Q9H2U2 (IPYR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inorganic pyrophosphatase 2, mitochondrial
EC=3.6.1.1

Alternative name(s):
Pyrophosphatase SID6-306
Pyrophosphate phospho-hydrolase 2
Short name=PPase 2

Gene names

Name:	PPA2
ORF Names:	HSPC124

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 › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.9
Sequence similarities	Belongs to the PPase family.
Sequence caution	The sequence AAF29088.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAF29088.1 differs from that shown. Reason: Aberrant splicing. The sequence BAA84701.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA91184.1 differs from that shown. Reason: Erroneous termination at position 59. Translated as Tyr. The sequence BAG59609.1 differs from that shown. Reason: Intron retention. The sequence CAB66590.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAB66590.2 differs from that shown. Reason: Frameshift at position 75.

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 Reference proteome
Gene Ontology (GO)
Biological_process	diphosphate metabolic process Traceable author statement. Source: Reactome phosphate-containing compound metabolic process Inferred from electronic annotation. Source: InterPro tRNA aminoacylation for protein translation Traceable author statement. Source: Reactome
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome
Molecular_function	inorganic diphosphatase activity Traceable author statement. Source: Reactome magnesium ion binding Inferred from electronic annotation. Source: InterPro
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

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

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: Q9H2U2-6)

The sequence of this isoform differs from the canonical sequence as follows:
     75-176: Missing.

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.8
	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	261	1	N6-acetyllysine Ref.12
	Modified residue	317	1	Phosphoserine Ref.13 Ref.15
Natural variations
	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	75 – 176	102	Missing in isoform 5.		VSP_046256
	Alternative sequence	148 – 176	29	Missing in isoform 3.		VSP_011652
	Natural variant	282	1	K → N. Ref.3 Ref.6 Ref.7 Corresponds to variant rs13787 [ dbSNP | Ensembl ].		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	19	1	R → G in CAB66590. Ref.7
	Sequence conflict	103	1	N → K in CAB66590. Ref.7
	Sequence conflict	241	1	Y → C in CAB66590. Ref.7
	Sequence conflict	288	1	I → T in CAB66590. Ref.7

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 [UniParc]. 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 [UniParc]. 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 [UniParc]. 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 [UniParc]. Checksum: 2D41198AF19951A5	FASTA	232	25,992
	10 20 30 40 50 60 MSALLRLLRT GAPAAACLRL GTSAGTGSRR AMALYHTEER GQPCSQNYRL FFKNVTGHYI 70 80 90 100 110 120 SPFHDIPLKV NSKEILSCGE VIHVKILGIL ALIDEGETDW KLIAINANDP EASKFHDIDD 130 140 150 160 170 180 VKKFKPGYLE ATLNWFRLYK VPDGKPENQF AFNGEFKNKA FALEVIKSTH QCWKALLMKK 190 200 210 220 230 CNGGAINCTN VQISDSPFRC TQEEARSLVE SVSSSPNKES NEEEQVWHFL GK

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASN-282. Tissue: Fibroblast and Gastric carcinoma.
[4]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-334 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-334 (ISOFORM 5). Tissue: Lung, Ovary and Skeletal muscle.
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-334 (ISOFORM 2), VARIANT ASN-282. Tissue: Umbilical cord blood.
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-334 (ISOFORM 2), VARIANT ASN-282. Tissue: Brain.
[8]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 33-40. Tissue: Platelet.
[9]	"Hypothetical proteins with putative enzyme activity in human amnion, lymphocyte, bronchial epithelial and kidney cell lines." Afjehi-Sadat L., Krapfenbauer K., Slavc I., Fountoulakis M., Lubec G. Biochim. Biophys. Acta 1700:65-74(2004) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY, TISSUE SPECIFICITY.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-261, MASS SPECTROMETRY.
[13]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB026722 mRNA. Translation: BAA84701.1. Different initiation. AF217187 mRNA. Translation: AAG36781.1. AK000466 mRNA. Translation: BAA91184.1. Sequence problems. AK297096 mRNA. Translation: BAG59609.1. Sequence problems. AC004066 Genomic DNA. No translation available. AC106888 Genomic DNA. Translation: AAY41040.1. BC022803 mRNA. Translation: AAH22803.1. BC039462 mRNA. Translation: AAH39462.2. BC057219 mRNA. Translation: AAH57219.1. AF161473 mRNA. Translation: AAF29088.1. Sequence problems. AL136655 mRNA. Translation: CAB66590.2. Sequence problems.
IPI	IPI00301109. IPI00413014. IPI00470502. IPI00470503. IPI00470504.
RefSeq	NP_008834.3. NM_006903.4. NP_789842.2. NM_176866.2. NP_789843.2. NM_176867.3. NP_789845.1. NM_176869.2.
UniGene	Hs.654957.
3D structure databases
ProteinModelPortal	Q9H2U2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H2U2. 1 interaction.
PTM databases
PhosphoSite	Q9H2U2.
Polymorphism databases
DMDM	116242592.
2D gel databases
OGP	Q9H2U2.
Proteomic databases
PaxDb	Q9H2U2.
PeptideAtlas	Q9H2U2.
PRIDE	Q9H2U2.
Protocols and materials databases
DNASU	27068.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000341695; ENSP00000343885; ENSG00000138777. ENST00000348706; ENSP00000313061; ENSG00000138777. ENST00000354147; ENSP00000340352; ENSG00000138777. ENST00000357415; ENSP00000349996; ENSG00000138777. ENST00000432483; ENSP00000389957; ENSG00000138777. ENST00000509031; ENSP00000423467; ENSG00000138777.
GeneID	27068.
KEGG	hsa:27068.
UCSC	uc003hxl.3. human. uc003hxn.3. human. uc003hxp.3. human.
Organism-specific databases
CTD	27068.
GeneCards	GC04M106290.
HGNC	HGNC:28883. PPA2.
HPA	HPA031671.
MIM	609988. gene.
neXtProt	NX_Q9H2U2.
PharmGKB	PA142671159.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0221.
HOVERGEN	HBG000491.
KO	K01507.
OMA	KSTHQCW.
OrthoDB	EOG4KPTBC.
PhylomeDB	Q9H2U2.
Enzyme and pathway databases
BRENDA	3.6.1.1. 2681.
Reactome	REACT_21259. Pyrophosphate hydrolysis. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q9H2U2.
Bgee	Q9H2U2.
CleanEx	HS_PPA2.
Genevestigator	Q9H2U2.
GermOnline	ENSG00000138777. Homo sapiens.
Family and domain databases
Gene3D	3.90.80.10. 1 hit.
InterPro	IPR008162. Pyrophosphatase. [Graphical view]
PANTHER	PTHR10286. PTHR10286. 1 hit.
Pfam	PF00719. Pyrophosphatase. 1 hit. [Graphical view]
SUPFAM	SSF50324. Pyrophosphatase. 1 hit.
PROSITE	PS00387. PPASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PPA2. human.
GenomeRNAi	27068.
NextBio	35533887.
SOURCE	Search...

Entry information

Entry name

IPYR2_HUMAN

Accession

Primary (citable) accession number: Q9H2U2
Secondary accession number(s): B4DLP7 , F8WDN9, I6L9B6, Q4W5E9, 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:	May 1, 2013
This is version 108 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.