Protein:BIRC5 |
Protein Summary |
 Gene summary |
| Gene name: BIRC5 | ASpdb.0 ID: 332 | Gene | Gene symbol | BIRC5 | Gene ID | 332 |
| Gene name | baculoviral IAP repeat containing 5 |
| Synonyms | API4|EPR-1 |
| Cytomap | 17q25.3 |
| Type of gene | protein-coding |
| Description | baculoviral IAP repeat-containing protein 5apoptosis inhibitor 4apoptosis inhibitor survivin |
| Modification date | 20240323 |
| UniProtAcc | O15392 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | BIRC5 | GO:0000228 | nuclear chromosome | 16322459 |
| Gene | BIRC5 | GO:0000775 | chromosome, centromeric region | 11084331|16322459 |
| Gene | BIRC5 | GO:0000776 | kinetochore | 15665297 |
| Gene | BIRC5 | GO:0005634 | nucleus | 15665297|20627126|20826784|21364656 |
| Gene | BIRC5 | GO:0005737 | cytoplasm | 20627126|21364656 |
| Gene | BIRC5 | GO:0005829 | cytosol | 18591255 |
| Gene | BIRC5 | GO:0006468 | protein phosphorylation | 21252625 |
| Gene | BIRC5 | GO:0015630 | microtubule cytoskeleton | 9859993 |
| Gene | BIRC5 | GO:0030496 | midbody | 11084331|15665297 |
| Gene | BIRC5 | GO:0043066 | negative regulation of apoptotic process | 10949038|20627126|21364656 |
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 |
| O15392-1 | O15392-1_3ued_C.pdb | 3UED | X-ray | 2.7 | C | 4 | 142 |
| 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 |
| O15392 | BIRC5 | O15392-1 | O15392-2 | 142 | 165 | 74 | 74 | Substitution | I | IGPGTVAYACNTSTLGGRGGRITR | 74 | 97 |
| O15392 | BIRC5 | O15392-1 | O15392-3 | 142 | 137 | 74 | 142 | Substitution | IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD | MQRKPTIRRKNLRKLRRKCAVPSSSWLPWIEASGRSCLVPEWLHHFQGLFPGATSLPVGPLAMS | 74 | 137 |
| O15392 | BIRC5 | O15392-1 | O15392-4 | 142 | 120 | 114 | 142 | Substitution | AKETNNKKKEFEETAKKVRRAIEQLAAMD | ERALLAE | 114 | 120 |
| O15392 | BIRC5 | O15392-1 | O15392-5 | 142 | 117 | 105 | 142 | Substitution | DRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD | VRETLPPPRSFIR | 105 | 117 |
| O15392 | BIRC5 | O15392-1 | O15392-6 | 142 | 78 | 74 | 142 | Substitution | IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD | MRELC | 74 | 78 |
| O15392 | BIRC5 | O15392-1 | O15392-7 | 142 | 74 | 74 | 142 | Substitution | IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD | M | 74 | 74 |
| Multiple sequence alignment of our canonical and alternatively spliced BIRC5 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of BIRC5 |
| UniProt-id | ENSG | ENST | ENSP |
| O15392-3 | ENSG00000089685.15 | ENST00000374948.6 | ENSP00000364086.1 |
| O15392-4 | ENSG00000089685.15 | ENST00000590925.6 | ENSP00000467336.1 |
| O15392-6 | ENSG00000089685.15 | ENST00000592734.5 | ENSP00000466617.1 |
| O15392-7 | ENSG00000089685.15 | ENST00000590449.1 | ENSP00000465868.1 |
| UniProt-id | NM ID | NP ID |
| O15392-3 | NM_001012270.1 | NP_001012270.1 |
| Amino acid sequences of our canonical and alternatively spliced BIRC5 |
| accession_id | Protein sequence |
| O15392-1 | MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVK |
| O15392-2 | MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIGPGTVAYACNTSTLGG |
| O15392-3 | MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPMQRKPTIRRKNLRKLRR |
| O15392-4 | MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVK |
| O15392-5 | MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVK |
| O15392-6 | |
| O15392-7 |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| BIRC5 (go to UniProt):O15392 |
| 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 |
| O15392 | Repeat | 18 | 88 | Note=BIR | Type=Substitution;Start=74;End=74 |
| O15392 | Repeat | 18 | 88 | Note=BIR | Type=Substitution;Start=74;End=142 |
| O15392 | Repeat | 18 | 88 | Note=BIR | Type=Substitution;Start=74;End=142 |
| O15392 | Repeat | 18 | 88 | Note=BIR | Type=Substitution;Start=74;End=142 |
Gene Isoform Structures and Expression Levels for BIRC5 |
| Gene structures of our canonical and alternative spliced genes of BIRC5 * 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 O15392-1 |
| 3D view using mol* of O15392-2 |
| 3D view using mol* of O15392-3 |
| 3D view using mol* of O15392-4 |
| 3D view using mol* of O15392-5 |
| 3D view using mol* of O15392-6 |
| 3D view using mol* of O15392-7 |
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 O15392-1 |
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| pLDDT distribution across the protein length of O15392-2 |
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| pLDDT distribution across the protein length of O15392-3 |
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| pLDDT distribution across the protein length of O15392-4 |
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| pLDDT distribution across the protein length of O15392-5 |
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| pLDDT distribution across the protein length of O15392-6 |
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| pLDDT distribution across the protein length of O15392-7 |
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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 O15392-1 |
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| Ramachandran plot of O15392-3 |
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| Ramachandran plot of O15392-6 |
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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 |
| O15392-1 | 0.924 | 88 | 0.906 | 183.162 | 0.573 | 0.652 | 0.858 | 0.407 | 1.126 | 0.362 | 1.262 | 13,14,15,16,18,40,41,58,74,86,87,89,90,91,92,93,94 ,95,96,104 |
| O15392-2 | 0.972 | 109 | 0.963 | 235.641 | 0.574 | 0.656 | 0.814 | 0.308 | 1.138 | 0.271 | 1.317 | 13,14,15,16,18,40,41,58,59,74,109,110,112,113,114, 115,116,117,119,127 |
| O15392-3 | 1.092 | 189 | 1.189 | 771.407 | 0.627 | 0.671 | 0.844 | 1.449 | 0.47 | 3.086 | 1.294 | 3,4,5,6,9,10,11,12,13,14,58,59,60,61,84,87,88,91,9 2,93,94,95,96,97,98,99,100,102,103,110,113,115,116 ,118,119,120,122,123 |
| O15392-4 | 0.937 | 89 | 0.855 | 193.109 | 0.564 | 0.665 | 0.858 | 0.187 | 1.322 | 0.142 | 0.97 | 13,14,15,16,18,40,41,58,74,86,87,89,90,91,92,93,94 ,96,104 |
| O15392-5 | 1.014 | 97 | 0.928 | 190.365 | 0.461 | 0.736 | 0.998 | 0.452 | 1.347 | 0.336 | 1.103 | 13,14,15,16,18,40,41,58,59,74,78,86,87,89,90,91,92 ,93,94,96,104 |
| O15392-6 | 0.462 | 18 | 0.414 | 28.126 | 0.795 | 0.45 | 0.559 | 0.262 | 0.783 | 0.335 | 5.177 | 62,64,65,66,67,71,76
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| O15392-7 | 0.47 | 12 | 0.427 | 25.039 | 0.812 | 0.496 | 0.662 | 0.677 | 0.601 | 1.126 | 2.389 | 3,4,11,14,15,16,17
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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 O15392-1_O15392-1_3ued_C.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of O15392-1_3ued_C_O15392-2.pdb |
| 3D view using mol* of O15392-1_3ued_C_O15392-3.pdb |
| 3D view using mol* of O15392-1_3ued_C_O15392-4.pdb |
| 3D view using mol* of O15392-1_3ued_C_O15392-5.pdb |
| 3D view using mol* of O15392-1_3ued_C_O15392-6.pdb |
| 3D view using mol* of O15392-1_3ued_C_O15392-7.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of O15392-1_O15392-2.pdb |
| 3D view using mol* of O15392-1_O15392-3.pdb |
| 3D view using mol* of O15392-1_O15392-4.pdb |
| 3D view using mol* of O15392-1_O15392-5.pdb |
| 3D view using mol* of O15392-1_O15392-6.pdb |
| 3D view using mol* of O15392-1_O15392-7.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/O15392-1_vs_O15392-2.png |
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| ./stats/secondary_structure/figure/O15392-1_vs_O15392-3.png |
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| ./stats/secondary_structure/figure/O15392-1_vs_O15392-4.png |
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| ./stats/secondary_structure/figure/O15392-1_vs_O15392-5.png |
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| ./stats/secondary_structure/figure/O15392-1_vs_O15392-6.png |
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| ./stats/secondary_structure/figure/O15392-1_vs_O15392-7.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/O15392-1_vs_O15392-2.png |
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| ./stats/relative_asa/O15392-1_vs_O15392-3.png |
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| ./stats/relative_asa/O15392-1_vs_O15392-4.png |
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| ./stats/relative_asa/O15392-1_vs_O15392-5.png |
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| ./stats/relative_asa/O15392-1_vs_O15392-6.png |
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| ./stats/relative_asa/O15392-1_vs_O15392-7.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 BIRC5 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| O15392 | BIRC5 | DB05141 | LY2181308 | investigational | |
| O15392 | BIRC5 | DB04115 | Berberine | approved, investigational | |
| O15392 | BIRC5 | DB00206 | Reserpine | approved, investigational, withdrawn |
Related Diseases to BIRC5 |
| Previous studies relating to the alternative splicing of BIRC5 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| BIRC5 | 17127378 | Survivin is not only a death encounter but also a survival protein for invading tumor cells. | Cell proliferation and cell death pathways meet at a pivotal crossroad, crucial to maintain normal homeostasis and to eliminate dangerous cells before they start dividing. Survivin (SVV) is an intriguing and fascinating protein at this crossroad that interfaces life and death, through its dual role in facilitating cell division and encountering apoptosis. SVV's prominent expression in essentially all human malignancies, and low or no expression in most normal tissues, suggests that it would be an ideal target for cancer-directed therapy. However, SVV has been recently described as a target for fine tuning by alternative splicing mechanism generating five defined splice variants and a number of other uncharacterized/bizarre isoforms. This diversity indicates that SVV, in addition to its known functions in tumorgenesis, angiogenesis and cardiovascular diseases, might be associated with other unknown functions. Intriguingly, new accumulating evidence from our own work and others, suggest a novel role for SVV in the mechanisms of tumor invasion and metastasis. The SVV pathway has now provided tangible opportunities for targeted, rational cancer therapy. It is therefore an attractive and promising therapeutic target not only for cancer but also for other diseases. Although a number of studies utilizing SVV as an anti-cancer strategy are well underway, further investigation into the exact molecular interactions underpinning its functions is critical for the success of such trials. Impeding development of safe and effective SVV antagonists for clinical use is due to a lack of understanding the molecular mechanisms by which SVV differentially affects apoptosis and cell division in both normal and malignant cells. In this report, in addition to reviewing the SVV known functions, we discuss the newly proposed mechanisms by which SVV might serve as a survival tool for invading tumor cells. | D009361 | Neoplasm Invasiveness |
| BIRC5 | 17127378 | Survivin is not only a death encounter but also a survival protein for invading tumor cells. | Cell proliferation and cell death pathways meet at a pivotal crossroad, crucial to maintain normal homeostasis and to eliminate dangerous cells before they start dividing. Survivin (SVV) is an intriguing and fascinating protein at this crossroad that interfaces life and death, through its dual role in facilitating cell division and encountering apoptosis. SVV's prominent expression in essentially all human malignancies, and low or no expression in most normal tissues, suggests that it would be an ideal target for cancer-directed therapy. However, SVV has been recently described as a target for fine tuning by alternative splicing mechanism generating five defined splice variants and a number of other uncharacterized/bizarre isoforms. This diversity indicates that SVV, in addition to its known functions in tumorgenesis, angiogenesis and cardiovascular diseases, might be associated with other unknown functions. Intriguingly, new accumulating evidence from our own work and others, suggest a novel role for SVV in the mechanisms of tumor invasion and metastasis. The SVV pathway has now provided tangible opportunities for targeted, rational cancer therapy. It is therefore an attractive and promising therapeutic target not only for cancer but also for other diseases. Although a number of studies utilizing SVV as an anti-cancer strategy are well underway, further investigation into the exact molecular interactions underpinning its functions is critical for the success of such trials. Impeding development of safe and effective SVV antagonists for clinical use is due to a lack of understanding the molecular mechanisms by which SVV differentially affects apoptosis and cell division in both normal and malignant cells. In this report, in addition to reviewing the SVV known functions, we discuss the newly proposed mechanisms by which SVV might serve as a survival tool for invading tumor cells. | D009362 | Neoplasm Metastasis |
| BIRC5 | 17127378 | Survivin is not only a death encounter but also a survival protein for invading tumor cells. | Cell proliferation and cell death pathways meet at a pivotal crossroad, crucial to maintain normal homeostasis and to eliminate dangerous cells before they start dividing. Survivin (SVV) is an intriguing and fascinating protein at this crossroad that interfaces life and death, through its dual role in facilitating cell division and encountering apoptosis. SVV's prominent expression in essentially all human malignancies, and low or no expression in most normal tissues, suggests that it would be an ideal target for cancer-directed therapy. However, SVV has been recently described as a target for fine tuning by alternative splicing mechanism generating five defined splice variants and a number of other uncharacterized/bizarre isoforms. This diversity indicates that SVV, in addition to its known functions in tumorgenesis, angiogenesis and cardiovascular diseases, might be associated with other unknown functions. Intriguingly, new accumulating evidence from our own work and others, suggest a novel role for SVV in the mechanisms of tumor invasion and metastasis. The SVV pathway has now provided tangible opportunities for targeted, rational cancer therapy. It is therefore an attractive and promising therapeutic target not only for cancer but also for other diseases. Although a number of studies utilizing SVV as an anti-cancer strategy are well underway, further investigation into the exact molecular interactions underpinning its functions is critical for the success of such trials. Impeding development of safe and effective SVV antagonists for clinical use is due to a lack of understanding the molecular mechanisms by which SVV differentially affects apoptosis and cell division in both normal and malignant cells. In this report, in addition to reviewing the SVV known functions, we discuss the newly proposed mechanisms by which SVV might serve as a survival tool for invading tumor cells. | D009369 | Neoplasms |
Clinically important variants in BIRC5 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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