Protein:HIF3A |
Protein Summary |
 Gene summary |
| Gene name: HIF3A | ASpdb.0 ID: 64344 | Gene | Gene symbol | HIF3A | Gene ID | 64344 |
| Gene name | hypoxia inducible factor 3 subunit alpha |
| Synonyms | HIF-3A|HIF3-alpha-1|IPAS|MOP7|PASD7|bHLHe17 |
| Cytomap | 19q13.32 |
| Type of gene | protein-coding |
| Description | hypoxia-inducible factor 3-alphaPAS domain-containing protein 7basic-helix-loop-helix-PAS protein MOP7class E basic helix-loop-helix protein 17hypoxia inducible factor 3 alpha subunitinhibitory PAS domain proteinmember of PAS protein 7 |
| Modification date | 20240411 |
| UniProtAcc | Q9Y2N7 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | HIF3A | GO:0000785 | chromatin | 31768607 |
| Gene | HIF3A | GO:0000978 | RNA polymerase II cis-regulatory region sequence-specific DNA binding | 31768607 |
| Gene | HIF3A | GO:0000981 | DNA-binding transcription factor activity, RNA polymerase II-specific | 11573933|31768607 |
| Gene | HIF3A | GO:0005654 | nucleoplasm | - |
| Gene | HIF3A | GO:0005829 | cytosol | - |
| Gene | HIF3A | GO:0005886 | plasma membrane | - |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| Q9Y2N7-1 | Q9Y2N7-1_4wn5_A.pdb | 4WN5 | X-ray | 1.15 | A | 237 | 343 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| Q9Y2N7 | HIF3A | Q9Y2N7-1 | Q9Y2N7-2 | 669 | 667 | 1 | 8 | Substitution | MALGLQRA | MDWQDH | 1 | 6 |
| Q9Y2N7 | HIF3A | Q9Y2N7-1 | Q9Y2N7-3 | 669 | 632 | 611 | 669 | Substitution | SFLLTGGPAPGSLQDPSTPLLNLNEPLGLGPSLLSPYSDEDTTQPGGPFQPRAGSAQAD | VCWGINGILWPSLPSWLKPTVL | 611 | 632 |
| Q9Y2N7 | HIF3A | Q9Y2N7-1 | Q9Y2N7-4 | 669 | 363 | 293 | 363 | Substitution | LLSKGQAVTGQYRFLARSGGYLWTQTQATVVSGGRGPQSESIVCVHFLISQVEETGVVLSLEQTEQHSRRP | CMYPISPGAKPAATWPPADTRTPQLPIPQDALPPHLNTSSLLPKPQGTVSFLAPSYPVPRSFSPHLPPWWP | 293 | 363 |
| Q9Y2N7 | HIF3A | Q9Y2N7-1 | Q9Y2N7-4 | 669 | 363 | 364 | 669 | Deletion | none | none | 363 | 363 |
| Q9Y2N7 | HIF3A | Q9Y2N7-1 | Q9Y2N7-5 | 669 | 613 | 1 | 56 | Deletion | none | none | 0 | 0 |
| Q9Y2N7 | HIF3A | Q9Y2N7-1 | Q9Y2N7-6 | 669 | 583 | 1 | 86 | Deletion | none | none | 0 | 0 |
| Q9Y2N7 | HIF3A | Q9Y2N7-1 | Q9Y2N7-6 | 669 | 583 | 87 | 137 | Substitution | ACYLKALEGFVMVLTAEGDMAYLSENVSKHLGLSQLELIGHSIFDFIHPCD | MRPAAGAARRPRCCTSWLTRCPSPAASAPTWTRPLSCASPSATCACTASAP | 1 | 51 |
| Q9Y2N7 | HIF3A | Q9Y2N7-1 | Q9Y2N7-7 | 669 | 600 | 1 | 120 | Substitution | MALGLQRARSTTELRKEKSRDAARSRRSQETEVLYQLAHTLPFARGVSAHLDKASIMRLTISYLRMHRLCAAGEWNQVGAGGEPLDACYLKALEGFVMVLTAEGDMAYLSENVSKHLGLS | MRPAAGAARRPRCCTSWLTRCPSPAASAPTWTRPLSCASPSATCACTASAP | 1 | 51 |
| Multiple sequence alignment of our canonical and alternatively spliced HIF3A |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of HIF3A |
| UniProt-id | ENSG | ENST | ENSP |
| Q9Y2N7-1 | ENSG00000124440.16 | ENST00000377670.9 | ENSP00000366898.3 |
| Q9Y2N7-2 | ENSG00000124440.16 | ENST00000300862.7 | ENSP00000300862.3 |
| Q9Y2N7-7 | ENSG00000124440.16 | ENST00000244303.10 | ENSP00000244303.6 |
| UniProt-id | NM ID | NP ID |
| Q9Y2N7-1 | NM_152795.3 | NP_690008.2 |
| Q9Y2N7-2 | NM_152794.3 | NP_690007.1 |
| Q9Y2N7-7 | NM_022462.4 | NP_071907.4 |
| Amino acid sequences of our canonical and alternatively spliced HIF3A |
| accession_id | Protein sequence |
| Q9Y2N7-1 | MALGLQRARSTTELRKEKSRDAARSRRSQETEVLYQLAHTLPFARGVSAHLDKASIMRLTISYLRMHRLCAAGEWNQVGAGGEPLDACYL KALEGFVMVLTAEGDMAYLSENVSKHLGLSQLELIGHSIFDFIHPCDQEELQDALTPQQTLSRRKVEAPTERCFSLRMKSTLTSRGRTLN LKAATWKVLNCSGHMRAYKPPAQTSPAGSPDSEPPLQCLVLICEAIPHPGSLEPPLGRGAFLSRHSLDMKFTYCDDRIAEVAGYSPDDLI GCSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQATVVSGGRGPQSESIVCVHFLISQVEETGVVLSLEQTEQHS RRPIQRGAPSQKDTPNPGDSLDTPGPRILAFLHPPSLSEAALAADPRRFCSPDLRRLLGPILDGASVAATPSTPLATRHPQSPLSADLPD ELPVGTENVHRLFTSGKDTEAVETDLDIAQDADALDLEMLAPYISMDDDFQLNASEQLPRAYHRPLGAVPRPRARSFHGLSPPALEPSLL PRWGSDPRLSCSSPSRGDPSASSPMAGARKRTLAQSSEDEDEGVELLGVRPPKRSPSPEHENFLLFPLSLSFLLTGGPAPGSLQDPSTPL |
| Q9Y2N7-2 | MDWQDHRSTTELRKEKSRDAARSRRSQETEVLYQLAHTLPFARGVSAHLDKASIMRLTISYLRMHRLCAAGEWNQVGAGGEPLDACYLKA LEGFVMVLTAEGDMAYLSENVSKHLGLSQLELIGHSIFDFIHPCDQEELQDALTPQQTLSRRKVEAPTERCFSLRMKSTLTSRGRTLNLK AATWKVLNCSGHMRAYKPPAQTSPAGSPDSEPPLQCLVLICEAIPHPGSLEPPLGRGAFLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGC SAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQATVVSGGRGPQSESIVCVHFLISQVEETGVVLSLEQTEQHSRR PIQRGAPSQKDTPNPGDSLDTPGPRILAFLHPPSLSEAALAADPRRFCSPDLRRLLGPILDGASVAATPSTPLATRHPQSPLSADLPDEL PVGTENVHRLFTSGKDTEAVETDLDIAQDADALDLEMLAPYISMDDDFQLNASEQLPRAYHRPLGAVPRPRARSFHGLSPPALEPSLLPR WGSDPRLSCSSPSRGDPSASSPMAGARKRTLAQSSEDEDEGVELLGVRPPKRSPSPEHENFLLFPLSLSFLLTGGPAPGSLQDPSTPLLN |
| Q9Y2N7-3 | MALGLQRARSTTELRKEKSRDAARSRRSQETEVLYQLAHTLPFARGVSAHLDKASIMRLTISYLRMHRLCAAGEWNQVGAGGEPLDACYL KALEGFVMVLTAEGDMAYLSENVSKHLGLSQLELIGHSIFDFIHPCDQEELQDALTPQQTLSRRKVEAPTERCFSLRMKSTLTSRGRTLN LKAATWKVLNCSGHMRAYKPPAQTSPAGSPDSEPPLQCLVLICEAIPHPGSLEPPLGRGAFLSRHSLDMKFTYCDDRIAEVAGYSPDDLI GCSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQATVVSGGRGPQSESIVCVHFLISQVEETGVVLSLEQTEQHS RRPIQRGAPSQKDTPNPGDSLDTPGPRILAFLHPPSLSEAALAADPRRFCSPDLRRLLGPILDGASVAATPSTPLATRHPQSPLSADLPD ELPVGTENVHRLFTSGKDTEAVETDLDIAQDADALDLEMLAPYISMDDDFQLNASEQLPRAYHRPLGAVPRPRARSFHGLSPPALEPSLL PRWGSDPRLSCSSPSRGDPSASSPMAGARKRTLAQSSEDEDEGVELLGVRPPKRSPSPEHENFLLFPLSLVCWGINGILWPSLPSWLKPT |
| Q9Y2N7-4 | MALGLQRARSTTELRKEKSRDAARSRRSQETEVLYQLAHTLPFARGVSAHLDKASIMRLTISYLRMHRLCAAGEWNQVGAGGEPLDACYL KALEGFVMVLTAEGDMAYLSENVSKHLGLSQLELIGHSIFDFIHPCDQEELQDALTPQQTLSRRKVEAPTERCFSLRMKSTLTSRGRTLN LKAATWKVLNCSGHMRAYKPPAQTSPAGSPDSEPPLQCLVLICEAIPHPGSLEPPLGRGAFLSRHSLDMKFTYCDDRIAEVAGYSPDDLI GCSAYEYIHALDSDAVSKSIHTCMYPISPGAKPAATWPPADTRTPQLPIPQDALPPHLNTSSLLPKPQGTVSFLAPSYPVPRSFSPHLPP |
| Q9Y2N7-5 | MRLTISYLRMHRLCAAGEWNQVGAGGEPLDACYLKALEGFVMVLTAEGDMAYLSENVSKHLGLSQLELIGHSIFDFIHPCDQEELQDALT PQQTLSRRKVEAPTERCFSLRMKSTLTSRGRTLNLKAATWKVLNCSGHMRAYKPPAQTSPAGSPDSEPPLQCLVLICEAIPHPGSLEPPL GRGAFLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQATVVSGG RGPQSESIVCVHFLISQVEETGVVLSLEQTEQHSRRPIQRGAPSQKDTPNPGDSLDTPGPRILAFLHPPSLSEAALAADPRRFCSPDLRR LLGPILDGASVAATPSTPLATRHPQSPLSADLPDELPVGTENVHRLFTSGKDTEAVETDLDIAQDADALDLEMLAPYISMDDDFQLNASE QLPRAYHRPLGAVPRPRARSFHGLSPPALEPSLLPRWGSDPRLSCSSPSRGDPSASSPMAGARKRTLAQSSEDEDEGVELLGVRPPKRSP |
| Q9Y2N7-6 | MRPAAGAARRPRCCTSWLTRCPSPAASAPTWTRPLSCASPSATCACTASAPQEELQDALTPQQTLSRRKVEAPTERCFSLRMKSTLTSRG RTLNLKAATWKVLNCSGHMRAYKPPAQTSPAGSPDSEPPLQCLVLICEAIPHPGSLEPPLGRGAFLSRHSLDMKFTYCDDRIAEVAGYSP DDLIGCSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQATVVSGGRGPQSESIVCVHFLISQVEETGVVLSLEQT EQHSRRPIQRGAPSQKDTPNPGDSLDTPGPRILAFLHPPSLSEAALAADPRRFCSPDLRRLLGPILDGASVAATPSTPLATRHPQSPLSA DLPDELPVGTENVHRLFTSGKDTEAVETDLDIAQDADALDLEMLAPYISMDDDFQLNASEQLPRAYHRPLGAVPRPRARSFHGLSPPALE PSLLPRWGSDPRLSCSSPSRGDPSASSPMAGARKRTLAQSSEDEDEGVELLGVRPPKRSPSPEHENFLLFPLSLSFLLTGGPAPGSLQDP |
| Q9Y2N7-7 | MRPAAGAARRPRCCTSWLTRCPSPAASAPTWTRPLSCASPSATCACTASAPQLELIGHSIFDFIHPCDQEELQDALTPQQTLSRRKVEAP TERCFSLRMKSTLTSRGRTLNLKAATWKVLNCSGHMRAYKPPAQTSPAGSPDSEPPLQCLVLICEAIPHPGSLEPPLGRGAFLSRHSLDM KFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQATVVSGGRGPQSESIVCVHF LISQVEETGVVLSLEQTEQHSRRPIQRGAPSQKDTPNPGDSLDTPGPRILAFLHPPSLSEAALAADPRRFCSPDLRRLLGPILDGASVAA TPSTPLATRHPQSPLSADLPDELPVGTENVHRLFTSGKDTEAVETDLDIAQDADALDLEMLAPYISMDDDFQLNASEQLPRAYHRPLGAV PRPRARSFHGLSPPALEPSLLPRWGSDPRLSCSSPSRGDPSASSPMAGARKRTLAQSSEDEDEGVELLGVRPPKRSPSPEHENFLLFPLS |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| HIF3A (go to UniProt):Q9Y2N7 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q9Y2N7 | Domain | 14 | 67 | Note=BHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981 | Type=Deletion;Start=1;End=56 |
| Q9Y2N7 | Domain | 14 | 67 | Note=BHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981 | Type=Deletion;Start=1;End=86 |
| Q9Y2N7 | Domain | 14 | 67 | Note=BHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981 | Type=Substitution;Start=1;End=120 |
| Q9Y2N7 | Domain | 82 | 154 | Note=PAS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00140 | Type=Deletion;Start=1;End=86 |
| Q9Y2N7 | Domain | 82 | 154 | Note=PAS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00140 | Type=Substitution;Start=87;End=137 |
| Q9Y2N7 | Domain | 82 | 154 | Note=PAS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00140 | Type=Substitution;Start=1;End=120 |
| Q9Y2N7 | Domain | 227 | 297 | Note=PAS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00140 | Type=Substitution;Start=293;End=363 |
| Q9Y2N7 | Region | 1 | 27 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=1;End=8 |
| Q9Y2N7 | Region | 1 | 27 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=56 |
| Q9Y2N7 | Region | 1 | 27 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=86 |
| Q9Y2N7 | Region | 1 | 27 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=1;End=120 |
| Q9Y2N7 | Region | 77 | 100 | Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q0VBL6 | Type=Deletion;Start=1;End=86 |
| Q9Y2N7 | Region | 77 | 100 | Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q0VBL6 | Type=Substitution;Start=87;End=137 |
| Q9Y2N7 | Region | 77 | 100 | Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q0VBL6 | Type=Substitution;Start=1;End=120 |
| Q9Y2N7 | Region | 354 | 389 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=293;End=363 |
| Q9Y2N7 | Region | 354 | 389 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=364;End=669 |
| Q9Y2N7 | Region | 430 | 451 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=364;End=669 |
| Q9Y2N7 | Region | 452 | 581 | Note=ODD | Type=Deletion;Start=364;End=669 |
| Q9Y2N7 | Region | 454 | 506 | Note=NTAD | Type=Deletion;Start=364;End=669 |
| Q9Y2N7 | Region | 523 | 600 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=364;End=669 |
| Q9Y2N7 | Region | 619 | 669 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=611;End=669 |
| Q9Y2N7 | Region | 619 | 669 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=364;End=669 |
| Q9Y2N7 | Motif | 414 | 418 | Note=LRRLL | Type=Deletion;Start=364;End=669 |
| Q9Y2N7 | Motif | 490 | 497 | Note=LAPYISMD | Type=Deletion;Start=364;End=669 |
| Q9Y2N7 | Compositional bias | 10 | 27 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=56 |
| Q9Y2N7 | Compositional bias | 10 | 27 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=86 |
| Q9Y2N7 | Compositional bias | 10 | 27 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=1;End=120 |
| Q9Y2N7 | Compositional bias | 354 | 378 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=293;End=363 |
| Q9Y2N7 | Compositional bias | 354 | 378 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=364;End=669 |
| Q9Y2N7 | Compositional bias | 573 | 588 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=364;End=669 |
| Q9Y2N7 | Compositional bias | 646 | 669 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=611;End=669 |
| Q9Y2N7 | Compositional bias | 646 | 669 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=364;End=669 |
Gene Isoform Structures and Expression Levels for HIF3A |
| Gene structures of our canonical and alternative spliced genes of HIF3A * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of Q9Y2N7-1 |
| 3D view using mol* of Q9Y2N7-2 |
| 3D view using mol* of Q9Y2N7-3 |
| 3D view using mol* of Q9Y2N7-4 |
| 3D view using mol* of Q9Y2N7-5 |
| 3D view using mol* of Q9Y2N7-6 |
| 3D view using mol* of Q9Y2N7-7 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of Q9Y2N7-1 |
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| pLDDT distribution across the protein length of Q9Y2N7-2 |
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| pLDDT distribution across the protein length of Q9Y2N7-3 |
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| pLDDT distribution across the protein length of Q9Y2N7-4 |
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| pLDDT distribution across the protein length of Q9Y2N7-5 |
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| pLDDT distribution across the protein length of Q9Y2N7-6 |
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| pLDDT distribution across the protein length of Q9Y2N7-7 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of Q9Y2N7-1 |
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| Ramachandran plot of Q9Y2N7-2 |
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| Ramachandran plot of Q9Y2N7-3 |
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| Ramachandran plot of Q9Y2N7-4 |
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| Ramachandran plot of Q9Y2N7-5 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| Q9Y2N7-1 | 1.116 | 54 | 1.141 | 71.344 | 0.325 | 0.987 | 1.301 | 4.415 | 0.435 | 10.156 | 1.888 | 241,245,249,251,274,277,278,286,289,290,293,299,30 0,301,304,306,318,320,336,338 |
| Q9Y2N7-2 | 1.092 | 52 | 1.106 | 78.547 | 0.316 | 0.987 | 1.283 | 4.622 | 0.502 | 9.206 | 2.909 | 239,243,247,249,272,276,284,287,288,291,297,299,30 2,304,316,318,334,336 |
| Q9Y2N7-3 | 1.025 | 91 | 1.067 | 164.297 | 0.533 | 0.713 | 0.894 | 1.634 | 0.789 | 2.071 | 0.836 | 41,42,43,44,59,62,63,66,107,108,110,111,114,120,12 1,122,125,623,624,626,627 |
| Q9Y2N7-4 | 1.03 | 478 | 1.067 | 1484.847 | 0.54 | 0.705 | 0.915 | 0.759 | 0.907 | 0.836 | 1.337 | 93,94,140,143,144,162,163,164,165,170,172,173,174, 185,186,187,188,190,224,225,226,227,228,229,231,23 2,237,240,241,242,243,245,249,251,258,261,262,264, 269,274,276,277,278,279,280,282,285,286,288,289,29 0,292,293,294,295,296,297,339,340,341,342,343,344, 345,346,347,348,349,350,351,352,353,354,355,356 |
| Q9Y2N7-5 | 1.097 | 56 | 1.105 | 77.518 | 0.385 | 0.988 | 1.244 | 3.778 | 0.585 | 6.455 | 3.111 | 185,189,193,195,202,213,218,222,230,233,234,237,24 3,244,245,248,250,262,264,280,282 |
| Q9Y2N7-6 | 1.042 | 112 | 1.091 | 229.81 | 0.484 | 0.696 | 0.994 | 1.225 | 0.818 | 1.496 | 0.901 | 19,20,21,22,23,24,26,29,30,31,32,33,56,59,60,61,12 8,129,130,131 |
| Q9Y2N7-7 | 1.028 | 245 | 1.086 | 592.704 | 0.495 | 0.664 | 0.905 | 0.759 | 0.774 | 0.98 | 1.183 | 14,15,16,17,18,19,20,41,43,44,45,47,52,56,57,129,1 30,131,132,133,134,136,140,141,142,143,144,146,147 ,149,151,152,153,538,539,540,541,542,543,544,545,5 46,547,548 |
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of Q9Y2N7-1_Q9Y2N7-1_4wn5_A.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q9Y2N7-1_4wn5_A_Q9Y2N7-2.pdb |
| 3D view using mol* of Q9Y2N7-1_4wn5_A_Q9Y2N7-3.pdb |
| 3D view using mol* of Q9Y2N7-1_4wn5_A_Q9Y2N7-4.pdb |
| 3D view using mol* of Q9Y2N7-1_4wn5_A_Q9Y2N7-5.pdb |
| 3D view using mol* of Q9Y2N7-1_4wn5_A_Q9Y2N7-6.pdb |
| 3D view using mol* of Q9Y2N7-1_4wn5_A_Q9Y2N7-7.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q9Y2N7-1_Q9Y2N7-2.pdb |
| 3D view using mol* of Q9Y2N7-1_Q9Y2N7-3.pdb |
| 3D view using mol* of Q9Y2N7-1_Q9Y2N7-4.pdb |
| 3D view using mol* of Q9Y2N7-1_Q9Y2N7-5.pdb |
| 3D view using mol* of Q9Y2N7-1_Q9Y2N7-6.pdb |
| 3D view using mol* of Q9Y2N7-1_Q9Y2N7-7.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/Q9Y2N7-1_vs_Q9Y2N7-2.png |
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| ./stats/secondary_structure/figure/Q9Y2N7-1_vs_Q9Y2N7-3.png |
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| ./stats/secondary_structure/figure/Q9Y2N7-1_vs_Q9Y2N7-4.png |
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| ./stats/secondary_structure/figure/Q9Y2N7-1_vs_Q9Y2N7-5.png |
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| ./stats/secondary_structure/figure/Q9Y2N7-1_vs_Q9Y2N7-6.png |
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| ./stats/secondary_structure/figure/Q9Y2N7-1_vs_Q9Y2N7-7.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/Q9Y2N7-1_vs_Q9Y2N7-2.png |
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| ./stats/relative_asa/Q9Y2N7-1_vs_Q9Y2N7-3.png |
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| ./stats/relative_asa/Q9Y2N7-1_vs_Q9Y2N7-4.png |
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| ./stats/relative_asa/Q9Y2N7-1_vs_Q9Y2N7-5.png |
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| ./stats/relative_asa/Q9Y2N7-1_vs_Q9Y2N7-6.png |
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| ./stats/relative_asa/Q9Y2N7-1_vs_Q9Y2N7-7.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to HIF3A |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to HIF3A |
| Previous studies relating to the alternative splicing of HIF3A and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| HIF3A | 12119283 | Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxia-inducible factor-3alpha locus. | The inhibitory PAS (Per/Arnt/Sim) domain protein, IPAS, functions as a dominant negative regulator of hypoxia-inducible transcription factors (HIFs) by forming complexes with those proteins that fail to bind to hypoxia response elements of target genes. We have previously observed that IPAS is predominantly expressed in mice in Purkinje cells of the cerebellum and in corneal epithelium of the eye where it appears to play a role in negative regulation of angiogenesis and maintenance of an avascular phenotype. Sequencing of the mouse IPAS genomic structure revealed that IPAS is a splicing variant of the HIF-3alpha locus. Thus, in addition to three unique exons (1a, 4a, and 16) IPAS shares three exons (2, 4, and 5) with HIF-3alpha as well as alternatively spliced variants of exons 3 and 6. In experiments using normal mice and mice exposed to hypoxia (6% O(2)) for 6 h we observed alternative splicing of the HIF-3alpha transcript in the heart and lung. The alternatively spliced transcript was only observed under hypoxic conditions, thus defining a novel mechanism of hypoxia-dependent regulation of gene expression. Importantly, this mechanism may establish negative feedback loop regulation of adaptive responses to hypoxia/ischemia in these tissues. | D000860 | Hypoxia |
| HIF3A | 12119283 | Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxia-inducible factor-3alpha locus. | The inhibitory PAS (Per/Arnt/Sim) domain protein, IPAS, functions as a dominant negative regulator of hypoxia-inducible transcription factors (HIFs) by forming complexes with those proteins that fail to bind to hypoxia response elements of target genes. We have previously observed that IPAS is predominantly expressed in mice in Purkinje cells of the cerebellum and in corneal epithelium of the eye where it appears to play a role in negative regulation of angiogenesis and maintenance of an avascular phenotype. Sequencing of the mouse IPAS genomic structure revealed that IPAS is a splicing variant of the HIF-3alpha locus. Thus, in addition to three unique exons (1a, 4a, and 16) IPAS shares three exons (2, 4, and 5) with HIF-3alpha as well as alternatively spliced variants of exons 3 and 6. In experiments using normal mice and mice exposed to hypoxia (6% O(2)) for 6 h we observed alternative splicing of the HIF-3alpha transcript in the heart and lung. The alternatively spliced transcript was only observed under hypoxic conditions, thus defining a novel mechanism of hypoxia-dependent regulation of gene expression. Importantly, this mechanism may establish negative feedback loop regulation of adaptive responses to hypoxia/ischemia in these tissues. | D009389 | Neovascularization, Pathologic |
| HIF3A | 20416395 | Hypoxia-inducible factor (HIF)-3alpha is subject to extensive alternative splicing in human tissues and cancer cells and is regulated by HIF-1 but not HIF-2. | The hypoxia-inducible transcription factors (HIFs) play a central role in the response of cells to hypoxia. HIFs are alphabeta dimers, the human alpha subunit having three isoforms. HIF-3alpha is unique among the HIF-alpha isoforms in that its gene is subject to extensive alternative splicing. Database analyses have predicted the generation of six HIF-3alpha splice variants that utilize three alternative transcription initiation sites. None of these variants is likely to act as an efficient transcription factor, but some of them have been reported to inhibit HIF-1 and HIF-2 functions. We analyzed here for the first time in detail whether these six variants are indeed generated in various human tissues and cell lines. We identified four novel variants, named here HIF-3alpha7 to HIF-3alpha10, whereas we obtained no evidence for the predicted HIF-3alpha3 and HIF-3alpha5. Distinct differences in the expression patterns of the variants were found between human tissues, the levels being particularly low in many cancer cell lines. Hypoxia upregulated transcription from all three alternative HIF-3alpha promoters. siRNA experiments showed that this induction is mediated specifically by HIF-1 and not by HIF-2. The tissue-specific differences in the expression patterns and levels of the HIF-3alpha variants can be expected to modulate the hypoxia response of various tissues and cell types to different extents during development and in pathological situations. A further level of regulation is brought about by the fact that the levels of the HIF-3alpha transcripts themselves are regulated by hypoxia and by changes in HIF-1 levels. | D009369 | Neoplasms |
Clinically important variants in HIF3A |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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