UniProtKB - P05186 (PPBT_HUMAN)
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- BLAST
>sp|P05186|PPBT_HUMAN Alkaline phosphatase, tissue-nonspecific isozyme OS=Homo sapiens OX=9606 GN=ALPL PE=1 SV=4 MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGD GMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCG VKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAH SADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDE KARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELN RNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIG QAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPG YKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYV PHVMAYAACIGANLGHCAPASSAGSLAAGPLLLALALYPLSVLF
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Protein
Alkaline phosphatase, tissue-nonspecific isozyme
Gene
ALPL
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
This isozyme may play a role in skeletal mineralization.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
A phosphate monoester + H2O = an alcohol + phosphate.PROSITE-ProRule annotation
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.41"An asparagine at position 417 of tissue-nonspecific alkaline phosphatase is essential for its structure and function as revealed by analysis of the N417S mutation associated with severe hypophosphatasia."
Sultana S., Al-Shawafi H.A., Makita S., Sohda M., Amizuka N., Takagi R., Oda K.
Mol. Genet. Metab. 109:282-288(2013) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT HOPS SER-417, SUBUNIT, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY. - Ref.42"Molecular phenotype of tissue-nonspecific alkaline phosphatase with a proline (108) to leucine substitution associated with dominant odontohypophosphatasia."
Numa-Kinjoh N., Komaru K., Ishida Y., Sohda M., Oda K.
Mol. Genet. Metab. 115:180-185(2015) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT HOPS LEU-108, SUBCELLULAR LOCATION, SUBUNIT, CATALYTIC ACTIVITY.
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Protein has several cofactor binding sites:- Mg2+By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
Note: Binds 1 Mg2+ ion.By similarityManual assertion inferred from sequence similarity toi
- Zn2+By similarity
Manual assertion inferred from sequence similarity toi
Note: Binds 2 Zn2+ ions.By similarityManual assertion inferred from sequence similarity toi
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 60 | MagnesiumBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Metal bindingi | 60 | Zinc 1By similarity Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 110 | Phosphoserine intermediateBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Metal bindingi | 110 | Zinc 1By similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Metal bindingi | 173 | MagnesiumBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Metal bindingi | 332 | MagnesiumBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Metal bindingi | 337 | Zinc 2By similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Metal bindingi | 341 | Zinc 2; via tele nitrogenBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Metal bindingi | 378 | Zinc 1By similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Metal bindingi | 379 | Zinc 1; via tele nitrogenBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Metal bindingi | 454 | Zinc 2; via tele nitrogenBy similarity Manual assertion inferred from sequence similarity toi | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- alkaline phosphatase activity Source: UniProtKB-EC
- metal ion binding Source: UniProtKB-KW
- pyrophosphatase activity Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
GO - Biological processi
- cellular response to organic cyclic compound Source: Ensembl
- cementum mineralization Source: Ensembl
- developmental process involved in reproduction Source: Ensembl
- endochondral ossification Source: Ensembl
- osteoblast differentiation Source: UniProtKBInferred from high throughput direct assayi
- response to antibiotic Source: Ensembl
- response to glucocorticoid Source: Ensembl
- response to lipopolysaccharide Source: Ensembl
- response to vitamin D Source: BHF-UCL <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- skeletal system development Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Hydrolase |
| Biological process | Biomineralization |
| Ligand | Magnesium, Metal-binding, Zinc |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.1.3.1 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-163125 Post-translational modification: synthesis of GPI-anchored proteins |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P05186 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P05186 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Alkaline phosphatase, tissue-nonspecific isozyme (EC:3.1.3.12 PublicationsManual assertion based on experiment ini
Short name: AP-TNAP Short name: TNSALP Alternative name(s): Alkaline phosphatase liver/bone/kidney isozyme |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:ALPL |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000162551.13 |
Human Gene Nomenclature Database More...HGNCi | HGNC:438 ALPL |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 171760 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P05186 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Plasma membrane
- Cell membrane 2 Publications
Manual assertion based on experiment ini
- Ref.41"An asparagine at position 417 of tissue-nonspecific alkaline phosphatase is essential for its structure and function as revealed by analysis of the N417S mutation associated with severe hypophosphatasia."
Sultana S., Al-Shawafi H.A., Makita S., Sohda M., Amizuka N., Takagi R., Oda K.
Mol. Genet. Metab. 109:282-288(2013) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT HOPS SER-417, SUBUNIT, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY. - Ref.42"Molecular phenotype of tissue-nonspecific alkaline phosphatase with a proline (108) to leucine substitution associated with dominant odontohypophosphatasia."
Numa-Kinjoh N., Komaru K., Ishida Y., Sohda M., Oda K.
Mol. Genet. Metab. 115:180-185(2015) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT HOPS LEU-108, SUBCELLULAR LOCATION, SUBUNIT, CATALYTIC ACTIVITY.
Manual assertion based on experiment ini
- Ref.41"An asparagine at position 417 of tissue-nonspecific alkaline phosphatase is essential for its structure and function as revealed by analysis of the N417S mutation associated with severe hypophosphatasia."
Sultana S., Al-Shawafi H.A., Makita S., Sohda M., Amizuka N., Takagi R., Oda K.
Mol. Genet. Metab. 109:282-288(2013) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT HOPS SER-417, SUBUNIT, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY. - Ref.42"Molecular phenotype of tissue-nonspecific alkaline phosphatase with a proline (108) to leucine substitution associated with dominant odontohypophosphatasia."
Numa-Kinjoh N., Komaru K., Ishida Y., Sohda M., Oda K.
Mol. Genet. Metab. 115:180-185(2015) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT HOPS LEU-108, SUBCELLULAR LOCATION, SUBUNIT, CATALYTIC ACTIVITY.
- Cell membrane 2 Publications
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- extracellular matrix Source: Ensembl
- extracellular membrane-bounded organelle Source: Ensembl
- extracellular region Source: Reactome
Plasma Membrane
- plasma membrane Source: Reactome
Other locations
- anchored component of membrane Source: UniProtKB-KW
- membrane Source: UniProtKBInferred from high throughput direct assayi
Keywords - Cellular componenti
Cell membrane, Membrane<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Hypophosphatasia (HOPS)29 PublicationsManual assertion based on experiment ini
- Ref.4"A novel missense mutation of the tissue-nonspecific alkaline phosphatase gene detected in a patient with hypophosphatasia."
Sugimoto N., Iwamoto S., Hoshino Y., Kajii E.
J. Hum. Genet. 43:160-164(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT HOPS PHE-289. - Ref.15"A missense mutation in the human liver/bone/kidney alkaline phosphatase gene causing a lethal form of hypophosphatasia."
Weiss M.J., Cole D.E.C., Ray K., Whyte M.P., Lafferty M.A., Mulivor R.A., Harris H.
Proc. Natl. Acad. Sci. U.S.A. 85:7666-7669(1988) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HOPS THR-179. - Ref.16"Different missense mutations at the tissue-nonspecific alkaline phosphatase gene locus in autosomal recessively inherited forms of mild and severe hypophosphatasia."
Henthorn P.S., Raducha M., Fedde K.N., Lafferty M.A., Whyte M.P.
Proc. Natl. Acad. Sci. U.S.A. 89:9924-9928(1992) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPS VAL-33; CYS-71; PRO-71; LYS-191; PRO-207; ALA-294; VAL-378 AND HIS-436, VARIANT HIS-263. - Ref.17"A homoallelic Gly317-->Asp mutation in ALPL causes the perinatal (lethal) form of hypophosphatasia in Canadian mennonites."
Greenberg C.R., Taylor C.L., Haworth J.C., Seargeant L.E., Philipps S., Triggs-Raine B., Chodirker B.N.
Genomics 17:215-217(1993) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HOPS ASP-334. - Ref.18"Novel missense and frameshift mutations in the tissue-nonspecific alkaline phosphatase gene in a Japanese patient with hypophosphatasia."
Orimo H., Hayashi Z., Watanabe A., Hirayama T., Hirayama T., Shimada T.
Hum. Mol. Genet. 3:1683-1684(1994) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN HOPSI, VARIANT HOPSI LYS-298. - Ref.19"Identification of novel missense mutations (Phe310Leu and Gly439Arg) in a neonatal case of hypophosphatasia."
Ozono K., Yamagata M., Michigami T., Nakajima S., Sakai N., Cai G., Satomura K., Yasui N., Okada S., Nakayama M.
J. Clin. Endocrinol. Metab. 81:4458-4461(1996) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN HOPSI, VARIANTS HOPSI LEU-327 AND ARG-456. - Ref.20"Identification of fifteen novel mutations in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in European patients with severe hypophosphatasia."
Mornet E., Taillandier A., Peyramaure S., Kaper F., Muller F., Brenner R., Bussiere P., Freisinger P., Godard J., Le Merrer M., Oury J.F., Plauchu H., Puddu R., Rival J.M., Superti-Furga A., Touraine R.L., Serre J.L., Simon-Bouy B.
Eur. J. Hum. Genet. 6:308-314(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPS PHE-17; VAL-40; SER-75; ARG-120; ARG-129; ASP-170; TRP-184; LYS-191; TRP-223; LYS-291; ASP-334; PRO-445; CYS-450; SER-473 AND ARG-491, VARIANT HIS-263. - Ref.21"Hypophosphatasia: identification of five novel missense mutations (G507A, G705A, A748G, T1155C, G1320A) in the tissue-nonspecific alkaline phosphatase gene among Japanese patients."
Goseki-Sone M., Orimo H., Iimura T., Takagi Y., Watanabe H., Taketa K., Sato S., Mayanagi H., Shimada T., Oida S.
Hum. Mutat. Suppl. 1:S263-S267(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPS THR-111; THR-177; GLY-191; LEU-327 AND ILE-382. - Ref.22"Correlations of genotype and phenotype in hypophosphatasia."
Zurutuza L., Muller F., Gibrat J.F., Taillandier A., Simon-Bouy B., Serre J.L., Mornet E.
Hum. Mol. Genet. 8:1039-1046(1999) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPS VAL-40; LEU-62; SER-75; THR-111; ARG-120; ARG-129; HIS-136; VAL-162; ASP-170; TYR-171; TRP-184; LYS-191; TRP-223; VAL-249; LYS-291; VAL-306; ASP-334; CYS-391; PRO-445; CYS-450; SER-473; LYS-476 AND ARG-491, 3D-STRUCTURE MODELING, CHARACTERIZATION OF VARIANTS. - Ref.23"Characterization of eleven novel mutations (M45L, R119H, 544delG, G145V, H154Y, C184Y, D289V, 862+5A, 1172delC, R411X, E459K) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with severe hypophosphatasia."
Taillandier A., Zurutuza L., Muller F., Simon-Bouy B., Serre J.L., Bird L., Brenner R., Boute O., Cousin J., Gaillard D., Heidemann P.H., Steinmann B., Wallot M., Mornet E.
Hum. Mutat. 13:171-172(1999) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPS LEU-62; HIS-136; VAL-162; TYR-171; LYS-191; TYR-201; VAL-249; VAL-306 AND LYS-476. - Ref.24"Severe hypercalcaemia and respiratory insufficiency associated with infantile hypophosphatasia caused by two novel mutations of the tissue-nonspecific alkaline phosphatase gene."
Mochizuki H., Saito M., Michigami T., Ohashi H., Koda N., Yamaguchi S., Ozono K.
Eur. J. Pediatr. 159:375-379(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPSI GLU-224 AND CYS-426. - Ref.25"Fifteen new mutations (-195C>T, L-12X, 298-2A>G, T117N, A159T, R229S, 997+2T>A, E274X, A331T, H364R, D389G, 1256delC, R433H, N461I, C472S) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with hypophosphatasia."
Taillandier A., Cozien E., Muller F., Merrien Y., Bonnin E., Fribourg C., Simon-Bouy B., Serre J.L., Bieth E., Brenner R., Cordier M.P., De Bie S., Fellmann F., Freisinger P., Hesse V., Hennekam R.C.M., Josifova D., Kerzin-Storrar L. , Leporrier N., Zabot M.-T., Mornet E.
Hum. Mutat. 15:293-293(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPS VAL-40; THR-111; ASN-134; THR-176; LYS-191; TYR-201; SER-246; THR-348; ARG-381; GLY-406; HIS-450; ILE-478 AND SER-489. - Ref.26"Asp361Val mutant of alkaline phosphatase found in patients with dominantly inherited hypophosphatasia inhibits the activity of the wild-type enzyme."
Mueller H.L., Yamazaki M., Michigami T., Kageyama T., Schoenau E., Schneider P., Ozono K.
J. Clin. Endocrinol. Metab. 85:743-747(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HOPS VAL-378, VARIANT ALA-522. - Ref.27"Perinatal hypophosphatasia: radiology, pathology and molecular biology studies in a family harboring a splicing mutation (648+1A) and a novel missense mutation (N400S) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene."
Sergi C., Mornet E., Troeger J., Voigtlaender T.
Am. J. Med. Genet. 103:235-240(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HOPS SER-417. - Ref.28"A molecular approach to dominance in hypophosphatasia."
Lia-Baldini A.S., Muller F., Taillandier A., Gibrat J.F., Mouchard M., Robin B., Simon-Bouy B., Serre J.L., Aylsworth A.S., Bieth E., Delanote S., Freisinger P., Hu J.C.-C., Krohn H.-P., Nunes M.E., Mornet E.
Hum. Genet. 109:99-108(2001) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS HOPS VAL-40; VAL-63; THR-116; LEU-181; TRP-184; TRP-223; VAL-249; VAL-378; ILE-478 AND PHE-490. - Ref.29"Twelve novel mutations in the tissue-nonspecific alkaline phosphatase gene (ALPL) in patients with various forms of hypophosphatasia."
Taillandier A., Lia-Baldini A.S., Mouchard M., Robin B., Muller F., Simon-Bouy B., Serre J.L., Bera-Louville A., Bonduelle M., Eckhardt J., Gaillard D., Myhre A.G., Koertge-Jung S., Larget-Piet L., Malou E., Sillence D., Temple I.K., Viot G., Mornet E.
Hum. Mutat. 18:83-84(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPSI CYS-28 AND MET-459, VARIANTS HOPS VAL-40; VAL-51; HIS-71; THR-116; HIS-136; HIS-152; THR-176; THR-179; LYS-191; ASP-211; VAL-220; GLY-235; TYR-294; GLY-327; SER-399 AND ALA-423. - Ref.30"Mutational analysis and functional correlation with phenotype in German patients with childhood-type hypophosphatasia."
Orimo H., Girschick H.J., Goseki-Sone M., Ito M., Oda K., Shimada T.
J. Bone Miner. Res. 16:2313-2319(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN HOPSC, VARIANTS HOPSC MET-68; SER-71; THR-177; TRP-223; PRO-275 AND HIS-391, CHARACTERIZATION OF VARIANTS HOPSC MET-68; SER-71; THR-177; TRP-223; PRO-275 AND HIS-391, VARIANT ALA-522, CHARACTERIZATION OF VARIANT ALA-522. - Ref.31"A novel point mutation (C571T) in the tissue-non-specific alkaline phosphatase gene in a case of adult-type hypophosphatasia."
Watanabe H., Hashimoto-Uoshima M., Goseki-Sone M., Orimo H., Ishikawa I.
Oral Dis. 7:331-335(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HOPS VAL-132. - Ref.32"Glu274Lys/Gly309Arg mutation of the tissue-nonspecific alkaline phosphatase gene in neonatal hypophosphatasia associated with convulsions."
Litmanovitz I., Reish O., Dolfin T., Arnon S., Regev R., Grinshpan G., Yamazaki M., Ozono K.
J. Inherit. Metab. Dis. 25:35-40(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPS LYS-291 AND ARG-326. - Ref.33"Denaturing gradient gel electrophoresis analysis of the tissue nonspecific alkaline phosphatase isoenzyme gene in hypophosphatasia."
Mumm S., Jones J., Finnegan P., Henthorn P.S., Podgornik M.N., Whyte M.P.
Mol. Genet. Metab. 75:143-153(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPS SER-51; HIS-71; THR-111; MET-128; HIS-134; HIS-136; THR-176; LYS-191; GLN-223; TRP-223; SER-246; ALA-294; PRO-299; PHE-327 DEL; ARG-339; THR-348; VAL-378; MET-414; ASP-426 AND LYS-476, VARIANTS HIS-263 AND ALA-522. - Ref.34"Severe hypophosphatasia: characterization of fifteen novel mutations in the ALPL gene."
Spentchian M., Merrien Y., Herasse M., Dobbie Z., Glaeser D., Holder S.E., Ivarsson S.-A., Kostiner D., Mansour S., Norman A., Roth J., Stipoljev F., Taillemite J.-L., van der Smagt J.J., Serre J.-L., Simon-Bouy B., Taillandier A., Mornet E.
Hum. Mutat. 22:105-106(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPS VAL-62; ARG-63; THR-111; ILE-148; SER-162; GLU-189; ALA-220; LEU-272; GLY-293-294-ASP DEL; LYS-311; LYS-452 AND THR-468. - Ref.35"Molecular study of three cases of odontohypophosphatasia resulting from heterozygosity for mutations in the tissue non-specific alkaline phosphatase gene."
Herasse M., Spentchian M., Taillandier A., Keppler-Noreuil K., Fliorito A.N.M., Bergoffen J., Wallerstein R., Muti C., Simon-Bouy B., Mornet E.
J. Med. Genet. 40:605-609(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPS LEU-108; THR-116 AND MET-414, CHARACTERIZATION OF VARIANT HOPS LEU-108. - Ref.36"Childhood hypophosphatasia: a case report due to a novel mutation."
Draguet C., Gillerot Y., Mornet E.
Arch. Pediatr. 11:440-443(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT HOPS GLY-114. - Ref.37"Characterization of 11 novel mutations in the tissue non-specific alkaline phosphatase gene responsible for hypophosphatasia and genotype-phenotype correlations."
Brun-Heath I., Taillandier A., Serre J.-L., Mornet E.
Mol. Genet. Metab. 84:273-277(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPS VAL-33; HIS-136; GLN-223; TRP-223; HIS-272; THR-292; ALA-294; THR-295; ASP-297; ASP-334 AND ALA-411, CHARACTERIZATION OF VARIANTS HOPS VAL-33; HIS-272; THR-292; THR-295; ASP-297 AND ALA-411. - Ref.38"Mild forms of hypophosphatasia mostly result from dominant negative effect of severe alleles or from compound heterozygosity for severe and moderate alleles."
Fauvert D., Brun-Heath I., Lia-Baldini A.S., Bellazi L., Taillandier A., Serre J.L., de Mazancourt P., Mornet E.
BMC Med. Genet. 10:51-51(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPS CYS-71; HIS-71; THR-111; THR-176; LYS-191; ARG-334; ASP-334; ARG-339; ILE-382; CYS-391; HIS-391; MET-414; ALA-420; LYS-452; LEU-459 AND ALA-476, CHARACTERIZATION OF VARIANTS HOPS CYS-71; HIS-71; THR-111; THR-176; LYS-191; ARG-334; ASP-334; ARG-339; ILE-382; CYS-391; HIS-391; MET-414; LYS-452; LEU-459 AND ALA-476. - Ref.39"Disulfide bonds are critical for tissue-nonspecific alkaline phosphatase function revealed by analysis of mutant proteins bearing a C(201)-Y or C(489)-S substitution associated with severe hypophosphatasia."
Satou Y., Al-Shawafi H.A., Sultana S., Makita S., Sohda M., Oda K.
Biochim. Biophys. Acta 1822:581-588(2012) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPS TYR-201 AND SER-489, CHARACTERIZATION OF VARIANTS HOPS TYR-201 AND SER-489. - Ref.40"A dimerization defect caused by a glycine substitution at position 420 by serine in tissue-nonspecific alkaline phosphatase associated with perinatal hypophosphatasia."
Makita S., Al-Shawafi H.A., Sultana S., Sohda M., Nomura S., Oda K.
FEBS J. 279:4327-4337(2012) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS HOPS SER-420 AND ALA-420. - Ref.41"An asparagine at position 417 of tissue-nonspecific alkaline phosphatase is essential for its structure and function as revealed by analysis of the N417S mutation associated with severe hypophosphatasia."
Sultana S., Al-Shawafi H.A., Makita S., Sohda M., Amizuka N., Takagi R., Oda K.
Mol. Genet. Metab. 109:282-288(2013) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT HOPS SER-417, SUBUNIT, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY. - Ref.42"Molecular phenotype of tissue-nonspecific alkaline phosphatase with a proline (108) to leucine substitution associated with dominant odontohypophosphatasia."
Numa-Kinjoh N., Komaru K., Ishida Y., Sohda M., Oda K.
Mol. Genet. Metab. 115:180-185(2015) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT HOPS LEU-108, SUBCELLULAR LOCATION, SUBUNIT, CATALYTIC ACTIVITY.
Ref.4
"A novel missense mutation of the tissue-nonspecific alkaline phosphatase gene detected in a patient with hypophosphatasia."
Sugimoto N., Iwamoto S., Hoshino Y., Kajii E.
J. Hum. Genet. 43:160-164(1998) [PubMed] [Europe PMC] [Abstract]
Sugimoto N., Iwamoto S., Hoshino Y., Kajii E.
J. Hum. Genet. 43:160-164(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT HOPS PHE-289.
Ref.15
"A missense mutation in the human liver/bone/kidney alkaline phosphatase gene causing a lethal form of hypophosphatasia."
Weiss M.J., Cole D.E.C., Ray K., Whyte M.P., Lafferty M.A., Mulivor R.A., Harris H.
Proc. Natl. Acad. Sci. U.S.A. 85:7666-7669(1988) [PubMed] [Europe PMC] [Abstract]
Weiss M.J., Cole D.E.C., Ray K., Whyte M.P., Lafferty M.A., Mulivor R.A., Harris H.
Proc. Natl. Acad. Sci. U.S.A. 85:7666-7669(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HOPS THR-179.
Ref.16
"Different missense mutations at the tissue-nonspecific alkaline phosphatase gene locus in autosomal recessively inherited forms of mild and severe hypophosphatasia."
Henthorn P.S., Raducha M., Fedde K.N., Lafferty M.A., Whyte M.P.
Proc. Natl. Acad. Sci. U.S.A. 89:9924-9928(1992) [PubMed] [Europe PMC] [Abstract]
Henthorn P.S., Raducha M., Fedde K.N., Lafferty M.A., Whyte M.P.
Proc. Natl. Acad. Sci. U.S.A. 89:9924-9928(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPS VAL-33; CYS-71; PRO-71; LYS-191; PRO-207; ALA-294; VAL-378 AND HIS-436, VARIANT HIS-263.
Ref.17
"A homoallelic Gly317-->Asp mutation in ALPL causes the perinatal (lethal) form of hypophosphatasia in Canadian mennonites."
Greenberg C.R., Taylor C.L., Haworth J.C., Seargeant L.E., Philipps S., Triggs-Raine B., Chodirker B.N.
Genomics 17:215-217(1993) [PubMed] [Europe PMC] [Abstract]
Greenberg C.R., Taylor C.L., Haworth J.C., Seargeant L.E., Philipps S., Triggs-Raine B., Chodirker B.N.
Genomics 17:215-217(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HOPS ASP-334.
Ref.18
"Novel missense and frameshift mutations in the tissue-nonspecific alkaline phosphatase gene in a Japanese patient with hypophosphatasia."
Orimo H., Hayashi Z., Watanabe A., Hirayama T., Hirayama T., Shimada T.
Hum. Mol. Genet. 3:1683-1684(1994) [PubMed] [Europe PMC] [Abstract]
Orimo H., Hayashi Z., Watanabe A., Hirayama T., Hirayama T., Shimada T.
Hum. Mol. Genet. 3:1683-1684(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HOPSI, VARIANT HOPSI LYS-298.
Ref.19
"Identification of novel missense mutations (Phe310Leu and Gly439Arg) in a neonatal case of hypophosphatasia."
Ozono K., Yamagata M., Michigami T., Nakajima S., Sakai N., Cai G., Satomura K., Yasui N., Okada S., Nakayama M.
J. Clin. Endocrinol. Metab. 81:4458-4461(1996) [PubMed] [Europe PMC] [Abstract]
Ozono K., Yamagata M., Michigami T., Nakajima S., Sakai N., Cai G., Satomura K., Yasui N., Okada S., Nakayama M.
J. Clin. Endocrinol. Metab. 81:4458-4461(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HOPSI, VARIANTS HOPSI LEU-327 AND ARG-456.
Ref.20
"Identification of fifteen novel mutations in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in European patients with severe hypophosphatasia."
Mornet E., Taillandier A., Peyramaure S., Kaper F., Muller F., Brenner R., Bussiere P., Freisinger P., Godard J., Le Merrer M., Oury J.F., Plauchu H., Puddu R., Rival J.M., Superti-Furga A., Touraine R.L., Serre J.L., Simon-Bouy B.
Eur. J. Hum. Genet. 6:308-314(1998) [PubMed] [Europe PMC] [Abstract]
Mornet E., Taillandier A., Peyramaure S., Kaper F., Muller F., Brenner R., Bussiere P., Freisinger P., Godard J., Le Merrer M., Oury J.F., Plauchu H., Puddu R., Rival J.M., Superti-Furga A., Touraine R.L., Serre J.L., Simon-Bouy B.
Eur. J. Hum. Genet. 6:308-314(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPS PHE-17; VAL-40; SER-75; ARG-120; ARG-129; ASP-170; TRP-184; LYS-191; TRP-223; LYS-291; ASP-334; PRO-445; CYS-450; SER-473 AND ARG-491, VARIANT HIS-263.
Ref.21
"Hypophosphatasia: identification of five novel missense mutations (G507A, G705A, A748G, T1155C, G1320A) in the tissue-nonspecific alkaline phosphatase gene among Japanese patients."
Goseki-Sone M., Orimo H., Iimura T., Takagi Y., Watanabe H., Taketa K., Sato S., Mayanagi H., Shimada T., Oida S.
Hum. Mutat. Suppl. 1:S263-S267(1998) [PubMed] [Europe PMC] [Abstract]
Goseki-Sone M., Orimo H., Iimura T., Takagi Y., Watanabe H., Taketa K., Sato S., Mayanagi H., Shimada T., Oida S.
Hum. Mutat. Suppl. 1:S263-S267(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPS THR-111; THR-177; GLY-191; LEU-327 AND ILE-382.
Ref.22
"Correlations of genotype and phenotype in hypophosphatasia."
Zurutuza L., Muller F., Gibrat J.F., Taillandier A., Simon-Bouy B., Serre J.L., Mornet E.
Hum. Mol. Genet. 8:1039-1046(1999) [PubMed] [Europe PMC] [Abstract]
Zurutuza L., Muller F., Gibrat J.F., Taillandier A., Simon-Bouy B., Serre J.L., Mornet E.
Hum. Mol. Genet. 8:1039-1046(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPS VAL-40; LEU-62; SER-75; THR-111; ARG-120; ARG-129; HIS-136; VAL-162; ASP-170; TYR-171; TRP-184; LYS-191; TRP-223; VAL-249; LYS-291; VAL-306; ASP-334; CYS-391; PRO-445; CYS-450; SER-473; LYS-476 AND ARG-491, 3D-STRUCTURE MODELING, CHARACTERIZATION OF VARIANTS.
Ref.23
"Characterization of eleven novel mutations (M45L, R119H, 544delG, G145V, H154Y, C184Y, D289V, 862+5A, 1172delC, R411X, E459K) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with severe hypophosphatasia."
Taillandier A., Zurutuza L., Muller F., Simon-Bouy B., Serre J.L., Bird L., Brenner R., Boute O., Cousin J., Gaillard D., Heidemann P.H., Steinmann B., Wallot M., Mornet E.
Hum. Mutat. 13:171-172(1999) [PubMed] [Europe PMC] [Abstract]
Taillandier A., Zurutuza L., Muller F., Simon-Bouy B., Serre J.L., Bird L., Brenner R., Boute O., Cousin J., Gaillard D., Heidemann P.H., Steinmann B., Wallot M., Mornet E.
Hum. Mutat. 13:171-172(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPS LEU-62; HIS-136; VAL-162; TYR-171; LYS-191; TYR-201; VAL-249; VAL-306 AND LYS-476.
Ref.24
"Severe hypercalcaemia and respiratory insufficiency associated with infantile hypophosphatasia caused by two novel mutations of the tissue-nonspecific alkaline phosphatase gene."
Mochizuki H., Saito M., Michigami T., Ohashi H., Koda N., Yamaguchi S., Ozono K.
Eur. J. Pediatr. 159:375-379(2000) [PubMed] [Europe PMC] [Abstract]
Mochizuki H., Saito M., Michigami T., Ohashi H., Koda N., Yamaguchi S., Ozono K.
Eur. J. Pediatr. 159:375-379(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPSI GLU-224 AND CYS-426.
Ref.25
"Fifteen new mutations (-195C>T, L-12X, 298-2A>G, T117N, A159T, R229S, 997+2T>A, E274X, A331T, H364R, D389G, 1256delC, R433H, N461I, C472S) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with hypophosphatasia."
Taillandier A., Cozien E., Muller F., Merrien Y., Bonnin E., Fribourg C., Simon-Bouy B., Serre J.L., Bieth E., Brenner R., Cordier M.P., De Bie S., Fellmann F., Freisinger P., Hesse V., Hennekam R.C.M., Josifova D., Kerzin-Storrar L. , Leporrier N., Zabot M.-T., Mornet E.
Hum. Mutat. 15:293-293(2000) [PubMed] [Europe PMC] [Abstract]
Taillandier A., Cozien E., Muller F., Merrien Y., Bonnin E., Fribourg C., Simon-Bouy B., Serre J.L., Bieth E., Brenner R., Cordier M.P., De Bie S., Fellmann F., Freisinger P., Hesse V., Hennekam R.C.M., Josifova D., Kerzin-Storrar L. , Leporrier N., Zabot M.-T., Mornet E.
Hum. Mutat. 15:293-293(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPS VAL-40; THR-111; ASN-134; THR-176; LYS-191; TYR-201; SER-246; THR-348; ARG-381; GLY-406; HIS-450; ILE-478 AND SER-489.
Ref.26
"Asp361Val mutant of alkaline phosphatase found in patients with dominantly inherited hypophosphatasia inhibits the activity of the wild-type enzyme."
Mueller H.L., Yamazaki M., Michigami T., Kageyama T., Schoenau E., Schneider P., Ozono K.
J. Clin. Endocrinol. Metab. 85:743-747(2000) [PubMed] [Europe PMC] [Abstract]
Mueller H.L., Yamazaki M., Michigami T., Kageyama T., Schoenau E., Schneider P., Ozono K.
J. Clin. Endocrinol. Metab. 85:743-747(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HOPS VAL-378, VARIANT ALA-522.
Ref.27
"Perinatal hypophosphatasia: radiology, pathology and molecular biology studies in a family harboring a splicing mutation (648+1A) and a novel missense mutation (N400S) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene."
Sergi C., Mornet E., Troeger J., Voigtlaender T.
Am. J. Med. Genet. 103:235-240(2001) [PubMed] [Europe PMC] [Abstract]
Sergi C., Mornet E., Troeger J., Voigtlaender T.
Am. J. Med. Genet. 103:235-240(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HOPS SER-417.
Ref.28
"A molecular approach to dominance in hypophosphatasia."
Lia-Baldini A.S., Muller F., Taillandier A., Gibrat J.F., Mouchard M., Robin B., Simon-Bouy B., Serre J.L., Aylsworth A.S., Bieth E., Delanote S., Freisinger P., Hu J.C.-C., Krohn H.-P., Nunes M.E., Mornet E.
Hum. Genet. 109:99-108(2001) [PubMed] [Europe PMC] [Abstract]
Lia-Baldini A.S., Muller F., Taillandier A., Gibrat J.F., Mouchard M., Robin B., Simon-Bouy B., Serre J.L., Aylsworth A.S., Bieth E., Delanote S., Freisinger P., Hu J.C.-C., Krohn H.-P., Nunes M.E., Mornet E.
Hum. Genet. 109:99-108(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS HOPS VAL-40; VAL-63; THR-116; LEU-181; TRP-184; TRP-223; VAL-249; VAL-378; ILE-478 AND PHE-490.
Ref.29
"Twelve novel mutations in the tissue-nonspecific alkaline phosphatase gene (ALPL) in patients with various forms of hypophosphatasia."
Taillandier A., Lia-Baldini A.S., Mouchard M., Robin B., Muller F., Simon-Bouy B., Serre J.L., Bera-Louville A., Bonduelle M., Eckhardt J., Gaillard D., Myhre A.G., Koertge-Jung S., Larget-Piet L., Malou E., Sillence D., Temple I.K., Viot G., Mornet E.
Hum. Mutat. 18:83-84(2001) [PubMed] [Europe PMC] [Abstract]
Taillandier A., Lia-Baldini A.S., Mouchard M., Robin B., Muller F., Simon-Bouy B., Serre J.L., Bera-Louville A., Bonduelle M., Eckhardt J., Gaillard D., Myhre A.G., Koertge-Jung S., Larget-Piet L., Malou E., Sillence D., Temple I.K., Viot G., Mornet E.
Hum. Mutat. 18:83-84(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPSI CYS-28 AND MET-459, VARIANTS HOPS VAL-40; VAL-51; HIS-71; THR-116; HIS-136; HIS-152; THR-176; THR-179; LYS-191; ASP-211; VAL-220; GLY-235; TYR-294; GLY-327; SER-399 AND ALA-423.
Ref.30
"Mutational analysis and functional correlation with phenotype in German patients with childhood-type hypophosphatasia."
Orimo H., Girschick H.J., Goseki-Sone M., Ito M., Oda K., Shimada T.
J. Bone Miner. Res. 16:2313-2319(2001) [PubMed] [Europe PMC] [Abstract]
Orimo H., Girschick H.J., Goseki-Sone M., Ito M., Oda K., Shimada T.
J. Bone Miner. Res. 16:2313-2319(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HOPSC, VARIANTS HOPSC MET-68; SER-71; THR-177; TRP-223; PRO-275 AND HIS-391, CHARACTERIZATION OF VARIANTS HOPSC MET-68; SER-71; THR-177; TRP-223; PRO-275 AND HIS-391, VARIANT ALA-522, CHARACTERIZATION OF VARIANT ALA-522.
Ref.31
"A novel point mutation (C571T) in the tissue-non-specific alkaline phosphatase gene in a case of adult-type hypophosphatasia."
Watanabe H., Hashimoto-Uoshima M., Goseki-Sone M., Orimo H., Ishikawa I.
Oral Dis. 7:331-335(2001) [PubMed] [Europe PMC] [Abstract]
Watanabe H., Hashimoto-Uoshima M., Goseki-Sone M., Orimo H., Ishikawa I.
Oral Dis. 7:331-335(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HOPS VAL-132.
Ref.32
"Glu274Lys/Gly309Arg mutation of the tissue-nonspecific alkaline phosphatase gene in neonatal hypophosphatasia associated with convulsions."
Litmanovitz I., Reish O., Dolfin T., Arnon S., Regev R., Grinshpan G., Yamazaki M., Ozono K.
J. Inherit. Metab. Dis. 25:35-40(2002) [PubMed] [Europe PMC] [Abstract]
Litmanovitz I., Reish O., Dolfin T., Arnon S., Regev R., Grinshpan G., Yamazaki M., Ozono K.
J. Inherit. Metab. Dis. 25:35-40(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPS LYS-291 AND ARG-326.
Ref.33
"Denaturing gradient gel electrophoresis analysis of the tissue nonspecific alkaline phosphatase isoenzyme gene in hypophosphatasia."
Mumm S., Jones J., Finnegan P., Henthorn P.S., Podgornik M.N., Whyte M.P.
Mol. Genet. Metab. 75:143-153(2002) [PubMed] [Europe PMC] [Abstract]
Mumm S., Jones J., Finnegan P., Henthorn P.S., Podgornik M.N., Whyte M.P.
Mol. Genet. Metab. 75:143-153(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPS SER-51; HIS-71; THR-111; MET-128; HIS-134; HIS-136; THR-176; LYS-191; GLN-223; TRP-223; SER-246; ALA-294; PRO-299; PHE-327 DEL; ARG-339; THR-348; VAL-378; MET-414; ASP-426 AND LYS-476, VARIANTS HIS-263 AND ALA-522.
Ref.34
"Severe hypophosphatasia: characterization of fifteen novel mutations in the ALPL gene."
Spentchian M., Merrien Y., Herasse M., Dobbie Z., Glaeser D., Holder S.E., Ivarsson S.-A., Kostiner D., Mansour S., Norman A., Roth J., Stipoljev F., Taillemite J.-L., van der Smagt J.J., Serre J.-L., Simon-Bouy B., Taillandier A., Mornet E.
Hum. Mutat. 22:105-106(2003) [PubMed] [Europe PMC] [Abstract]
Spentchian M., Merrien Y., Herasse M., Dobbie Z., Glaeser D., Holder S.E., Ivarsson S.-A., Kostiner D., Mansour S., Norman A., Roth J., Stipoljev F., Taillemite J.-L., van der Smagt J.J., Serre J.-L., Simon-Bouy B., Taillandier A., Mornet E.
Hum. Mutat. 22:105-106(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPS VAL-62; ARG-63; THR-111; ILE-148; SER-162; GLU-189; ALA-220; LEU-272; GLY-293-294-ASP DEL; LYS-311; LYS-452 AND THR-468.
Ref.35
"Molecular study of three cases of odontohypophosphatasia resulting from heterozygosity for mutations in the tissue non-specific alkaline phosphatase gene."
Herasse M., Spentchian M., Taillandier A., Keppler-Noreuil K., Fliorito A.N.M., Bergoffen J., Wallerstein R., Muti C., Simon-Bouy B., Mornet E.
J. Med. Genet. 40:605-609(2003) [PubMed] [Europe PMC] [Abstract]
Herasse M., Spentchian M., Taillandier A., Keppler-Noreuil K., Fliorito A.N.M., Bergoffen J., Wallerstein R., Muti C., Simon-Bouy B., Mornet E.
J. Med. Genet. 40:605-609(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPS LEU-108; THR-116 AND MET-414, CHARACTERIZATION OF VARIANT HOPS LEU-108.
Ref.36
"Childhood hypophosphatasia: a case report due to a novel mutation."
Draguet C., Gillerot Y., Mornet E.
Arch. Pediatr. 11:440-443(2004) [PubMed] [Europe PMC] [Abstract]
Draguet C., Gillerot Y., Mornet E.
Arch. Pediatr. 11:440-443(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HOPS GLY-114.
Ref.37
"Characterization of 11 novel mutations in the tissue non-specific alkaline phosphatase gene responsible for hypophosphatasia and genotype-phenotype correlations."
Brun-Heath I., Taillandier A., Serre J.-L., Mornet E.
Mol. Genet. Metab. 84:273-277(2005) [PubMed] [Europe PMC] [Abstract]
Brun-Heath I., Taillandier A., Serre J.-L., Mornet E.
Mol. Genet. Metab. 84:273-277(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPS VAL-33; HIS-136; GLN-223; TRP-223; HIS-272; THR-292; ALA-294; THR-295; ASP-297; ASP-334 AND ALA-411, CHARACTERIZATION OF VARIANTS HOPS VAL-33; HIS-272; THR-292; THR-295; ASP-297 AND ALA-411.
Ref.38
"Mild forms of hypophosphatasia mostly result from dominant negative effect of severe alleles or from compound heterozygosity for severe and moderate alleles."
Fauvert D., Brun-Heath I., Lia-Baldini A.S., Bellazi L., Taillandier A., Serre J.L., de Mazancourt P., Mornet E.
BMC Med. Genet. 10:51-51(2009) [PubMed] [Europe PMC] [Abstract]
Fauvert D., Brun-Heath I., Lia-Baldini A.S., Bellazi L., Taillandier A., Serre J.L., de Mazancourt P., Mornet E.
BMC Med. Genet. 10:51-51(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPS CYS-71; HIS-71; THR-111; THR-176; LYS-191; ARG-334; ASP-334; ARG-339; ILE-382; CYS-391; HIS-391; MET-414; ALA-420; LYS-452; LEU-459 AND ALA-476, CHARACTERIZATION OF VARIANTS HOPS CYS-71; HIS-71; THR-111; THR-176; LYS-191; ARG-334; ASP-334; ARG-339; ILE-382; CYS-391; HIS-391; MET-414; LYS-452; LEU-459 AND ALA-476.
Ref.39
"Disulfide bonds are critical for tissue-nonspecific alkaline phosphatase function revealed by analysis of mutant proteins bearing a C(201)-Y or C(489)-S substitution associated with severe hypophosphatasia."
Satou Y., Al-Shawafi H.A., Sultana S., Makita S., Sohda M., Oda K.
Biochim. Biophys. Acta 1822:581-588(2012) [PubMed] [Europe PMC] [Abstract]
Satou Y., Al-Shawafi H.A., Sultana S., Makita S., Sohda M., Oda K.
Biochim. Biophys. Acta 1822:581-588(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPS TYR-201 AND SER-489, CHARACTERIZATION OF VARIANTS HOPS TYR-201 AND SER-489.
Ref.40
"A dimerization defect caused by a glycine substitution at position 420 by serine in tissue-nonspecific alkaline phosphatase associated with perinatal hypophosphatasia."
Makita S., Al-Shawafi H.A., Sultana S., Sohda M., Nomura S., Oda K.
FEBS J. 279:4327-4337(2012) [PubMed] [Europe PMC] [Abstract]
Makita S., Al-Shawafi H.A., Sultana S., Sohda M., Nomura S., Oda K.
FEBS J. 279:4327-4337(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS HOPS SER-420 AND ALA-420.
Ref.41
"An asparagine at position 417 of tissue-nonspecific alkaline phosphatase is essential for its structure and function as revealed by analysis of the N417S mutation associated with severe hypophosphatasia."
Sultana S., Al-Shawafi H.A., Makita S., Sohda M., Amizuka N., Takagi R., Oda K.
Mol. Genet. Metab. 109:282-288(2013) [PubMed] [Europe PMC] [Abstract]
Sultana S., Al-Shawafi H.A., Makita S., Sohda M., Amizuka N., Takagi R., Oda K.
Mol. Genet. Metab. 109:282-288(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT HOPS SER-417, SUBUNIT, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
Ref.42
"Molecular phenotype of tissue-nonspecific alkaline phosphatase with a proline (108) to leucine substitution associated with dominant odontohypophosphatasia."
Numa-Kinjoh N., Komaru K., Ishida Y., Sohda M., Oda K.
Mol. Genet. Metab. 115:180-185(2015) [PubMed] [Europe PMC] [Abstract]
Numa-Kinjoh N., Komaru K., Ishida Y., Sohda M., Oda K.
Mol. Genet. Metab. 115:180-185(2015) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT HOPS LEU-108, SUBCELLULAR LOCATION, SUBUNIT, CATALYTIC ACTIVITY.
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA metabolic bone disease characterized by defective skeletal mineralization and biochemically by deficient activity of the tissue non-specific isoenzyme of alkaline phosphatase. Four forms are distinguished, depending on the age of onset: perinatal, infantile, childhood and adult type. The perinatal form is the most severe and is almost always fatal. The adult form is mild and characterized by recurrent fractures, osteomalacia, rickets, and loss of teeth. Some cases are asymptomatic, while some patients manifest dental features without skeletal manifestations (odontohypophosphatasia).
See also OMIM:146300| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_025903 | 17 | S → F in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006147 | 33 | A → V in HOPS; 7.2% of wild-type activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011081 | 40 | A → V in HOPS; 2% of activity. 5 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025904 | 51 | A → S in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013973 | 51 | A → V in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006148 | 62 | M → L in HOPS; moderate; 27% of activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025905 | 62 | M → V in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025906 | 63 | G → R in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013974 | 63 | G → V in HOPS; loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006149 | 71 | R → C in HOPS; 35% of alkaline phosphatase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013975 | 71 | R → H in HOPS; loss of alkaline phosphatase activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006150 | 71 | R → P in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013976 | 75 | G → S in HOPS; severe; 3.5% of activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025909 | 76 | Q → R in HOPS. Corresponds to variant dbSNP:rs1057521085Ensembl. | 1 | |
| Natural variantiVAR_025910 | 108 | P → L in HOPS; 0.4% of alkaline phosphatase activity; severe allele; no effect on subcellular location; fails to assemble into dimeric structure; dominant negative effect. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006151 | 111 | A → T in HOPS; odonto; 50% of alkaline phosphatase activity. 6 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025911 | 114 | A → G in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013977 | 116 | A → T in HOPS; loss of alkaline phosphatase activity. 4 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013978 | 120 | G → R in HOPS. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025912 | 128 | V → M in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013979 | 129 | G → R in HOPS. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013146 | 132 | A → V in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025913 | 134 | T → H in HOPS; requires 2 nucleotide substitutions. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011082 | 134 | T → N in HOPS; 9% of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006152 | 136 | R → H in HOPS; moderate; 33% of activity. 5 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025914 | 148 | T → I in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013980 | 152 | R → H in HOPS. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025915 | 162 | G → S in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006153 | 162 | G → V in HOPS; severe; 1% of activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013981 | 170 | N → D in HOPS. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025916 | 171 | H → R in HOPS. Corresponds to variant dbSNP:rs778232217Ensembl. | 1 | |
| Natural variantiVAR_006154 | 171 | H → Y in HOPS; severe; 2% of activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011083 | 176 | A → T in HOPS; 30% of alkaline phosphatase activity. 4 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006156 | 179 | A → T in HOPS. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013982 | 181 | S → L in HOPS; 1% of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013983 | 184 | R → W in HOPS; loss of activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025917 | 189 | D → E in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006157 | 191 | E → G in HOPS; odonto. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006158 | 191 | E → K in HOPS; moderate; frequent mutation in European countries; 56% of alkaline phosphatase activity. 8 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006159 | 201 | C → Y in HOPS; weak alkaline phosphatase activity; severely affects homodimerization; reduced cell surface expression. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006160 | 207 | Q → P in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013984 | 211 | N → D in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025918 | 212 | I → F in HOPS. | 1 | |
| Natural variantiVAR_025919 | 220 | G → A in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013985 | 220 | G → V in HOPS; odonto. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025920 | 223 | R → Q in HOPS. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013987 | 235 | E → G in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011085 | 246 | R → S in HOPS; 4% of activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013988 | 249 | G → V in HOPS; partial loss of activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025921 | 272 | R → H in HOPS; 6.8% of wild-type activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025922 | 272 | R → L in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006162 | 289 | L → F in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013989 | 291 | E → K in HOPS; moderate; 8% of activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025924 | 292 | P → T in HOPS; 4% of wild-type activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025925 | 293 – 294 | Missing in HOPS. | 2 | |
| Natural variantiVAR_006163 | 294 | D → A in HOPS. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013990 | 294 | D → Y in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025926 | 295 | M → T in HOPS; 8.5% of wild-type activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025927 | 297 | Y → D in HOPS; 1.3% of wild-type activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025929 | 299 | L → P in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006164 | 306 | D → V in HOPS. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025930 | 311 | E → K in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013991 | 326 | G → R in HOPS; in a patient carrying also K-291. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013992 | 327 | F → G in HOPS; requires 2 nucleotide substitutions. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025931 | 327 | Missing in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006166 | 334 | G → D in HOPS; loss of alkaline phosphatase activity. 5 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075557 | 334 | G → R in HOPS; weak alkaline phosphatase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025932 | 339 | G → R in HOPS; loss of alkaline phosphatase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011086 | 348 | A → T in HOPS. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025933 | 354 | E → D in HOPS. | 1 | |
| Natural variantiVAR_006167 | 378 | D → V in HOPS; loss of activity. 4 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011087 | 381 | H → R in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006168 | 382 | V → I in HOPS; loss of alkaline phosphatase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013993 | 391 | R → C in HOPS; moderate; 4-10% of alkaline phosphatase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013994 | 399 | A → S in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011088 | 406 | D → G in HOPS; 15% of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025935 | 411 | T → A in HOPS; absence of residual enzymatic activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025936 | 414 | L → M in HOPS; loss of alkaline phosphatase activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025937 | 417 | N → S in HOPS; very low alkaline phosphatase activity; does not affect subcellular location; fails to assemble into dimeric structure. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075558 | 420 | G → A in HOPS; very low alkaline phosphatase activity; does not affect subcellular location. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075559 | 420 | G → S in HOPS; very low alkaline phosphatase activity; does not affect subcellular location. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013995 | 423 | V → A in HOPS; 16% alkaline of phosphatase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025938 | 426 | G → D in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006169 | 436 | Y → H in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013996 | 445 | S → P in HOPS; severe; 2% of activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013997 | 450 | R → C in HOPS; severe; 4% of activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011090 | 450 | R → H in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025939 | 452 | E → K in HOPS; loss of alkaline phosphatase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075560 | 459 | V → L in HOPS; loss of alkaline phosphatase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025940 | 468 | A → T in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013999 | 473 | G → S in HOPS. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_075561 | 476 | E → A in HOPS; loss of alkaline phosphatase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006170 | 476 | E → K in HOPS. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011092 | 478 | N → I in HOPS; 9% of activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011093 | 489 | C → S in HOPS; reduces alkaline phosphatase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_014000 | 490 | I → F in HOPS; odonto; partial loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_014001 | 491 | G → R in HOPS. 2 Publications Manual assertion based on experiment ini
| 1 |
Hypophosphatasia childhood type (HOPSC)1 PublicationManual assertion based on experiment ini
- Ref.30"Mutational analysis and functional correlation with phenotype in German patients with childhood-type hypophosphatasia."
Orimo H., Girschick H.J., Goseki-Sone M., Ito M., Oda K., Shimada T.
J. Bone Miner. Res. 16:2313-2319(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN HOPSC, VARIANTS HOPSC MET-68; SER-71; THR-177; TRP-223; PRO-275 AND HIS-391, CHARACTERIZATION OF VARIANTS HOPSC MET-68; SER-71; THR-177; TRP-223; PRO-275 AND HIS-391, VARIANT ALA-522, CHARACTERIZATION OF VARIANT ALA-522.
Ref.30
"Mutational analysis and functional correlation with phenotype in German patients with childhood-type hypophosphatasia."
Orimo H., Girschick H.J., Goseki-Sone M., Ito M., Oda K., Shimada T.
J. Bone Miner. Res. 16:2313-2319(2001) [PubMed] [Europe PMC] [Abstract]
Orimo H., Girschick H.J., Goseki-Sone M., Ito M., Oda K., Shimada T.
J. Bone Miner. Res. 16:2313-2319(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HOPSC, VARIANTS HOPSC MET-68; SER-71; THR-177; TRP-223; PRO-275 AND HIS-391, CHARACTERIZATION OF VARIANTS HOPSC MET-68; SER-71; THR-177; TRP-223; PRO-275 AND HIS-391, VARIANT ALA-522, CHARACTERIZATION OF VARIANT ALA-522.
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA bone disease characterized by defective skeletal mineralization and biochemically by deficient activity of the tissue non-specific isoenzyme of alkaline phosphatase.
See also OMIM:241510| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_025907 | 68 | T → M in HOPSC; severe allele. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025908 | 71 | R → S in HOPSC; severe allele. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025923 | 275 | L → P in HOPSC; severe allele. 1 Publication Manual assertion based on experiment ini
| 1 |
Hypophosphatasia infantile type (HOPSI)4 PublicationsManual assertion based on experiment ini
- Ref.18"Novel missense and frameshift mutations in the tissue-nonspecific alkaline phosphatase gene in a Japanese patient with hypophosphatasia."
Orimo H., Hayashi Z., Watanabe A., Hirayama T., Hirayama T., Shimada T.
Hum. Mol. Genet. 3:1683-1684(1994) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN HOPSI, VARIANT HOPSI LYS-298. - Ref.19"Identification of novel missense mutations (Phe310Leu and Gly439Arg) in a neonatal case of hypophosphatasia."
Ozono K., Yamagata M., Michigami T., Nakajima S., Sakai N., Cai G., Satomura K., Yasui N., Okada S., Nakayama M.
J. Clin. Endocrinol. Metab. 81:4458-4461(1996) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN HOPSI, VARIANTS HOPSI LEU-327 AND ARG-456. - Ref.24"Severe hypercalcaemia and respiratory insufficiency associated with infantile hypophosphatasia caused by two novel mutations of the tissue-nonspecific alkaline phosphatase gene."
Mochizuki H., Saito M., Michigami T., Ohashi H., Koda N., Yamaguchi S., Ozono K.
Eur. J. Pediatr. 159:375-379(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPSI GLU-224 AND CYS-426. - Ref.29"Twelve novel mutations in the tissue-nonspecific alkaline phosphatase gene (ALPL) in patients with various forms of hypophosphatasia."
Taillandier A., Lia-Baldini A.S., Mouchard M., Robin B., Muller F., Simon-Bouy B., Serre J.L., Bera-Louville A., Bonduelle M., Eckhardt J., Gaillard D., Myhre A.G., Koertge-Jung S., Larget-Piet L., Malou E., Sillence D., Temple I.K., Viot G., Mornet E.
Hum. Mutat. 18:83-84(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS HOPSI CYS-28 AND MET-459, VARIANTS HOPS VAL-40; VAL-51; HIS-71; THR-116; HIS-136; HIS-152; THR-176; THR-179; LYS-191; ASP-211; VAL-220; GLY-235; TYR-294; GLY-327; SER-399 AND ALA-423.
Ref.18
"Novel missense and frameshift mutations in the tissue-nonspecific alkaline phosphatase gene in a Japanese patient with hypophosphatasia."
Orimo H., Hayashi Z., Watanabe A., Hirayama T., Hirayama T., Shimada T.
Hum. Mol. Genet. 3:1683-1684(1994) [PubMed] [Europe PMC] [Abstract]
Orimo H., Hayashi Z., Watanabe A., Hirayama T., Hirayama T., Shimada T.
Hum. Mol. Genet. 3:1683-1684(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HOPSI, VARIANT HOPSI LYS-298.
Ref.19
"Identification of novel missense mutations (Phe310Leu and Gly439Arg) in a neonatal case of hypophosphatasia."
Ozono K., Yamagata M., Michigami T., Nakajima S., Sakai N., Cai G., Satomura K., Yasui N., Okada S., Nakayama M.
J. Clin. Endocrinol. Metab. 81:4458-4461(1996) [PubMed] [Europe PMC] [Abstract]
Ozono K., Yamagata M., Michigami T., Nakajima S., Sakai N., Cai G., Satomura K., Yasui N., Okada S., Nakayama M.
J. Clin. Endocrinol. Metab. 81:4458-4461(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HOPSI, VARIANTS HOPSI LEU-327 AND ARG-456.
Ref.24
"Severe hypercalcaemia and respiratory insufficiency associated with infantile hypophosphatasia caused by two novel mutations of the tissue-nonspecific alkaline phosphatase gene."
Mochizuki H., Saito M., Michigami T., Ohashi H., Koda N., Yamaguchi S., Ozono K.
Eur. J. Pediatr. 159:375-379(2000) [PubMed] [Europe PMC] [Abstract]
Mochizuki H., Saito M., Michigami T., Ohashi H., Koda N., Yamaguchi S., Ozono K.
Eur. J. Pediatr. 159:375-379(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPSI GLU-224 AND CYS-426.
Ref.29
"Twelve novel mutations in the tissue-nonspecific alkaline phosphatase gene (ALPL) in patients with various forms of hypophosphatasia."
Taillandier A., Lia-Baldini A.S., Mouchard M., Robin B., Muller F., Simon-Bouy B., Serre J.L., Bera-Louville A., Bonduelle M., Eckhardt J., Gaillard D., Myhre A.G., Koertge-Jung S., Larget-Piet L., Malou E., Sillence D., Temple I.K., Viot G., Mornet E.
Hum. Mutat. 18:83-84(2001) [PubMed] [Europe PMC] [Abstract]
Taillandier A., Lia-Baldini A.S., Mouchard M., Robin B., Muller F., Simon-Bouy B., Serre J.L., Bera-Louville A., Bonduelle M., Eckhardt J., Gaillard D., Myhre A.G., Koertge-Jung S., Larget-Piet L., Malou E., Sillence D., Temple I.K., Viot G., Mornet E.
Hum. Mutat. 18:83-84(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HOPSI CYS-28 AND MET-459, VARIANTS HOPS VAL-40; VAL-51; HIS-71; THR-116; HIS-136; HIS-152; THR-176; THR-179; LYS-191; ASP-211; VAL-220; GLY-235; TYR-294; GLY-327; SER-399 AND ALA-423.
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe bone disease characterized by defective skeletal mineralization and biochemically by deficient activity of the tissue non-specific isoenzyme of alkaline phosphatase. Three more or less distinct types of infantile hypophosphatasia can be identified: (1) type 1 with onset in utero or in early postnatal life, craniostenosis, severe skeletal abnormalities, hypercalcemia, and death in the first year or so of life; (2) type 2 with later, more gradual development of symptoms, moderately severe 'rachitic' skeletal changes and premature loss of teeth; (3) type 3 with no symptoms, the condition being determined on routine studies.
See also OMIM:241500| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_013972 | 28 | Y → C in HOPSI; 7% of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011084 | 224 | K → E in HOPSI; partial loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025928 | 298 | E → K in HOPSI. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011089 | 426 | G → C in HOPSI; partial loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011091 | 456 | G → R in HOPSI; loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013998 | 459 | V → M in HOPSI. 1 Publication Manual assertion based on experiment ini
| 1 |
Keywords - Diseasei
Disease mutationOrganism-specific databases
DisGeNET More...DisGeNETi | 249 |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | ALPL |
MalaCards human disease database More...MalaCardsi | ALPL |
| MIMi | 146300 phenotype 241500 phenotype 241510 phenotype |
Open Targets More...OpenTargetsi | ENSG00000162551 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 247676 Adult hypophosphatasia 247667 Childhood-onset hypophosphatasia 247651 Infantile hypophosphatasia 247685 Odontohypophosphatasia 247623 Perinatal lethal hypophosphatasia 247638 Prenatal benign hypophosphatasia |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA24729 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL5979 |
Drug and drug target database More...DrugBanki | DB01143 Amifostine DB06716 Fospropofol |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | ALPL |
Domain mapping of disease mutations (DMDM) More...DMDMi | 68067533 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 17 | 2 Publications Manual assertion based on experiment ini
| 17 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000024023 | 18 – 501 | Alkaline phosphatase, tissue-nonspecific isozymeAdd BLAST | 484 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000024024 | 502 – 524 | Removed in mature formCuratedAdd BLAST | 23 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 110 | PhosphoserineBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 139 ↔ 201 | By similarity Manual assertion inferred from sequence similarity toi | ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 140 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 230 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 271 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 303 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 430 | N-linked (GlcNAc...) asparagine1 Publication Manual assertion based on experiment ini
| 1 | |
| Disulfide bondi | 489 ↔ 497 | By similarity Manual assertion inferred from sequence similarity toi | ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 501 | GPI-anchor amidated serineSequence analysis | 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
N-glycosylated.2 Publications
Manual assertion based on experiment ini
- Ref.11"Chemical nature of intestinal-type alkaline phosphatase in human kidney."
Nishihara Y., Hayashi Y., Adachi T., Koyama I., Stigbrand T., Hirano K.
Clin. Chem. 38:2539-2542(1992) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 18-32, GLYCOSYLATION. - Ref.13"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-430.
Keywords - PTMi
Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P05186 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P05186 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P05186 |
PeptideAtlas More...PeptideAtlasi | P05186 |
PRoteomics IDEntifications database More...PRIDEi | P05186 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 51821 51822 [P05186-2] |
PTM databases
DEPOD human dephosphorylation database More...DEPODi | P05186 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P05186 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P05186 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000162551 Expressed in 143 organ(s), highest expression level in blood |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P05186 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P05186 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB020829 HPA007105 HPA008765 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer.2 Publications
Manual assertion based on experiment ini
- Ref.41"An asparagine at position 417 of tissue-nonspecific alkaline phosphatase is essential for its structure and function as revealed by analysis of the N417S mutation associated with severe hypophosphatasia."
Sultana S., Al-Shawafi H.A., Makita S., Sohda M., Amizuka N., Takagi R., Oda K.
Mol. Genet. Metab. 109:282-288(2013) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT HOPS SER-417, SUBUNIT, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY. - Ref.42"Molecular phenotype of tissue-nonspecific alkaline phosphatase with a proline (108) to leucine substitution associated with dominant odontohypophosphatasia."
Numa-Kinjoh N., Komaru K., Ishida Y., Sohda M., Oda K.
Mol. Genet. Metab. 115:180-185(2015) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT HOPS LEU-108, SUBCELLULAR LOCATION, SUBUNIT, CATALYTIC ACTIVITY.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| MAP3K14 | Q99558 | 4 | EBI-1054354,EBI-358011 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 106750, 7 interactors |
Protein interaction database and analysis system More...IntActi | P05186, 4 interactors |
Molecular INTeraction database More...MINTi | P05186 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000363965 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P05186 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P05186 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P05186 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the alkaline phosphatase family.Curated
Keywords - Domaini
SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG4126 Eukaryota COG1785 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000008704 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG007345 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P05186 |
KEGG Orthology (KO) More...KOi | K01077 |
Identification of Orthologs from Complete Genome Data More...OMAi | EHTGTQL |
Database of Orthologous Groups More...OrthoDBi | EOG091G067H |
Database for complete collections of gene phylogenies More...PhylomeDBi | P05186 |
TreeFam database of animal gene trees More...TreeFami | TF323513 |
Family and domain databases
Conserved Domains Database More...CDDi | cd16012 ALP, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.720.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR017849 Alkaline_Pase-like_a/b/a IPR001952 Alkaline_phosphatase IPR018299 Alkaline_phosphatase_AS IPR017850 Alkaline_phosphatase_core_sf |
The PANTHER Classification System More...PANTHERi | PTHR11596 PTHR11596, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00245 Alk_phosphatase, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00113 ALKPHPHTASE |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00098 alkPPc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53649 SSF53649, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00123 ALKALINE_PHOSPHATASE, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basketThis entry has 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All
Isoform 1 (identifier: P05186-1) [UniParc]FASTAAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
« Hide
Show »10 20 30 40 50
MISPFLVLAI GTCLTNSLVP EKEKDPKYWR DQAQETLKYA LELQKLNTNV
60 70 80 90 100
AKNVIMFLGD GMGVSTVTAA RILKGQLHHN PGEETRLEMD KFPFVALSKT
110 120 130 140 150
YNTNAQVPDS AGTATAYLCG VKANEGTVGV SAATERSRCN TTQGNEVTSI
160 170 180 190 200
LRWAKDAGKS VGIVTTTRVN HATPSAAYAH SADRDWYSDN EMPPEALSQG
210 220 230 240 250
CKDIAYQLMH NIRDIDVIMG GGRKYMYPKN KTDVEYESDE KARGTRLDGL
260 270 280 290 300
DLVDTWKSFK PRYKHSHFIW NRTELLTLDP HNVDYLLGLF EPGDMQYELN
310 320 330 340 350
RNNVTDPSLS EMVVVAIQIL RKNPKGFFLL VEGGRIDHGH HEGKAKQALH
360 370 380 390 400
EAVEMDRAIG QAGSLTSSED TLTVVTADHS HVFTFGGYTP RGNSIFGLAP
410 420 430 440 450
MLSDTDKKPF TAILYGNGPG YKVVGGEREN VSMVDYAHNN YQAQSAVPLR
460 470 480 490 500
HETHGGEDVA VFSKGPMAHL LHGVHEQNYV PHVMAYAACI GANLGHCAPA
510 520
SSAGSLAAGP LLLALALYPL SVLF
Length:524
Mass (Da):57,305
Last modified:June 21, 2005 - v4
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i71B45F17F6211900
Isoform 2 (identifier: P05186-2) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-99: MISPFLVLAI...DKFPFVALSK → MPWSFRSSTPTWLRMSSCSWEM
« Hide
10 20 30 40 50
MPWSFRSSTP TWLRMSSCSW EMTYNTNAQV PDSAGTATAY LCGVKANEGT
60 70 80 90 100
VGVSAATERS RCNTTQGNEV TSILRWAKDA GKSVGIVTTT RVNHATPSAA
110 120 130 140 150
YAHSADRDWY SDNEMPPEAL SQGCKDIAYQ LMHNIRDIDV IMGGGRKYMY
160 170 180 190 200
PKNKTDVEYE SDEKARGTRL DGLDLVDTWK SFKPRYKHSH FIWNRTELLT
210 220 230 240 250
LDPHNVDYLL GLFEPGDMQY ELNRNNVTDP SLSEMVVVAI QILRKNPKGF
260 270 280 290 300
FLLVEGGRID HGHHEGKAKQ ALHEAVEMDR AIGQAGSLTS SEDTLTVVTA
310 320 330 340 350
DHSHVFTFGG YTPRGNSIFG LAPMLSDTDK KPFTAILYGN GPGYKVVGGE
360 370 380 390 400
RENVSMVDYA HNNYQAQSAV PLRHETHGGE DVAVFSKGPM AHLLHGVHEQ
410 420 430 440
NYVPHVMAYA ACIGANLGHC APASSAGSLA AGPLLLALAL YPLSVLF
Note: No experimental confirmation available.
Show »Isoform 3 (identifier: P05186-3) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
1-55: Missing.
« Hide
Show »10 20 30 40 50
MFLGDGMGVS TVTAARILKG QLHHNPGEET RLEMDKFPFV ALSKTYNTNA
60 70 80 90 100
QVPDSAGTAT AYLCGVKANE GTVGVSAATE RSRCNTTQGN EVTSILRWAK
110 120 130 140 150
DAGKSVGIVT TTRVNHATPS AAYAHSADRD WYSDNEMPPE ALSQGCKDIA
160 170 180 190 200
YQLMHNIRDI DVIMGGGRKY MYPKNKTDVE YESDEKARGT RLDGLDLVDT
210 220 230 240 250
WKSFKPRYKH SHFIWNRTEL LTLDPHNVDY LLGLFEPGDM QYELNRNNVT
260 270 280 290 300
DPSLSEMVVV AIQILRKNPK GFFLLVEGGR IDHGHHEGKA KQALHEAVEM
310 320 330 340 350
DRAIGQAGSL TSSEDTLTVV TADHSHVFTF GGYTPRGNSI FGLAPMLSDT
360 370 380 390 400
DKKPFTAILY GNGPGYKVVG GERENVSMVD YAHNNYQAQS AVPLRHETHG
410 420 430 440 450
GEDVAVFSKG PMAHLLHGVH EQNYVPHVMA YAACIGANLG HCAPASSAGS
460
LAAGPLLLAL ALYPLSVLF
<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket| Entry | Entry name | Protein names | Gene names | Length | Annotation | ||
|---|---|---|---|---|---|---|---|
| B1ANL0 | B1ANL0_HUMAN | Alkaline phosphatase, tissue-nonspe... Alkaline phosphatase, tissue-nonspecific isozyme | ALPL | 216 | Annotation score: Annotation score:1 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
The sequence BAD93051 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 29 | W → A AA sequence (PubMed:3954357).Curated | 1 | |
| Sequence conflicti | 104 | N → K in CAA32376 (PubMed:2928120).Curated | 1 | |
| Sequence conflicti | 361 | Q → H in BAA32129 (PubMed:3532105).Curated | 1 | |
| Sequence conflicti | 446 | A → P in BAA32129 (PubMed:3532105).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_025903 | 17 | S → F in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013972 | 28 | Y → C in HOPSI; 7% of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006147 | 33 | A → V in HOPS; 7.2% of wild-type activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011081 | 40 | A → V in HOPS; 2% of activity. 5 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025904 | 51 | A → S in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013973 | 51 | A → V in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006148 | 62 | M → L in HOPS; moderate; 27% of activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025905 | 62 | M → V in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025906 | 63 | G → R in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013974 | 63 | G → V in HOPS; loss of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025907 | 68 | T → M in HOPSC; severe allele. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006149 | 71 | R → C in HOPS; 35% of alkaline phosphatase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013975 | 71 | R → H in HOPS; loss of alkaline phosphatase activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006150 | 71 | R → P in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025908 | 71 | R → S in HOPSC; severe allele. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013976 | 75 | G → S in HOPS; severe; 3.5% of activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025909 | 76 | Q → R in HOPS. Corresponds to variant dbSNP:rs1057521085Ensembl. | 1 | |
| Natural variantiVAR_025910 | 108 | P → L in HOPS; 0.4% of alkaline phosphatase activity; severe allele; no effect on subcellular location; fails to assemble into dimeric structure; dominant negative effect. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006151 | 111 | A → T in HOPS; odonto; 50% of alkaline phosphatase activity. 6 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025911 | 114 | A → G in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013977 | 116 | A → T in HOPS; loss of alkaline phosphatase activity. 4 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013978 | 120 | G → R in HOPS. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025912 | 128 | V → M in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013979 | 129 | G → R in HOPS. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013146 | 132 | A → V in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025913 | 134 | T → H in HOPS; requires 2 nucleotide substitutions. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011082 | 134 | T → N in HOPS; 9% of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006152 | 136 | R → H in HOPS; moderate; 33% of activity. 5 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025914 | 148 | T → I in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013980 | 152 | R → H in HOPS. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025915 | 162 | G → S in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006153 | 162 | G → V in HOPS; severe; 1% of activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013981 | 170 | N → D in HOPS. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025916 | 171 | H → R in HOPS. Corresponds to variant dbSNP:rs778232217Ensembl. | 1 | |
| Natural variantiVAR_006154 | 171 | H → Y in HOPS; severe; 2% of activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_011083 | 176 | A → T in HOPS; 30% of alkaline phosphatase activity. 4 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006155 | 177 | A → T in HOPS and HOPSC; moderate allele. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006156 | 179 | A → T in HOPS. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013982 | 181 | S → L in HOPS; 1% of activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013983 | 184 | R → W in HOPS; loss of activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025917 | 189 | D → E in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006157 | 191 | E → G in HOPS; odonto. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006158 | 191 | E → K in HOPS; moderate; frequent mutation in European countries; 56% of alkaline phosphatase activity. 8 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006159 | 201 | C → Y in HOPS; weak alkaline phosphatase activity; severely affects homodimerization; reduced cell surface expression. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_006160 | 207 | Q → P in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013984 | 211 | N → D in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025918 | 212 | I → F in HOPS. | 1 | |
| Natural variantiVAR_025919 | 220 | G → A in HOPS. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013985 | 220 | G → V in HOPS; odonto. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_025920 | 223 | R → Q in HOPS. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_013986 | 223 | R → W in HOPS and HOPSC; 3% of activity; severe allele. 6 Publications Manual assertion based on experiment ini
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