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Protein Page:
H2A.1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
H2A.1 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
Reference #:  P0C0S8 (UniProtKB)
Alt. Names/Synonyms: FLJ92027; H2A histone family, member C; H2A.1; H2A/c; H2A1; H2AFC; H2AFD; H2AFI; H2AFN; H2AFP; HIST1H2AG; HIST1H2AI; HIST1H2AK; HIST1H2AL; HIST1H2AM; histone 1, H2ai; histone cluster 1, H2ai; Histone H2A type 1; Histone H2A/p
Gene Symbols: HIST1H2AI
Molecular weight: 14,091 Da
Basal Isoelectric point: 10.9  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

H2A.1

Protein Structure Not Found.


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Sites Implicated In
transcription, inhibited: S2‑p
activity, inhibited: S2‑p

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

 
2 2 S2-p ______MsGRGkQGG
8 133 K6-a __MsGRGkQGGkARA
2 133 K10-a GRGkQGGkARAkAKT
1 1 K14-a QGGkARAkAKTRSSR
1 0 R30-m2 GLQFPVGrVHRLLRk
0 14 K37-u rVHRLLRkGNYAERV
1 0 R89 RHLQLAIRNDEELNk
0 7 K96-a RNDEELNkLLGkVtI
0 121 K96-u RNDEELNkLLGkVtI
0 2 K100-a ELNkLLGkVtIAQGG
0 71 K100-u ELNkLLGkVtIAQGG
0 7 T102-p NkLLGkVtIAQGGVL
0 39 K119-a IQAVLLPkktESHHk
0 1 K119 IQAVLLPKktESHHk
0 1 K119 IQAVLLPKktESHHk
5 164 K119-u IQAVLLPkktESHHk
1 16 K120-a QAVLLPkktESHHkA
8 150 K120-u QAVLLPkktESHHkA
6 3 T121-p AVLLPkktESHHkAk
0 133 K126-u kktESHHkAkGk___
0 3 K128-u tESHHkAkGk_____
0 2 K130-u SHHkAkGk_______
2576 : Acetyl-Histone H2A (Lys5) Antibody
  mouse

 
S2-p ______MsGRGkQGG
K6-a __MsGRGkQGGkARA
K10-a GRGkQGGkARAkAKT
K14-a QGGkARAkAKTRSSR
R30 GLQFPVGRVHRLLRk
K37-u RVHRLLRkGNYSERV
R89-m1 RHLQLAIrNDEELNk
K96-a rNDEELNkLLGRVtI
K96-u rNDEELNkLLGRVtI
R100 ELNkLLGRVtIAQGG
R100 ELNkLLGRVtIAQGG
T102-p NkLLGRVtIAQGGVL
K119-a IQAVLLPkktESHHk
K119-m1 IQAVLLPkktESHHk
K119-m2 IQAVLLPkktESHHk
K119-u IQAVLLPkktESHHk
K120-a QAVLLPkktESHHkA
K120-u QAVLLPkktESHHkA
T121-p AVLLPkktESHHkAK
K126-u kktESHHkAKGK___
K128 tESHHkAKGK_____
K130 SHHkAKGK_______
2576 : Acetyl-Histone H2A (Lys5) Antibody
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