P84243

PTMD Annotation Information


※ Protein Information

Tag Content
UniProt Accession H33_HUMAN; P84243;
Entrez ID 3020
GenBank Protein ID NM_002107.4; NM_005324.4;
GenBank Nucleotide ID NP_002098.1; NP_005315.1;
Protein Name Histone H3.3
Gene Name H3F3A; H3.3A; H3F3; PP781;; H3F3B; H3.3B
Organism Homo sapiens
NCBI Taxa ID 9606
Functional DescriptionVariant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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.
Sequence
(Fasta)
MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE 60
LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI 120
MPKDIQLARR IRGERA 137

※ PTM-Disease Association

NumPTMDiseaseCell TypeTypePTM SitePMID
1AcetylationBlast crisis chronic myeloid leukemiaA15514006
[Reference]: Present studies show that LBH589, a novel cinnamic hydroxamic acid analog histone deacetylase inhibitor, induces acetylation of histone H3 and H4 and of heat shock protein 90 (hsp90), increases p21 levels, as well as induces cell-cycle G(1) phase accumulation and apoptosis of the human chronic myeloid leukemia blast crisis (CML-BC) K562 cells and acute leukemia MV4-11 cells with the activating length mutation of FLT-3.
2AcetylationMelanomaD16909117
[Reference]: In the six OSM-resistant cell lines that expressed a low level of OSMR mRNA, chromatin immunoprecipitations (ChIPs) demonstrated a low level of acetylated histone H3 and H4 associated with the promoter region of OSMR (Figure 4a, top panel).
3MethylationGiant cell tumor of bonetumor tissueN24788576
[Reference]: In most cases the primary driver of the malignant cell appears to be a mutation in H3F3A leading to a substitution of Gly34 to either Trp or Leu in Histone H3.3. This change presumably alters the methylation of the protein, and thus, its effect on gene expression
4AcetylationBladder cancerU16024609
[Reference]: These data suggested that the degree of histone acetylation associated with DOC-2/DAB2 promoter in 253J may be higher than in the other two cell lines.

※ Disease Cross-ref Annotation

DatabaseAnnotation
Cancer Gene Census
glioma
CTD (Curated)
(count: 3)
MESH:D018212 ; Giant Cell Tumor of Bone
MESH:D005909 ; Glioblastoma
MESH:D005910 ; Glioma
DisGeNet (Curated)
(count: 3)
C0017636; Glioblastoma
C0017638; Glioma
C0206638; Giant Cell Tumor of Bone
GWASdb
(count: 1)
rs6664668; Alcohol and nictotine co-dependence; alcohol dependence|nicotine dependence

※ PTM Sites

PTM Modification Sites
Phosphorylation
(count: 15)
(view all)
100       LQEASEAYLVGLFED     dbPAF
108       LVGLFEDTNLCAIHA     dbPAF
11        TKQTARKSTGGKAPR     dbPAF
12        KQTARKSTGGKAPRK     dbPAF
29        ATKAARKSAPSTGGV     dbPAF
32        AARKSAPSTGGVKKP     dbPAF
Acetylation
(count: 3)
28        LATKAARKSAPSTGG     PLMD
37        APSTGGVKKPHRYRP     PLMD
38        PSTGGVKKPHRYRPG     PLMD
Ubiquitination
(count: 3)
28        LATKAARKSAPSTGG     PLMD
37        APSTGGVKKPHRYRP     PLMD
38        PSTGGVKKPHRYRPG     PLMD
Sumoylation
(count: 2)
24        PRKQLATKAARKSAP     PLMD
80        REIAQDFKTDLRFQS     PLMD
Butyrylation
(count: 1)
28        LATKAARKSAPSTGG     PLMD
Crotonylation
(count: 6)
10        RTKQTARKSTGGKAP     PLMD
19        TGGKAPRKQLATKAA     PLMD
24        PRKQLATKAARKSAP     PLMD
28        LATKAARKSAPSTGG     PLMD
5         ***MARTKQTARKST     PLMD
57        REIRRYQKSTELLIR     PLMD
Methylation
(count: 3)
28        LATKAARKSAPSTGG     PLMD
37        APSTGGVKKPHRYRP     PLMD
38        PSTGGVKKPHRYRPG     PLMD

※ Protein-Protein Interaction

NetworkInteraction
ABSource
A2ABF9P84243HPRD
B4DJV2P84243BioGRID
E7ETL0P84243BioGRID
E9PE28P84243BioGRID
F8VPJ2P84243BioGRID
F8WCM3P84243BioGRID
H0YBT0P84243IntAct
O00257P84243DIP
O14646P84243HPRD
O14949P84243BioGRID
O14965P84243MINT
O60264P84243HPRD
O95150P84243BioGRID
O95503P84243DIP
O95931P84243DIP
P11166P84243BioGRID
P16615P84243BioGRID
P17612P84243BioGRID
P28370P84243HPRD
P29034P84243BioGRID
P29474P84243IntAct
P30405P84243BioGRID
P30542P84243BioGRID
P37837P84243BioGRID
P45378P84243BioGRID
P45973P84243MINT
P45984P84243HPRD
P46100P84243IntAct
P46776P84243BioGRID
P49407P84243IntAct
P50748P84243BioGRID
P54198P84243HPRD; IntAct
P54707P84243BioGRID
P61224P84243BioGRID
P62805P84243BioGRID
P78396P84243BioGRID
P84243Q01628BioGRID
P84243Q04725HPRD
P84243Q09028IntAct
P84243Q09470BioGRID
P84243Q12830MINT;HPRD
P84243Q14781DIP
P84243Q15428BioGRID
P84243Q15532HPRD
P84243Q15542MINT
P84243Q4LE28HPRD
P84243Q4VX62BioGRID
P84243Q53GL7HPRD
P84243Q5JSP0BioGRID
P84243Q5VWG9MINT
P84243Q5VX52BioGRID
P84243Q5VZP5BioGRID
P84243Q6ZP83BioGRID
P84243Q86WJ1DIP
P84243Q86X55HPRD
P84243Q8IY51BioGRID
P84243Q8IZL8MINT
P84243Q8TF76MINT
P84243Q92831HPRD
P84243Q92993HPRD
P84243Q93077BioGRID
P84243Q96BD5MINT
P84243Q96GD4MINT
P84243Q96KQ7IntAct
P84243Q96KR4BioGRID
P84243Q9H160MINT
P84243Q9HBD4HPRD
P84243Q9HC52DIP
P84243Q9NVP2HPRD
P84243Q9UER7IntAct
P84243Q9UNL4MINT
P84243Q9Y294HPRD
P84243Q9Y3T9IntAct
P84243Q9Y5B9HPRD
P84243Q9Y6K1MINT