Reviewed, UniProtKB/Swiss-Prot Q9H2U2 (IPYR2_HUMAN)

Names and origin

Protein names

Recommended name:
    Inorganic pyrophosphatase 2, mitochondrial
      Short name=PPase 2
    EC=3.6.1.1
Alternative name(s):
    Pyrophosphatase SID6-306

Gene names

Name:	PPA2
ORF Names:	HSPC124

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	334 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Diphosphate + H2O = 2 phosphate.
Cofactor	Magnesium By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion Potential.
Tissue specificity	Detected in brain, gastric carcinoma, lung, ovary, skeletal muscle, umbilical cord blood and a cell line derived from kidney proximal tubule epithelium. Ref.8
Sequence similarities	Belongs to the PPase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	phosphate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	inorganic diphosphatase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9H2U2-1)

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: Q9H2U2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     74-74: E → EDTEAQGIFIDLSKIW

Isoform 3 (identifier: Q9H2U2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     148-176: Missing.

Isoform 4 (identifier: Q9H2U2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     53-53: K → N
     54-219: Missing.

Note: No experimental confirmation available.

Isoform 5 (identifier: Q9H2U2-5)

The sequence of this isoform differs from the canonical sequence as follows:
     53-334: KNVTGHYISP...EEQVWHFLGK → RPSAVAARSR...PAHTPAFLEA

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 32	32	Mitochondrion Ref.7
	Chain	33 – 334	302	Inorganic pyrophosphatase 2, mitochondrial		PRO_0000025411
Sites
	Metal binding	164	1	Magnesium 1 By similarity
	Metal binding	169	1	Magnesium 1 By similarity
	Metal binding	169	1	Magnesium 2 By similarity
	Metal binding	201	1	Magnesium 1 By similarity
Amino acid modifications
	Modified residue	53	1	N6-acetyllysine Ref.11
	Modified residue	216	1	N6-acetyllysine Ref.11
	Modified residue	261	1	N6-acetyllysine Ref.11
	Modified residue	276	1	N6-acetyllysine Ref.11
	Modified residue	317	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	53 – 334	282	KNVTG…HFLGK → RPSAVAARSRPPYFPRERAP SHENCQRGGGGSRPQSGEQR RRAAGWGVDSALCPASRPPR GVGRVQAATPRRPAAISRPG RRSRFTQLSEEGKAEPAHTP AFLEA in isoform 5.		VSP_011648
	Alternative sequence	53	1	K → N in isoform 4.		VSP_011649
	Alternative sequence	54 – 219	166	Missing in isoform 4.		VSP_011650
	Alternative sequence	74	1	E → EDTEAQGIFIDLSKIW in isoform 2.		VSP_011651
	Alternative sequence	148 – 176	29	Missing in isoform 3.		VSP_011652
	Natural variant	282	1	K → N: dbSNP rs13787. Ref.3 Ref.5 Ref.6		VAR_019723
Experimental info
	Sequence conflict	11	1	G → V in BAA84701. Ref.1
	Sequence conflict	11	1	G → V in AAG36781. Ref.2
	Sequence conflict	75 – 79	5	ENGIP → DTEAQGIFIDLSKIWKMAFL Ref.6
	Sequence conflict	103	1	N → K Ref.6
	Sequence conflict	241	1	Y → C Ref.6
	Sequence conflict	288	1	I → T Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: F8C85F64CDA447F1	FASTA	334	37,920
	10 20 30 40 50 60 MSALLRLLRT GAPAAACLRL GTSAGTGSRR AMALYHTEER GQPCSQNYRL FFKNVTGHYI 70 80 90 100 110 120 SPFHDIPLKV NSKEENGIPM KKARNDEYEN LFNMIVEIPR WTNAKMEIAT KEPMNPIKQY 130 140 150 160 170 180 VKDGKLRYVA NIFPYKGYIW NYGTLPQTWE DPHEKDKSTN CFGDNDPIDV CEIGSKILSC 190 200 210 220 230 240 GEVIHVKILG ILALIDEGET DWKLIAINAN DPEASKFHDI DDVKKFKPGY LEATLNWFRL 250 260 270 280 290 300 YKVPDGKPEN QFAFNGEFKN KAFALEVIKS THQCWKALLM KKCNGGAINC TNVQISDSPF 310 320 330 RCTQEEARSL VESVSSSPNK ESNEEEQVWH FLGK
	Isoform 2. Checksum: 44938DDEB36C8789	FASTA	349	39,638
	10 20 30 40 50 60 MSALLRLLRT GAPAAACLRL GTSAGTGSRR AMALYHTEER GQPCSQNYRL FFKNVTGHYI 70 80 90 100 110 120 SPFHDIPLKV NSKEDTEAQG IFIDLSKIWE NGIPMKKARN DEYENLFNMI VEIPRWTNAK 130 140 150 160 170 180 MEIATKEPMN PIKQYVKDGK LRYVANIFPY KGYIWNYGTL PQTWEDPHEK DKSTNCFGDN 190 200 210 220 230 240 DPIDVCEIGS KILSCGEVIH VKILGILALI DEGETDWKLI AINANDPEAS KFHDIDDVKK 250 260 270 280 290 300 FKPGYLEATL NWFRLYKVPD GKPENQFAFN GEFKNKAFAL EVIKSTHQCW KALLMKKCNG 310 320 330 340 GAINCTNVQI SDSPFRCTQE EARSLVESVS SSPNKESNEE EQVWHFLGK
	Isoform 3. Checksum: ACC551F07BE228AE	FASTA	305	34,658
	10 20 30 40 50 60 MSALLRLLRT GAPAAACLRL GTSAGTGSRR AMALYHTEER GQPCSQNYRL FFKNVTGHYI 70 80 90 100 110 120 SPFHDIPLKV NSKEENGIPM KKARNDEYEN LFNMIVEIPR WTNAKMEIAT KEPMNPIKQY 130 140 150 160 170 180 VKDGKLRYVA NIFPYKGYIW NYGTLPQILS CGEVIHVKIL GILALIDEGE TDWKLIAINA 190 200 210 220 230 240 NDPEASKFHD IDDVKKFKPG YLEATLNWFR LYKVPDGKPE NQFAFNGEFK NKAFALEVIK 250 260 270 280 290 300 STHQCWKALL MKKCNGGAIN CTNVQISDSP FRCTQEEARS LVESVSSSPN KESNEEEQVW HFLGK
	Isoform 4. Checksum: 9CADD542FA7E7569	FASTA	168	18,916
	10 20 30 40 50 60 MSALLRLLRT GAPAAACLRL GTSAGTGSRR AMALYHTEER GQPCSQNYRL FFNIDDVKKF 70 80 90 100 110 120 KPGYLEATLN WFRLYKVPDG KPENQFAFNG EFKNKAFALE VIKSTHQCWK ALLMKKCNGG 130 140 150 160 AINCTNVQIS DSPFRCTQEE ARSLVESVSS SPNKESNEEE QVWHFLGK
	Isoform 5. Checksum: 01E850636E6D3F33	FASTA	157	16,961
	10 20 30 40 50 60 MSALLRLLRT GAPAAACLRL GTSAGTGSRR AMALYHTEER GQPCSQNYRL FFRPSAVAAR 70 80 90 100 110 120 SRPPYFPRER APSHENCQRG GGGSRPQSGE QRRRAAGWGV DSALCPASRP PRGVGRVQAA 130 140 150 TPRRPAAISR PGRRSRFTQL SEEGKAEPAH TPAFLEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Putative inorganic pyrophosphatase." Saito T., Hattori A., Miyajima N. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Brain.
[2]	"Cloning of the mitochondrial inorganic pyrophosphatase 2 cDNA." Kanni L., Johansson M., Karlsson A. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), VARIANT ASN-282. Tissue: Gastric carcinoma.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5). Tissue: Lung, Ovary and Skeletal muscle.
[5]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-334 (ISOFORM 2), VARIANT ASN-282. Tissue: Umbilical cord blood.
[6]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-334 (ISOFORM 1), VARIANT ASN-282. Tissue: Brain.
[7]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 33-40. Tissue: Platelet.
[8]	"Hypothetical proteins with putative enzyme activity in human amnion, lymphocyte, bronchial epithelial and kidney cell lines, AND MASS SPECTROMETRY." Afjehi-Sadat L., Krapfenbauer K., Slavc I., Fountoulakis M., Lubec G. Biochim. Biophys. Acta 1700:65-74(2004) [PubMed: 15210126] [Abstract] Cited for: MASS SPECTROMETRY, TISSUE SPECIFICITY.
[9]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53; LYS-216; LYS-261 AND LYS-276, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB026722 mRNA. Translation: BAA84701.1. Different initiation. AF217187 mRNA. Translation: AAG36781.1. AK000466 mRNA. Translation: BAA91184.1. Different initiation. AK297096 mRNA. Translation: BAG59609.1. BC012903 mRNA. Translation: AAH12903.1. BC022803 mRNA. Translation: AAH22803.1. BC057219 mRNA. Translation: AAH57219.1. AF161473 mRNA. Translation: AAF29088.1. Different initiation. AL136655 mRNA. Translation: CAB66590.2. Different initiation.
IPI	IPI00301109. IPI00470502. IPI00470503. IPI00470504. IPI00470505.
RefSeq	NP_001029363.1. NP_008834.3. NP_789842.2. NP_789843.2. NP_789845.1.
UniGene	Hs.654957
3D structure databases
HSSP	HSSP built from PDB template 1WGI based on UniProtKB P00817.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9H2U2.
PTM databases
PhosphoSite	Q9H2U2.
2-D gel databases
OGP	Q9H2U2.
Proteomic databases
PeptideAtlas	Q9H2U2.
PRIDE	Q9H2U2.
Genome annotation databases
Ensembl	ENST00000310267; ENSP00000311150; ENSG00000138777; Homo sapiens. [Genome view] ENST00000341695; ENSP00000343885; ENSG00000138777; Homo sapiens. [Genome view] ENST00000348706; ENSP00000313061; ENSG00000138777; Homo sapiens. [Genome view] ENST00000351450; ENSP00000273977; ENSG00000138777; Homo sapiens. [Genome view] ENST00000354147; ENSP00000340352; ENSG00000138777; Homo sapiens. [Genome view] ENST00000357415; ENSP00000349996; ENSG00000138777; Homo sapiens. [Genome view] ENST00000380004; ENSP00000369340; ENSG00000138777; Homo sapiens. [Genome view] ENST00000432483; ENSP00000389957; ENSG00000138777; Homo sapiens. [Genome view] ENST00000457404; ENSP00000412634; ENSG00000138777; Homo sapiens. [Genome view]
GeneID	27068.
KEGG	hsa:27068.
UCSC	uc003hxl.1. human. uc003hxn.1. human. uc003hxp.1. human.
Organism-specific databases
CTD	27068.
GeneCards	GC04M106509.
H-InvDB	HIX0004419.
HGNC	HGNC:28883. PPA2.
MIM	609988. gene.
PharmGKB	PA134944028.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q9H2U2.
OMA	WFFISGS.
Enzyme and pathway databases
BRENDA	3.6.1.1. 247.
Gene expression databases
ArrayExpress	Q9H2U2.
Bgee	Q9H2U2.
CleanEx	HS_PPA2.
Genevestigator	Q9H2U2.
GermOnline	ENSG00000138777. Homo sapiens.
Family and domain databases
InterPro	IPR008162. Pyrophosphatase. [Graphical view]
Gene3D	G3DSA:3.90.80.10. Pyrophosphatase. 1 hit.
PANTHER	PTHR10286. Pyrophosphatase. 1 hit.
Pfam	PF00719. Pyrophosphatase. 1 hit. [Graphical view]
ProDom	PD002014. Inorg_pphsph. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00387. PPASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	49643.
SOURCE	Search...

Entry information

Entry name

IPYR2_HUMAN

Accession

Primary (citable) accession number: Q9H2U2
Secondary accession number(s): B4DLP7 , Q6PG51, Q8TBW0, Q96E55, Q9H0T0, Q9NX37, Q9P033, Q9ULX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	October 17, 2006
Last modified:	November 3, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.