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Reviewed (UniProtKB/Swiss-Prot)

Note: Proteins listed in ProtBank™ database are NOT off-the-shelf [catalog] proteins. Customized protein production request can be made for any protein in this database by clicking on the corresponding button under "Quick Quote". Please ensure sequence accuracy and/or make any necessary modifications prior to submitting your quote request

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Reviewed (UniProtKB/Swiss-Prot)


Name Gene Symbol Rec Full Name Protein Information Quick Quote  Price,
Turnaround
H2A4_RAT, Rattus norvegicus (Norway rat) Histone H2A, testis Functions
wild_type
Starting from $1600,
4 weeks
Protein Domains
mutant
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Protein Names | ProteinIDs  | Organism | Gene Names  | GeneID | Genome Annotation(Ensembl) |  Protein Sequence | 
General annotation |  References | Order
Protein Names
Recommended name:
 Histone H2A type 4;
Alternative name(s):
 Histone H2A, testis
Protein IDs
(Accession numbers)
UniProtKB
 Q00728
NCBI RefSeq

NP_068611.1, NM_021839.1.
Organism
Latin Name/
(Common Name)
Rattus norvegicus (Rat).
Taxonomic Identifier (NCBI)
 10116
Gene Names
 [GenPool]
GeneID

24828
Genome
Annotation (Ensembl)

ENSRNOT00000050526, ENSRNOP00000039289; ENSRNOG00000033377
Protein Sequence
 
SEQUENCE   130 AA;  14284 MW;  084CC395F7E72D05 CRC64;
MSGRAKQGGK ARAKAKSRSF RAGLQFPVGR VHRLLRQGNY AERIGAGTPV YLAAVLEYLT
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGR VTIAQGGVLP NIQAVLLPKK
TESHHKSQTK
General annotation
Function
 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.
Cofactor
Subunit structure
 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.
Subcellular location

Nucleus. Chromosome.
Tissue specificity
 Testis.
Induction
Domain
 The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.
Post-translational modification

The chromatin-associated form is phosphorylated on Thr-121during mitosis (By similarity).

Monoubiquitination of Lys-120 by RING1 and RNF2/RING2 complexgives a specific tag for epigenetic transcriptional repression.Following DNA double-strand breaks (DSBs), it is ubiquitinatedthrough 'Lys-63' linkage of ubiquitin moieties by the E2 ligaseUBE2N and the E3 ligases RNF8 and RNF168, leading to therecruitment of repair proteins to sites of DNA damage.Monoubiquitination and ionizing radiation-induced 'Lys-63'-linkedubiquitination are distinct events (By similarity).

Phosphorylation on Ser-2 is enhanced during mitosis.Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly repressestranscription. Acetylation of H3 inhibits Ser-2 phosphorylation byRPS6KA5/MSK1 (By similarity).
Involvement in disease

References

  • "Presence of a bi-directional S phase-specific transcriptionregulatory element in the promoter shared by testis-specific TH2A andTH2B histone genes.";,Huh N.E., Hwang I., Lim K., You K.H., Chae C.-B.;,Nucleic Acids Res. 19:93-98(1991)., PubMeb:2011515 DOI:10.1093/nar/19.1.93

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Protein Domain Databases | 3D Structure Database  | Sequence Annotation | Protein-protein Interaction Databases  | 
Binary Interactions | Enzyme and Pathway Databases |  Phylogenomic Database | Proteomics Database | 
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Protein Domain Databases
InterPro

IPR009072, Histone-fold.

IPR007125, Histone_core_D.

IPR002119, Histone_H2A.
Gene3D

G3DSA:1.10.20.10, Histone-fold; 1.
PANTHER
Pfam

PF00125, Histone; 1.
PRINTS

PR00620, HISTONEH2A.
SUPFAM

SSF47113, Histone-fold; 1.
PROSITE

PS00046, HISTONE_H2A; 1.
3D Structure
Database (PDB)
Entry
Method
Resolution (A)
Chain
Positions
PDBsum
Sequence
Annotation
Feature key
Position(s)
Length
Description
Initiator methionine 1 1 Removed (By similarity).
Polypeptide chain 2 - 130 129 Histone H2A type 4. /FTId=PRO_0000055276.
Sequence motif 127 - 128 2 [ST]-Q motif.
Posttranslational modification of a residue 2 1 N-acetylserine (By similarity).
Posttranslational modification of a residue 2 1 Phosphoserine (By similarity).
Posttranslational modification of a residue 4 1 Citrulline (By similarity).
Posttranslational modification of a residue 6 1 N6-acetyllysine (By similarity).
Posttranslational modification of a residue 121 1 Phosphothreonine (By similarity).
Posttranslationally formed amino acid bonds 120 1 Glycyl lysine isopeptide (Lys-Gly)
Protein-protein
Interaction
Databases
DIP
IntAct
MINT
STRING
Binary Interactions
With
Entry
#Exp.
IntAct
Enzyme and Pathway Databases
Pathway
Interaction DB
Reactome
Phylogenomic Database
HOVERGEN

HBG009342
InParanoid

Q00728
OMA

LAIHNDE
OrthoDB
Proteomics
Database (PRIDE)

Q00728
Comparative
Toxicogenomics
Database (CTD)

221613
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Phone: 1-877-436-7274 (Toll-Free) 1-732-885-9188
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