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H2A.1 (human)

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®

Select Structure to View Below H2A.1

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  DISEASE 602787 602788 602793 602796  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Sites Implicated In
transcription, altered: S2‑p inhibition: 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

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
4	164		K119-u	IQAVLLPkktESHHk
1	16		K120-a	QAVLLPkktESHHkA
8	150		K120-u	QAVLLPkktESHHkA
3	2		T121-p	AVLLPkktESHHkAk
0	133		K126-u	kktESHHkAkGk___
0	3		K128-u	tESHHkAkGk_____
0	2		K130-u	SHHkAkGk_______

	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_______

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