HIF1A | ENSG00000100644 | NCBI 3091

Details for: HIF1A

Gene ID: 3091

Symbol: HIF1A

Ensembl ID: ENSG00000100644

Description: hypoxia inducible factor 1 subunit alpha

Associated with

Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Cellular response to hypoxia
(R-HSA-1234174)
Circadian clock
(R-HSA-400253)
Cytokine signaling in immune system
(R-HSA-1280215)
Deubiquitination
(R-HSA-5688426)
Immune system
(R-HSA-168256)
Interleukin-4 and interleukin-13 signaling
(R-HSA-6785807)
Metabolism of proteins
(R-HSA-392499)
Neddylation
(R-HSA-8951664)
Notch1 intracellular domain regulates transcription
(R-HSA-2122947)
Oxygen-dependent proline hydroxylation of hypoxia-inducible factor alpha
(R-HSA-1234176)
Post-translational protein modification
(R-HSA-597592)
Ptk6 expression
(R-HSA-8849473)
Ptk6 promotes hif1a stabilization
(R-HSA-8857538)
Regulation of gene expression by hypoxia-inducible factor
(R-HSA-1234158)
Signaling by alk
(R-HSA-201556)
Signaling by interleukins
(R-HSA-449147)
Signaling by non-receptor tyrosine kinases
(R-HSA-9006927)
Signaling by notch
(R-HSA-157118)
Signaling by notch1
(R-HSA-1980143)
Signaling by ptk6
(R-HSA-8848021)
Signaling by receptor tyrosine kinases
(R-HSA-9006934)
Stat3 nuclear events downstream of alk signaling
(R-HSA-9701898)
Ub-specific processing proteases
(R-HSA-5689880)
Angiogenesis
(GO:0001525)
Axonal transport of mitochondrion
(GO:0019896)
B-1 b cell homeostasis
(GO:0001922)
Bone mineralization
(GO:0030282)
Cardiac ventricle morphogenesis
(GO:0003208)
Cerebral cortex development
(GO:0021987)
Chondrocyte differentiation
(GO:0002062)
Cis-regulatory region sequence-specific dna binding
(GO:0000987)
Connective tissue replacement involved in inflammatory response wound healing
(GO:0002248)
Dna-binding transcription activator activity
(GO:0001216)
Dna-binding transcription activator activity, rna polymerase ii-specific
(GO:0001228)
Dna-binding transcription factor activity
(GO:0003700)
Dna-binding transcription factor activity, rna polymerase ii-specific
(GO:0000981)
Dna-binding transcription repressor activity
(GO:0001217)
E-box binding
(GO:0070888)
Embryonic placenta development
(GO:0001892)
Enzyme binding
(GO:0019899)
Epithelial to mesenchymal transition
(GO:0001837)
Glandular epithelial cell maturation
(GO:0002071)
Heart looping
(GO:0001947)
Histone deacetylase binding
(GO:0042826)
Hsp90 protein binding
(GO:0051879)
Intracellular glucose homeostasis
(GO:0001678)
Intracellular iron ion homeostasis
(GO:0006879)
Lactate metabolic process
(GO:0006089)
Lactation
(GO:0007595)
Negative regulation of bone mineralization
(GO:0030502)
Negative regulation of gene expression
(GO:0010629)
Negative regulation of tor signaling
(GO:0032007)
Neural crest cell migration
(GO:0001755)
Neural fold elevation formation
(GO:0021502)
Neuroblast proliferation
(GO:0007405)
Nuclear receptor binding
(GO:0016922)
Outflow tract morphogenesis
(GO:0003151)
P53 binding
(GO:0002039)
Positive regulation of endothelial cell proliferation
(GO:0001938)
Positive regulation of epithelial cell migration
(GO:0010634)
Positive regulation of gene expression
(GO:0010628)
Positive regulation of neuroblast proliferation
(GO:0002052)
Positive regulation of vascular endothelial growth factor production
(GO:0010575)
Positive regulation of vascular endothelial growth factor receptor signaling pathway
(GO:0030949)
Protein binding
(GO:0005515)
Protein domain specific binding
(GO:0019904)
Protein heterodimerization activity
(GO:0046982)
Protein kinase binding
(GO:0019901)
Regulation of dna-templated transcription
(GO:0006355)
Regulation of gene expression
(GO:0010468)
Regulation of glycolytic process
(GO:0006110)
Regulation of transcription by rna polymerase ii
(GO:0006357)
Response to hypoxia
(GO:0001666)
Response to iron ion
(GO:0010039)
Response to muscle activity
(GO:0014850)
Response to reactive oxygen species
(GO:0000302)
Rna polymerase ii-specific dna-binding transcription factor binding
(GO:0061629)
Rna polymerase ii cis-regulatory region sequence-specific dna binding
(GO:0000978)
Rna polymerase ii transcription regulatory region sequence-specific dna binding
(GO:0000977)
Sequence-specific dna binding
(GO:0043565)
Signal transduction
(GO:0007165)
Tor signaling
(GO:0031929)
Transcription coactivator binding
(GO:0001223)
Transcription regulator activator activity
(GO:0140537)
Ubiquitin protein ligase binding
(GO:0031625)
Vascular endothelial growth factor production
(GO:0010573)
Visual learning
(GO:0008542)

Cells (max top 100)

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

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 498.7617
Cell Significance Index: -77.5800
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 298.4111
Cell Significance Index: -75.6900
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 184.3438
Cell Significance Index: -75.9400
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 175.2723
Cell Significance Index: -82.7500
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 170.6801
Cell Significance Index: -69.3400
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 150.2473
Cell Significance Index: -77.2900
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 123.6621
Cell Significance Index: -82.9800
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 73.7057
Cell Significance Index: -70.3700
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 64.7590
Cell Significance Index: -79.8500
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 27.6498
Cell Significance Index: -74.0700
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 20.3877
Cell Significance Index: -62.6200
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 20.3368
Cell Significance Index: -80.2500
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 18.5896
Cell Significance Index: -40.6900
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 3.1111
Cell Significance Index: 174.5800
Cell Name: granulosa cell (CL0000501)
Fold Change: 2.9363
Cell Significance Index: 77.2100
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 2.5170
Cell Significance Index: 46.5200
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 2.4372
Cell Significance Index: 299.6700
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 2.3336
Cell Significance Index: 420.6800
Cell Name: peg cell (CL4033014)
Fold Change: 2.0629
Cell Significance Index: 47.6600
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 2.0625
Cell Significance Index: 56.1400
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 1.9928
Cell Significance Index: 103.8000
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: 1.9796
Cell Significance Index: 53.0500
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 1.7446
Cell Significance Index: 133.8800
Cell Name: cell in vitro (CL0001034)
Fold Change: 1.5397
Cell Significance Index: 840.8400
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 1.5211
Cell Significance Index: 179.3900
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 1.4850
Cell Significance Index: 2019.1500
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 1.4735
Cell Significance Index: 41.1800
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 1.3909
Cell Significance Index: 151.2900
Cell Name: neoplastic cell (CL0001063)
Fold Change: 1.3301
Cell Significance Index: 263.9700
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 1.3026
Cell Significance Index: 261.3000
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 1.0139
Cell Significance Index: 60.8700
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.9578
Cell Significance Index: 864.7900
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.9091
Cell Significance Index: 124.8400
Cell Name: odontoblast (CL0000060)
Fold Change: 0.8192
Cell Significance Index: 105.0200
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 0.7146
Cell Significance Index: 1100.0800
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.6532
Cell Significance Index: 234.2900
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 0.5575
Cell Significance Index: 28.9600
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: 0.5214
Cell Significance Index: 3.1500
Cell Name: anterior lens cell (CL0002223)
Fold Change: 0.4855
Cell Significance Index: 895.3200
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 0.4811
Cell Significance Index: 33.2700
Cell Name: vascular lymphangioblast (CL0005022)
Fold Change: 0.4422
Cell Significance Index: 7.8200
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.4348
Cell Significance Index: 192.2500
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.4292
Cell Significance Index: 42.4600
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: 0.3984
Cell Significance Index: 180.8400
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.3481
Cell Significance Index: 240.7600
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.3144
Cell Significance Index: 59.8300
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 0.2979
Cell Significance Index: 22.2000
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 0.2734
Cell Significance Index: 12.8500
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.2714
Cell Significance Index: 12.3000
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 0.2334
Cell Significance Index: 10.8800
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.2218
Cell Significance Index: 6.3900
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 0.2123
Cell Significance Index: 5.6700
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.1977
Cell Significance Index: 372.1900
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 0.1095
Cell Significance Index: 5.7500
Cell Name: lactocyte (CL0002325)
Fold Change: 0.0670
Cell Significance Index: 8.6600
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: 0.0318
Cell Significance Index: 20.1800
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.0156
Cell Significance Index: 2.6700
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: 0.0112
Cell Significance Index: 0.6900
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: 0.0087
Cell Significance Index: 0.0800
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.0031
Cell Significance Index: 0.1100
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0191
Cell Significance Index: -14.0200
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0274
Cell Significance Index: -20.2800
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0402
Cell Significance Index: -30.4300
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: -0.0475
Cell Significance Index: -1.0300
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.0504
Cell Significance Index: -7.3200
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0838
Cell Significance Index: -8.5600
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0957
Cell Significance Index: -53.9500
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0999
Cell Significance Index: -62.3900
Cell Name: retinal rod cell (CL0000604)
Fold Change: -0.1200
Cell Significance Index: -1.4300
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: -0.1720
Cell Significance Index: -4.9300
Cell Name: early pro-B cell (CL0002046)
Fold Change: -0.2168
Cell Significance Index: -13.9900
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.2424
Cell Significance Index: -69.7500
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.2816
Cell Significance Index: -59.3200
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.2957
Cell Significance Index: -30.7900
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.3196
Cell Significance Index: -36.6200
Cell Name: leptomeningeal cell (CL0000708)
Fold Change: -0.3408
Cell Significance Index: -7.2900
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -0.3545
Cell Significance Index: -22.3400
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: -0.4058
Cell Significance Index: -66.0100
Cell Name: sebum secreting cell (CL0000317)
Fold Change: -0.4171
Cell Significance Index: -29.5000
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.4199
Cell Significance Index: -48.9400
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.4288
Cell Significance Index: -28.8300
Cell Name: cardiac muscle cell (CL0000746)
Fold Change: -0.5046
Cell Significance Index: -7.4500
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -0.5673
Cell Significance Index: -25.1000
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.6101
Cell Significance Index: -69.6400
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.6271
Cell Significance Index: -10.5000
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.6733
Cell Significance Index: -14.3400
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.7809
Cell Significance Index: -61.8500
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -0.8007
Cell Significance Index: -30.3200
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: -0.8553
Cell Significance Index: -29.7200
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -0.8587
Cell Significance Index: -43.4000
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: -0.9588
Cell Significance Index: -28.1600
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -1.0396
Cell Significance Index: -27.8100
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -1.0464
Cell Significance Index: -33.5200
Cell Name: microcirculation associated smooth muscle cell (CL0008035)
Fold Change: -1.0738
Cell Significance Index: -9.0200
Cell Name: OFF midget ganglion cell (CL4033047)
Fold Change: -1.1323
Cell Significance Index: -14.1200
Cell Name: cone retinal bipolar cell (CL0000752)
Fold Change: -1.1391
Cell Significance Index: -8.7800
Cell Name: periportal region hepatocyte (CL0019026)
Fold Change: -1.2456
Cell Significance Index: -18.3900
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -1.3122
Cell Significance Index: -80.4500
Cell Name: basal cell of epidermis (CL0002187)
Fold Change: -1.3498
Cell Significance Index: -20.5000
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: -1.3526
Cell Significance Index: -23.1800

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 Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**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.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

ARNT-interacting protein

Genular Protein ID: 373320539

Symbol: HIF1A_HUMAN

Name: ARNT-interacting protein

UniProtKB Accession Codes:

Q16665 C0LZJ3 Q53XP6 Q96PT9 Q9UPB1

Database IDs:

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.

Details for: HIF1A

Associated with

Cells (max top 100)

Other Information

Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. PubMed ID: 7539918

Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway. PubMed ID: 9079689

The human hypoxia-inducible factor 1alpha gene: HIF1A structure and evolutionary conservation. PubMed ID: 9782081

Preferential expression of the novel alternative isoform I.3 of hypoxia-inducible factor 1alpha in activated human T lymphocytes. PubMed ID: 18638657

The DNA sequence and analysis of human chromosome 14. PubMed ID: 12508121

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

An essential role for p300/CBP in the cellular response to hypoxia. PubMed ID: 8917528

Transactivation and inhibitory domains of hypoxia-inducible factor 1alpha. Modulation of transcriptional activity by oxygen tension. PubMed ID: 9235919

Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1alpha. PubMed ID: 9822602

Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway. PubMed ID: 9653127

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

Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1. PubMed ID: 9887100

Drosophila von Hippel-Lindau tumor suppressor complex possesses E3 ubiquitin ligase activity. PubMed ID: 11006129

Mechanism of regulation of the hypoxia-inducible factor-1 alpha by the von Hippel-Lindau tumor suppressor protein. PubMed ID: 10944113

Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha. PubMed ID: 10594042

Hypoxia-inducible factor 1alpha protein expression is controlled by oxygen-regulated ubiquitination that is disrupted by deletions and missense mutations. PubMed ID: 10758161

Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation. PubMed ID: 11566883

Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7. PubMed ID: 11389899

Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. PubMed ID: 11292861

Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation. PubMed ID: 12464182

FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. PubMed ID: 12080085

Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor. PubMed ID: 12351678

S-nitrosation of Cys-800 of HIF-1alpha protein activates its interaction with p300 and stimulates its transcriptional activity. PubMed ID: 12914934

HIF-1 alpha protein as a target for S-nitrosation. PubMed ID: 12560087

Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2. PubMed ID: 12778114

Sumoylation increases HIF-1alpha stability and its transcriptional activity. PubMed ID: 15465032

Molecular cloning and characterization of the von Hippel-Lindau-like protein. PubMed ID: 14757845

VHL protein-interacting deubiquitinating enzyme 2 deubiquitinates and stabilizes HIF-1alpha. PubMed ID: 15776016

Interaction between HIF-1 alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1 alpha. PubMed ID: 16288748

Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha. PubMed ID: 16543236

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

SUMOylation of hypoxia-inducible factor-1alpha reduces its transcriptional activity. PubMed ID: 17610843

RSUME, a small RWD-containing protein, enhances SUMO conjugation and stabilizes HIF-1alpha during hypoxia. PubMed ID: 17956732

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

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

Transcriptional activation of HIF-1 by RORalpha and its role in hypoxia signaling. PubMed ID: 18658046

HIF-1 regulation: not so easy come, easy go. PubMed ID: 18809331

Transcriptional regulation of hypoxia-inducible factor 1alpha by HIPK2 suggests a novel mechanism to restrain tumor growth. PubMed ID: 19046997

HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters mitochondrial distribution and transport. PubMed ID: 19528298

Hypoxia-inducible protein 2 is a novel lipid droplet protein and a specific target gene of hypoxia-inducible factor-1. PubMed ID: 20624928

Plk3 functions as an essential component of the hypoxia regulatory pathway by direct phosphorylation of HIF-1alpha. PubMed ID: 20889502

Casein kinase 1 regulates human hypoxia-inducible factor HIF-1. PubMed ID: 20699359

UBXN7 docks on neddylated cullin complexes using its UIM motif and causes HIF1alpha accumulation. PubMed ID: 22537386

RSUME is implicated in HIF-1-induced VEGF-A production in pituitary tumour cells. PubMed ID: 22009797

Ubiquitin-specific protease 19 (USP19) regulates hypoxia-inducible factor 1alpha (HIF-1alpha) during hypoxia. PubMed ID: 22128162

The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity. PubMed ID: 22286099

DCNL1 functions as a substrate sensor and activator of cullin 2-RING ligase. PubMed ID: 23401859

In silico structural and functional characterization of the RSUME splice variants. PubMed ID: 23469069

SIRT2 regulates tumour hypoxia response by promoting HIF-1alpha hydroxylation. PubMed ID: 24681946

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

Myeloid translocation gene-16 co-repressor promotes degradation of hypoxia-inducible factor 1. PubMed ID: 25974097

UCHL1 provides diagnostic and antimetastatic strategies due to its deubiquitinating effect on HIF-1alpha. PubMed ID: 25615526

The vacuolar-ATPase complex and assembly factors, TMEM199 and CCDC115, control HIF1alpha prolyl hydroxylation by regulating cellular iron levels. PubMed ID: 28296633

A pathogen-derived effector modulates host glucose metabolism by arginine GlcNAcylation of HIF-1alpha protein. PubMed ID: 30125331

Elevated Glucose Levels Favor SARS-CoV-2 Infection and Monocyte Response through a HIF-1alpha/Glycolysis-Dependent Axis. PubMed ID: 32697943

A model for the complex between the hypoxia-inducible factor-1 (HIF-1) and its consensus DNA sequence. PubMed ID: 11089639

Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha. PubMed ID: 12446723

Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha. PubMed ID: 11959990

Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response. PubMed ID: 11959977

Structure of an HIF-1alpha-pVHL complex: hydroxyproline recognition in signaling. PubMed ID: 12004076

Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL. PubMed ID: 12050673