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Protein Page:
H2A.4 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
H2A.4 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
Chromosomal Location of Human Ortholog: 6p22.2
Cellular Component: nuclear chromatin; nuclear chromosome, telomeric region; nucleosome; nucleus
Molecular Function: DNA binding; protein heterodimerization activity
Biological Process: chromatin silencing
Reference #:  Q96QV6 (UniProtKB)
Alt. Names/Synonyms: bA317E16.2; H2A histone family, member R; H2A1A; H2AFR; HIST1H2AA; histone 1, H2aa; histone cluster 1, H2aa; Histone H2A type 1-A; Histone H2A/r
Gene Symbols: HIST1H2AA
Molecular weight: 14,102 Da
Basal Isoelectric point: 10.86  Predict pI for various phosphorylation states
Select Structure to View Below

H2A.4

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


 LTP 

LTP: 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.


 HTP 

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


       human

 
0 82 K5‑ac ___SGRGkQGGkARA
0 81 K9‑ac GRGkQGGkARAKSKS
0 13 K36‑ub RIHRLLRkGNYAERI
0 4 K95 RNDEELNKLLGGVtI
0 31 K95‑ub RNDEELNkLLGGVtI
0 8 T101‑p NkLLGGVtIAQGGVL
0 16 K118‑ac IQAVLLPkkTESHHH
0 149 K118‑ub IQAVLLPkkTESHHH
0 13 K119‑ac QAVLLPkkTESHHHk
0 130 K119‑ub QAVLLPkkTESHHHk
0 1 T120 AVLLPkkTESHHHkA
0 1 S122 LLPkkTESHHHkAQS
0 1 K126‑ac kTESHHHkAQSK___
0 9 K126 kTESHHHKAQSK___
8240 : Ubiquityl-Histone H2A (Lys119) (D27C4) XP(R) Rabbit mAb
  mouse

 
K5 ___SGPTKRGGKARA
K9 GPTKRGGKARAKVKS
Q36 RVHRLLRQGNYAQRI
K95‑ac RNDEELNkLLGRVtI
K95‑ub RNDEELNkLLGRVtI
T101‑p NkLLGRVtIAQGGVL
K118‑ac IQAVLLPkkTESHkS
K118‑ub IQAVLLPkkTESHkS
K119‑ac QAVLLPkkTESHkSQ
K119‑ub QAVLLPkkTESHkSQ
T120 AVLLPkkTESHkSQT
S122 LLPkkTESHkSQTK_
K124 PkkTESHKSQTK___
K124‑ub PkkTESHkSQTK___
8240 : Ubiquityl-Histone H2A (Lys119) (D27C4) XP(R) Rabbit mAb
  rat

 
K5 ___SGRAKQGGKARA
K9 GRAKQGGKARAKAKS
Q36 RVHRLLRQGNYAERI
K95‑ac RNDEELNkLLGRVtI
K95 RNDEELNKLLGRVtI
T101‑p NkLLGRVtIAQGGVL
K118 IQAVLLPKKtEsHHK
K118‑ub IQAVLLPkKtEsHHK
K119 QAVLLPkKtEsHHKS
K119 QAVLLPkKtEsHHKS
T120‑p AVLLPkKtEsHHKSQ
S122‑p LLPkKtEsHHKSQTK
K125 kKtEsHHKSQTK___
K125 kKtEsHHKSQTK___
8240 : Ubiquityl-Histone H2A (Lys119) (D27C4) XP(R) Rabbit mAb
  chicken

 
K5‑ac ___SGRGkQGGKARA
K9 GRGkQGGKARAKAKS
K36 RVHRLLRKGNYAERV
K95 RNDEELNKLLGKVTI
K95 RNDEELNKLLGKVTI
T101 NKLLGKVTIAQGGVL
K118 IQAVLLPKKTDSHKA
K118 IQAVLLPKKTDSHKA
K119 QAVLLPKKTDSHKAK
K119 QAVLLPKKTDSHKAK
T120 AVLLPKKTDSHKAKA
S122 LLPKKTDSHKAKAK_
K124 PKKTDSHKAKAK___
K124 PKKTDSHKAKAK___
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