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Q9H2U2 (IPYR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Mitochondrion Ref.8
Chain33 – 334302Inorganic pyrophosphatase 2, mitochondrial
PRO_0000025411

Sites

Metal binding1641Magnesium 1 By similarity
Metal binding1691Magnesium 1 By similarity
Metal binding1691Magnesium 2 By similarity
Metal binding2011Magnesium 1 By similarity

Amino acid modifications

Modified residue2161N6-succinyllysine By similarity
Modified residue2241N6-acetyllysine By similarity
Modified residue2591N6-succinyllysine By similarity
Modified residue2611N6-acetyllysine Ref.12
Modified residue3171Phosphoserine Ref.13 Ref.15

Natural variations

Alternative sequence531K → N in isoform 4.
VSP_011649
Alternative sequence54 – 219166Missing in isoform 4.
VSP_011650
Alternative sequence741E → EDTEAQGIFIDLSKIW in isoform 2.
VSP_011651
Alternative sequence75 – 176102Missing in isoform 5.
VSP_046256
Alternative sequence148 – 17629Missing in isoform 3.
VSP_011652
Natural variant2821K → N. Ref.3 Ref.6 Ref.7
Corresponds to variant rs13787 [ dbSNP | Ensembl ].
VAR_019723

Experimental info

Sequence conflict111G → V in BAA84701. Ref.1
Sequence conflict111G → V in AAG36781. Ref.2
Sequence conflict191R → G in CAB66590. Ref.7
Sequence conflict1031N → K in CAB66590. Ref.7
Sequence conflict2411Y → C in CAB66590. Ref.7
Sequence conflict2881I → T in CAB66590. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: F8C85F64CDA447F1

FASTA33437,920
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 44938DDEB36C8789
Show »

FASTA34939,638
Isoform 3 [UniParc].

Checksum: ACC551F07BE228AE
Show »

FASTA30534,658
Isoform 4 [UniParc].

Checksum: 9CADD542FA7E7569
Show »

FASTA16818,916
Isoform 5 [UniParc].

Checksum: 2D41198AF19951A5
Show »

FASTA23225,992

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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: TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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.
CCDSCCDS34043.1. [Q9H2U2-4]
CCDS3667.1. [Q9H2U2-1]
CCDS3668.2. [Q9H2U2-3]
CCDS3669.2. [Q9H2U2-6]
RefSeqNP_008834.3. NM_006903.4. [Q9H2U2-3]
NP_789842.2. NM_176866.2. [Q9H2U2-6]
NP_789843.2. NM_176867.3. [Q9H2U2-4]
NP_789845.1. NM_176869.2. [Q9H2U2-1]
UniGeneHs.654957.

3D structure databases

ProteinModelPortalQ9H2U2.
SMRQ9H2U2. Positions 35-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117979. 3 interactions.
IntActQ9H2U2. 2 interactions.
MINTMINT-3066899.

PTM databases

PhosphoSiteQ9H2U2.

Polymorphism databases

DMDM116242592.

2D gel databases

OGPQ9H2U2.

Proteomic databases

MaxQBQ9H2U2.
PaxDbQ9H2U2.
PeptideAtlasQ9H2U2.
PRIDEQ9H2U2.

Protocols and materials databases

DNASU27068.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341695; ENSP00000343885; ENSG00000138777. [Q9H2U2-1]
ENST00000348706; ENSP00000313061; ENSG00000138777. [Q9H2U2-3]
ENST00000354147; ENSP00000340352; ENSG00000138777. [Q9H2U2-4]
ENST00000357415; ENSP00000349996; ENSG00000138777. [Q9H2U2-2]
ENST00000432483; ENSP00000389957; ENSG00000138777. [Q9H2U2-6]
ENST00000509031; ENSP00000423467; ENSG00000138777.
GeneID27068.
KEGGhsa:27068.
UCSCuc003hxl.3. human. [Q9H2U2-1]
uc003hxn.3. human. [Q9H2U2-3]
uc003hxp.3. human. [Q9H2U2-4]

Organism-specific databases

CTD27068.
GeneCardsGC04M106290.
HGNCHGNC:28883. PPA2.
HPAHPA031671.
MIM609988. gene.
neXtProtNX_Q9H2U2.
PharmGKBPA142671159.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0221.
HOVERGENHBG000491.
KOK01507.
OMASTHQCWK.
OrthoDBEOG7R2BKH.
PhylomeDBQ9H2U2.
TreeFamTF300887.

Enzyme and pathway databases

BRENDA3.6.1.1. 2681.
ReactomeREACT_21259. Pyrophosphate hydrolysis.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9H2U2.
BgeeQ9H2U2.
CleanExHS_PPA2.
GenevestigatorQ9H2U2.

Family and domain databases

Gene3D3.90.80.10. 1 hit.
InterProIPR008162. Pyrophosphatase.
[Graphical view]
PANTHERPTHR10286. PTHR10286. 1 hit.
PfamPF00719. Pyrophosphatase. 1 hit.
[Graphical view]
SUPFAMSSF50324. SSF50324. 1 hit.
PROSITEPS00387. PPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPA2. human.
GenomeRNAi27068.
NextBio35533887.
PROQ9H2U2.
SOURCESearch...

Entry information

Entry nameIPYR2_HUMAN
AccessionPrimary (citable) accession number: Q9H2U2
Secondary accession number(s): B4DLP7 expand/collapse secondary AC list , 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: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM