Details for: HIF1A

Gene ID: 3091

Symbol: HIF1A

Ensembl ID: ENSG00000100644

Description: hypoxia inducible factor 1 subunit alpha

Associated with

Cells (max top 100)

(Marker Scores and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: cortical cell of adrenal gland (CL0002097)
    Fold Change: 3.37
    Marker Score: 59,793
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: 3.24
    Marker Score: 3,920
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: 3
    Marker Score: 4,030
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: 2.89
    Marker Score: 6,340
  • Cell Name: CD38-negative naive B cell (CL0002102)
    Fold Change: 2.83
    Marker Score: 5,939
  • Cell Name: alveolar type 2 fibroblast cell (CL4028006)
    Fold Change: 2.79
    Marker Score: 1,554
  • Cell Name: glandular epithelial cell (CL0000150)
    Fold Change: 2.65
    Marker Score: 6,519
  • Cell Name: skeletal muscle satellite stem cell (CL0008011)
    Fold Change: 2.59
    Marker Score: 2,764
  • Cell Name: kidney loop of Henle thin ascending limb epithelial cell (CL1001107)
    Fold Change: 2.55
    Marker Score: 2,589
  • Cell Name: endothelial cell of vascular tree (CL0002139)
    Fold Change: 2.53
    Marker Score: 3,677
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: 2.52
    Marker Score: 1,474
  • Cell Name: kidney interstitial fibroblast (CL1000692)
    Fold Change: 2.45
    Marker Score: 4,715
  • Cell Name: kidney loop of Henle thin descending limb epithelial cell (CL1001111)
    Fold Change: 2.43
    Marker Score: 2,620
  • Cell Name: regular ventricular cardiac myocyte (CL0002131)
    Fold Change: 2.37
    Marker Score: 52,934
  • Cell Name: renal interstitial pericyte (CL1001318)
    Fold Change: 2.37
    Marker Score: 2,257
  • Cell Name: epithelial cell of lower respiratory tract (CL0002632)
    Fold Change: 2.37
    Marker Score: 9,869
  • Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
    Fold Change: 2.3
    Marker Score: 128,687
  • Cell Name: corneal endothelial cell (CL0000132)
    Fold Change: 2.26
    Marker Score: 1,317
  • Cell Name: astrocyte (CL0000127)
    Fold Change: 2.2
    Marker Score: 1,909
  • Cell Name: kidney distal convoluted tubule epithelial cell (CL1000849)
    Fold Change: 2.16
    Marker Score: 2,291
  • Cell Name: astrocyte of the cerebral cortex (CL0002605)
    Fold Change: 2.16
    Marker Score: 46,060
  • Cell Name: A2 amacrine cell (CL0004219)
    Fold Change: 2.15
    Marker Score: 681
  • Cell Name: lung macrophage (CL1001603)
    Fold Change: 2.12
    Marker Score: 2,425
  • Cell Name: stromal cell of lamina propria of small intestine (CL0009022)
    Fold Change: 2.09
    Marker Score: 471
  • Cell Name: kidney collecting duct principal cell (CL1001431)
    Fold Change: 2.09
    Marker Score: 5,277
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: 2.04
    Marker Score: 70,551
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: 2.02
    Marker Score: 639
  • Cell Name: lymphocyte (CL0000542)
    Fold Change: 2.02
    Marker Score: 1,020
  • Cell Name: OFF retinal ganglion cell (CL4023033)
    Fold Change: 1.98
    Marker Score: 830
  • Cell Name: blood cell (CL0000081)
    Fold Change: 1.97
    Marker Score: 22,851
  • Cell Name: malignant cell (CL0001064)
    Fold Change: 1.96
    Marker Score: 26,381
  • Cell Name: kidney loop of Henle thick ascending limb epithelial cell (CL1001106)
    Fold Change: 1.95
    Marker Score: 5,229
  • Cell Name: medullary thymic epithelial cell (CL0002365)
    Fold Change: 1.94
    Marker Score: 3,176
  • Cell Name: taste receptor cell (CL0000209)
    Fold Change: 1.93
    Marker Score: 1,667
  • Cell Name: classical monocyte (CL0000860)
    Fold Change: 1.93
    Marker Score: 8,006
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: 1.89
    Marker Score: 5,615
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: 1.89
    Marker Score: 2,783
  • Cell Name: prostate gland microvascular endothelial cell (CL2000059)
    Fold Change: 1.86
    Marker Score: 722
  • Cell Name: rod bipolar cell (CL0000751)
    Fold Change: 1.85
    Marker Score: 969
  • Cell Name: granulocyte (CL0000094)
    Fold Change: 1.84
    Marker Score: 826
  • Cell Name: IgG-negative class switched memory B cell (CL0002117)
    Fold Change: 1.84
    Marker Score: 1,812
  • Cell Name: myelocyte (CL0002193)
    Fold Change: 1.84
    Marker Score: 793
  • Cell Name: microfold cell of epithelium of small intestine (CL1000353)
    Fold Change: 1.83
    Marker Score: 438
  • Cell Name: CD1c-positive myeloid dendritic cell (CL0002399)
    Fold Change: 1.83
    Marker Score: 4,731
  • Cell Name: cortical thymic epithelial cell (CL0002364)
    Fold Change: 1.82
    Marker Score: 6,749
  • Cell Name: mature microglial cell (CL0002629)
    Fold Change: 1.81
    Marker Score: 656
  • Cell Name: memory B cell (CL0000787)
    Fold Change: 1.81
    Marker Score: 1,367
  • Cell Name: lactocyte (CL0002325)
    Fold Change: 1.8
    Marker Score: 28,936
  • Cell Name: myeloid leukocyte (CL0000766)
    Fold Change: 1.8
    Marker Score: 2,169
  • Cell Name: kidney connecting tubule epithelial cell (CL1000768)
    Fold Change: 1.79
    Marker Score: 2,537
  • Cell Name: CD14-positive, CD16-positive monocyte (CL0002397)
    Fold Change: 1.78
    Marker Score: 3,463
  • Cell Name: kidney loop of Henle epithelial cell (CL1000909)
    Fold Change: 1.78
    Marker Score: 1,114
  • Cell Name: vascular leptomeningeal cell (CL4023051)
    Fold Change: 1.77
    Marker Score: 2,038
  • Cell Name: cerebral cortex endothelial cell (CL1001602)
    Fold Change: 1.77
    Marker Score: 1,057
  • Cell Name: Mueller cell (CL0000636)
    Fold Change: 1.76
    Marker Score: 2,445
  • Cell Name: endothelial cell of uterus (CL0009095)
    Fold Change: 1.76
    Marker Score: 3,517
  • Cell Name: pulmonary artery endothelial cell (CL1001568)
    Fold Change: 1.76
    Marker Score: 1,514
  • Cell Name: CD14-positive monocyte (CL0001054)
    Fold Change: 1.75
    Marker Score: 4,368
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: 1.75
    Marker Score: 15,381
  • Cell Name: lens fiber cell (CL0011004)
    Fold Change: 1.75
    Marker Score: 554
  • Cell Name: renal principal cell (CL0005009)
    Fold Change: 1.75
    Marker Score: 1,348
  • Cell Name: neutrophil (CL0000775)
    Fold Change: 1.74
    Marker Score: 1,063
  • Cell Name: choroid plexus epithelial cell (CL0000706)
    Fold Change: 1.73
    Marker Score: 1,586
  • Cell Name: epicardial adipocyte (CL1000309)
    Fold Change: 1.72
    Marker Score: 833
  • Cell Name: podocyte (CL0000653)
    Fold Change: 1.72
    Marker Score: 634
  • Cell Name: granulosa cell (CL0000501)
    Fold Change: 1.71
    Marker Score: 17,229
  • Cell Name: naive B cell (CL0000788)
    Fold Change: 1.71
    Marker Score: 1,525
  • Cell Name: cardiac mesenchymal cell (CL0000569)
    Fold Change: 1.7
    Marker Score: 419
  • Cell Name: mesothelial cell of epicardium (CL0011019)
    Fold Change: 1.69
    Marker Score: 543
  • Cell Name: activated CD8-positive, alpha-beta T cell, human (CL0001049)
    Fold Change: 1.69
    Marker Score: 383
  • Cell Name: epithelial cell of proximal tubule (CL0002306)
    Fold Change: 1.68
    Marker Score: 5,970
  • Cell Name: T follicular helper cell (CL0002038)
    Fold Change: 1.68
    Marker Score: 1,393
  • Cell Name: thyroid follicular cell (CL0002258)
    Fold Change: 1.67
    Marker Score: 1,308
  • Cell Name: pro-B cell (CL0000826)
    Fold Change: 1.67
    Marker Score: 1,609
  • Cell Name: fibroblast of mammary gland (CL0002555)
    Fold Change: 1.67
    Marker Score: 56,665
  • Cell Name: endothelial cell of sinusoid (CL0002262)
    Fold Change: 1.67
    Marker Score: 404
  • Cell Name: regular atrial cardiac myocyte (CL0002129)
    Fold Change: 1.66
    Marker Score: 5,919
  • Cell Name: mature astrocyte (CL0002627)
    Fold Change: 1.66
    Marker Score: 1,094
  • Cell Name: endothelial cell (CL0000115)
    Fold Change: 1.66
    Marker Score: 1,490
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: 1.66
    Marker Score: 1,882
  • Cell Name: microglial cell (CL0000129)
    Fold Change: 1.66
    Marker Score: 3,022
  • Cell Name: tendon cell (CL0000388)
    Fold Change: 1.66
    Marker Score: 408
  • Cell Name: contractile cell (CL0000183)
    Fold Change: 1.65
    Marker Score: 895
  • Cell Name: smooth muscle cell of prostate (CL1000487)
    Fold Change: 1.65
    Marker Score: 420
  • Cell Name: decidual cell (CL2000002)
    Fold Change: 1.64
    Marker Score: 7,093
  • Cell Name: eurydendroid cell (CL0000253)
    Fold Change: 1.64
    Marker Score: 669
  • Cell Name: stromal cell (CL0000499)
    Fold Change: 1.63
    Marker Score: 1,914
  • Cell Name: Kupffer cell (CL0000091)
    Fold Change: 1.62
    Marker Score: 1,619
  • Cell Name: vascular lymphangioblast (CL0005022)
    Fold Change: 1.62
    Marker Score: 2,736
  • Cell Name: ON retinal ganglion cell (CL4023032)
    Fold Change: 1.61
    Marker Score: 439
  • Cell Name: basophil (CL0000767)
    Fold Change: 1.61
    Marker Score: 763
  • Cell Name: type I enteroendocrine cell (CL0002277)
    Fold Change: 1.6
    Marker Score: 399
  • Cell Name: Bergmann glial cell (CL0000644)
    Fold Change: 1.6
    Marker Score: 652
  • Cell Name: progenitor cell of endocrine pancreas (CL0002351)
    Fold Change: 1.6
    Marker Score: 347
  • Cell Name: tracheobronchial goblet cell (CL0019003)
    Fold Change: 1.59
    Marker Score: 436
  • Cell Name: non-classical monocyte (CL0000875)
    Fold Change: 1.59
    Marker Score: 3,837
  • Cell Name: macrophage (CL0000235)
    Fold Change: 1.59
    Marker Score: 1,768
  • Cell Name: photoreceptor cell (CL0000210)
    Fold Change: 1.59
    Marker Score: 1,196
  • Cell Name: ependymal cell (CL0000065)
    Fold Change: 1.59
    Marker Score: 554
  • Cell Name: melanocyte (CL0000148)
    Fold Change: 1.58
    Marker Score: 642

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Marker Score to the Marker Score Threshold, indicating how much the gene expression has changed compared to a baseline.
Marker Score: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Marker Score to the Marker Score Threshold, indicating how much the gene expression has changed compared to a baseline.
Marker Score: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Marker Score to the Marker Score Threshold, indicating how much the gene expression has changed compared to a baseline.
Marker Score: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Other Information

**Key Characteristics:** HIF1A is a 420-amino acid protein that is encoded by the HIF1A gene. It is a subunit of the HIF1 heterodimer, which also consists of the HIF1B subunit. HIF1A is characterized by its ability to bind to specific DNA sequences, known as hypoxia response elements (HREs), and to interact with a variety of transcription factors and co-factors. HIF1A is also known for its post-translational modifications, including ubiquitination, acetylation, and phosphorylation, which regulate its stability, activity, and subcellular localization. **Pathways and Functions:** HIF1A plays a critical role in the cellular response to hypoxia by regulating the expression of genes involved in energy metabolism, angiogenesis, and cell survival. The HIF1 signaling pathway is composed of several key steps, including: 1. Hypoxia-induced stabilization of HIF1A: HIF1A is stabilized under hypoxic conditions through the inhibition of its ubiquitination and degradation. 2. HIF1A dimerization: HIF1A forms a heterodimer with HIF1B, which is essential for its transcriptional activity. 3. DNA binding: HIF1A binds to HREs, which are specific DNA sequences that are present in the promoters of target genes. 4. Transcriptional regulation: HIF1A regulates the expression of target genes through the recruitment of co-factors and the modulation of chromatin structure. HIF1A regulates the expression of numerous genes involved in energy metabolism, including: * Glycolytic genes: HIF1A regulates the expression of genes involved in glycolysis, including the glucose transporter GLUT1. * Angiogenic genes: HIF1A regulates the expression of genes involved in angiogenesis, including vascular endothelial growth factor (VEGF). * Cell survival genes: HIF1A regulates the expression of genes involved in cell survival, including the anti-apoptotic protein BCL-2. **Clinical Significance:** HIF1A has been implicated in various physiological and pathological processes, including: 1. Cancer: HIF1A is overexpressed in many types of cancer, including solid tumors and hematological malignancies. 2. Cardiovascular disease: HIF1A is involved in the regulation of cardiac function and is overexpressed in patients with heart failure. 3. Neurological disorders: HIF1A is involved in the regulation of neuronal function and is overexpressed in patients with neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. 4. Inflammation: HIF1A is involved in the regulation of inflammatory responses and is overexpressed in patients with inflammatory diseases, such as rheumatoid arthritis and asthma. In conclusion, HIF1A is a critical transcriptional regulator that plays a central role in the cellular response to hypoxia and beyond. Its dysregulation has been implicated in various physiological and pathological processes, including cancer, cardiovascular disease, neurological disorders, and inflammation. Further studies are needed to fully understand the mechanisms by which HIF1A regulates gene expression and to develop novel therapeutic strategies for the treatment of HIF1A-related diseases.

Genular Protein ID: 373320539

Symbol: HIF1A_HUMAN

Name: ARNT-interacting protein

UniProtKB Accession Codes:

Q16665 C0LZJ3 Q53XP6 Q96PT9 Q9UPB1

Database IDs:

ABCD 1 AGR 1 AlphaFoldDB 1 Antibodypedia 1 Bgee 1 BindingDB 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 2 CDD 2 CORUM 1 CTD 1 ChEMBL 1 ChiTaRS 1 ComplexPortal 1 DIP 1 DMDM 1 DNASU 1 DisGeNET 1 DisProt 1 DrugBank 7 DrugCentral 1 ELM 1 EMBL 24 Ensembl 3 EvolutionaryTrace 1 ExpressionAtlas 1 GO 100 Gene3D 2 GeneCards 1 GeneTree 1 GeneWiki 1 Genevisible 1 GenomeRNAi 1 GlyCosmos 1 GlyGen 1 HGNC 2 HPA 1 IDEAL 1 InParanoid 1 IntAct 1 InterPro 10 KEGG 1 MANE-Select 1 MIM 1 MINT 1 MassIVE 1 MaxQB 1 NCBI Taxonomy 1 NCBIfam 1 OMA 1 OpenTargets 1 OrthoDB 1 PANTHER 2 PDB 31 PDBsum 24 PIR 1 PRINTS 1 PRO 1 PROSITE 2 PROSITE-ProRule 2 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 4 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 3 RNAct 1 Reactome 11 RefSeq 3 SAM 1 SIGNOR 1 SMART 3 SMR 1 STRING 1 SUPFAM 2 SignaLink 1 TreeFam 1 UCSC 1 UniProtKB 1 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 7539918

Title: Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension.

PubMed ID: 7539918

DOI: 10.1073/pnas.92.12.5510

PubMed ID: 9079689

Title: Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway.

PubMed ID: 9079689

DOI: 10.1074/jbc.272.13.8581

PubMed ID: 9782081

Title: The human hypoxia-inducible factor 1alpha gene: HIF1A structure and evolutionary conservation.

PubMed ID: 9782081

DOI: 10.1006/geno.1998.5416

PubMed ID: 18638657

Title: Preferential expression of the novel alternative isoform I.3 of hypoxia-inducible factor 1alpha in activated human T lymphocytes.

PubMed ID: 18638657

DOI: 10.1016/j.humimm.2008.05.004

PubMed ID: 12508121

Title: The DNA sequence and analysis of human chromosome 14.

PubMed ID: 12508121

DOI: 10.1038/nature01348

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8917528

Title: An essential role for p300/CBP in the cellular response to hypoxia.

PubMed ID: 8917528

DOI: 10.1073/pnas.93.23.12969

PubMed ID: 9235919

Title: Transactivation and inhibitory domains of hypoxia-inducible factor 1alpha. Modulation of transcriptional activity by oxygen tension.

PubMed ID: 9235919

DOI: 10.1074/jbc.272.31.19253

PubMed ID: 9822602

Title: Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1alpha.

PubMed ID: 9822602

DOI: 10.1093/emboj/17.22.6573

PubMed ID: 9653127

Title: Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway.

PubMed ID: 9653127

DOI: 10.1073/pnas.95.14.7987

PubMed ID: 10202154

Title: Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300.

PubMed ID: 10202154

DOI: 10.1093/emboj/18.7.1905

PubMed ID: 9887100

Title: Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1.

PubMed ID: 9887100

DOI: 10.1101/gad.13.1.64

PubMed ID: 11006129

Title: Drosophila von Hippel-Lindau tumor suppressor complex possesses E3 ubiquitin ligase activity.

PubMed ID: 11006129

DOI: 10.1006/bbrc.2000.3451

PubMed ID: 10944113

Title: Mechanism of regulation of the hypoxia-inducible factor-1 alpha by the von Hippel-Lindau tumor suppressor protein.

PubMed ID: 10944113

DOI: 10.1093/emboj/19.16.4298

PubMed ID: 10594042

Title: Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha.

PubMed ID: 10594042

DOI: 10.1128/mcb.20.1.402-415.2000

PubMed ID: 10758161

Title: Hypoxia-inducible factor 1alpha protein expression is controlled by oxygen-regulated ubiquitination that is disrupted by deletions and missense mutations.

PubMed ID: 10758161

DOI: 10.1073/pnas.080072497

PubMed ID: 11566883

Title: Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation.

PubMed ID: 11566883

DOI: 10.1093/emboj/20.18.5197

PubMed ID: 11389899

Title: Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7.

PubMed ID: 11389899

DOI: 10.1016/s0014-5793(01)02499-1

PubMed ID: 11292861

Title: Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation.

PubMed ID: 11292861

DOI: 10.1126/science.1059796

PubMed ID: 12464182

Title: Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation.

PubMed ID: 12464182

DOI: 10.1016/s0092-8674(02)01085-1

PubMed ID: 12080085

Title: FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor.

PubMed ID: 12080085

DOI: 10.1101/gad.991402

PubMed ID: 12351678

Title: Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor.

PubMed ID: 12351678

DOI: 10.1073/pnas.192342099

PubMed ID: 12914934

Title: S-nitrosation of Cys-800 of HIF-1alpha protein activates its interaction with p300 and stimulates its transcriptional activity.

PubMed ID: 12914934

DOI: 10.1016/s0014-5793(03)00807-x

PubMed ID: 12560087

Title: HIF-1 alpha protein as a target for S-nitrosation.

PubMed ID: 12560087

DOI: 10.1016/s0014-5793(02)03887-5

PubMed ID: 12778114

Title: Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2.

PubMed ID: 12778114

DOI: 10.1038/nsb936

PubMed ID: 15465032

Title: Sumoylation increases HIF-1alpha stability and its transcriptional activity.

PubMed ID: 15465032

DOI: 10.1016/j.bbrc.2004.09.068

PubMed ID: 14757845

Title: Molecular cloning and characterization of the von Hippel-Lindau-like protein.

PubMed ID: 14757845

PubMed ID: 15776016

Title: VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF-1alpha.

PubMed ID: 15776016

DOI: 10.1038/sj.embor.7400377

PubMed ID: 16288748

Title: Interaction between HIF-1 alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1 alpha.

PubMed ID: 16288748

DOI: 10.1016/j.febslet.2005.10.036

PubMed ID: 16543236

Title: Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha.

PubMed ID: 16543236

DOI: 10.1074/jbc.m600456200

PubMed ID: 16973622

Title: Clioquinol, a Cu(II)/Zn(II) chelator, inhibits both ubiquitination and asparagine hydroxylation of hypoxia-inducible factor-1alpha, leading to expression of vascular endothelial growth factor and erythropoietin in normoxic cells.

PubMed ID: 16973622

DOI: 10.1074/jbc.m603913200

PubMed ID: 17610843

Title: SUMOylation of hypoxia-inducible factor-1alpha reduces its transcriptional activity.

PubMed ID: 17610843

DOI: 10.1016/j.bbrc.2007.06.103

PubMed ID: 17956732

Title: RSUME, a small RWD-containing protein, enhances SUMO conjugation and stabilizes HIF-1alpha during hypoxia.

PubMed ID: 17956732

DOI: 10.1016/j.cell.2007.07.044

PubMed ID: 17244529

Title: RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha.

PubMed ID: 17244529

DOI: 10.1016/j.molcel.2007.01.001

PubMed ID: 16862177

Title: HIF-1alpha and EPAS ubiquitination mediated by the VHL tumour suppressor involves flexibility in the ubiquitination mechanism, similar to other RING E3 ligases.

PubMed ID: 16862177

DOI: 10.1038/sj.onc.1209818

PubMed ID: 18658046

Title: Transcriptional activation of HIF-1 by RORalpha and its role in hypoxia signaling.

PubMed ID: 18658046

DOI: 10.1161/atvbaha.108.171546

PubMed ID: 18809331

Title: HIF-1 regulation: not so easy come, easy go.

PubMed ID: 18809331

DOI: 10.1016/j.tibs.2008.08.002

PubMed ID: 19046997

Title: Transcriptional regulation of hypoxia-inducible factor 1alpha by HIPK2 suggests a novel mechanism to restrain tumor growth.

PubMed ID: 19046997

DOI: 10.1016/j.bbamcr.2008.10.013

PubMed ID: 19528298

Title: HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters mitochondrial distribution and transport.

PubMed ID: 19528298

DOI: 10.1083/jcb.200811033

PubMed ID: 20624928

Title: Hypoxia-inducible protein 2 is a novel lipid droplet protein and a specific target gene of hypoxia-inducible factor-1.

PubMed ID: 20624928

DOI: 10.1096/fj.10-159806

PubMed ID: 20889502

Title: Plk3 functions as an essential component of the hypoxia regulatory pathway by direct phosphorylation of HIF-1alpha.

PubMed ID: 20889502

DOI: 10.1074/jbc.m110.160325

PubMed ID: 20699359

Title: Casein kinase 1 regulates human hypoxia-inducible factor HIF-1.

PubMed ID: 20699359

DOI: 10.1242/jcs.068122

PubMed ID: 22537386

Title: UBXN7 docks on neddylated cullin complexes using its UIM motif and causes HIF1alpha accumulation.

PubMed ID: 22537386

DOI: 10.1186/1741-7007-10-36

PubMed ID: 22009797

Title: RSUME is implicated in HIF-1-induced VEGF-A production in pituitary tumour cells.

PubMed ID: 22009797

DOI: 10.1530/erc-11-0211

PubMed ID: 22128162

Title: Ubiquitin-specific protease 19 (USP19) regulates hypoxia-inducible factor 1alpha (HIF-1alpha) during hypoxia.

PubMed ID: 22128162

DOI: 10.1074/jbc.m111.305615

PubMed ID: 22286099

Title: The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity.

PubMed ID: 22286099

DOI: 10.1038/ncb2424

PubMed ID: 23401859

Title: DCNL1 functions as a substrate sensor and activator of cullin 2-RING ligase.

PubMed ID: 23401859

DOI: 10.1128/mcb.01342-12

PubMed ID: 23469069

Title: In silico structural and functional characterization of the RSUME splice variants.

PubMed ID: 23469069

DOI: 10.1371/journal.pone.0057795

PubMed ID: 24681946

Title: SIRT2 regulates tumour hypoxia response by promoting HIF-1alpha hydroxylation.

PubMed ID: 24681946

DOI: 10.1038/onc.2014.76

PubMed ID: 26517842

Title: Client proteins and small molecule inhibitors display distinct binding preferences for constitutive and stress-induced HSP90 isoforms and their conformationally restricted mutants.

PubMed ID: 26517842

DOI: 10.1371/journal.pone.0141786

PubMed ID: 25974097

Title: Myeloid translocation gene-16 co-repressor promotes degradation of hypoxia-inducible factor 1.

PubMed ID: 25974097

DOI: 10.1371/journal.pone.0123725

PubMed ID: 25615526

Title: UCHL1 provides diagnostic and antimetastatic strategies due to its deubiquitinating effect on HIF-1alpha.

PubMed ID: 25615526

DOI: 10.1038/ncomms7153

PubMed ID: 28296633

Title: The vacuolar-ATPase complex and assembly factors, TMEM199 and CCDC115, control HIF1alpha prolyl hydroxylation by regulating cellular iron levels.

PubMed ID: 28296633

DOI: 10.7554/elife.22693

PubMed ID: 30125331

Title: A pathogen-derived effector modulates host glucose metabolism by arginine GlcNAcylation of HIF-1alpha protein.

PubMed ID: 30125331

DOI: 10.1371/journal.ppat.1007259

PubMed ID: 32697943

Title: Elevated Glucose Levels Favor SARS-CoV-2 Infection and Monocyte Response through a HIF-1alpha/Glycolysis-Dependent Axis.

PubMed ID: 32697943

DOI: 10.1016/j.cmet.2020.07.007

PubMed ID: 11089639

Title: A model for the complex between the hypoxia-inducible factor-1 (HIF-1) and its consensus DNA sequence.

PubMed ID: 11089639

DOI: 10.1080/07391102.2000.10506656

PubMed ID: 12446723

Title: Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha.

PubMed ID: 12446723

DOI: 10.1074/jbc.c200644200

PubMed ID: 11959990

Title: Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha.

PubMed ID: 11959990

DOI: 10.1073/pnas.082117899

PubMed ID: 11959977

Title: Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response.

PubMed ID: 11959977

DOI: 10.1073/pnas.082121399

PubMed ID: 12004076

Title: Structure of an HIF-1alpha-pVHL complex: hydroxyproline recognition in signaling.

PubMed ID: 12004076

DOI: 10.1126/science.1073440

PubMed ID: 12050673

Title: Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL.

PubMed ID: 12050673

DOI: 10.1038/nature00767

Sequence Information:

  • Length: 826
  • Mass: 92670
  • Checksum: ABD4F7DAA135BE2D
  • Sequence:
    • MEGAGGANDK KKISSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV SSHLDKASVM 
RLTISYLRVR KLLDAGDLDI EDDMKAQMNC FYLKALDGFV MVLTDDGDMI YISDNVNKYM 
GLTQFELTGH SVFDFTHPCD HEEMREMLTH RNGLVKKGKE QNTQRSFFLR MKCTLTSRGR 
TMNIKSATWK VLHCTGHIHV YDTNSNQPQC GYKKPPMTCL VLICEPIPHP SNIEIPLDSK 
TFLSRHSLDM KFSYCDERIT ELMGYEPEEL LGRSIYEYYH ALDSDHLTKT HHDMFTKGQV 
TTGQYRMLAK RGGYVWVETQ ATVIYNTKNS QPQCIVCVNY VVSGIIQHDL IFSLQQTECV 
LKPVESSDMK MTQLFTKVES EDTSSLFDKL KKEPDALTLL APAAGDTIIS LDFGSNDTET 
DDQQLEEVPL YNDVMLPSPN EKLQNINLAM SPLPTAETPK PLRSSADPAL NQEVALKLEP 
NPESLELSFT MPQIQDQTPS PSDGSTRQSS PEPNSPSEYC FYVDSDMVNE FKLELVEKLF 
AEDTEAKNPF STQDTDLDLE MLAPYIPMDD DFQLRSFDQL SPLESSSASP ESASPQSTVT 
VFQQTQIQEP TANATTTTAT TDELKTVTKD RMEDIKILIA SPSPTHIHKE TTSATSSPYR 
DTQSRTASPN RAGKGVIEQT EKSHPRSPNV LSVALSQRTT VPEEELNPKI LALQNAQRKR 
KMEHDGSLFQ AVGIGTLLQQ PDDHAATTSL SWKRVKGCKS SEQNGMEQKT IILIPSDLAC 
RLLGQSMDES GLPQLTSYDC EVNAPIQGSR NLLQGEELLR ALDQVN

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.