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P05186 (PPBT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 173. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alkaline phosphatase, tissue-nonspecific isozyme

Short name=AP-TNAP
Short name=TNSALP
EC=3.1.3.1
Alternative name(s):
Alkaline phosphatase liver/bone/kidney isozyme
Gene names
Name:ALPL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length524 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This isozyme may play a role in skeletal mineralization.

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate.

Cofactor

Binds 1 magnesium ion By similarity.

Binds 2 zinc ions By similarity.

Subunit structure

Homodimer.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor.

Post-translational modification

Glycosylated. Ref.11

Involvement in disease

Hypophosphatasia (HOPS) [MIM:146300]: A 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).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38

Hypophosphatasia childhood type (HOPSC) [MIM:241510]: A bone disease characterized by defective skeletal mineralization and biochemically by deficient activity of the tissue non-specific isoenzyme of alkaline phosphatase.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Hypophosphatasia infantile type (HOPSI) [MIM:241500]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the alkaline phosphatase family.

Sequence caution

The sequence BAD93051.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processBiomineralization
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainSignal
Transmembrane
   LigandMagnesium
Metal-binding
Zinc
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

cementum mineralization

Inferred from electronic annotation. Source: Ensembl

developmental process involved in reproduction

Inferred from electronic annotation. Source: Ensembl

endochondral ossification

Inferred from electronic annotation. Source: Ensembl

response to antibiotic

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to vitamin D

Inferred from expression pattern PubMed 17023519. Source: BHF-UCL

skeletal system development

Traceable author statement Ref.21. Source: ProtInc

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular matrix

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalkaline phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pyrophosphatase activity

Inferred from direct assay PubMed 19874193. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MAP3K14Q995584EBI-1054354,EBI-358011

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P05186-1)

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.
Isoform 2 (identifier: P05186-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-99: MISPFLVLAI...DKFPFVALSK → MPWSFRSSTPTWLRMSSCSWEM
Note: No experimental confirmation available.
Isoform 3 (identifier: P05186-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.10 Ref.11
Chain18 – 502485Alkaline phosphatase, tissue-nonspecific isozyme
PRO_0000024023
Propeptide503 – 52422Removed in mature form Probable
PRO_0000024024

Sites

Active site1101Phosphoserine intermediate
Metal binding601Magnesium By similarity
Metal binding601Zinc 1 By similarity
Metal binding1101Zinc 1 By similarity
Metal binding1731Magnesium By similarity
Metal binding3321Magnesium By similarity
Metal binding3371Zinc 2 By similarity
Metal binding3411Zinc 2; via tele nitrogen By similarity
Metal binding3781Zinc 1 By similarity
Metal binding3791Zinc 1; via tele nitrogen By similarity
Metal binding4541Zinc 2; via tele nitrogen By similarity

Amino acid modifications

Lipidation5021GPI-anchor amidated serine Probable
Glycosylation1401N-linked (GlcNAc...) Potential
Glycosylation2301N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Potential
Glycosylation4301N-linked (GlcNAc...) Ref.14
Disulfide bond139 ↔ 201 By similarity
Disulfide bond489 ↔ 497 By similarity

Natural variations

Alternative sequence1 – 9999MISPF…VALSK → MPWSFRSSTPTWLRMSSCSW EM in isoform 2.
VSP_042711
Alternative sequence1 – 5555Missing in isoform 3.
VSP_044228
Natural variant171S → F in HOPS. Ref.21
VAR_025903
Natural variant281Y → C in HOPS; infantile; 7% of activity. Ref.30
VAR_013972
Natural variant331A → V in HOPS; 7.2% of wild-type activity. Ref.17 Ref.38
VAR_006147
Natural variant401A → V in HOPS; 2% of activity. Ref.21 Ref.23 Ref.26 Ref.29 Ref.30
VAR_011081
Natural variant511A → S in HOPS. Ref.34
VAR_025904
Natural variant511A → V in HOPS. Ref.30
VAR_013973
Natural variant621M → L in HOPS; moderate; 27% of activity. Ref.23 Ref.24
VAR_006148
Natural variant621M → V in HOPS. Ref.35
VAR_025905
Natural variant631G → R in HOPS. Ref.35
VAR_025906
Natural variant631G → V in HOPS; loss of activity. Ref.29
VAR_013974
Natural variant681T → M in HOPS; childhood-type; severe allele. Ref.31
VAR_025907
Natural variant711R → C in HOPS. Ref.17
VAR_006149
Natural variant711R → H in HOPS. Ref.30 Ref.34
VAR_013975
Natural variant711R → P in HOPS. Ref.17
VAR_006150
Natural variant711R → S in HOPS; childhood-type; severe allele. Ref.31
VAR_025908
Natural variant751G → S in HOPS; severe; 3.5% of activity. Ref.21 Ref.23
VAR_013976
Natural variant761Q → R in HOPS.
VAR_025909
Natural variant1081P → L in HOPS; 0.4% of wild-type activity; severe allele. Ref.36
Corresponds to variant rs28933975 [ dbSNP | Ensembl ].
VAR_025910
Natural variant1111A → T in HOPS; odonto. Ref.22 Ref.23 Ref.26 Ref.34 Ref.35
VAR_006151
Natural variant1141A → G in HOPS. Ref.37
VAR_025911
Natural variant1161A → T in HOPS; loss of activity. Ref.29 Ref.30 Ref.36
Corresponds to variant rs28933974 [ dbSNP | Ensembl ].
VAR_013977
Natural variant1201G → R in HOPS. Ref.21 Ref.23
VAR_013978
Natural variant1281V → M in HOPS. Ref.34
VAR_025912
Natural variant1291G → R in HOPS. Ref.21 Ref.23
VAR_013979
Natural variant1321A → V in HOPS. Ref.32
VAR_013146
Natural variant1341T → H in HOPS; requires 2 nucleotide substitutions. Ref.34
VAR_025913
Natural variant1341T → N in HOPS; 9% of activity. Ref.26
VAR_011082
Natural variant1361R → H in HOPS; moderate; 33% of activity. Ref.23 Ref.24 Ref.30 Ref.34 Ref.38
VAR_006152
Natural variant1481T → I in HOPS. Ref.35
VAR_025914
Natural variant1521R → H in HOPS. Ref.6 Ref.30
Corresponds to variant rs149344982 [ dbSNP | Ensembl ].
VAR_013980
Natural variant1621G → S in HOPS. Ref.35
VAR_025915
Natural variant1621G → V in HOPS; severe; 1% of activity. Ref.23 Ref.24
VAR_006153
Natural variant1701N → D in HOPS. Ref.21 Ref.23
VAR_013981
Natural variant1711H → R in HOPS.
VAR_025916
Natural variant1711H → Y in HOPS; severe; 2% of activity. Ref.23 Ref.24
VAR_006154
Natural variant1761A → T in HOPS. Ref.26 Ref.30 Ref.34
Corresponds to variant rs121918019 [ dbSNP | Ensembl ].
VAR_011083
Natural variant1771A → T in HOPS; adult type; moderate allele. Ref.22 Ref.31
Corresponds to variant rs199669988 [ dbSNP | Ensembl ].
VAR_006155
Natural variant1791A → T in HOPS. Ref.16 Ref.30
VAR_006156
Natural variant1811S → L in HOPS; 1% of activity. Ref.29
VAR_013982
Natural variant1841R → W in HOPS; loss of activity. Ref.21 Ref.23 Ref.29
VAR_013983
Natural variant1891D → E in HOPS. Ref.35
VAR_025917
Natural variant1911E → G in HOPS; odonto. Ref.22
VAR_006157
Natural variant1911E → K in HOPS; moderate; frequent mutation in European countries. Ref.17 Ref.21 Ref.23 Ref.24 Ref.26 Ref.30 Ref.34
Corresponds to variant rs121918007 [ dbSNP | Ensembl ].
VAR_006158
Natural variant2011C → Y in HOPS. Ref.24 Ref.26
VAR_006159
Natural variant2071Q → P in HOPS. Ref.17
VAR_006160
Natural variant2111N → D in HOPS. Ref.30
VAR_013984
Natural variant2121I → F in HOPS.
VAR_025918
Natural variant2201G → A in HOPS. Ref.35
VAR_025919
Natural variant2201G → V in HOPS; odonto. Ref.30
VAR_013985
Natural variant2231R → Q in HOPS. Ref.34 Ref.38
VAR_025920
Natural variant2231R → W in HOPS; 3% of activity; severe allele. Ref.21 Ref.23 Ref.29 Ref.31 Ref.34 Ref.38
VAR_013986
Natural variant2241K → E in HOPS; infantile; partial loss of activity. Ref.25
VAR_011084
Natural variant2351E → G in HOPS. Ref.30
VAR_013987
Natural variant2461R → S in HOPS; 4% of activity. Ref.26 Ref.34
VAR_011085
Natural variant2491G → V in HOPS; partial loss of activity. Ref.23 Ref.24 Ref.29
VAR_013988
Natural variant2631Y → H Common polymorphism. Ref.3 Ref.9 Ref.17 Ref.21 Ref.34
Corresponds to variant rs3200254 [ dbSNP | Ensembl ].
VAR_006161
Natural variant2721R → H in HOPS; 6.8% of wild-type activity. Ref.38
VAR_025921
Natural variant2721R → L in HOPS. Ref.35
VAR_025922
Natural variant2751L → P in HOPS; childhood-type; severe allele. Ref.31
VAR_025923
Natural variant2891L → F in HOPS. Ref.4
VAR_006162
Natural variant2911E → K in HOPS; moderate; 8% of activity. Ref.21 Ref.23 Ref.33
VAR_013989
Natural variant2921P → T in HOPS; 4% of wild-type activity. Ref.38
VAR_025924
Natural variant293 – 2942Missing in HOPS.
VAR_025925
Natural variant2941D → A in HOPS. Ref.17 Ref.34 Ref.38
VAR_006163
Natural variant2941D → Y in HOPS. Ref.30
VAR_013990
Natural variant2951M → T in HOPS; 8.5% of wild-type activity. Ref.38
VAR_025926
Natural variant2971Y → D in HOPS; 1.3% of wild-type activity. Ref.38
VAR_025927
Natural variant2981E → K in HOPS. Ref.19
VAR_025928
Natural variant2991L → P in HOPS. Ref.34
VAR_025929
Natural variant3061D → V in HOPS. Ref.23 Ref.24
VAR_006164
Natural variant3111E → K in HOPS. Ref.35
VAR_025930
Natural variant3261G → R in HOPS; in a patient carrying also K-291. Ref.33
VAR_013991
Natural variant3271F → G in HOPS; requires 2 nucleotide substitutions. Ref.30
VAR_013992
Natural variant3271F → L in HOPS; childhood. Ref.20 Ref.22
VAR_006165
Natural variant3271Missing in HOPS. Ref.34
VAR_025931
Natural variant3341G → D in HOPS. Ref.18 Ref.21 Ref.23 Ref.38
VAR_006166
Natural variant3391G → R in HOPS. Ref.34
VAR_025932
Natural variant3481A → T in HOPS. Ref.26 Ref.34
VAR_011086
Natural variant3541E → D in HOPS.
VAR_025933
Natural variant3781D → V in HOPS; loss of activity. Ref.17 Ref.27 Ref.29 Ref.34
VAR_006167
Natural variant3811H → R in HOPS. Ref.26
VAR_011087
Natural variant3821V → I in HOPS. Ref.22
VAR_006168
Natural variant3911R → C in HOPS; moderate; 10% of activity. Ref.23
VAR_013993
Natural variant3911R → H in HOPS; childhood-type; severe allele.
VAR_025934
Natural variant3991A → S in HOPS. Ref.30
VAR_013994
Natural variant4061D → G in HOPS; 15% of activity. Ref.26
VAR_011088
Natural variant4111T → A in HOPS; absence of residual enzymatic activity. Ref.38
VAR_025935
Natural variant4141L → M in HOPS. Ref.34 Ref.36
VAR_025936
Natural variant4171N → S in HOPS. Ref.28
VAR_025937
Natural variant4231V → A in HOPS; 16% of activity. Ref.30
VAR_013995
Natural variant4261G → C in HOPS; infantile; partial loss of activity. Ref.25
VAR_011089
Natural variant4261G → D in HOPS. Ref.34
VAR_025938
Natural variant4361Y → H in HOPS. Ref.17
VAR_006169
Natural variant4451S → P in HOPS; severe; 2% of activity. Ref.21 Ref.23
VAR_013996
Natural variant4501R → C in HOPS; severe; 4% of activity. Ref.21 Ref.23
VAR_013997
Natural variant4501R → H in HOPS. Ref.26
VAR_011090
Natural variant4521E → K in HOPS. Ref.35
VAR_025939
Natural variant4561G → R in HOPS; loss of activity. Ref.20
VAR_011091
Natural variant4591V → M in HOPS; infantile. Ref.30
VAR_013998
Natural variant4681A → T in HOPS. Ref.35
VAR_025940
Natural variant4731G → S in HOPS. Ref.21 Ref.23
VAR_013999
Natural variant4761E → K in HOPS. Ref.23 Ref.24 Ref.34
VAR_006170
Natural variant4781N → I in HOPS; 9% of activity. Ref.26 Ref.29
VAR_011092
Natural variant4891C → S in HOPS; 9% of activity. Ref.26
VAR_011093
Natural variant4901I → F in HOPS; odonto; partial loss of activity. Ref.29
VAR_014000
Natural variant4911G → R in HOPS. Ref.21 Ref.23
VAR_014001
Natural variant5221V → A. Ref.27 Ref.31 Ref.34
Corresponds to variant rs34605986 [ dbSNP | Ensembl ].
VAR_011094

Experimental info

Sequence conflict291W → A AA sequence Ref.10
Sequence conflict1041N → K in CAA32376. Ref.3
Sequence conflict3611Q → H in BAA32129. Ref.1
Sequence conflict4461A → P in BAA32129. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 21, 2005. Version 4.
Checksum: 71B45F17F6211900

FASTA52457,305
        10         20         30         40         50         60 
MISPFLVLAI GTCLTNSLVP EKEKDPKYWR DQAQETLKYA LELQKLNTNV AKNVIMFLGD 

        70         80         90        100        110        120 
GMGVSTVTAA RILKGQLHHN PGEETRLEMD KFPFVALSKT YNTNAQVPDS AGTATAYLCG 

       130        140        150        160        170        180 
VKANEGTVGV SAATERSRCN TTQGNEVTSI LRWAKDAGKS VGIVTTTRVN HATPSAAYAH 

       190        200        210        220        230        240 
SADRDWYSDN EMPPEALSQG CKDIAYQLMH NIRDIDVIMG GGRKYMYPKN KTDVEYESDE 

       250        260        270        280        290        300 
KARGTRLDGL DLVDTWKSFK PRYKHSHFIW NRTELLTLDP HNVDYLLGLF EPGDMQYELN 

       310        320        330        340        350        360 
RNNVTDPSLS EMVVVAIQIL RKNPKGFFLL VEGGRIDHGH HEGKAKQALH EAVEMDRAIG 

       370        380        390        400        410        420 
QAGSLTSSED TLTVVTADHS HVFTFGGYTP RGNSIFGLAP MLSDTDKKPF TAILYGNGPG 

       430        440        450        460        470        480 
YKVVGGEREN VSMVDYAHNN YQAQSAVPLR HETHGGEDVA VFSKGPMAHL LHGVHEQNYV 

       490        500        510        520 
PHVMAYAACI GANLGHCAPA SSAGSLAAGP LLLALALYPL SVLF 

« Hide

Isoform 2 [UniParc].

Checksum: 4433599B70DBDB88
Show »

FASTA44748,909
Isoform 3 [UniParc].

Checksum: D57207402F616985
Show »

FASTA46951,045

References

« Hide 'large scale' references
[1]"Isolation and characterization of a cDNA encoding a human liver/bone/kidney-type alkaline phosphatase."
Weiss M.J., Henthorn P.S., Lafferty M.A., Slaughter C., Raducha M., Harris H.
Proc. Natl. Acad. Sci. U.S.A. 83:7182-7186(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Osteosarcoma.
[2]"Structure of the human liver/bone/kidney alkaline phosphatase gene."
Weiss M.J., Ray K., Henthorn P.S., Lamb B., Kadesch T., Harris H.
J. Biol. Chem. 263:12002-12010(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Osteosarcoma.
[3]"Nucleotide sequence of the human liver-type alkaline phosphatase cDNA."
Kishi F., Matsuura S., Kajii T.
Nucleic Acids Res. 17:2129-2129(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT HIS-263.
Tissue: Liver.
[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.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Hippocampus.
[6]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-152.
Tissue: Brain.
[7]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-263.
Tissue: Brain, Cerebellum, Lymphoma and Peripheral nerve.
[10]"Human liver alkaline phosphatase, purification and partial sequencing: homology with the placental isozyme."
Garattini E., Hua J.-C., Pan Y.C.E., Udenfriend S.
Arch. Biochem. Biophys. 245:331-337(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-49.
Tissue: Liver.
[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.
[12]"Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins."
Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C., Jensen O.N.
Mol. Cell. Proteomics 2:1261-1270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."
Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N.
J. Proteome Res. 5:935-943(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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.
Tissue: Liver.
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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.
[17]"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.
[18]"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.
[19]"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: VARIANT HOPS LYS-298.
[20]"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: VARIANTS HOPS LEU-327 AND ARG-456.
[21]"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.
[22]"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.
[23]"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.
[24]"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.
[25]"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 HOPS GLU-224 AND CYS-426.
[26]"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. expand/collapse author list , 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.
[27]"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.
[28]"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.
[29]"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.
[30]"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 HOPS CYS-28; 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; ALA-423 AND MET-459.
[31]"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: VARIANTS HOPS MET-68; SER-71; THR-177; TRP-223; PRO-275 AND HIS-391, CHARACTERIZATION OF VARIANTS HOPS MET-68; SER-71; THR-177; TRP-223; PRO-275 AND HIS-391, VARIANT ALA-522, CHARACTERIZATION OF VARIANT ALA-522.
[32]"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.
[33]"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.
[34]"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.
[35]"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.
[36]"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.
[37]"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.
[38]"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.
+Additional computationally mapped references.

Web resources

ALPL

Tissue nonspecific alkaline phosphatase gene mutations database

GeneReviews
Wikipedia

Alkaline phosphatase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24439 expand/collapse EMBL AC list , M24429, M24430, M24431, M24432, M24433, M24434, M24435, M24436, M24437, M24438 Genomic DNA. Translation: AAB59378.1.
X14174 mRNA. Translation: CAA32376.1.
AB011406 mRNA. Translation: BAA32129.1.
AK295608 mRNA. Translation: BAH12123.1.
AK298085 mRNA. Translation: BAH12722.1.
AB209814 mRNA. Translation: BAD93051.1. Different initiation.
AL592309, AL359815 Genomic DNA. Translation: CAH72079.1.
AL359815, AL592309 Genomic DNA. Translation: CAI16259.1.
CH471134 Genomic DNA. Translation: EAW94977.1.
BC021289 mRNA. Translation: AAH21289.3.
BC066116 mRNA. Translation: AAH66116.2.
BC090861 mRNA. Translation: AAH90861.2.
BC110909 mRNA. Translation: AAI10910.2.
BC126165 mRNA. Translation: AAI26166.1.
BC136325 mRNA. Translation: AAI36326.1.
PIRPAHUH. S03613.
RefSeqNP_000469.3. NM_000478.4.
NP_001120973.2. NM_001127501.2.
NP_001170991.1. NM_001177520.1.
XP_005245875.1. XM_005245818.1.
UniGeneHs.75431.

3D structure databases

ProteinModelPortalP05186.
SMRP05186. Positions 18-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106750. 1 interaction.
IntActP05186. 6 interactions.

Chemistry

BindingDBP05186.
ChEMBLCHEMBL5979.
DrugBankDB01143. Amifostine.

PTM databases

PhosphoSiteP05186.

Polymorphism databases

DMDM68067533.

Proteomic databases

PaxDbP05186.
PeptideAtlasP05186.
PRIDEP05186.

Protocols and materials databases

DNASU249.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374832; ENSP00000363965; ENSG00000162551. [P05186-1]
ENST00000374840; ENSP00000363973; ENSG00000162551. [P05186-1]
ENST00000425315; ENSP00000394765; ENSG00000162551. [P05186-1]
ENST00000539907; ENSP00000437674; ENSG00000162551. [P05186-2]
ENST00000540617; ENSP00000442672; ENSG00000162551. [P05186-3]
GeneID249.
KEGGhsa:249.
UCSCuc001bet.3. human. [P05186-1]
uc010odp.2. human. [P05186-2]

Organism-specific databases

CTD249.
GeneCardsGC01P021835.
HGNCHGNC:438. ALPL.
HPACAB020829.
HPA007105.
HPA008765.
MIM146300. phenotype.
171760. gene.
241500. phenotype.
241510. phenotype.
neXtProtNX_P05186.
Orphanet247676. Adult hypophosphatasia.
247667. Childhood-onset hypophosphatasia.
247651. Infantile hypophosphatasia.
247685. Odontohypophosphatasia.
247623. Perinatal lethal hypophosphatasia.
247638. Prenatal benign hypophosphatasia.
PharmGKBPA24729.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1785.
HOVERGENHBG007345.
InParanoidP05186.
KOK01077.
OMAMQEALVP.
OrthoDBEOG7SN8CH.
PhylomeDBP05186.
TreeFamTF323513.

Enzyme and pathway databases

BRENDA3.1.3.1. 2681.

Gene expression databases

ArrayExpressP05186.
BgeeP05186.
GenevestigatorP05186.

Family and domain databases

Gene3D3.40.720.10. 1 hit.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view]
PfamPF00245. Alk_phosphatase. 1 hit.
[Graphical view]
PRINTSPR00113. ALKPHPHTASE.
SMARTSM00098. alkPPc. 1 hit.
[Graphical view]
SUPFAMSSF53649. SSF53649. 1 hit.
PROSITEPS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiALPL.
GenomeRNAi249.
NextBio997.
PROP05186.
SOURCESearch...

Entry information

Entry namePPBT_HUMAN
AccessionPrimary (citable) accession number: P05186
Secondary accession number(s): A1A4E7 expand/collapse secondary AC list , B2RMP8, B7Z387, B7Z4Y6, O75090, Q2TAI7, Q59EJ7, Q5BKZ5, Q5VTG5, Q6NZI8, Q8WU32, Q9UBK0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: June 21, 2005
Last modified: March 19, 2014
This is version 173 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM