MPPE1

Functionⁱ

Metallophosphoesterase required for transport of GPI-anchor proteins from the endoplasmic reticulum to the Golgi. Acts in lipid remodeling steps of GPI-anchor maturation by mediating the removal of a side-chain ethanolamine-phosphate (EtNP) from the second Man (Man2) of the GPI intermediate, an essential step for efficient transport of GPI-anchor proteins.1 Publication

Cofactorⁱ

Mn²⁺1 PublicationNote: Binds 2 manganese ions per subunit.1 Publication

Sites

Feature key	Position(s)	Length	Description
Metal bindingⁱ	77 – 77	1	Divalent metal cation 2Curated
Metal bindingⁱ	119 – 119	1	Divalent metal cation 1Curated
Metal bindingⁱ	119 – 119	1	Divalent metal cation 2Curated
Metal bindingⁱ	157 – 157	1	Divalent metal cation 1Curated
Metal bindingⁱ	249 – 249	1	Divalent metal cation 1Curated
Metal bindingⁱ	303 – 303	1	Divalent metal cation 1Curated
Metal bindingⁱ	305 – 305	1	Divalent metal cation 2Curated

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Metallophosphoesterase 1 (EC:3.1.-.-) Alternative name(s): Post-GPI attachment to proteins factor 5
Gene namesⁱ	Name:MPPE1 Synonyms:PGAP5 ORF Names:PP579
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 18

Organism-specific databases

HGNCⁱ	HGNC:15988. MPPE1.

HGNCⁱ

HGNC:15988. MPPE1.

Subcellular locationⁱ

Endoplasmic reticulum-Golgi intermediate compartment membrane
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi."
  Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T.
  Cell 139:352-365(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, COFACTOR, DOMAIN DI-LYSINE MOTIF, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-77; HIS-79; ASP-119; ASN-157; HIS-158; HIS-249; HIS-303; HIS-305 AND 392-LYS--LYS-394, INTERACTION WITH GPI-ANCHOR PROTEINS AND TMED10.
; Multi-pass membrane protein
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi."
  Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T.
  Cell 139:352-365(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, COFACTOR, DOMAIN DI-LYSINE MOTIF, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-77; HIS-79; ASP-119; ASN-157; HIS-158; HIS-249; HIS-303; HIS-305 AND 392-LYS--LYS-394, INTERACTION WITH GPI-ANCHOR PROTEINS AND TMED10.
Golgi apparatus › cis-Golgi network membrane
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi."
  Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T.
  Cell 139:352-365(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, COFACTOR, DOMAIN DI-LYSINE MOTIF, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-77; HIS-79; ASP-119; ASN-157; HIS-158; HIS-249; HIS-303; HIS-305 AND 392-LYS--LYS-394, INTERACTION WITH GPI-ANCHOR PROTEINS AND TMED10.
; Multi-pass membrane protein
1 Publication
Manual assertion based on experiment inⁱ
- Ref.9
  "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi."
  Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T.
  Cell 139:352-365(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, COFACTOR, DOMAIN DI-LYSINE MOTIF, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-77; HIS-79; ASP-119; ASN-157; HIS-158; HIS-249; HIS-303; HIS-305 AND 392-LYS--LYS-394, INTERACTION WITH GPI-ANCHOR PROTEINS AND TMED10.

Note:

Also localizes to endoplasmic reticulum exit site.

Topology

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Transmembraneⁱ	27 – 47	21	HelicalSequence analysis			Add BLAST
Transmembraneⁱ	356 – 376	21	HelicalSequence analysis			Add BLAST

GO - Cellular componentⁱ

cis-Golgi network Source: UniProtKB
endoplasmic reticulum exit site Source: UniProtKB
endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
endoplasmic reticulum-Golgi intermediate compartment membrane Source: UniProtKB-SubCell
Golgi apparatus Source: HPA
integral component of membrane Source: UniProtKB-KW
nucleoplasm Source: HPA

Complete GO annotation...

Keywords - Cellular componentⁱ

Golgi apparatus, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	Length	Description
Mutagenesisⁱ	77 – 77	1	D → A: Affects transport of GPI-anchor proteins. 1 Publication Manual assertion based on experiment inⁱ Ref.9 "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi." Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T. Cell 139:352-365(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTOR, DOMAIN DI-LYSINE MOTIF, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-77; HIS-79; ASP-119; ASN-157; HIS-158; HIS-249; HIS-303; HIS-305 AND 392-LYS--LYS-394, INTERACTION WITH GPI-ANCHOR PROTEINS AND TMED10.
Mutagenesisⁱ	79 – 79	1	H → A: Affects transport of GPI-anchor proteins. 1 Publication Manual assertion based on experiment inⁱ Ref.9 "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi." Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T. Cell 139:352-365(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTOR, DOMAIN DI-LYSINE MOTIF, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-77; HIS-79; ASP-119; ASN-157; HIS-158; HIS-249; HIS-303; HIS-305 AND 392-LYS--LYS-394, INTERACTION WITH GPI-ANCHOR PROTEINS AND TMED10.
Mutagenesisⁱ	119 – 119	1	D → A or N: Affects transport of GPI-anchor proteins. 1 Publication Manual assertion based on experiment inⁱ Ref.9 "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi." Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T. Cell 139:352-365(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTOR, DOMAIN DI-LYSINE MOTIF, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-77; HIS-79; ASP-119; ASN-157; HIS-158; HIS-249; HIS-303; HIS-305 AND 392-LYS--LYS-394, INTERACTION WITH GPI-ANCHOR PROTEINS AND TMED10.
Mutagenesisⁱ	157 – 157	1	N → A: Affects transport of GPI-anchor proteins. 1 Publication Manual assertion based on experiment inⁱ Ref.9 "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi." Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T. Cell 139:352-365(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTOR, DOMAIN DI-LYSINE MOTIF, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-77; HIS-79; ASP-119; ASN-157; HIS-158; HIS-249; HIS-303; HIS-305 AND 392-LYS--LYS-394, INTERACTION WITH GPI-ANCHOR PROTEINS AND TMED10.
Mutagenesisⁱ	158 – 158	1	H → A: Affects transport of GPI-anchor proteins. 1 Publication Manual assertion based on experiment inⁱ Ref.9 "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi." Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T. Cell 139:352-365(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTOR, DOMAIN DI-LYSINE MOTIF, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-77; HIS-79; ASP-119; ASN-157; HIS-158; HIS-249; HIS-303; HIS-305 AND 392-LYS--LYS-394, INTERACTION WITH GPI-ANCHOR PROTEINS AND TMED10.
Mutagenesisⁱ	249 – 249	1	H → A: Affects transport of GPI-anchor proteins. 1 Publication Manual assertion based on experiment inⁱ Ref.9 "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi." Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T. Cell 139:352-365(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTOR, DOMAIN DI-LYSINE MOTIF, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-77; HIS-79; ASP-119; ASN-157; HIS-158; HIS-249; HIS-303; HIS-305 AND 392-LYS--LYS-394, INTERACTION WITH GPI-ANCHOR PROTEINS AND TMED10.
Mutagenesisⁱ	303 – 303	1	H → A: Affects transport of GPI-anchor proteins. 1 Publication Manual assertion based on experiment inⁱ Ref.9 "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi." Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T. Cell 139:352-365(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTOR, DOMAIN DI-LYSINE MOTIF, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-77; HIS-79; ASP-119; ASN-157; HIS-158; HIS-249; HIS-303; HIS-305 AND 392-LYS--LYS-394, INTERACTION WITH GPI-ANCHOR PROTEINS AND TMED10.
Mutagenesisⁱ	305 – 305	1	H → A: Affects transport of GPI-anchor proteins. 1 Publication Manual assertion based on experiment inⁱ Ref.9 "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi." Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T. Cell 139:352-365(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTOR, DOMAIN DI-LYSINE MOTIF, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-77; HIS-79; ASP-119; ASN-157; HIS-158; HIS-249; HIS-303; HIS-305 AND 392-LYS--LYS-394, INTERACTION WITH GPI-ANCHOR PROTEINS AND TMED10.
Mutagenesisⁱ	392 – 394	3	KRK → ARA: Affects subcellular localization. 1 Publication Manual assertion based on experiment inⁱ Ref.9 "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi." Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T. Cell 139:352-365(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTOR, DOMAIN DI-LYSINE MOTIF, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-77; HIS-79; ASP-119; ASN-157; HIS-158; HIS-249; HIS-303; HIS-305 AND 392-LYS--LYS-394, INTERACTION WITH GPI-ANCHOR PROTEINS AND TMED10.

Organism-specific databases

PharmGKBⁱ	PA134913534.

PharmGKBⁱ

PA134913534.

Polymorphism and mutation databases

BioMutaⁱ	MPPE1.
DMDMⁱ	215274110.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 396	396	Metallophosphoesterase 1		PRO_0000315727	Add BLAST

Proteomic databases

MaxQBⁱ	Q53F39.
PaxDbⁱ	Q53F39.
PeptideAtlasⁱ	Q53F39.
PRIDEⁱ	Q53F39.

PTM databases

iPTMnetⁱ	Q53F39.
PhosphoSiteⁱ	Q53F39.

Expressionⁱ

Tissue specificityⁱ

Expressed in brain.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000154889.
ExpressionAtlasⁱ	Q53F39. baseline and differential.
Genevisibleⁱ	Q53F39. HS.

Organism-specific databases

HPAⁱ	HPA012639.

Interactionⁱ

Subunit structureⁱ

Interacts with GPI-anchor proteins. Interacts with TMED10.1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
FLJ13057	Q53SE7	3	EBI-10242229,EBI-10172181
ZNF426	Q9BUY5	3	EBI-10242229,EBI-743265

With

Entry

#Exp.

IntAct

Notes

FLJ13057

Q53SE7

3

EBI-10242229,EBI-10172181

ZNF426

Q9BUY5

3

EBI-10242229,EBI-743265

Protein-protein interaction databases

BioGridⁱ	122415. 73 interactions.
IntActⁱ	Q53F39. 2 interactions.
STRINGⁱ	9606.ENSP00000465894.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q53F39.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Motif

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Motifⁱ	392 – 396	5	Di-lysine motif

Domainⁱ

The di-lysine motif (KxKxx) acts as an endoplasmic reticulum retrieval signal.1 Publication

Sequence similaritiesⁱ

Belongs to the metallophosphoesterase superfamily. MPPE1 family.Curated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG3662. Eukaryota. ENOG410ZM57. LUCA.
GeneTreeⁱ	ENSGT00390000013236.
HOVERGENⁱ	HBG101555.
InParanoidⁱ	Q53F39.
OMAⁱ	YCGAAGF.
OrthoDBⁱ	EOG091G0LJF.
PhylomeDBⁱ	Q53F39.

Family and domain databases

Gene3Dⁱ	3.60.21.10. 1 hit.
InterProⁱ	IPR004843. Calcineurin-like_PHP_apaH. IPR029052. Metallo-depent_PP-like. IPR033308. PGAP5/Cdc1/Ted1. [Graphical view]
PANTHERⁱ	PTHR13315. PTHR13315. 1 hit.
Pfamⁱ	PF00149. Metallophos. 1 hit. [Graphical view]
SUPFAMⁱ	SSF56300. SSF56300. 1 hit.

Sequences (5)ⁱ

Sequence statusⁱ: Complete.

This entry describes 5 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Isoform 1 (identifier: Q53F39-1) [UniParc]FASTA Add to basket

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.

« Hide

        10         20         30         40         50
MAMIELGFGR QNFHPLKRKS SLLLKLIAVV FAVLLFCEFL IYYLAIFQCN 
        60         70         80         90        100
WPEVKTTASD GEQTTREPVL KAMFLADTHL LGEFLGHWLD KLRREWQMER 
       110        120        130        140        150
AFQTALWLLQ PEVVFILGDI FDEGKWSTPE AWADDVERFQ KMFRHPSHVQ 
       160        170        180        190        200
LKVVAGNHDI GFHYEMNTYK VERFEKVFSS ERLFSWKGIN FVMVNSVALN 
       210        220        230        240        250
GDGCGICSET EAELIEVSHR LNCSREARGS SRCGPGPLLP TSAPVLLQHY 
       260        270        280        290        300
PLYRRSDANC SGEDAAPAEE RDIPFKENYD VLSREASQKL LWWLQPRLVL 
       310        320        330        340        350
SGHTHSACEV HHGGRVPELS VPSFSWRNRN NPSFIMGSIT PTDYTLSKCY 
       360        370        380        390 
LPREDVVLII YCGVVGFLVV LTLTHFGLLA SPFLSGLNLL GKRKTR

Length:396

Mass (Da):45,141

Last modified:November 25, 2008 - v2

Checksum:ⁱD117BCDB1630560A

GO

Isoform 2 (identifier: Q53F39-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
338-396: SITPTDYTLSKCYLPREDVVLIIYCGVVGFLVVLTLTHFGLLASPFLSGLNLLGKRKTR → TDA

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        10         20         30         40         50
MAMIELGFGR QNFHPLKRKS SLLLKLIAVV FAVLLFCEFL IYYLAIFQCN 
        60         70         80         90        100
WPEVKTTASD GEQTTREPVL KAMFLADTHL LGEFLGHWLD KLRREWQMER 
       110        120        130        140        150
AFQTALWLLQ PEVVFILGDI FDEGKWSTPE AWADDVERFQ KMFRHPSHVQ 
       160        170        180        190        200
LKVVAGNHDI GFHYEMNTYK VERFEKVFSS ERLFSWKGIN FVMVNSVALN 
       210        220        230        240        250
GDGCGICSET EAELIEVSHR LNCSREARGS SRCGPGPLLP TSAPVLLQHY 
       260        270        280        290        300
PLYRRSDANC SGEDAAPAEE RDIPFKENYD VLSREASQKL LWWLQPRLVL 
       310        320        330        340
SGHTHSACEV HHGGRVPELS VPSFSWRNRN NPSFIMGTDA

Show »

Length:340

Mass (Da):38,933

Checksum:ⁱ3F0B26CB0C48B354

GO

Isoform 3 (identifier: Q53F39-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
226-226: E → EQ
338-396: SITPTDYTLSKCYLPREDVVLIIYCGVVGFLVVLTLTHFGLLASPFLSGLNLLGKRKTR → TDA

« Hide

        10         20         30         40         50
MAMIELGFGR QNFHPLKRKS SLLLKLIAVV FAVLLFCEFL IYYLAIFQCN 
        60         70         80         90        100
WPEVKTTASD GEQTTREPVL KAMFLADTHL LGEFLGHWLD KLRREWQMER 
       110        120        130        140        150
AFQTALWLLQ PEVVFILGDI FDEGKWSTPE AWADDVERFQ KMFRHPSHVQ 
       160        170        180        190        200
LKVVAGNHDI GFHYEMNTYK VERFEKVFSS ERLFSWKGIN FVMVNSVALN 
       210        220        230        240        250
GDGCGICSET EAELIEVSHR LNCSREQARG SSRCGPGPLL PTSAPVLLQH 
       260        270        280        290        300
YPLYRRSDAN CSGEDAAPAE ERDIPFKENY DVLSREASQK LLWWLQPRLV 
       310        320        330        340 
LSGHTHSACE VHHGGRVPEL SVPSFSWRNR NNPSFIMGTD A

Show »

Length:341

Mass (Da):39,061

Checksum:ⁱ39DED2417CD4BBD4

GO

Isoform 4 (identifier: Q53F39-4) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
227-289: Missing.

« Hide

        10         20         30         40         50
MAMIELGFGR QNFHPLKRKS SLLLKLIAVV FAVLLFCEFL IYYLAIFQCN 
        60         70         80         90        100
WPEVKTTASD GEQTTREPVL KAMFLADTHL LGEFLGHWLD KLRREWQMER 
       110        120        130        140        150
AFQTALWLLQ PEVVFILGDI FDEGKWSTPE AWADDVERFQ KMFRHPSHVQ 
       160        170        180        190        200
LKVVAGNHDI GFHYEMNTYK VERFEKVFSS ERLFSWKGIN FVMVNSVALN 
       210        220        230        240        250
GDGCGICSET EAELIEVSHR LNCSRELLWW LQPRLVLSGH THSACEVHHG 
       260        270        280        290        300
GRVPELSVPS FSWRNRNNPS FIMGSITPTD YTLSKCYLPR EDVVLIIYCG 
       310        320        330 
VVGFLVVLTL THFGLLASPF LSGLNLLGKR KTR

Note: No experimental confirmation available.

Show »

Length:333

Mass (Da):38,270

Checksum:ⁱ6691B3999DC34E9E

GO

Isoform 5 (identifier: Q53F39-5) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
227-256: ARGSSRCGPGPLLPTSAPVLLQHYPLYRRS → VGEHLNATGAFCPVLLRFGCSLSPLALLAL
257-396: Missing.

« Hide

        10         20         30         40         50
MAMIELGFGR QNFHPLKRKS SLLLKLIAVV FAVLLFCEFL IYYLAIFQCN 
        60         70         80         90        100
WPEVKTTASD GEQTTREPVL KAMFLADTHL LGEFLGHWLD KLRREWQMER 
       110        120        130        140        150
AFQTALWLLQ PEVVFILGDI FDEGKWSTPE AWADDVERFQ KMFRHPSHVQ 
       160        170        180        190        200
LKVVAGNHDI GFHYEMNTYK VERFEKVFSS ERLFSWKGIN FVMVNSVALN 
       210        220        230        240        250
GDGCGICSET EAELIEVSHR LNCSREVGEH LNATGAFCPV LLRFGCSLSP 

LALLAL

Note: No experimental confirmation available.

Show »

Length:256

Mass (Da):29,351

Checksum:ⁱ4BBDA145C3984B9D

GO

Sequence cautionⁱ

The sequence BAB13863 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

The sequence BAB14378 differs from that shown. Reason: Frameshift at position 201. Curated

Experimental Info

Feature key	Position(s)	Length	Description
Sequence conflictⁱ	22 – 22	1	L → S in BAB14378 (PubMed:14702039).Curated
Sequence conflictⁱ	32 – 32	1	A → T in BAB14378 (PubMed:14702039).Curated
Sequence conflictⁱ	97 – 97	1	Q → R in AAL55744 (PubMed:15498874).Curated
Sequence conflictⁱ	301 – 301	1	S → I in AAH73994 (PubMed:15489334).Curated
Sequence conflictⁱ	364 – 364	1	V → E in AAM00279 (PubMed:11978971).Curated
Sequence conflictⁱ	364 – 364	1	V → E in AAM00277 (PubMed:11978971).Curated

Natural variant

Feature key	Position(s)	Length	Description	Feature identifier
Natural variantⁱ	138 – 138	1	R → Q. Corresponds to variant rs11872520 [ dbSNP \| Ensembl ].	VAR_038294
Natural variantⁱ	197 – 197	1	V → M. Corresponds to variant rs35611363 [ dbSNP \| Ensembl ].	VAR_038295
Natural variantⁱ	268 – 268	1	A → P.4 Publications Manual assertion based on experiment inⁱ Ref.2 "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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 185-340 (ISOFORM 2), VARIANT PRO-268. Ref.3 Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PRO-268. Ref.4 "Large-scale cDNA transfection screening for genes related to cancer development and progression." Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. Gu J. Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT PRO-268. Ref.7 Mural R.J., Istrail S., Sutton G.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. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-268. Corresponds to variant rs662515 [ dbSNP \| Ensembl ].	VAR_038296
Natural variantⁱ	336 – 336	1	M → L. Corresponds to variant rs16976814 [ dbSNP \| Ensembl ].	VAR_038297

Alternative sequence

Feature key	Position(s)	Length	Description	Feature identifier	Actions
Alternative sequenceⁱ	226 – 226	1	E → EQ in isoform 3. 1 Publication Manual assertion based on opinion inⁱ Ref.8 "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] (ISOFORMS 3 AND 4).	VSP_030679
Alternative sequenceⁱ	227 – 289	63	Missing in isoform 4. 1 Publication Manual assertion based on opinion inⁱ Ref.8 "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] (ISOFORMS 3 AND 4).	VSP_030680	Add BLAST
Alternative sequenceⁱ	227 – 256	30	ARGSS…LYRRS → VGEHLNATGAFCPVLLRFGC SLSPLALLAL in isoform 5. 1 Publication Manual assertion based on opinion inⁱ Ref.2 "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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 185-340 (ISOFORM 2), VARIANT PRO-268.	VSP_030681	Add BLAST
Alternative sequenceⁱ	257 – 396	140	Missing in isoform 5. 1 Publication Manual assertion based on opinion inⁱ Ref.2 "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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 185-340 (ISOFORM 2), VARIANT PRO-268.	VSP_030682	Add BLAST
Alternative sequenceⁱ	338 – 396	59	SITPT…KRKTR → TDA in isoform 2 and isoform 3. 4 Publications Manual assertion based on opinion inⁱ Ref.1 "cDNA cloning, genomic organization and expression of the novel human metallophosphoesterase gene MPPE1 on chromosome 18p11.2." Vuoristo J.T., Ala-Kokko L. Cytogenet. Cell Genet. 95:60-63(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY. Ref.2 "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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 185-340 (ISOFORM 2), VARIANT PRO-268. Ref.4 "Large-scale cDNA transfection screening for genes related to cancer development and progression." Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. Gu J. Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT PRO-268. Ref.8 "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] (ISOFORMS 3 AND 4).	VSP_030683	Add BLAST

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF363483, AF363482 Genomic DNA. Translation: AAM00277.1. AF363483, AF363482 Genomic DNA. Translation: AAM00278.1. AF363484 mRNA. Translation: AAM00279.1. AK021647 mRNA. Translation: BAB13863.1. Different initiation. AK023052 mRNA. Translation: BAB14378.1. Frameshift. AK223450 mRNA. Translation: BAD97170.1. AF289560 mRNA. Translation: AAL55744.1. EF444996 Genomic DNA. Translation: ACA06017.1. EF444996 Genomic DNA. Translation: ACA06018.1. EF444996 Genomic DNA. Translation: ACA06019.1. AP001269 Genomic DNA. No translation available. CH471113 Genomic DNA. Translation: EAX01562.1. CH471113 Genomic DNA. Translation: EAX01565.1. CH471113 Genomic DNA. Translation: EAX01564.1. CH471113 Genomic DNA. Translation: EAX01569.1. CH471113 Genomic DNA. Translation: EAX01571.1. CH471113 Genomic DNA. Translation: EAX01567.1. CH471113 Genomic DNA. Translation: EAX01568.1. BC002877 mRNA. Translation: AAH02877.1. BC073994 mRNA. Translation: AAH73994.1.
CCDSⁱ	CCDS11853.1. [Q53F39-1] CCDS56054.1. [Q53F39-4]
RefSeqⁱ	NP_001229833.1. NM_001242904.1. [Q53F39-4] NP_001306083.1. NM_001319154.1. [Q53F39-4] NP_075563.3. NM_023075.5. [Q53F39-1] XP_006722409.1. XM_006722346.2. [Q53F39-1] XP_011524034.1. XM_011525732.1. [Q53F39-3]
UniGeneⁱ	Hs.712666. Hs.734268.

Genome annotation databases

Ensemblⁱ	ENST00000309976; ENSP00000311200; ENSG00000154889. [Q53F39-4] ENST00000317235; ENSP00000327257; ENSG00000154889. [Q53F39-4] ENST00000496196; ENSP00000433950; ENSG00000154889. [Q53F39-2] ENST00000588072; ENSP00000465894; ENSG00000154889. [Q53F39-1]
GeneIDⁱ	65258.
KEGGⁱ	hsa:65258.
UCSCⁱ	uc002kqf.5. human. [Q53F39-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF363483, AF363482 Genomic DNA. Translation: AAM00277.1. AF363483, AF363482 Genomic DNA. Translation: AAM00278.1. AF363484 mRNA. Translation: AAM00279.1. AK021647 mRNA. Translation: BAB13863.1. Different initiation. AK023052 mRNA. Translation: BAB14378.1. Frameshift. AK223450 mRNA. Translation: BAD97170.1. AF289560 mRNA. Translation: AAL55744.1. EF444996 Genomic DNA. Translation: ACA06017.1. EF444996 Genomic DNA. Translation: ACA06018.1. EF444996 Genomic DNA. Translation: ACA06019.1. AP001269 Genomic DNA. No translation available. CH471113 Genomic DNA. Translation: EAX01562.1. CH471113 Genomic DNA. Translation: EAX01565.1. CH471113 Genomic DNA. Translation: EAX01564.1. CH471113 Genomic DNA. Translation: EAX01569.1. CH471113 Genomic DNA. Translation: EAX01571.1. CH471113 Genomic DNA. Translation: EAX01567.1. CH471113 Genomic DNA. Translation: EAX01568.1. BC002877 mRNA. Translation: AAH02877.1. BC073994 mRNA. Translation: AAH73994.1.
CCDSⁱ	CCDS11853.1. [Q53F39-1] CCDS56054.1. [Q53F39-4]
RefSeqⁱ	NP_001229833.1. NM_001242904.1. [Q53F39-4] NP_001306083.1. NM_001319154.1. [Q53F39-4] NP_075563.3. NM_023075.5. [Q53F39-1] XP_006722409.1. XM_006722346.2. [Q53F39-1] XP_011524034.1. XM_011525732.1. [Q53F39-3]
UniGeneⁱ	Hs.712666. Hs.734268.

3D structure databases

ProteinModelPortalⁱ	Q53F39.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	122415. 73 interactions.
IntActⁱ	Q53F39. 2 interactions.
STRINGⁱ	9606.ENSP00000465894.

PTM databases

iPTMnetⁱ	Q53F39.
PhosphoSiteⁱ	Q53F39.

Polymorphism and mutation databases

BioMutaⁱ	MPPE1.
DMDMⁱ	215274110.

Proteomic databases

MaxQBⁱ	Q53F39.
PaxDbⁱ	Q53F39.
PeptideAtlasⁱ	Q53F39.
PRIDEⁱ	Q53F39.

Protocols and materials databases

DNASUⁱ	65258.
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000309976; ENSP00000311200; ENSG00000154889. [Q53F39-4] ENST00000317235; ENSP00000327257; ENSG00000154889. [Q53F39-4] ENST00000496196; ENSP00000433950; ENSG00000154889. [Q53F39-2] ENST00000588072; ENSP00000465894; ENSG00000154889. [Q53F39-1]
GeneIDⁱ	65258.
KEGGⁱ	hsa:65258.
UCSCⁱ	uc002kqf.5. human. [Q53F39-1]

Organism-specific databases

CTDⁱ	65258.
GeneCardsⁱ	MPPE1.
H-InvDB	HIX0014342.
HGNCⁱ	HGNC:15988. MPPE1.
HPAⁱ	HPA012639.
MIMⁱ	611900. gene.
neXtProtⁱ	NX_Q53F39.
PharmGKBⁱ	PA134913534.
GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3662. Eukaryota. ENOG410ZM57. LUCA.
GeneTreeⁱ	ENSGT00390000013236.
HOVERGENⁱ	HBG101555.
InParanoidⁱ	Q53F39.
OMAⁱ	YCGAAGF.
OrthoDBⁱ	EOG091G0LJF.
PhylomeDBⁱ	Q53F39.

Miscellaneous databases

ChiTaRSⁱ	MPPE1. human.
GenomeRNAiⁱ	65258.
PROⁱ	Q53F39.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000154889.
ExpressionAtlasⁱ	Q53F39. baseline and differential.
Genevisibleⁱ	Q53F39. HS.

Family and domain databases

Gene3Dⁱ	3.60.21.10. 1 hit.
InterProⁱ	IPR004843. Calcineurin-like_PHP_apaH. IPR029052. Metallo-depent_PP-like. IPR033308. PGAP5/Cdc1/Ted1. [Graphical view]
PANTHERⁱ	PTHR13315. PTHR13315. 1 hit.
Pfamⁱ	PF00149. Metallophos. 1 hit. [Graphical view]
SUPFAMⁱ	SSF56300. SSF56300. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

MPPE1_HUMAN

Accessionⁱ

Primary (citable) accession number: Q53F39
Secondary accession number(s): B0YJ39

Q9HAI4

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 25, 2008
Last modified:	September 7, 2016
This is version 95 of the entry and version 2 of the sequence. [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

Complete proteome, Reference proteome

Documents

Human chromosome 18
Human chromosome 18: 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
SIMILARITY comments
Index of protein domains and families

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q53F39 (MPPE1_HUMAN)

UniProt

Q53F39 - MPPE1_HUMAN

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Metallophosphoesterase 1

Select a section on the left to see content.

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>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><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Provides information on the disease(s) and phenotype(s) associated with a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Polymorphism and mutation databases

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (5)i

<p>Reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.</p><p><a href='../manual/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

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

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequences (5)ⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ