ALPP

Functionⁱ

Miscellaneous

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

Catalytic activityⁱ

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

Cofactorⁱ

Protein has several cofactor binding sites:

Mg²⁺
4 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.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.
- Ref.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.
- Ref.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.
Note: Binds 1 Mg²⁺ ion.
4 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.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.
- Ref.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.
- Ref.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.
Zn²⁺
4 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.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.
- Ref.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.
- Ref.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.
Note: Binds 2 Zn²⁺ ions.
4 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.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.
- Ref.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.
- Ref.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.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	64	Magnesium4 Publications	1
Metal bindingⁱ	64	Zinc 14 Publications	1
Active siteⁱ	114	Phosphoserine intermediate	1
Metal bindingⁱ	114	Zinc 14 Publications	1
Metal bindingⁱ	177	Magnesium4 Publications	1
Metal bindingⁱ	333	Magnesium4 Publications	1
Metal bindingⁱ	338	Zinc 24 Publications	1
Metal bindingⁱ	342	Zinc 2; via tele nitrogen4 Publications	1
Metal bindingⁱ	379	Zinc 14 Publications	1
Metal bindingⁱ	380	Zinc 1; via tele nitrogen4 Publications	1
Metal bindingⁱ	454	Zinc 2; via tele nitrogen4 Publications	1

GO - Molecular functionⁱ

alkaline phosphatase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 2017684
magnesium ion binding Source: UniProtKB
zinc ion binding Source: UniProtKB

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase
Ligand	Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAⁱ	3.1.3.1 2681
Reactomeⁱ	R-HSA-6811438 Intra-Golgi traffic
SABIO-RKⁱ	P05187

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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
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
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 2

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000163283.6
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:439 ALPP
MIMⁱ	171800 gene
neXtProtⁱ	NX_P05187

Topology

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transmembraneⁱ	513 – 529	HelicalAdd BLAST		17

Keywords - Cellular componentⁱ

Cell membrane, Membrane

Pathology & Biotechⁱ

Organism-specific databases

DisGeNET More...DisGeNETⁱ	250
Open Targets More...OpenTargetsⁱ	ENSG00000163283
PharmGKBⁱ	PA24730

Chemistry databases

ChEMBLⁱ	CHEMBL4458
Drug and drug target database More...DrugBankⁱ	DB08413 METHYL-PHOSPHONIC ACID MONO-(4-NITRO-PHENYL) ESTER

Polymorphism and mutation databases

BioMutaⁱ	ALPP
DMDMⁱ	130737

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
Signal peptideⁱ	1 – 22	1 PublicationAdd BLAST	22
ChainⁱPRO_0000024031	23 – 506	Alkaline phosphatase, placental typeAdd BLAST	484
PropeptideⁱPRO_0000024032	507 – 535	Removed in mature formAdd BLAST	29

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Disulfide bondⁱ	143 ↔ 205	5 Publications
Glycosylationⁱ	144	N-linked (GlcNAc...) asparagine3 Publications	1
Glycosylationⁱ	271	N-linked (GlcNAc...) asparagine3 Publications	1
Disulfide bondⁱ	489 ↔ 496	5 Publications
Lipidationⁱ	506	GPI-anchor amidated aspartate1 Publication	1

Keywords - PTMⁱ

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

EPDⁱ	P05187
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P05187
PaxDbⁱ	P05187
PeptideAtlas More...PeptideAtlasⁱ	P05187
PRIDEⁱ	P05187
ProteomicsDBⁱ	51823

PTM databases

DEPODⁱ	P05187
iPTMnetⁱ	P05187
PhosphoSitePlusⁱ	P05187

Expressionⁱ

Tissue specificityⁱ

Detected in placenta (at protein level).1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000163283 Expressed in 35 organ(s), highest expression level in placenta
CleanExⁱ	HS_ALPP
Genevisibleⁱ	P05187 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB026327 HPA038764 HPA038765 HPA051699

HPAⁱ

CAB026327
HPA038764
HPA038765
HPA051699

Interactionⁱ

Subunit structureⁱ

Homodimer.4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
KRTAP4-12	Q9BQ66	3	EBI-1211484,EBI-739863
KRTAP5-9	P26371	5	EBI-1211484,EBI-3958099

Protein-protein interaction databases

BioGridⁱ	106751, 27 interactors
IntActⁱ	P05187, 46 interactors
Molecular INTeraction database More...MINTⁱ	P05187
STRINGⁱ	9606.ENSP00000375881

Chemistry databases

BindingDBⁱ

P05187

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	26 – 29	Combined sources	4
Helixⁱ	31 – 47	Combined sources	17
Beta strandⁱ	56 – 63	Combined sources	8
Helixⁱ	68 – 81	Combined sources	14
Helixⁱ	93 – 95	Combined sources	3
Beta strandⁱ	97 – 103	Combined sources	7
Helixⁱ	114 – 123	Combined sources	10
Beta strandⁱ	132 – 134	Combined sources	3
Helixⁱ	143 – 145	Combined sources	3
Helixⁱ	154 – 160	Combined sources	7
Beta strandⁱ	164 – 172	Combined sources	9
Helixⁱ	176 – 179	Combined sources	4
Turnⁱ	180 – 182	Combined sources	3
Helixⁱ	193 – 195	Combined sources	3
Helixⁱ	198 – 202	Combined sources	5
Helixⁱ	208 – 214	Combined sources	7
Beta strandⁱ	219 – 224	Combined sources	6
Helixⁱ	226 – 229	Combined sources	4
Helixⁱ	243 – 245	Combined sources	3
Beta strandⁱ	249 – 251	Combined sources	3
Helixⁱ	255 – 261	Combined sources	7
Beta strandⁱ	266 – 269	Combined sources	4
Helixⁱ	272 – 279	Combined sources	8
Beta strandⁱ	285 – 290	Combined sources	6
Beta strandⁱ	292 – 295	Combined sources	4
Helixⁱ	299 – 301	Combined sources	3
Turnⁱ	304 – 306	Combined sources	3
Helixⁱ	310 – 321	Combined sources	12
Beta strandⁱ	328 – 334	Combined sources	7
Helixⁱ	337 – 342	Combined sources	6
Helixⁱ	346 – 366	Combined sources	21
Turnⁱ	369 – 371	Combined sources	3
Beta strandⁱ	372 – 379	Combined sources	8
Beta strandⁱ	381 – 386	Combined sources	6
Beta strandⁱ	411 – 418	Combined sources	8
Helixⁱ	433 – 436	Combined sources	4
Beta strandⁱ	445 – 447	Combined sources	3
Beta strandⁱ	459 – 465	Combined sources	7
Helixⁱ	468 – 470	Combined sources	3
Beta strandⁱ	473 – 476	Combined sources	4
Helixⁱ	479 – 487	Combined sources	9
Helixⁱ	491 – 493	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P05187
SMRⁱ	P05187
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P05187

EvolutionaryTraceⁱ

P05187

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the alkaline phosphatase family.Curated

Keywords - Domainⁱ

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG4126 Eukaryota COG1785 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000008704
HOGENOMⁱ	HOG000099118
HOVERGENⁱ	HBG007345
InParanoidⁱ	P05187
KEGG Orthology (KO) More...KOⁱ	K01077
OMAⁱ	MKNKDFM
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G067H
PhylomeDBⁱ	P05187
TreeFamⁱ	TF323513

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd16012 ALP, 1 hit
Gene3Dⁱ	3.40.720.10, 1 hit
InterProⁱ	View protein in InterPro IPR017849 Alkaline_Pase-like_a/b/a IPR001952 Alkaline_phosphatase IPR018299 Alkaline_phosphatase_AS IPR017850 Alkaline_phosphatase_core_sf
PANTHERⁱ	PTHR11596 PTHR11596, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00245 Alk_phosphatase, 1 hit
PRINTSⁱ	PR00113 ALKPHPHTASE
SMARTⁱ	View protein in SMART SM00098 alkPPc, 1 hit
SUPFAMⁱ	SSF53649 SSF53649, 1 hit
PROSITEⁱ	View protein in PROSITE PS00123 ALKALINE_PHOSPHATASE, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P05187-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MLGPCMLLLL LLLGLRLQLS LGIIPVEEEN PDFWNREAAE ALGAAKKLQP 
        60         70         80         90        100
AQTAAKNLII FLGDGMGVST VTAARILKGQ KKDKLGPEIP LAMDRFPYVA 
       110        120        130        140        150
LSKTYNVDKH VPDSGATATA YLCGVKGNFQ TIGLSAAARF NQCNTTRGNE 
       160        170        180        190        200
VISVMNRAKK AGKSVGVVTT TRVQHASPAG TYAHTVNRNW YSDADVPASA 
       210        220        230        240        250
RQEGCQDIAT QLISNMDIDV ILGGGRKYMF RMGTPDPEYP DDYSQGGTRL 
       260        270        280        290        300
DGKNLVQEWL AKRQGARYVW NRTELMQASL DPSVTHLMGL FEPGDMKYEI 
       310        320        330        340        350
HRDSTLDPSL MEMTEAALRL LSRNPRGFFL FVEGGRIDHG HHESRAYRAL 
       360        370        380        390        400
TETIMFDDAI ERAGQLTSEE DTLSLVTADH SHVFSFGGYP LRGSSIFGLA 
       410        420        430        440        450
PGKARDRKAY TVLLYGNGPG YVLKDGARPD VTESESGSPE YRQQSAVPLD 
       460        470        480        490        500
EETHAGEDVA VFARGPQAHL VHGVQEQTFI AHVMAFAACL EPYTACDLAP 
       510        520        530 
PAGTTDAAHP GRSVVPALLP LLAGTLLLLE TATAP

Length:535

Mass (Da):57,954

Last modified:July 1, 1989 - v2

Checksum:ⁱ13C136679A70C76B

GO

Sequence cautionⁱ

The sequence AAA51708 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	66	M → V in AAA51709 (PubMed:3461452).Curated	1
Sequence conflictⁱ	261 – 262	AK → GE in AAA51706 (PubMed:3001717).Curated	2
Sequence conflictⁱ	277	Q → R in AAA51709 (PubMed:3461452).Curated	1
Sequence conflictⁱ	285	T → A in AAA51709 (PubMed:3461452).Curated	1
Sequence conflictⁱ	324	N → H in AAA51706 (PubMed:3001717).Curated	1
Sequence conflictⁱ	389	Y → C in AAA51709 (PubMed:3461452).Curated	1
Sequence conflictⁱ	394	S → G in AAA51709 (PubMed:3461452).Curated	1
Sequence conflictⁱ	396 – 397	IF → FI in AAA51706 (PubMed:3001717).Curated	2
Sequence conflictⁱ	401	P → A in AAA51706 (PubMed:3001717).Curated	1
Sequence conflictⁱ	436	S → T (PubMed:3459156).Curated	1

Polymorphismⁱ

Placental ALP is highly polymorphic, there are at least three common alleles.1 Publication

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_017419	25	P → L2 PublicationsCorresponds to variant dbSNP:rs1130335EnsemblClinVar.	1
Natural variantⁱVAR_050520	89	I → L1 PublicationCorresponds to variant dbSNP:rs13026692Ensembl.	1
Natural variantⁱVAR_050521	231	R → P1 PublicationCorresponds to variant dbSNP:rs1048988Ensembl.	1
Natural variantⁱVAR_050522	263	R → H1 PublicationCorresponds to variant dbSNP:rs2853378Ensembl.	1
Natural variantⁱVAR_050523	451	E → G. Corresponds to variant dbSNP:rs1048994Ensembl.	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS2490.1
PIRⁱ	A31074 PAHUA
NCBI Reference Sequences More...RefSeqⁱ	NP_001623.3, NM_001632.4
UniGeneⁱ	Hs.284255

Genome annotation databases

Ensemblⁱ	ENST00000392027; ENSP00000375881; ENSG00000163283
GeneIDⁱ	250
KEGGⁱ	hsa:250
UCSC genome browser More...UCSCⁱ	uc002vsq.4 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P05187	Alkaline phosphatase, germ cell type		HUMAN		532	UniRef90_P05187
Alkaline phosphatase		PANTR		534
Alkaline phosphatase		PANPA		534
Alkaline phosphatase		CERAT		532
UPI000B7B8ADA		PAPAN		626
+6

Protein	Similar proteins		Species	Score	Length	Source
P05187	Alkaline phosphatase, germ cell type		HUMAN		532	UniRef50_P05187
Alkaline phosphatase, tissue-nonspecific isozyme		BOVIN		524
Alkaline phosphatase, tissue-nonspecific isozyme		RAT		524
Alkaline phosphatase, tissue-nonspecific isozyme		FELCA		524
Alkaline phosphatase		PANPA		534
+127

Cross-referencesⁱ

Web resourcesⁱ

Wikipedia

Alkaline phosphatase entry

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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_001632.4
UniGeneⁱ	Hs.284255

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	106751, 27 interactors
IntActⁱ	P05187, 46 interactors
MINTⁱ	P05187
STRINGⁱ	9606.ENSP00000375881

Chemistry databases

BindingDBⁱ	P05187
ChEMBLⁱ	CHEMBL4458
DrugBankⁱ	DB08413 METHYL-PHOSPHONIC ACID MONO-(4-NITRO-PHENYL) ESTER

PTM databases

DEPODⁱ	P05187
iPTMnetⁱ	P05187
PhosphoSitePlusⁱ	P05187

Polymorphism and mutation databases

BioMutaⁱ	ALPP
DMDMⁱ	130737

Proteomic databases

EPDⁱ	P05187
MaxQBⁱ	P05187
PaxDbⁱ	P05187
PeptideAtlasⁱ	P05187
PRIDEⁱ	P05187
ProteomicsDBⁱ	51823

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	250
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000392027; ENSP00000375881; ENSG00000163283
GeneIDⁱ	250
KEGGⁱ	hsa:250
UCSCⁱ	uc002vsq.4 human

Organism-specific databases

CTDⁱ	250
DisGeNETⁱ	250
EuPathDBⁱ	HostDB:ENSG00000163283.6
GeneCardsⁱ	ALPP
HGNCⁱ	HGNC:439 ALPP
HPAⁱ	CAB026327 HPA038764 HPA038765 HPA051699
MIMⁱ	171800 gene
neXtProtⁱ	NX_P05187
OpenTargetsⁱ	ENSG00000163283
PharmGKBⁱ	PA24730
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG4126 Eukaryota COG1785 LUCA
GeneTreeⁱ	ENSGT00390000008704
HOGENOMⁱ	HOG000099118
HOVERGENⁱ	HBG007345
InParanoidⁱ	P05187
KOⁱ	K01077
OMAⁱ	MKNKDFM
OrthoDBⁱ	EOG091G067H
PhylomeDBⁱ	P05187
TreeFamⁱ	TF323513

Enzyme and pathway databases

BRENDAⁱ	3.1.3.1 2681
Reactomeⁱ	R-HSA-6811438 Intra-Golgi traffic
SABIO-RKⁱ	P05187

Miscellaneous databases

ChiTaRSⁱ	ALPP human
EvolutionaryTraceⁱ	P05187
GeneWikiⁱ	Placental_alkaline_phosphatase
GenomeRNAiⁱ	250
Protein Ontology More...PROⁱ	PR:P05187
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000163283 Expressed in 35 organ(s), highest expression level in placenta
CleanExⁱ	HS_ALPP
Genevisibleⁱ	P05187 HS

Family and domain databases

CDDⁱ	cd16012 ALP, 1 hit
Gene3Dⁱ	3.40.720.10, 1 hit
InterProⁱ	View protein in InterPro IPR017849 Alkaline_Pase-like_a/b/a IPR001952 Alkaline_phosphatase IPR018299 Alkaline_phosphatase_AS IPR017850 Alkaline_phosphatase_core_sf
PANTHERⁱ	PTHR11596 PTHR11596, 1 hit
Pfamⁱ	View protein in Pfam PF00245 Alk_phosphatase, 1 hit
PRINTSⁱ	PR00113 ALKPHPHTASE
SMARTⁱ	View protein in SMART SM00098 alkPPc, 1 hit
SUPFAMⁱ	SSF53649 SSF53649, 1 hit
PROSITEⁱ	View protein in PROSITE PS00123 ALKALINE_PHOSPHATASE, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PPB1_HUMAN
Accessionⁱ	P05187Primary (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:	November 7, 2018
	This is version 205 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

Keywords - Technical termⁱ

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

Documents

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

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UniProtKB - P05187 (PPB1_HUMAN)

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Alkaline phosphatase, placental type

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<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

Miscellaneous

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Enzyme and pathway databases

<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

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Keywords - Cellular componenti

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<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

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Keywords - PTMi

Proteomic databases

PTM databases

<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

Organism-specific databases

<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

Protein-protein interaction databases

Chemistry databases

<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

Secondary structure

3D structure databases

Miscellaneous databases

<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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<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

Experimental Info

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Genome annotation databases

Keywords - Coding sequence diversityi

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Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ