Protein:AMPD2 |
Protein Summary |
 Gene summary |
| Gene name: AMPD2 | ASpdb.0 ID: 271 | Gene | Gene symbol | AMPD2 | Gene ID | 271 |
| Gene name | adenosine monophosphate deaminase 2 |
| Synonyms | AMPD|PCH9|SPG63 |
| Cytomap | 1p13.3 |
| Type of gene | protein-coding |
| Description | AMP deaminase 2adenosine monophosphate deaminase 2 (isoform L) |
| Modification date | 20240305 |
| UniProtAcc | Q01433 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | AMPD2 | GO:0005829 | cytosol | - |
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 |
| Q01433-1 | Q01433-1_4no3_C.pdb | 4NO3 | X-ray | 1.7 | C | 165 | 173 |
| 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 |
| Q01433 | AMPD2 | Q01433-1 | Q01433-2 | 879 | 798 | 1 | 81 | Deletion | none | none | 0 | 0 |
| Q01433 | AMPD2 | Q01433-1 | Q01433-2 | 879 | 798 | 82 | 84 | Substitution | AAP | MAS | 1 | 3 |
| Q01433 | AMPD2 | Q01433-1 | Q01433-3 | 879 | 760 | 1 | 128 | Substitution | MRNRGQGLFRLRSRCFLHQSLPLGAGRRKGLDVAEPGPSRCRSDSPAVAAVVPAMASYPSGSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPGPAPCLKHFPLDLRTSMDGKCKEIAE | MLTFLPSPQ | 1 | 9 |
| Q01433 | AMPD2 | Q01433-1 | Q01433-4 | 879 | 804 | 1 | 128 | Substitution | MRNRGQGLFRLRSRCFLHQSLPLGAGRRKGLDVAEPGPSRCRSDSPAVAAVVPAMASYPSGSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPGPAPCLKHFPLDLRTSMDGKCKEIAE | MWQSQAPAGAAQTPPLSPPWSQPWHPIHLALASPRPNIPLRSGPACRPPLQLQ | 1 | 53 |
| Q01433 | AMPD2 | Q01433-1 | Q01433-5 | 879 | 761 | 1 | 118 | Deletion | none | none | 0 | 0 |
| Multiple sequence alignment of our canonical and alternatively spliced AMPD2 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of AMPD2 |
| UniProt-id | ENSG | ENST | ENSP |
| Q01433-1 | ENSG00000116337.20 | ENST00000256578.8 | ENSP00000256578.4 |
| Q01433-1 | ENSG00000116337.20 | ENST00000528667.7 | ENSP00000436541.2 |
| Q01433-2 | ENSG00000116337.20 | ENST00000342115.8 | ENSP00000345498.4 |
| Q01433-2 | ENSG00000116337.20 | ENST00000531734.6 | ENSP00000433739.2 |
| Q01433-5 | ENSG00000116337.20 | ENST00000528454.5 | ENSP00000437164.1 |
| Q01433-5 | ENSG00000116337.20 | ENST00000531203.6 | ENSP00000431975.2 |
| UniProt-id | NM ID | NP ID |
| Q01433-1 | NM_004037.7 | NP_004028.3 |
| Q01433-2 | NM_139156.3 | NP_631895.1 |
| Q01433-4 | NM_001308170.1 | NP_001295099.1 |
| Q01433-5 | NM_001257361.1 | NP_001244290.1 |
| Amino acid sequences of our canonical and alternatively spliced AMPD2 |
| accession_id | Protein sequence |
| Q01433-1 | MRNRGQGLFRLRSRCFLHQSLPLGAGRRKGLDVAEPGPSRCRSDSPAVAAVVPAMASYPSGSGKPKAKYPFKKRASLQASTAAPEARGGL GAPPLQSARSLPGPAPCLKHFPLDLRTSMDGKCKEIAEELFTRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDVKLEPDILLR AKQDFLKTDSDSDLQLYKEQGEGQGDRSLRERDVLEREFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYL QQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYEHCEPSTMPGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVN VLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQ GREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELR LSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDE SKPENHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQ YLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHK |
| Q01433-2 | MASEARGGLGAPPLQSARSLPGPAPCLKHFPLDLRTSMDGKCKEIAEELFTRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDV KLEPDILLRAKQDFLKTDSDSDLQLYKEQGEGQGDRSLRERDVLEREFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMALSLQS FCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYEHCEPSTMPGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPD LQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRH LEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEE SKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHV DGFDSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGL LLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNS |
| Q01433-3 | MLTFLPSPQELFTRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDVKLEPDILLRAKQDFLKTDSDSDLQLYKEQGEGQGDRSL RERDVLEREFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHP PALEQHPYEHCEPSTMPGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMH VLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHA DRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVR WLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYY LYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPL PEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIR |
| Q01433-4 | MWQSQAPAGAAQTPPLSPPWSQPWHPIHLALASPRPNIPLRSGPACRPPLQLQELFTRSLAESELRSAPYEFPEESPIEQLEERRQRLER QISQDVKLEPDILLRAKQDFLKTDSDSDLQLYKEQGEGQGDRSLRERDVLEREFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYM ALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYEHCEPSTMPGDLGLGLRMVRGVVHVYTRREPDEHCSEV ELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIK RAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEV MSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELH LFLEHVDGFDSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAE NISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMC |
| Q01433-5 | MDGKCKEIAEELFTRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDVKLEPDILLRAKQDFLKTDSDSDLQLYKEQGEGQGDRS LRERDVLEREFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVH PPALEQHPYEHCEPSTMPGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQM HVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVH ADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNV RWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPLPEAWVEEDNPPYAY YLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNP LPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDI |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| AMPD2 (go to UniProt):Q01433 |
| 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 |
| Q01433 | Region | 1 | 49 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=81 |
| Q01433 | Region | 1 | 49 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=1;End=128 |
| Q01433 | Region | 1 | 49 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Substitution;Start=1;End=128 |
| Q01433 | Region | 1 | 49 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=1;End=118 |
Gene Isoform Structures and Expression Levels for AMPD2 |
| Gene structures of our canonical and alternative spliced genes of AMPD2 * 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 Q01433-1 |
| 3D view using mol* of Q01433-2 |
| 3D view using mol* of Q01433-3 |
| 3D view using mol* of Q01433-4 |
| 3D view using mol* of Q01433-5 |
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 Q01433-1 |
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| pLDDT distribution across the protein length of Q01433-2 |
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| pLDDT distribution across the protein length of Q01433-3 |
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| pLDDT distribution across the protein length of Q01433-4 |
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| pLDDT distribution across the protein length of Q01433-5 |
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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 Q01433-1 |
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| Ramachandran plot of Q01433-4 |
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| Ramachandran plot of Q01433-5 |
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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 |
| Q01433-1 | 1.077 | 377 | 1.018 | 1086.967 | 0.424 | 0.813 | 1.073 | 0.486 | 1.255 | 0.387 | 0.925 | 251,252,259,260,261,262,263,264,265,267,271,277,27 8,280,281,282,283,284,285,286,288,382,569,619,622, 675,679,680,681,682,683,685,705,706,724,726,727,72 8,729,753,755,756,757,758,759,796,799,800,803,804, 805,806,807,808,809,810,812,820,821,822,823,824,82 7,835,839,840,842,843,844,846,847 |
| Q01433-2 | 1.12 | 210 | 0.956 | 438.011 | 0.325 | 0.877 | 1.188 | 0.379 | 1.563 | 0.242 | 0.6 | 339,340,341,406,409,410,413,422,426,427,428,429,43 7,459,460,461,462,463,465,466,469,472,473,476,492, 494,496,546,547,548,549,550,551,606,609,610,628,66 0,683,684 |
| Q01433-3 | 1.103 | 109 | 1.154 | 210.945 | 0.513 | 0.772 | 1.039 | 1.535 | 0.765 | 2.007 | 0.907 | 8,9,11,12,13,236,237,240,241,244,245,247,248,515,5 17,518,519,520,536,538,575,576,580 |
| Q01433-4 | 1.086 | 391 | 1.046 | 1124.354 | 0.409 | 0.827 | 1.092 | 0.47 | 1.196 | 0.393 | 0.835 | 176,181,184,185,186,187,188,189,190,192,205,206,20 7,208,209,210,213,307,311,494,547,600,604,605,606, 607,608,610,630,631,649,651,652,653,654,678,680,68 1,682,683,684,721,724,725,728,729,730,731,732,733, 734,735,737,745,746,747,748,749,752,760,764,765,76 7,768,769,771,772 |
| Q01433-5 | 1.103 | 196 | 1.003 | 416.059 | 0.34 | 0.852 | 1.17 | 0.292 | 1.374 | 0.212 | 0.852 | 302,303,304,369,372,373,376,385,389,390,391,392,40 0,422,423,424,425,426,428,429,432,435,436,455,457, 458,459,509,510,511,512,569,572,591,618,622,623,64 6,647 |
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 Q01433-1_Q01433-1_4no3_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 Q01433-1_4no3_C_Q01433-2.pdb |
| 3D view using mol* of Q01433-1_4no3_C_Q01433-3.pdb |
| 3D view using mol* of Q01433-1_4no3_C_Q01433-4.pdb |
| 3D view using mol* of Q01433-1_4no3_C_Q01433-5.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q01433-1_Q01433-2.pdb |
| 3D view using mol* of Q01433-1_Q01433-3.pdb |
| 3D view using mol* of Q01433-1_Q01433-4.pdb |
| 3D view using mol* of Q01433-1_Q01433-5.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/Q01433-1_vs_Q01433-2.png |
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| ./stats/secondary_structure/figure/Q01433-1_vs_Q01433-3.png |
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| ./stats/secondary_structure/figure/Q01433-1_vs_Q01433-4.png |
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| ./stats/secondary_structure/figure/Q01433-1_vs_Q01433-5.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/Q01433-1_vs_Q01433-2.png |
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| ./stats/relative_asa/Q01433-1_vs_Q01433-3.png |
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| ./stats/relative_asa/Q01433-1_vs_Q01433-4.png |
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| ./stats/relative_asa/Q01433-1_vs_Q01433-5.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 AMPD2 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to AMPD2 |
| Previous studies relating to the alternative splicing of AMPD2 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| AMPD2 | 1400401 | Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons. | Higher eukaryotes express multiple isoforms of AMP deaminase (EC 3.5.4.6). In humans, four AMP deaminase variants, termed M (muscle), L (liver), E1, and E2 (erythrocyte) can be distinguished by a variety of biochemical and immunological criteria. Previous molecular studies have reported two genes, AMPD1 and AMPD2, that produce isoform M and L transcripts, respectively. This study identifies a third human AMP deaminase gene, AMPD3. Nucleotide sequence alignments between AMPD3 cDNAs isolated from several human libraries indicate three different extreme 5'-ends. Alternate forms of the AMPD3 cDNAs contain a common 2301-bp open reading frame (ORF) and 3'-untranslated region of 1245 bp. Two of the three forms, however, exhibit additional 5'-end nucleotide sequences that would extend their respective ORFs by 21 and 27 nucleotides. RNase protection analyses and the partial characterization of human AMPD3 genomic clones demonstrate alternative splicing of three different 5'-terminal exons. Western blot analyses detect anti-E-specific immunoreactivity in affinity-purified extracts derived from the bacterial expression of a truncated AMPD3 cDNA. These results are discussed in relation to AMP deaminase isoform diversity. | D015459 | Leukemia-Lymphoma, Adult T-Cell |
Clinically important variants in AMPD2 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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