Q53F39 (MPPE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Metallophosphoesterase 1
EC=3.1.-.-

Alternative name(s):
Post-GPI attachment to proteins factor 5

Gene names

Name:	MPPE1
Synonyms:	PGAP5
ORF Names:	PP579

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.9
Cofactor	Binds 2 manganese ions per subunit Probable. Ref.9
Subunit structure	Interacts with GPI-anchor proteins. Interacts with TMED10. Ref.9
Subcellular location	Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Golgi apparatus › cis-Golgi network membrane; Multi-pass membrane protein. Note: Also localizes to endoplasmic reticulum exit site. Ref.9
Tissue specificity	Expressed in brain. Ref.1
Domain	The di-lysine motif (KxKxx) acts as an endoplasmic reticulum retrieval signal. Ref.9
Sequence similarities	Belongs to the metallophosphoesterase superfamily. MPPE1 family.
Sequence caution	The sequence BAB13863.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB14378.1 differs from that shown. Reason: Frameshift at position 201.

Ontologies

Keywords
Biological process	ER-Golgi transport GPI-anchor biosynthesis Transport
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	Manganese Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER to Golgi vesicle-mediated transport Inferred from sequence or structural similarity. Source: UniProtKB GPI anchor biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell cis-Golgi network Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum exit site Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum-Golgi intermediate compartment Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum-Golgi intermediate compartment membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral component of membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	GPI anchor binding Inferred from sequence or structural similarity. Source: UniProtKB manganese ion binding Inferred from sequence or structural similarity. Source: UniProtKB phosphoric diester hydrolase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q53F39-1)

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.

Isoform 2 (identifier: Q53F39-2)

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

Isoform 3 (identifier: Q53F39-3)

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

Isoform 4 (identifier: Q53F39-4)

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

Note: No experimental confirmation available.

Isoform 5 (identifier: Q53F39-5)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 396	396	Metallophosphoesterase 1		PRO_0000315727
Regions
	Transmembrane	27 – 47	21	Helical; Potential
	Transmembrane	356 – 376	21	Helical; Potential
	Motif	392 – 396	5	Di-lysine motif
Sites
	Metal binding	77	1	Divalent metal cation 2 Probable
	Metal binding	119	1	Divalent metal cation 1 Probable
	Metal binding	119	1	Divalent metal cation 2 Probable
	Metal binding	157	1	Divalent metal cation 1 Probable
	Metal binding	249	1	Divalent metal cation 1 Probable
	Metal binding	303	1	Divalent metal cation 1 Probable
	Metal binding	305	1	Divalent metal cation 2 Probable
Natural variations
	Alternative sequence	226	1	E → EQ in isoform 3.		VSP_030679
	Alternative sequence	227 – 289	63	Missing in isoform 4.		VSP_030680
	Alternative sequence	227 – 256	30	ARGSS…LYRRS → VGEHLNATGAFCPVLLRFGC SLSPLALLAL in isoform 5.		VSP_030681
	Alternative sequence	257 – 396	140	Missing in isoform 5.		VSP_030682
	Alternative sequence	338 – 396	59	SITPT…KRKTR → TDA in isoform 2 and isoform 3.		VSP_030683
	Natural variant	138	1	R → Q. Corresponds to variant rs11872520 [ dbSNP | Ensembl ].		VAR_038294
	Natural variant	197	1	V → M. Corresponds to variant rs35611363 [ dbSNP | Ensembl ].		VAR_038295
	Natural variant	268	1	A → P. Ref.2 Ref.3 Ref.4 Ref.7 Corresponds to variant rs662515 [ dbSNP | Ensembl ].		VAR_038296
	Natural variant	336	1	M → L. Corresponds to variant rs16976814 [ dbSNP | Ensembl ].		VAR_038297
Experimental info
	Mutagenesis	77	1	D → A: Affects transport of GPI-anchor proteins. Ref.9
	Mutagenesis	79	1	H → A: Affects transport of GPI-anchor proteins. Ref.9
	Mutagenesis	119	1	D → A or N: Affects transport of GPI-anchor proteins. Ref.9
	Mutagenesis	157	1	N → A: Affects transport of GPI-anchor proteins. Ref.9
	Mutagenesis	158	1	H → A: Affects transport of GPI-anchor proteins. Ref.9
	Mutagenesis	249	1	H → A: Affects transport of GPI-anchor proteins. Ref.9
	Mutagenesis	303	1	H → A: Affects transport of GPI-anchor proteins. Ref.9
	Mutagenesis	305	1	H → A: Affects transport of GPI-anchor proteins. Ref.9
	Mutagenesis	392 – 394	3	KRK → ARA: Affects subcellular localization. Ref.9
	Sequence conflict	22	1	L → S in BAB14378. Ref.2
	Sequence conflict	32	1	A → T in BAB14378. Ref.2
	Sequence conflict	97	1	Q → R in AAL55744. Ref.4
	Sequence conflict	301	1	S → I in AAH73994. Ref.8
	Sequence conflict	364	1	V → E in AAM00279. Ref.1
	Sequence conflict	364	1	V → E in AAM00277. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: D117BCDB1630560A	FASTA	396	45,141
	10 20 30 40 50 60 MAMIELGFGR QNFHPLKRKS SLLLKLIAVV FAVLLFCEFL IYYLAIFQCN WPEVKTTASD 70 80 90 100 110 120 GEQTTREPVL KAMFLADTHL LGEFLGHWLD KLRREWQMER AFQTALWLLQ PEVVFILGDI 130 140 150 160 170 180 FDEGKWSTPE AWADDVERFQ KMFRHPSHVQ LKVVAGNHDI GFHYEMNTYK VERFEKVFSS 190 200 210 220 230 240 ERLFSWKGIN FVMVNSVALN GDGCGICSET EAELIEVSHR LNCSREARGS SRCGPGPLLP 250 260 270 280 290 300 TSAPVLLQHY PLYRRSDANC SGEDAAPAEE RDIPFKENYD VLSREASQKL LWWLQPRLVL 310 320 330 340 350 360 SGHTHSACEV HHGGRVPELS VPSFSWRNRN NPSFIMGSIT PTDYTLSKCY LPREDVVLII 370 380 390 YCGVVGFLVV LTLTHFGLLA SPFLSGLNLL GKRKTR
	Isoform 2 [UniParc]. Checksum: 3F0B26CB0C48B354	FASTA	340	38,933
	10 20 30 40 50 60 MAMIELGFGR QNFHPLKRKS SLLLKLIAVV FAVLLFCEFL IYYLAIFQCN WPEVKTTASD 70 80 90 100 110 120 GEQTTREPVL KAMFLADTHL LGEFLGHWLD KLRREWQMER AFQTALWLLQ PEVVFILGDI 130 140 150 160 170 180 FDEGKWSTPE AWADDVERFQ KMFRHPSHVQ LKVVAGNHDI GFHYEMNTYK VERFEKVFSS 190 200 210 220 230 240 ERLFSWKGIN FVMVNSVALN GDGCGICSET EAELIEVSHR LNCSREARGS SRCGPGPLLP 250 260 270 280 290 300 TSAPVLLQHY PLYRRSDANC SGEDAAPAEE RDIPFKENYD VLSREASQKL LWWLQPRLVL 310 320 330 340 SGHTHSACEV HHGGRVPELS VPSFSWRNRN NPSFIMGTDA
	Isoform 3 [UniParc]. Checksum: 39DED2417CD4BBD4	FASTA	341	39,061
	10 20 30 40 50 60 MAMIELGFGR QNFHPLKRKS SLLLKLIAVV FAVLLFCEFL IYYLAIFQCN WPEVKTTASD 70 80 90 100 110 120 GEQTTREPVL KAMFLADTHL LGEFLGHWLD KLRREWQMER AFQTALWLLQ PEVVFILGDI 130 140 150 160 170 180 FDEGKWSTPE AWADDVERFQ KMFRHPSHVQ LKVVAGNHDI GFHYEMNTYK VERFEKVFSS 190 200 210 220 230 240 ERLFSWKGIN FVMVNSVALN GDGCGICSET EAELIEVSHR LNCSREQARG SSRCGPGPLL 250 260 270 280 290 300 PTSAPVLLQH YPLYRRSDAN CSGEDAAPAE ERDIPFKENY DVLSREASQK LLWWLQPRLV 310 320 330 340 LSGHTHSACE VHHGGRVPEL SVPSFSWRNR NNPSFIMGTD A
	Isoform 4 [UniParc]. Checksum: 6691B3999DC34E9E	FASTA	333	38,270
	10 20 30 40 50 60 MAMIELGFGR QNFHPLKRKS SLLLKLIAVV FAVLLFCEFL IYYLAIFQCN WPEVKTTASD 70 80 90 100 110 120 GEQTTREPVL KAMFLADTHL LGEFLGHWLD KLRREWQMER AFQTALWLLQ PEVVFILGDI 130 140 150 160 170 180 FDEGKWSTPE AWADDVERFQ KMFRHPSHVQ LKVVAGNHDI GFHYEMNTYK VERFEKVFSS 190 200 210 220 230 240 ERLFSWKGIN FVMVNSVALN GDGCGICSET EAELIEVSHR LNCSRELLWW LQPRLVLSGH 250 260 270 280 290 300 THSACEVHHG GRVPELSVPS FSWRNRNNPS FIMGSITPTD YTLSKCYLPR EDVVLIIYCG 310 320 330 VVGFLVVLTL THFGLLASPF LSGLNLLGKR KTR
	Isoform 5 [UniParc]. Checksum: 4BBDA145C3984B9D	FASTA	256	29,351
	10 20 30 40 50 60 MAMIELGFGR QNFHPLKRKS SLLLKLIAVV FAVLLFCEFL IYYLAIFQCN WPEVKTTASD 70 80 90 100 110 120 GEQTTREPVL KAMFLADTHL LGEFLGHWLD KLRREWQMER AFQTALWLLQ PEVVFILGDI 130 140 150 160 170 180 FDEGKWSTPE AWADDVERFQ KMFRHPSHVQ LKVVAGNHDI GFHYEMNTYK VERFEKVFSS 190 200 210 220 230 240 ERLFSWKGIN FVMVNSVALN GDGCGICSET EAELIEVSHR LNCSREVGEH LNATGAFCPV 250 LLRFGCSLSP LALLAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
[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. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., 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. Tissue: Embryo and Teratocarcinoma.
[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. Tissue: Dermoid cancer.
[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. , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., 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.
[5]	NHLBI resequencing and genotyping service (RS&G) Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"DNA sequence and analysis of human chromosome 18." Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S. Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-268.
[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). Tissue: Lung and PNS.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
RefSeq	NP_001229833.1. NM_001242904.1. NP_075563.3. NM_023075.5.
UniGene	Hs.712666. Hs.734268.
3D structure databases
ProteinModelPortal	Q53F39.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	122415. 1 interaction.
PTM databases
PhosphoSite	Q53F39.
Polymorphism databases
DMDM	215274110.
Proteomic databases
PaxDb	Q53F39.
PRIDE	Q53F39.
Protocols and materials databases
DNASU	65258.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000309976; ENSP00000311200; ENSG00000154889. ENST00000317235; ENSP00000327257; ENSG00000154889. ENST00000399978; ENSP00000382860; ENSG00000154889. ENST00000496196; ENSP00000433950; ENSG00000154889. ENST00000588072; ENSP00000465894; ENSG00000154889.
GeneID	65258.
KEGG	hsa:65258.
UCSC	uc002kqf.3. human.
Organism-specific databases
CTD	65258.
GeneCards	GC18M012841.
H-InvDB	HIX0014342.
HGNC	HGNC:15988. MPPE1.
HPA	HPA012639.
MIM	611900. gene.
neXtProt	NX_Q53F39.
PharmGKB	PA134913534.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG246417.
HOVERGEN	HBG101555.
OMA	HSACEVH.
OrthoDB	EOG722J8P.
PhylomeDB	Q53F39.
Gene expression databases
ArrayExpress	Q53F39.
Bgee	Q53F39.
Genevestigator	Q53F39.
Family and domain databases
InterPro	IPR024654. Calcineurin-like_PEstase_dom. [Graphical view]
Pfam	PF12850. Metallophos_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MPPE1. human.
GenomeRNAi	65258.
NextBio	67378.
PRO	Q53F39.
SOURCE	Search...

Entry information

Entry name

MPPE1_HUMAN

Accession

Primary (citable) accession number: Q53F39
Secondary accession number(s): B0YJ39 , B0YJ40, B0YJ41, B5ME53, B7WNJ3, D3DUI5, D3DUI7, Q6GMP1, Q8TAD6, Q8TE26, Q8WZ32, Q9BU58, Q9H958, Q9HAI4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 25, 2008
Last modified:	February 19, 2014
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

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.