K125-ub PkkTESHkPGKNK__
K128 TESHkPGKNK_____
K128 TESHkPGKNK_____
K130 SHkPGKNK_______
  rat

 
K6-ac __MSGRGkQGGkARA
K10-ac GRGkQGGkARAKAKS
K14 QGGkARAKAKSRSSR
K37 RVHRLLRKGNYAERV
R89-m1 RHLQLAVrNDEELNK
K96 rNDEELNKLLGGVtI
T102-p NKLLGGVtIAQGGVL
K119 IQAVLLPKKTDSHKP
K119 IQAVLLPKKTDSHKP
K120 QAVLLPKKTDSHKPG
K120 QAVLLPKKTDSHKPG
K120 QAVLLPKKTDSHKPG
T121 AVLLPKKTDSHKPGK
K125 PKKTDSHKPGKNK__
K128 TDSHKPGKNK_____
K128 TDSHKPGKNK_____
K130 SHKPGKNK_______
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