Sequence of PPB1_HUMAN
EC Number:3.1.3.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
a phosphate monoester + H2O = an alcohol + phosphate
General information:
Sequence
0 MLGPCMLLLL LLLGLRLQLS LGIIPVEEEN PDFWNREAAE ALGAAKKLQP AQTAAKNLII
60 FLGDGMGVST VTAARILKGQ KKDKLGPEIP LAMDRFPYVA LSKTYNVDKH VPDSGATATA
120 YLCGVKGNFQ TIGLSAAARF NQCNTTRGNE VISVMNRAKK AGKSVGVVTT TRVQHASPAG
180 TYAHTVNRNW YSDADVPASA RQEGCQDIAT QLISNMDIDV ILGGGRKYMF RMGTPDPEYP
240 DDYSQGGTRL DGKNLVQEWL AKRQGARYVW NRTELMQASL DPSVTHLMGL FEPGDMKYEI
300 HRDSTLDPSL MEMTEAALRL LSRNPRGFFL FVEGGRIDHG HHESRAYRAL TETIMFDDAI
360 ERAGQLTSEE DTLSLVTADH SHVFSFGGYP LRGSSIFGLA PGKARDRKAY TVLLYGNGPG
420 YVLKDGARPD VTESESGSPE YRQQSAVPLD EETHAGEDVA VFARGPQAHL VHGVQEQTFI
480 AHVMAFAACL EPYTACDLAP PAGTTDAAHP GRSVVPALLP LLAGTLLLLE TATAP
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
344528
Knoll B.J.,Rothblum K.N.,Longley M.A.
Nucleotide sequence of the human placental alkaline phosphatase gene. Evolution of the 5' flanking region by deletion/substitution.
J. Biol. Chem.
263
12020-12027
1988
344529
Millan J.L.
Molecular cloning and sequence analysis of human placental alkaline phosphatase.
J. Biol. Chem.
261
3112-3115
1986
344530
Henthorn P.S.,Knoll B.J.,Raducha M.,Rothblum K.N.,Slaughter C.,Weiss M.,Lafferty M.A.,Fischer T.,Harris H.
Products of two common alleles at the locus for human placental alkaline phosphatase differ by seven amino acids.
Proc. Natl. Acad. Sci. U.S.A.
83
5597-5601
1986
344531
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.
Generation and annotation of the DNA sequences of human chromosomes 2 and 4.
Nature
434
724-731
2005
344532
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
344533
Kam W.,Clauser E.,Kim Y.S.,Kan Y.W.,Rutter W.J.
Cloning, sequencing, and chromosomal localization of human term placental alkaline phosphatase cDNA.
Proc. Natl. Acad. Sci. U.S.A.
82
8715-8719
1985
344534
Ezra E.,Blacher R.,Udenfriend S.
Purification and partial sequencing of human placental alkaline phosphatase.
Biochem. Biophys. Res. Commun.
116
1076-1083
1983
344535
Ovitt C.E.,Strauss A.W.,Alpers D.H.,Chou J.Y.,Boime I.
Expression of different-sized placental alkaline phosphatase mRNAs in placenta and choriocarcinoma cells.
Proc. Natl. Acad. Sci. U.S.A.
83
3781-3785
1986
344536
Micanovic R.,Bailey C.A.,Brink L.,Gerber L.,Pan Y.C.E.,Hulmes J.D.,Udenfriend S.
Aspartic acid-484 of nascent placental alkaline phosphatase condenses with a phosphatidylinositol glycan to become the carboxyl terminus of the mature enzyme.
Proc. Natl. Acad. Sci. U.S.A.
85
1398-1402
1988
344537
Micanovic R.,Gerber L.D.,Berger J.,Kodukula K.,Udenfriend S.
Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase.
Proc. Natl. Acad. Sci. U.S.A.
87
157-161
1990
344538
Watanabe T.,Wada N.,Kim E.E.,Wyckoff H.W.,Chou J.Y.
Mutation of a single amino acid converts germ cell alkaline phosphatase to placental alkaline phosphatase.
J. Biol. Chem.
266
21174-21178
1991
344539
Lowe M.E.
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.
J. Cell Biol.
116
799-807
1992
344540
Kozlenkov A.,Manes T.,Hoylaerts M.F.,Millan J.L.
Function assignment to conserved residues in mammalian alkaline phosphatases.
J. Biol. Chem.
277
22992-22999
2002
344541
Dephoure N.,Zhou C.,Villen J.,Beausoleil S.A.,Bakalarski C.E.,Elledge S.J.,Gygi S.P.
A quantitative atlas of mitotic phosphorylation.
Proc. Natl. Acad. Sci. U.S.A.
105
10762-10767
2008
344542
Hoylaerts M.F.,Van Kerckhoven S.,Kiffer-Moreira T.,Sheen C.,Narisawa S.,Millan J.L.
Functional significance of calcium binding to tissue-nonspecific alkaline phosphatase.
PLoS ONE
10
e0119874-e0119874
2015
344543
Le Du M.H.,Stigbrand T.,Taussig M.J.,Menez A.,Stura E.A.
Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity.
J. Biol. Chem.
276
9158-9165
2001
344544
Llinas P.,Stura E.A.,Menez A.,Kiss Z.,Stigbrand T.,Millan J.L.,Le Du M.H.
Structural studies of human placental alkaline phosphatase in complex with functional ligands.
J. Mol. Biol.
350
441-451
2005
344545
Llinas P.,Masella M.,Stigbrand T.,Menez A.,Stura E.A.,Le Du M.H.
Structural studies of human alkaline phosphatase in complex with strontium: implication for its secondary effect in bones.
Protein Sci.
15
1691-1700
2006
344546
Stec B.,Cheltsov A.,Millan J.L.
Refined structures of placental alkaline phosphatase show a consistent pattern of interactions at the peripheral site.
Acta Crystallogr. F
66
866-870
2010
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