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28 sources retrieved · Most recent: April 2026 · Index updated 14 days ago
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H1-2
H1.2 linker histone, cluster member
Chromosome 6 · 6p22.2
NCBI Gene: 3006Ensembl: ENSG00000187837.5HGNC: HGNC:4716UniProt: P16403
271PubMed Papers
20Diseases
0Drugs
0Pathogenic Variants
RESEARCH IMPACT
Trending
DATA QUALITY
✓ Experimental GO Evidence✓ Swiss-Prot Reviewed
nucleolusRNA bindingnucleoplasmprotein bindinghepatocellular carcinomaMiyoshi myopathynon-small cell lung carcinomachronic lymphocytic leukemia
✦AI Summary

H1-2 (H1.2 linker histone) is a chr6 structural protein that plays critical roles in chr6 compaction, gene regulation, and disease pathogenesis. H1-2 binds to linker DNA between nucleosomes and is essential for condensing nucleosome chains into higher-order chr6 fibers, with its absence causing global chr6 decompaction not observed with other H1 variants 1. The protein functions as a histone reader, specifically recognizing and binding H3K27me3 marks, which governs its recruitment to target chr6 regions 1. H1-2 acts as a gene-specific transcriptional regulator, repressing growth suppressive genes including p16 through direct promoter binding 12. In cancer, H1-2 demonstrates dual roles: it functions as a tumor suppressor in B-cell lymphomas where loss-of-function mutations drive malignant transformation through 3D genome reorganization and developmental gene derepression 3, while in solid tumors like pancreatic and lung cancers, H1-2 overexpression promotes metastasis and chemoresistance through mechanisms including c-MYC regulation and NRF2-mediated antioxidant responses 45. H1-2 also regulates metabolic processes, acting as a brake on white adipose tissue browning through IL10 receptor signaling 6, and contributes to neurodegenerative disease pathology through abnormal interactions with mutant FUS protein 7.

Sources cited
1
H1-2 binds linker DNA, recognizes H3K27me3 marks, and represses growth suppressive genes through chromatin compaction
PMID: 26581166
2
H1 proteins including H1-2 function as tumor suppressors in B-cell lymphomas, with mutations driving malignant transformation
PMID: 33299181
3
H1-2 overexpression in pancreatic cancer promotes chemoresistance and metastasis through c-MYC signaling
PMID: 38290407
4
H1-2 drives lung cancer progression and chemoresistance through NRF2-mediated antioxidant responses
PMID: 37729198
5
H1-2 directly binds to and represses p16 tumor suppressor gene transcription
PMID: 37500167
6
H1-2 regulates thermogenic genes and acts as a brake on white adipose tissue browning through IL10 receptor signaling
PMID: 37414781
7
H1-2 contributes to ALS pathology through abnormal interactions with mutant FUS protein
PMID: 39167487
Disease Associationsⓘ20
hepatocellular carcinomaOpen Targets
0.02Suggestive
Miyoshi myopathyOpen Targets
0.02Suggestive
non-small cell lung carcinomaOpen Targets
0.02Suggestive
chronic lymphocytic leukemiaOpen Targets
0.02Suggestive
allergic rhinitisOpen Targets
0.01Suggestive
neoplasmOpen Targets
0.01Suggestive
LeishmaniasisOpen Targets
0.01Suggestive
breast carcinomaOpen Targets
0.01Suggestive
diffuse large B-cell lymphomaOpen Targets
0.01Suggestive
age-related macular degenerationOpen Targets
0.01Suggestive
male infertilityOpen Targets
0.01Suggestive
pachyonychia congenitaOpen Targets
0.01Suggestive
ulcerative colitisOpen Targets
0.01Suggestive
cancerOpen Targets
0.01Suggestive
Leigh syndromeOpen Targets
0.01Suggestive
cystic fibrosisOpen Targets
0.01Suggestive
pituitary cancerOpen Targets
0.01Suggestive
chronic interstitial cystitisOpen Targets
0.01Suggestive
neuroblastomaOpen Targets
0.01Suggestive
islet cell tumorOpen Targets
0.01Suggestive
Pathogenic Variants
No pathogenic variants reported on ClinVar for this gene.
View on ClinVar ↗
Related Genes
H2AC8Protein interaction100%H2BC12Protein interaction100%H2AC6Protein interaction99%H2BC5Protein interaction99%H2BC4Protein interaction99%H3C3Protein interaction99%
Tissue Expression6 tissues
Liver
100%
Lung
69%
Heart
68%
Bone Marrow
62%
Ovary
59%
Brain
24%
Gene Interaction Network
Click a node to explore
H1-2H2AC8H2BC12H2AC6H2BC5H2BC4H3C3
PROTEIN STRUCTURE
Preparing viewer…
PDB8H0V · 3.80 Å · EM
View on RCSB ↗
Constraintⓘ
LOEUFⓘ
1.73LoF Tolerant
pLIⓘ
0.00Tolerant
Observed/Expected LoF0.98 [0.55–1.73]
RankingsWhere H1-2 stands among ~20K protein-coding genes
  • #1,358of 20,598
    Most Researched271 · top 10%
  • #16,231of 17,882
    Most Constrained (LOEUF)1.73
Genes detectedH1-2
Sources retrieved28 papers
Response time—
📄 Sources
28▼
1
Histone H1 loss drives lymphoma by disrupting 3D chromatin architecture.
PMID: 33299181
Nature · 2021
1.00
2
The role of histone H1.2 in pancreatic cancer metastasis and chemoresistance.
PMID: 38290407
Drug Resist Updat · 2024
0.90
3
Linker histone variant H1.2 is a brake on white adipose tissue browning.
PMID: 37414781
Nat Commun · 2023
0.80
4
ITCH nuclear translocation and H1.2 polyubiquitination negatively regulate the DNA damage response.
PMID: 30517763
Nucleic Acids Res · 2019
0.76
5
The role of linker histone H1 modifications in the regulation of gene expression and chromatin dynamics.
PMID: 26348411
Biochim Biophys Acta · 2016
0.72