Phospho-Histone H1.3 (Thr18) Antibody - #DF2946
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Cite Format: Affinity Biosciences Cat# DF2946, RRID:AB_2840930.
Fold/Unfold
H1 histone family member 4; H1.4; H14_HUMAN; H1E; H1F4; Hist1h1e; Histone 1 H1e; Histone cluster 1 H1e; Histone H1; Histone H1.4; Histone H1B; MGC116819; H1 histone family member 3; H1.3; H13_HUMAN; H1F3; HIST1 H1D; HIST1H1D; Histone 1 H1d; Histone cluster 1 H1d; Histone H1.3; Histone H1c; MGC138176;
Immunogens
A synthesized peptide derived from human Histone H1.3 around the phosphorylation site of T18.
- P10412 H14_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MSETAPAAPAAPAPAEKTPVKKKARKSAGAAKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGAAKKPKKATGAATPKKSAKKTPKKAKKPAAAAGAKKAKSPKKAKAAKPKKAPKSPAKAKAVKPKAAKPKTAKPKAAKPKKAAAKKK
- P16402 H13_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MSETAPLAPTIPAPAEKTPVKKKAKKAGATAGKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEGKPKAKKAGAAKPRKPAGAAKKPKKVAGAATPKKSIKKTPKKVKKPATAAGTKKVAKSAKKVKTPQPKKAAKSPAKAKAPKPKAAKPKSGKPKVTKAKKAAPKKK
PTMs - P10412/P16402 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
S2 | Acetylation | Uniprot | |
S2 | Phosphorylation | Uniprot | |
T4 | Phosphorylation | Uniprot | |
K17 | Acetylation | Uniprot | |
K17 | Ubiquitination | Uniprot | |
T18 | Phosphorylation | P24941 (CDK2) , P06493 (CDK1) | Uniprot |
K21 | Ubiquitination | Uniprot | |
K26 | Acetylation | Uniprot | |
K26 | Methylation | Uniprot | |
S27 | Phosphorylation | Q96GD4 (AURKB) | Uniprot |
K32 | Acetylation | Uniprot | |
K34 | Acetylation | Uniprot | |
K34 | Methylation | Uniprot | |
K34 | Ubiquitination | Uniprot | |
S36 | Phosphorylation | P17612 (PRKACA) | Uniprot |
S41 | Phosphorylation | Uniprot | |
T45 | Phosphorylation | Uniprot | |
K46 | Acetylation | Uniprot | |
K46 | Ubiquitination | Uniprot | |
S51 | Phosphorylation | Uniprot | |
K52 | Acetylation | Uniprot | |
K52 | Ubiquitination | Uniprot | |
R54 | Methylation | Uniprot | |
S55 | Phosphorylation | Uniprot | |
S58 | Phosphorylation | Uniprot | |
K63 | Acetylation | Uniprot | |
K63 | Ubiquitination | Uniprot | |
K64 | Methylation | Uniprot | |
K64 | Sumoylation | Uniprot | |
K64 | Ubiquitination | Uniprot | |
Y71 | Phosphorylation | Uniprot | |
K75 | Acetylation | Uniprot | |
K75 | Methylation | Uniprot | |
K75 | Ubiquitination | Uniprot | |
S78 | Phosphorylation | Uniprot | |
K85 | Acetylation | Uniprot | |
K85 | Ubiquitination | Uniprot | |
S86 | Phosphorylation | Uniprot | |
S89 | Phosphorylation | Uniprot | |
K90 | Acetylation | Uniprot | |
K90 | Ubiquitination | Uniprot | |
T92 | Phosphorylation | Uniprot | |
K97 | Methylation | Uniprot | |
K97 | Ubiquitination | Uniprot | |
T99 | Phosphorylation | Uniprot | |
S102 | Phosphorylation | Uniprot | |
S104 | Phosphorylation | Uniprot | |
K106 | Acetylation | Uniprot | |
K106 | Methylation | Uniprot | |
K106 | Ubiquitination | Uniprot | |
K109 | Ubiquitination | Uniprot | |
K110 | Ubiquitination | Uniprot | |
S113 | Phosphorylation | Uniprot | |
K117 | Ubiquitination | Uniprot | |
K119 | Methylation | Uniprot | |
K119 | Ubiquitination | Uniprot | |
K121 | Methylation | Uniprot | |
K129 | Acetylation | Uniprot | |
K129 | Methylation | Uniprot | |
K130 | Acetylation | Uniprot | |
K136 | Acetylation | Uniprot | |
K136 | Ubiquitination | Uniprot | |
K137 | Acetylation | Uniprot | |
K137 | Ubiquitination | Uniprot | |
K140 | Ubiquitination | Uniprot | |
T142 | Phosphorylation | Uniprot | |
T146 | Phosphorylation | Uniprot | |
K148 | Acetylation | Uniprot | |
K148 | Methylation | Uniprot | |
K148 | Ubiquitination | Uniprot | |
T154 | Phosphorylation | Uniprot | |
K159 | Methylation | Uniprot | |
K159 | Ubiquitination | Uniprot | |
K160 | Acetylation | Uniprot | |
K160 | Ubiquitination | Uniprot | |
K168 | Acetylation | Uniprot | |
K168 | Ubiquitination | Uniprot | |
K169 | Acetylation | Uniprot | |
K171 | Methylation | Uniprot | |
S172 | Phosphorylation | Uniprot | |
K177 | Methylation | Uniprot | |
S187 | Phosphorylation | Uniprot | |
K192 | Methylation | Uniprot | |
K195 | Ubiquitination | Uniprot | |
K197 | Ubiquitination | Uniprot |
Site | PTM Type | Enzyme | Source |
---|---|---|---|
S2 | Acetylation | Uniprot | |
S2 | Phosphorylation | Uniprot | |
T4 | Phosphorylation | Uniprot | |
T10 | Phosphorylation | Uniprot | |
K17 | Acetylation | Uniprot | |
K17 | Ubiquitination | Uniprot | |
T18 | Phosphorylation | Uniprot | |
K33 | Acetylation | Uniprot | |
K35 | Acetylation | Uniprot | |
K35 | Methylation | Uniprot | |
K35 | Ubiquitination | Uniprot | |
S37 | Phosphorylation | Uniprot | |
S42 | Phosphorylation | Uniprot | |
T46 | Phosphorylation | Uniprot | |
K47 | Acetylation | Uniprot | |
K47 | Ubiquitination | Uniprot | |
S52 | Phosphorylation | Uniprot | |
K53 | Acetylation | Uniprot | |
K53 | Ubiquitination | Uniprot | |
R55 | Methylation | Uniprot | |
S56 | Phosphorylation | Uniprot | |
S59 | Phosphorylation | Uniprot | |
K64 | Acetylation | Uniprot | |
K64 | Ubiquitination | Uniprot | |
K65 | Methylation | Uniprot | |
K65 | Sumoylation | Uniprot | |
K65 | Ubiquitination | Uniprot | |
Y72 | Phosphorylation | Uniprot | |
K76 | Acetylation | Uniprot | |
K76 | Ubiquitination | Uniprot | |
S79 | Phosphorylation | Uniprot | |
K86 | Acetylation | Uniprot | |
K86 | Ubiquitination | Uniprot | |
S87 | Phosphorylation | Uniprot | |
S90 | Phosphorylation | Uniprot | |
K91 | Acetylation | Uniprot | |
K91 | Ubiquitination | Uniprot | |
T93 | Phosphorylation | Uniprot | |
K98 | Methylation | Uniprot | |
K98 | Ubiquitination | Uniprot | |
T100 | Phosphorylation | Uniprot | |
S103 | Phosphorylation | Uniprot | |
S105 | Phosphorylation | Uniprot | |
K107 | Acetylation | Uniprot | |
K107 | Methylation | Uniprot | |
K107 | Ubiquitination | Uniprot | |
K110 | Ubiquitination | Uniprot | |
K111 | Ubiquitination | Uniprot | |
K118 | Ubiquitination | Uniprot | |
K141 | Ubiquitination | Uniprot | |
T147 | Phosphorylation | Uniprot | |
K149 | Ubiquitination | Uniprot | |
S151 | Phosphorylation | Uniprot | |
T155 | Phosphorylation | Uniprot | |
K160 | Ubiquitination | Uniprot | |
K161 | Ubiquitination | Uniprot | |
T164 | Phosphorylation | Uniprot | |
K169 | Acetylation | Uniprot | |
K170 | Acetylation | Uniprot | |
K173 | Acetylation | Uniprot | |
K176 | Acetylation | Uniprot | |
K179 | Ubiquitination | Uniprot | |
T180 | Phosphorylation | Uniprot | |
K188 | Acetylation | Uniprot | |
S189 | Phosphorylation | Uniprot | |
K207 | Acetylation | Uniprot | |
K209 | Acetylation | Uniprot | |
K212 | Acetylation | Uniprot |
Research Backgrounds
Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity).
H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter.
Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1.
Citrullination at Arg-54 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance.
ADP-ribosylated on Ser-150 in response to DNA damage.
Nucleus. Chromosome.
Note: Mainly localizes in heterochromatin. Dysplays a punctuate staining pattern in the nucleus.
The C-terminal domain is required for high-affinity binding to chromatin.
Belongs to the histone H1/H5 family.
Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity).
H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter.
Citrullination at Arg-55 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance.
Nucleus. Chromosome.
Note: According to PubMed:15911621 more commonly found in euchromatin. According to PubMed:10997781 is associated with inactive chromatin.
The C-terminal domain is required for high-affinity binding to chromatin.
Belongs to the histone H1/H5 family.
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