位置:首页 > 蛋白库 > IPYR2_HUMAN
IPYR2_HUMAN
ID   IPYR2_HUMAN             Reviewed;         334 AA.
AC   Q9H2U2; B4DLP7; F8WDN9; I6L9B6; Q4W5E9; Q6PG51; Q8TBW0; Q96E55; Q9H0T0;
AC   Q9NX37; Q9P033; Q9ULX0;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 175.
DE   RecName: Full=Inorganic pyrophosphatase 2, mitochondrial {ECO:0000305|PubMed:27523597};
DE            EC=3.6.1.1 {ECO:0000269|PubMed:27523597};
DE   AltName: Full=Pyrophosphatase SID6-306;
DE   AltName: Full=Pyrophosphate phospho-hydrolase 2;
DE            Short=PPase 2;
DE   Flags: Precursor;
GN   Name=PPA2; ORFNames=HSPC124;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RA   Saito T., Hattori A., Miyajima N.;
RT   "Putative inorganic pyrophosphatase.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Kanni L., Johansson M., Karlsson A.;
RT   "Cloning of the mitochondrial inorganic pyrophosphatase 2 cDNA.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-282.
RC   TISSUE=Fibroblast, and Gastric carcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 3-334 (ISOFORM 4), AND NUCLEOTIDE SEQUENCE [LARGE
RP   SCALE MRNA] OF 12-334 (ISOFORM 5).
RC   TISSUE=Lung, Ovary, and Skeletal muscle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-334 (ISOFORM 2), AND VARIANT
RP   ASN-282.
RC   TISSUE=Umbilical cord blood;
RX   PubMed=11042152; DOI=10.1101/gr.140200;
RA   Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA   Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA   Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT   "Cloning and functional analysis of cDNAs with open reading frames for 300
RT   previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT   cells.";
RL   Genome Res. 10:1546-1560(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-334 (ISOFORM 2), AND VARIANT
RP   ASN-282.
RC   TISSUE=Brain;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [8]
RP   PROTEIN SEQUENCE OF 33-40.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA   Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass spectrometric
RT   identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [9]
RP   TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15210126; DOI=10.1016/j.bbapap.2004.03.014;
RA   Afjehi-Sadat L., Krapfenbauer K., Slavc I., Fountoulakis M., Lubec G.;
RT   "Hypothetical proteins with putative enzyme activity in human amnion,
RT   lymphocyte, bronchial epithelial and kidney cell lines.";
RL   Biochim. Biophys. Acta 1700:65-74(2004).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-261, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [18]
RP   CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER MET-32, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [19]
RP   FUNCTION, INVOLVEMENT IN SCFI, VARIANTS SCFI PRO-61; VAL-94; ILE-106;
RP   LYS-172 AND PRO-294, AND CHARACTERIZATION OF VARIANTS SCFI PRO-61 AND
RP   LYS-172.
RX   PubMed=27523598; DOI=10.1016/j.ajhg.2016.06.021;
RA   Guimier A., Gordon C.T., Godard F., Ravenscroft G., Oufadem M., Vasnier C.,
RA   Rambaud C., Nitschke P., Bole-Feysot C., Masson C., Dauger S., Longman C.,
RA   Laing N.G., Kugener B., Bonnet D., Bouvagnet P., Di Filippo S., Probst V.,
RA   Redon R., Charron P., Roetig A., Lyonnet S., Dautant A., de Pontual L.,
RA   di Rago J.P., Delahodde A., Amiel J.;
RT   "Biallelic PPA2 mutations cause sudden unexpected cardiac arrest in
RT   infancy.";
RL   Am. J. Hum. Genet. 99:666-673(2016).
RN   [20]
RP   FUNCTION, CATALYTIC ACTIVITY, INVOLVEMENT IN SCFAI, INVOLVEMENT IN SCFI,
RP   VARIANTS SCFI LEU-127 AND LEU-167, CHARACTERIZATION OF VARIANT SCFI
RP   LEU-167, VARIANTS SCFAI LYS-172 AND LEU-228, CHARACTERIZATION OF VARIANTS
RP   SCFAI LYS-172 AND LEU-228, AND SUBCELLULAR LOCATION.
RX   PubMed=27523597; DOI=10.1016/j.ajhg.2016.06.027;
RA   Kennedy H., Haack T.B., Hartill V., Matakovic L., Baumgartner E.R.,
RA   Potter H., Mackay R., Alston C.L., O'Sullivan S., McFarland R.,
RA   Connolly G., Gannon C., King R., Mead S., Crozier I., Chan W.,
RA   Florkowski C.M., Sage M., Hoefken T., Alhaddad B., Kremer L.S.,
RA   Kopajtich R., Feichtinger R.G., Sperl W., Rodenburg R.J., Minet J.C.,
RA   Dobbie A., Strom T.M., Meitinger T., George P.M., Johnson C.A.,
RA   Taylor R.W., Prokisch H., Doudney K., Mayr J.A.;
RT   "Sudden cardiac death due to deficiency of the mitochondrial inorganic
RT   pyrophosphatase PPA2.";
RL   Am. J. Hum. Genet. 99:674-682(2016).
CC   -!- FUNCTION: Hydrolyzes inorganic pyrophosphate (PubMed:27523597). This
CC       activity is essential for correct regulation of mitochondrial membrane
CC       potential, and mitochondrial organization and function
CC       (PubMed:27523598). {ECO:0000269|PubMed:27523597,
CC       ECO:0000269|PubMed:27523598}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474; EC=3.6.1.1;
CC         Evidence={ECO:0000269|PubMed:27523597};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24577;
CC         Evidence={ECO:0000269|PubMed:27523597};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9H2U2-3; P42858: HTT; NbExp=3; IntAct=EBI-25972548, EBI-466029;
CC       Q9H2U2-6; P42858: HTT; NbExp=3; IntAct=EBI-25972564, EBI-466029;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:27523597}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q9H2U2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H2U2-2; Sequence=VSP_011651;
CC       Name=3;
CC         IsoId=Q9H2U2-3; Sequence=VSP_011652;
CC       Name=4;
CC         IsoId=Q9H2U2-4; Sequence=VSP_011649, VSP_011650;
CC       Name=5;
CC         IsoId=Q9H2U2-6; Sequence=VSP_046256;
CC   -!- TISSUE SPECIFICITY: Detected in brain, gastric carcinoma, lung, ovary,
CC       skeletal muscle, umbilical cord blood and a cell line derived from
CC       kidney proximal tubule epithelium. {ECO:0000269|PubMed:15210126}.
CC   -!- DISEASE: Sudden cardiac failure, alcohol-induced (SCFAI) [MIM:617223]:
CC       An autosomal recessive disease characterized by sudden death due to
CC       unexpected cardiac arrest following ingestion of small amounts of
CC       alcohol. {ECO:0000269|PubMed:27523597}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
CC   -!- DISEASE: Sudden cardiac failure, infantile (SCFI) [MIM:617222]: A
CC       disease characterized by sudden death within the first 2 years of life
CC       due to unexpected cardiac arrest. Some patients manifest hypertrophic
CC       cardiomyopathy, lipid accumulation in myocardium, degeneration of
CC       mitochondrial cristae, metabolic acidosis, and elevated plasma lactate
CC       levels. SCFI transmission pattern is consistent with autosomal
CC       recessive inheritance. {ECO:0000269|PubMed:27523597,
CC       ECO:0000269|PubMed:27523598}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF29088.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAF29088.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC       Sequence=BAA84701.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA91184.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAG59609.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC       Sequence=CAB66590.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAB66590.2; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB026722; BAA84701.1; ALT_INIT; mRNA.
DR   EMBL; AF217187; AAG36781.1; -; mRNA.
DR   EMBL; AK000466; BAA91184.1; ALT_SEQ; mRNA.
DR   EMBL; AK297096; BAG59609.1; ALT_SEQ; mRNA.
DR   EMBL; AC004066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC106888; AAY41040.1; -; Genomic_DNA.
DR   EMBL; BC022803; AAH22803.1; -; mRNA.
DR   EMBL; BC039462; AAH39462.2; -; mRNA.
DR   EMBL; BC057219; AAH57219.1; -; mRNA.
DR   EMBL; AF161473; AAF29088.1; ALT_SEQ; mRNA.
DR   EMBL; AL136655; CAB66590.2; ALT_SEQ; mRNA.
DR   CCDS; CCDS34043.1; -. [Q9H2U2-4]
DR   CCDS; CCDS3667.1; -. [Q9H2U2-1]
DR   CCDS; CCDS3668.2; -. [Q9H2U2-3]
DR   CCDS; CCDS3669.2; -. [Q9H2U2-6]
DR   RefSeq; NP_008834.3; NM_006903.4. [Q9H2U2-3]
DR   RefSeq; NP_789842.2; NM_176866.2. [Q9H2U2-6]
DR   RefSeq; NP_789843.2; NM_176867.3. [Q9H2U2-4]
DR   RefSeq; NP_789845.1; NM_176869.2. [Q9H2U2-1]
DR   AlphaFoldDB; Q9H2U2; -.
DR   SMR; Q9H2U2; -.
DR   BioGRID; 117979; 142.
DR   IntAct; Q9H2U2; 28.
DR   MINT; Q9H2U2; -.
DR   STRING; 9606.ENSP00000343885; -.
DR   GlyGen; Q9H2U2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9H2U2; -.
DR   PhosphoSitePlus; Q9H2U2; -.
DR   SwissPalm; Q9H2U2; -.
DR   BioMuta; PPA2; -.
DR   DMDM; 116242592; -.
DR   OGP; Q9H2U2; -.
DR   EPD; Q9H2U2; -.
DR   jPOST; Q9H2U2; -.
DR   MassIVE; Q9H2U2; -.
DR   MaxQB; Q9H2U2; -.
DR   PaxDb; Q9H2U2; -.
DR   PeptideAtlas; Q9H2U2; -.
DR   PRIDE; Q9H2U2; -.
DR   ProteomicsDB; 31561; -.
DR   ProteomicsDB; 80594; -. [Q9H2U2-1]
DR   ProteomicsDB; 80595; -. [Q9H2U2-2]
DR   ProteomicsDB; 80596; -. [Q9H2U2-3]
DR   ProteomicsDB; 80597; -. [Q9H2U2-4]
DR   Antibodypedia; 26143; 123 antibodies from 21 providers.
DR   DNASU; 27068; -.
DR   Ensembl; ENST00000341695.10; ENSP00000343885.5; ENSG00000138777.20. [Q9H2U2-1]
DR   Ensembl; ENST00000348706.9; ENSP00000313061.8; ENSG00000138777.20. [Q9H2U2-3]
DR   Ensembl; ENST00000354147.7; ENSP00000340352.3; ENSG00000138777.20. [Q9H2U2-4]
DR   Ensembl; ENST00000432483.6; ENSP00000389957.2; ENSG00000138777.20. [Q9H2U2-6]
DR   GeneID; 27068; -.
DR   KEGG; hsa:27068; -.
DR   MANE-Select; ENST00000341695.10; ENSP00000343885.5; NM_176869.3; NP_789845.1.
DR   UCSC; uc003hxl.4; human. [Q9H2U2-1]
DR   CTD; 27068; -.
DR   DisGeNET; 27068; -.
DR   GeneCards; PPA2; -.
DR   HGNC; HGNC:28883; PPA2.
DR   HPA; ENSG00000138777; Low tissue specificity.
DR   MalaCards; PPA2; -.
DR   MIM; 609988; gene.
DR   MIM; 617222; phenotype.
DR   MIM; 617223; phenotype.
DR   neXtProt; NX_Q9H2U2; -.
DR   OpenTargets; ENSG00000138777; -.
DR   PharmGKB; PA142671159; -.
DR   VEuPathDB; HostDB:ENSG00000138777; -.
DR   eggNOG; KOG1626; Eukaryota.
DR   GeneTree; ENSGT00390000017004; -.
DR   HOGENOM; CLU_1763017_0_0_1; -.
DR   InParanoid; Q9H2U2; -.
DR   OMA; HECWKAM; -.
DR   OrthoDB; 1398991at2759; -.
DR   PhylomeDB; Q9H2U2; -.
DR   TreeFam; TF300887; -.
DR   BRENDA; 3.6.1.1; 2681.
DR   PathwayCommons; Q9H2U2; -.
DR   Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation.
DR   Reactome; R-HSA-71737; Pyrophosphate hydrolysis.
DR   SignaLink; Q9H2U2; -.
DR   BioGRID-ORCS; 27068; 298 hits in 1088 CRISPR screens.
DR   ChiTaRS; PPA2; human.
DR   GenomeRNAi; 27068; -.
DR   Pharos; Q9H2U2; Tbio.
DR   PRO; PR:Q9H2U2; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q9H2U2; protein.
DR   Bgee; ENSG00000138777; Expressed in calcaneal tendon and 206 other tissues.
DR   ExpressionAtlas; Q9H2U2; baseline and differential.
DR   Genevisible; Q9H2U2; HS.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:Ensembl.
DR   GO; GO:0071344; P:diphosphate metabolic process; IMP:UniProtKB.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; IBA:GO_Central.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:UniProtKB.
DR   CDD; cd00412; pyrophosphatase; 1.
DR   Gene3D; 3.90.80.10; -; 1.
DR   InterPro; IPR008162; Pyrophosphatase.
DR   InterPro; IPR036649; Pyrophosphatase_sf.
DR   PANTHER; PTHR10286; PTHR10286; 1.
DR   Pfam; PF00719; Pyrophosphatase; 1.
DR   SUPFAM; SSF50324; SSF50324; 1.
DR   PROSITE; PS00387; PPASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Direct protein sequencing;
KW   Disease variant; Hydrolase; Magnesium; Metal-binding; Mitochondrion;
KW   Phosphoprotein; Reference proteome; Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:12665801,
FT                   ECO:0007744|PubMed:25944712"
FT   CHAIN           33..334
FT                   /note="Inorganic pyrophosphatase 2, mitochondrial"
FT                   /id="PRO_0000025411"
FT   BINDING         164
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         216
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VM9"
FT   MOD_RES         224
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VM9"
FT   MOD_RES         259
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VM9"
FT   MOD_RES         261
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         317
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         53
FT                   /note="K -> N (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_011649"
FT   VAR_SEQ         54..219
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_011650"
FT   VAR_SEQ         74
FT                   /note="E -> EDTEAQGIFIDLSKIW (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11042152,
FT                   ECO:0000303|PubMed:11230166"
FT                   /id="VSP_011651"
FT   VAR_SEQ         75..176
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_046256"
FT   VAR_SEQ         148..176
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT                   /id="VSP_011652"
FT   VARIANT         61
FT                   /note="S -> P (in SCFI; loss of function in regulation of
FT                   mitochondrial membrane potential)"
FT                   /evidence="ECO:0000269|PubMed:27523598"
FT                   /id="VAR_077866"
FT   VARIANT         94
FT                   /note="M -> V (in SCFI; dbSNP:rs1057517679)"
FT                   /evidence="ECO:0000269|PubMed:27523598"
FT                   /id="VAR_077867"
FT   VARIANT         106
FT                   /note="M -> I (in SCFI; dbSNP:rs1057517680)"
FT                   /evidence="ECO:0000269|PubMed:27523598"
FT                   /id="VAR_077868"
FT   VARIANT         127
FT                   /note="R -> L (in SCFI; dbSNP:rs139076647)"
FT                   /evidence="ECO:0000269|PubMed:27523597"
FT                   /id="VAR_077869"
FT   VARIANT         167
FT                   /note="P -> L (in SCFI; decreased inorganic diphosphatase
FT                   activity; dbSNP:rs546693824)"
FT                   /evidence="ECO:0000269|PubMed:27523597"
FT                   /id="VAR_077870"
FT   VARIANT         172
FT                   /note="E -> K (in SCFI and SCFAI; loss of function in
FT                   regulation of mitochondrial membrane potential; decreased
FT                   inorganic diphosphatase activity; dbSNP:rs146013446)"
FT                   /evidence="ECO:0000269|PubMed:27523597,
FT                   ECO:0000269|PubMed:27523598"
FT                   /id="VAR_077871"
FT   VARIANT         228
FT                   /note="P -> L (in SCFAI; decreased inorganic diphosphatase
FT                   activity; dbSNP:rs138215926)"
FT                   /evidence="ECO:0000269|PubMed:27523597"
FT                   /id="VAR_077872"
FT   VARIANT         282
FT                   /note="K -> N (in dbSNP:rs13787)"
FT                   /evidence="ECO:0000269|PubMed:11042152,
FT                   ECO:0000269|PubMed:11230166, ECO:0000269|PubMed:14702039"
FT                   /id="VAR_019723"
FT   VARIANT         294
FT                   /note="Q -> P (in SCFI; dbSNP:rs1057517678)"
FT                   /evidence="ECO:0000269|PubMed:27523598"
FT                   /id="VAR_077873"
FT   CONFLICT        11
FT                   /note="G -> V (in Ref. 1; BAA84701 and 2; AAG36781)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        19
FT                   /note="R -> G (in Ref. 7; CAB66590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103
FT                   /note="N -> K (in Ref. 7; CAB66590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241
FT                   /note="Y -> C (in Ref. 7; CAB66590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        288
FT                   /note="I -> T (in Ref. 7; CAB66590)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   334 AA;  37920 MW;  F8C85F64CDA447F1 CRC64;
     MSALLRLLRT GAPAAACLRL GTSAGTGSRR AMALYHTEER GQPCSQNYRL FFKNVTGHYI
     SPFHDIPLKV NSKEENGIPM KKARNDEYEN LFNMIVEIPR WTNAKMEIAT KEPMNPIKQY
     VKDGKLRYVA NIFPYKGYIW NYGTLPQTWE DPHEKDKSTN CFGDNDPIDV CEIGSKILSC
     GEVIHVKILG ILALIDEGET DWKLIAINAN DPEASKFHDI DDVKKFKPGY LEATLNWFRL
     YKVPDGKPEN QFAFNGEFKN KAFALEVIKS THQCWKALLM KKCNGGAINC TNVQISDSPF
     RCTQEEARSL VESVSSSPNK ESNEEEQVWH FLGK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024