Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P05187

- PPB1_HUMAN

UniProt

P05187 - PPB1_HUMAN

Protein

Alkaline phosphatase, placental type

Gene

ALPP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (01 Jul 1989)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    A phosphate monoester + H2O = an alcohol + phosphate.PROSITE-ProRule annotation

    Cofactori

    Binds 1 magnesium ion.
    Binds 2 zinc ions.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi64 – 641Magnesium4 Publications
    Metal bindingi64 – 641Zinc 14 Publications
    Active sitei114 – 1141Phosphoserine intermediate
    Metal bindingi114 – 1141Zinc 14 Publications
    Metal bindingi177 – 1771Magnesium4 Publications
    Metal bindingi333 – 3331Magnesium4 Publications
    Metal bindingi338 – 3381Zinc 24 Publications
    Metal bindingi342 – 3421Zinc 2; via tele nitrogen4 Publications
    Metal bindingi379 – 3791Zinc 14 Publications
    Metal bindingi380 – 3801Zinc 1; via tele nitrogen4 Publications
    Metal bindingi454 – 4541Zinc 2; via tele nitrogen4 Publications

    GO - Molecular functioni

    1. alkaline phosphatase activity Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. dephosphorylation Source: GOC

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alkaline phosphatase, placental type (EC:3.1.3.1)
    Alternative name(s):
    Alkaline phosphatase Regan isozyme
    Placental alkaline phosphatase 1
    Short name:
    PLAP-1
    Gene namesi
    Name:ALPP
    Synonyms:PLAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:439. ALPP.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. cell surface Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24730.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 506484Alkaline phosphatase, placental typePRO_0000024031Add
    BLAST
    Propeptidei507 – 53529Removed in mature formPRO_0000024032Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi143 ↔ 205
    Glycosylationi144 – 1441N-linked (GlcNAc...)3 Publications
    Glycosylationi271 – 2711N-linked (GlcNAc...)3 Publications
    Disulfide bondi489 ↔ 496
    Lipidationi506 – 5061GPI-anchor amidated aspartate1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP05187.
    PaxDbiP05187.
    PRIDEiP05187.

    PTM databases

    PhosphoSiteiP05187.

    Expressioni

    Tissue specificityi

    Detected in placenta (at protein level).1 Publication

    Gene expression databases

    BgeeiP05187.
    CleanExiHS_ALPP.
    GenevestigatoriP05187.

    Organism-specific databases

    HPAiCAB026327.
    HPA038764.
    HPA038765.
    HPA051699.

    Interactioni

    Subunit structurei

    Homodimer.4 Publications

    Protein-protein interaction databases

    BioGridi106751. 21 interactions.
    IntActiP05187. 9 interactions.
    MINTiMINT-4054397.
    STRINGi9606.ENSP00000375881.

    Structurei

    Secondary structure

    1
    535
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi26 – 294
    Helixi31 – 4717
    Beta strandi56 – 638
    Helixi68 – 8114
    Helixi93 – 953
    Beta strandi97 – 1037
    Helixi114 – 12310
    Beta strandi132 – 1343
    Helixi143 – 1453
    Helixi154 – 1607
    Beta strandi164 – 1729
    Helixi176 – 1794
    Turni180 – 1823
    Helixi193 – 1953
    Helixi198 – 2025
    Helixi208 – 2147
    Beta strandi219 – 2246
    Helixi226 – 2294
    Helixi243 – 2453
    Beta strandi249 – 2513
    Helixi255 – 2617
    Beta strandi266 – 2694
    Helixi272 – 2798
    Beta strandi285 – 2906
    Beta strandi292 – 2954
    Helixi299 – 3013
    Turni304 – 3063
    Helixi310 – 32112
    Beta strandi328 – 3347
    Helixi337 – 3426
    Helixi346 – 36621
    Turni369 – 3713
    Beta strandi372 – 3798
    Beta strandi381 – 3866
    Beta strandi411 – 4188
    Helixi433 – 4364
    Beta strandi445 – 4473
    Beta strandi459 – 4657
    Helixi468 – 4703
    Beta strandi473 – 4764
    Helixi479 – 4879
    Helixi491 – 4933

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EW2X-ray1.82A23-535[»]
    1ZEBX-ray1.90A23-506[»]
    1ZEDX-ray1.57A23-506[»]
    1ZEFX-ray1.90A23-506[»]
    2GLQX-ray1.60A23-506[»]
    3MK0X-ray1.90A23-506[»]
    3MK1X-ray1.57A23-506[»]
    3MK2X-ray1.89A23-503[»]
    ProteinModelPortaliP05187.
    SMRiP05187. Positions 23-503.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05187.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei513 – 52917HelicalAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alkaline phosphatase family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1785.
    HOGENOMiHOG000099118.
    HOVERGENiHBG007345.
    InParanoidiP05187.
    KOiK01077.
    OMAiLNAQPAY.
    OrthoDBiEOG7SN8CH.
    PhylomeDBiP05187.
    TreeFamiTF323513.

    Family and domain databases

    Gene3Di3.40.720.10. 1 hit.
    InterProiIPR017849. Alkaline_Pase-like_a/b/a.
    IPR001952. Alkaline_phosphatase.
    IPR018299. Alkaline_phosphatase_AS.
    IPR017850. Alkaline_phosphatase_core.
    [Graphical view]
    PfamiPF00245. Alk_phosphatase. 1 hit.
    [Graphical view]
    PRINTSiPR00113. ALKPHPHTASE.
    SMARTiSM00098. alkPPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF53649. SSF53649. 1 hit.
    PROSITEiPS00123. ALKALINE_PHOSPHATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P05187-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLGPCMLLLL LLLGLRLQLS LGIIPVEEEN PDFWNREAAE ALGAAKKLQP    50
    AQTAAKNLII FLGDGMGVST VTAARILKGQ KKDKLGPEIP LAMDRFPYVA 100
    LSKTYNVDKH VPDSGATATA YLCGVKGNFQ TIGLSAAARF NQCNTTRGNE 150
    VISVMNRAKK AGKSVGVVTT TRVQHASPAG TYAHTVNRNW YSDADVPASA 200
    RQEGCQDIAT QLISNMDIDV ILGGGRKYMF RMGTPDPEYP DDYSQGGTRL 250
    DGKNLVQEWL AKRQGARYVW NRTELMQASL DPSVTHLMGL FEPGDMKYEI 300
    HRDSTLDPSL MEMTEAALRL LSRNPRGFFL FVEGGRIDHG HHESRAYRAL 350
    TETIMFDDAI ERAGQLTSEE DTLSLVTADH SHVFSFGGYP LRGSSIFGLA 400
    PGKARDRKAY TVLLYGNGPG YVLKDGARPD VTESESGSPE YRQQSAVPLD 450
    EETHAGEDVA VFARGPQAHL VHGVQEQTFI AHVMAFAACL EPYTACDLAP 500
    PAGTTDAAHP GRSVVPALLP LLAGTLLLLE TATAP 535
    Length:535
    Mass (Da):57,954
    Last modified:July 1, 1989 - v2
    Checksum:i13C136679A70C76B
    GO

    Sequence cautioni

    The sequence AAA51708.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661M → V in AAA51709. (PubMed:3461452)Curated
    Sequence conflicti261 – 2622AK → GE in AAA51706. (PubMed:3001717)Curated
    Sequence conflicti277 – 2771Q → R in AAA51709. (PubMed:3461452)Curated
    Sequence conflicti285 – 2851T → A in AAA51709. (PubMed:3461452)Curated
    Sequence conflicti324 – 3241N → H in AAA51706. (PubMed:3001717)Curated
    Sequence conflicti389 – 3891Y → C in AAA51709. (PubMed:3461452)Curated
    Sequence conflicti394 – 3941S → G in AAA51709. (PubMed:3461452)Curated
    Sequence conflicti396 – 3972IF → FI in AAA51706. (PubMed:3001717)Curated
    Sequence conflicti401 – 4011P → A in AAA51706. (PubMed:3001717)Curated
    Sequence conflicti436 – 4361S → T(PubMed:3459156)Curated

    Polymorphismi

    Placental ALP is highly polymorphic, there are at least three common alleles.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251P → L.2 Publications
    Corresponds to variant rs1130335 [ dbSNP | Ensembl ].
    VAR_017419
    Natural varianti89 – 891I → L.1 Publication
    Corresponds to variant rs13026692 [ dbSNP | Ensembl ].
    VAR_050520
    Natural varianti231 – 2311R → P.1 Publication
    Corresponds to variant rs1048988 [ dbSNP | Ensembl ].
    VAR_050521
    Natural varianti263 – 2631R → H.1 Publication
    Corresponds to variant rs2853378 [ dbSNP | Ensembl ].
    VAR_050522
    Natural varianti451 – 4511E → G.
    Corresponds to variant rs1048994 [ dbSNP | Ensembl ].
    VAR_050523

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19159 Genomic DNA. Translation: AAA51710.1.
    M13077 mRNA. Translation: AAC97139.1.
    M14169 mRNA. Translation: AAA51708.1. Different initiation.
    M14170 mRNA. Translation: AAA51709.1.
    AC068134 Genomic DNA. Translation: AAY24087.1.
    BC009647 mRNA. Translation: AAH09647.1.
    BC068501 mRNA. Translation: AAH68501.1.
    BC094743 mRNA. Translation: AAH94743.1.
    M12551 mRNA. Translation: AAA51706.1.
    CCDSiCCDS2490.1.
    PIRiA31074. PAHUA.
    RefSeqiNP_001623.3. NM_001632.3.
    UniGeneiHs.284255.

    Genome annotation databases

    EnsembliENST00000392027; ENSP00000375881; ENSG00000163283.
    GeneIDi250.
    KEGGihsa:250.
    UCSCiuc002vsq.3. human.

    Polymorphism databases

    DMDMi130737.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Alkaline phosphatase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19159 Genomic DNA. Translation: AAA51710.1 .
    M13077 mRNA. Translation: AAC97139.1 .
    M14169 mRNA. Translation: AAA51708.1 . Different initiation.
    M14170 mRNA. Translation: AAA51709.1 .
    AC068134 Genomic DNA. Translation: AAY24087.1 .
    BC009647 mRNA. Translation: AAH09647.1 .
    BC068501 mRNA. Translation: AAH68501.1 .
    BC094743 mRNA. Translation: AAH94743.1 .
    M12551 mRNA. Translation: AAA51706.1 .
    CCDSi CCDS2490.1.
    PIRi A31074. PAHUA.
    RefSeqi NP_001623.3. NM_001632.3.
    UniGenei Hs.284255.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EW2 X-ray 1.82 A 23-535 [» ]
    1ZEB X-ray 1.90 A 23-506 [» ]
    1ZED X-ray 1.57 A 23-506 [» ]
    1ZEF X-ray 1.90 A 23-506 [» ]
    2GLQ X-ray 1.60 A 23-506 [» ]
    3MK0 X-ray 1.90 A 23-506 [» ]
    3MK1 X-ray 1.57 A 23-506 [» ]
    3MK2 X-ray 1.89 A 23-503 [» ]
    ProteinModelPortali P05187.
    SMRi P05187. Positions 23-503.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106751. 21 interactions.
    IntActi P05187. 9 interactions.
    MINTi MINT-4054397.
    STRINGi 9606.ENSP00000375881.

    Chemistry

    BindingDBi P05187.
    ChEMBLi CHEMBL4458.

    PTM databases

    PhosphoSitei P05187.

    Polymorphism databases

    DMDMi 130737.

    Proteomic databases

    MaxQBi P05187.
    PaxDbi P05187.
    PRIDEi P05187.

    Protocols and materials databases

    DNASUi 250.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000392027 ; ENSP00000375881 ; ENSG00000163283 .
    GeneIDi 250.
    KEGGi hsa:250.
    UCSCi uc002vsq.3. human.

    Organism-specific databases

    CTDi 250.
    GeneCardsi GC02P233244.
    HGNCi HGNC:439. ALPP.
    HPAi CAB026327.
    HPA038764.
    HPA038765.
    HPA051699.
    MIMi 171800. gene.
    neXtProti NX_P05187.
    PharmGKBi PA24730.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1785.
    HOGENOMi HOG000099118.
    HOVERGENi HBG007345.
    InParanoidi P05187.
    KOi K01077.
    OMAi LNAQPAY.
    OrthoDBi EOG7SN8CH.
    PhylomeDBi P05187.
    TreeFami TF323513.

    Miscellaneous databases

    ChiTaRSi ALPP. human.
    EvolutionaryTracei P05187.
    GeneWikii Placental_alkaline_phosphatase.
    GenomeRNAii 250.
    NextBioi 1001.
    PROi P05187.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05187.
    CleanExi HS_ALPP.
    Genevestigatori P05187.

    Family and domain databases

    Gene3Di 3.40.720.10. 1 hit.
    InterProi IPR017849. Alkaline_Pase-like_a/b/a.
    IPR001952. Alkaline_phosphatase.
    IPR018299. Alkaline_phosphatase_AS.
    IPR017850. Alkaline_phosphatase_core.
    [Graphical view ]
    Pfami PF00245. Alk_phosphatase. 1 hit.
    [Graphical view ]
    PRINTSi PR00113. ALKPHPHTASE.
    SMARTi SM00098. alkPPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53649. SSF53649. 1 hit.
    PROSITEi PS00123. ALKALINE_PHOSPHATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the human placental alkaline phosphatase gene. Evolution of the 5' flanking region by deletion/substitution."
      Knoll B.J., Rothblum K.N., Longley M.A.
      J. Biol. Chem. 263:12020-12027(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Molecular cloning and sequence analysis of human placental alkaline phosphatase."
      Millan J.L.
      J. Biol. Chem. 261:3112-3115(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-231.
    3. "Products of two common alleles at the locus for human placental alkaline phosphatase differ by seven amino acids."
      Henthorn P.S., Knoll B.J., Raducha M., Rothblum K.N., Slaughter C., Weiss M., Lafferty M.A., Fischer T., Harris H.
      Proc. Natl. Acad. Sci. U.S.A. 83:5597-5601(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANTS LEU-25 AND HIS-263.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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], VARIANT LEU-89.
      Tissue: Cervix and Placenta.
    6. "Cloning, sequencing, and chromosomal localization of human term placental alkaline phosphatase cDNA."
      Kam W., Clauser E., Kim Y.S., Kan Y.W., Rutter W.J.
      Proc. Natl. Acad. Sci. U.S.A. 82:8715-8719(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-535, VARIANT LEU-25.
    7. "Purification and partial sequencing of human placental alkaline phosphatase."
      Ezra E., Blacher R., Udenfriend S.
      Biochem. Biophys. Res. Commun. 116:1076-1083(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-64.
    8. "Expression of different-sized placental alkaline phosphatase mRNAs in placenta and choriocarcinoma cells."
      Ovitt C.E., Strauss A.W., Alpers D.H., Chou J.Y., Boime I.
      Proc. Natl. Acad. Sci. U.S.A. 83:3781-3785(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 382-535.
    9. "Aspartic acid-484 of nascent placental alkaline phosphatase condenses with a phosphatidylinositol glycan to become the carboxyl terminus of the mature enzyme."
      Micanovic R., Bailey C.A., Brink L., Gerber L., Pan Y.C.E., Hulmes J.D., Udenfriend S.
      Proc. Natl. Acad. Sci. U.S.A. 85:1398-1402(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 485-535.
    10. "Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase."
      Micanovic R., Gerber L.D., Berger J., Kodukula K., Udenfriend S.
      Proc. Natl. Acad. Sci. U.S.A. 87:157-161(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR AT ASP-506.
    11. "Site-specific mutations in the COOH-terminus of placental alkaline phosphatase: a single amino acid change converts a phosphatidylinositol-glycan-anchored protein to a secreted protein."
      Lowe M.E.
      J. Cell Biol. 116:799-807(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: EFFECT OF MUTAGENESIS OF C-TERMINAL PEPTIDE ON GPI-ANCHORING.
    12. "Function assignment to conserved residues in mammalian alkaline phosphatases."
      Kozlenkov A., Manes T., Hoylaerts M.F., Millan J.L.
      J. Biol. Chem. 277:22992-22999(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity."
      Le Du M.H., Stigbrand T., Taussig M.J., Menez A., Stura E.A.
      J. Biol. Chem. 276:9158-9165(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 23-535 IN COMPLEX WITH MAGNESIUM AND ZINC, COFACTOR, DISULFIDE BOND, SUBUNIT.
    15. "Structural studies of human placental alkaline phosphatase in complex with functional ligands."
      Llinas P., Stura E.A., Menez A., Kiss Z., Stigbrand T., Millan J.L., Le Du M.H.
      J. Mol. Biol. 350:441-451(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 23-506 IN COMPLEX WITH MAGNESIUM AND ZINC, GLYCOSYLATION AT ASN-144 AND ASN-271, COFACTOR, DISULFIDE BOND, SUBUNIT.
    16. "Structural studies of human alkaline phosphatase in complex with strontium: implication for its secondary effect in bones."
      Llinas P., Masella M., Stigbrand T., Menez A., Stura E.A., Le Du M.H.
      Protein Sci. 15:1691-1700(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 23-506 IN COMPLEX WITH MAGNESIUM AND ZINC, GLYCOSYLATION AT ASN-144 AND ASN-271, COFACTOR, DISULFIDE BOND, SUBUNIT.
    17. "Refined structures of placental alkaline phosphatase show a consistent pattern of interactions at the peripheral site."
      Stec B., Cheltsov A., Millan J.L.
      Acta Crystallogr. F 66:866-870(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 23-506 IN COMPLEX WITH MAGNESIUM AND ZINC, GLYCOSYLATION AT ASN-144 AND ASN-271, COFACTOR, DISULFIDE BOND, SUBUNIT, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiPPB1_HUMAN
    AccessioniPrimary (citable) accession number: P05187
    Secondary accession number(s): P05188
    , P06861, Q53S78, Q96DB7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 169 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Miscellaneous

    In most mammals there are four different isozymes: placental, placental-like, intestinal and tissue non-specific (liver/bone/kidney).

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3