SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P05187

- PPB1_HUMAN

UniProt

P05187 - PPB1_HUMAN

(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)

Protein
Alkaline phosphatase, placental type
Gene
ALPP, PLAP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.

Cofactori

Binds 1 magnesium ion.4 Publications
Binds 2 zinc ions.4 Publications

Sites

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

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
Complete GO annotation...

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

Cell membrane; Lipid-anchorGPI-anchor 2 Publications

Topology

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

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
Complete GO annotation...

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 Publication
Add
BLAST
Chaini23 – 506484Alkaline phosphatase, placental type
PRO_0000024031Add
BLAST
Propeptidei507 – 53529Removed in mature form
PRO_0000024032Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi143 ↔ 2055 Publications
Glycosylationi144 – 1441N-linked (GlcNAc...)3 Publications
Glycosylationi271 – 2711N-linked (GlcNAc...)3 Publications
Disulfide bondi489 ↔ 4965 Publications
Lipidationi506 – 5061GPI-anchor amidated aspartate2 Publications

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

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.

Miscellaneous databases

EvolutionaryTraceiP05187.

Family & Domainsi

Sequence similaritiesi

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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661M → V in AAA51709. 1 Publication
Sequence conflicti261 – 2622AK → GE in AAA51706. 1 Publication
Sequence conflicti277 – 2771Q → R in AAA51709. 1 Publication
Sequence conflicti285 – 2851T → A in AAA51709. 1 Publication
Sequence conflicti324 – 3241N → H in AAA51706. 1 Publication
Sequence conflicti389 – 3891Y → C in AAA51709. 1 Publication
Sequence conflicti394 – 3941S → G in AAA51709. 1 Publication
Sequence conflicti396 – 3972IF → FI in AAA51706. 1 Publication
Sequence conflicti401 – 4011P → A in AAA51706. 1 Publication
Sequence conflicti436 – 4361S → T1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 168 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

Similar proteinsi