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Protein

Inorganic pyrophosphatase 2, mitochondrial

Gene

PPA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Diphosphate + H2O = 2 phosphate.

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi164 – 1641Magnesium 1By similarity
Metal bindingi169 – 1691Magnesium 1By similarity
Metal bindingi169 – 1691Magnesium 2By similarity
Metal bindingi201 – 2011Magnesium 1By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.6.1.1. 2681.
ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PPA2
ORF Names:HSPC124
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:28883. PPA2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • mitochondrial matrix Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671159.

Polymorphism and mutation databases

BioMutaiPPA2.
DMDMi116242592.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3232Mitochondrion1 PublicationAdd
BLAST
Chaini33 – 334302Inorganic pyrophosphatase 2, mitochondrialPRO_0000025411Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei216 – 2161N6-succinyllysineBy similarity
Modified residuei224 – 2241N6-acetyllysineBy similarity
Modified residuei259 – 2591N6-succinyllysineBy similarity
Modified residuei261 – 2611N6-acetyllysine1 Publication
Modified residuei317 – 3171Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H2U2.
PaxDbiQ9H2U2.
PeptideAtlasiQ9H2U2.
PRIDEiQ9H2U2.

2D gel databases

OGPiQ9H2U2.

PTM databases

PhosphoSiteiQ9H2U2.

Expressioni

Tissue specificityi

Detected in brain, gastric carcinoma, lung, ovary, skeletal muscle, umbilical cord blood and a cell line derived from kidney proximal tubule epithelium.1 Publication

Gene expression databases

BgeeiQ9H2U2.
CleanExiHS_PPA2.
ExpressionAtlasiQ9H2U2. baseline and differential.
GenevisibleiQ9H2U2. HS.

Organism-specific databases

HPAiHPA030888.
HPA031671.
HPA031672.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi117979. 13 interactions.
IntActiQ9H2U2. 2 interactions.
MINTiMINT-3066899.

Structurei

3D structure databases

ProteinModelPortaliQ9H2U2.
SMRiQ9H2U2. Positions 35-332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0221.
GeneTreeiENSGT00390000017004.
HOVERGENiHBG000491.
InParanoidiQ9H2U2.
KOiK01507.
OMAiSTHQCWK.
OrthoDBiEOG7R2BKH.
PhylomeDBiQ9H2U2.
TreeFamiTF300887.

Family and domain databases

Gene3Di3.90.80.10. 1 hit.
InterProiIPR008162. Pyrophosphatase.
[Graphical view]
PANTHERiPTHR10286. PTHR10286. 1 hit.
PfamiPF00719. Pyrophosphatase. 1 hit.
[Graphical view]
SUPFAMiSSF50324. SSF50324. 1 hit.
PROSITEiPS00387. PPASE. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H2U2-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSALLRLLRT GAPAAACLRL GTSAGTGSRR AMALYHTEER GQPCSQNYRL
60 70 80 90 100
FFKNVTGHYI SPFHDIPLKV NSKEENGIPM KKARNDEYEN LFNMIVEIPR
110 120 130 140 150
WTNAKMEIAT KEPMNPIKQY VKDGKLRYVA NIFPYKGYIW NYGTLPQTWE
160 170 180 190 200
DPHEKDKSTN CFGDNDPIDV CEIGSKILSC GEVIHVKILG ILALIDEGET
210 220 230 240 250
DWKLIAINAN DPEASKFHDI DDVKKFKPGY LEATLNWFRL YKVPDGKPEN
260 270 280 290 300
QFAFNGEFKN KAFALEVIKS THQCWKALLM KKCNGGAINC TNVQISDSPF
310 320 330
RCTQEEARSL VESVSSSPNK ESNEEEQVWH FLGK
Length:334
Mass (Da):37,920
Last modified:October 17, 2006 - v2
Checksum:iF8C85F64CDA447F1
GO
Isoform 2 (identifier: Q9H2U2-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:349
Mass (Da):39,638
Checksum:i44938DDEB36C8789
GO
Isoform 3 (identifier: Q9H2U2-3) [UniParc]FASTAAdd to basket

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

Show »
Length:305
Mass (Da):34,658
Checksum:iACC551F07BE228AE
GO
Isoform 4 (identifier: Q9H2U2-4) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:168
Mass (Da):18,916
Checksum:i9CADD542FA7E7569
GO
Isoform 5 (identifier: Q9H2U2-6) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:232
Mass (Da):25,992
Checksum:i2D41198AF19951A5
GO

Sequence cautioni

The sequence AAF29088.1 differs from that shown.Aberrant splicing.Curated
The sequence AAF29088.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA84701.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA91184.1 differs from that shown. Reason: Erroneous termination at position 59. Translated as Tyr.Curated
The sequence BAG59609.1 differs from that shown.Intron retention.Curated
The sequence CAB66590.2 differs from that shown. Reason: Frameshift at position 75. Curated
The sequence CAB66590.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111G → V in BAA84701 (Ref. 1) Curated
Sequence conflicti11 – 111G → V in AAG36781 (Ref. 2) Curated
Sequence conflicti19 – 191R → G in CAB66590 (PubMed:11230166).Curated
Sequence conflicti103 – 1031N → K in CAB66590 (PubMed:11230166).Curated
Sequence conflicti241 – 2411Y → C in CAB66590 (PubMed:11230166).Curated
Sequence conflicti288 – 2881I → T in CAB66590 (PubMed:11230166).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti282 – 2821K → N.3 Publications
Corresponds to variant rs13787 [ dbSNP | Ensembl ].
VAR_019723

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei53 – 531K → N in isoform 4. 1 PublicationVSP_011649
Alternative sequencei54 – 219166Missing in isoform 4. 1 PublicationVSP_011650Add
BLAST
Alternative sequencei74 – 741E → EDTEAQGIFIDLSKIW in isoform 2. 2 PublicationsVSP_011651
Alternative sequencei75 – 176102Missing in isoform 5. 1 PublicationVSP_046256Add
BLAST
Alternative sequencei148 – 17629Missing in isoform 3. 2 PublicationsVSP_011652Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34043.1. [Q9H2U2-4]
CCDS3667.1. [Q9H2U2-1]
CCDS3668.2. [Q9H2U2-3]
CCDS3669.2. [Q9H2U2-6]
RefSeqiNP_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]
UniGeneiHs.654957.

Genome annotation databases

EnsembliENST00000341695; ENSP00000343885; ENSG00000138777. [Q9H2U2-1]
ENST00000348706; ENSP00000313061; ENSG00000138777. [Q9H2U2-3]
ENST00000354147; ENSP00000340352; ENSG00000138777. [Q9H2U2-4]
ENST00000432483; ENSP00000389957; ENSG00000138777. [Q9H2U2-6]
GeneIDi27068.
KEGGihsa:27068.
UCSCiuc003hxl.3. human. [Q9H2U2-1]
uc003hxn.3. human. [Q9H2U2-3]
uc003hxp.3. human. [Q9H2U2-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34043.1. [Q9H2U2-4]
CCDS3667.1. [Q9H2U2-1]
CCDS3668.2. [Q9H2U2-3]
CCDS3669.2. [Q9H2U2-6]
RefSeqiNP_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]
UniGeneiHs.654957.

3D structure databases

ProteinModelPortaliQ9H2U2.
SMRiQ9H2U2. Positions 35-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117979. 13 interactions.
IntActiQ9H2U2. 2 interactions.
MINTiMINT-3066899.

PTM databases

PhosphoSiteiQ9H2U2.

Polymorphism and mutation databases

BioMutaiPPA2.
DMDMi116242592.

2D gel databases

OGPiQ9H2U2.

Proteomic databases

MaxQBiQ9H2U2.
PaxDbiQ9H2U2.
PeptideAtlasiQ9H2U2.
PRIDEiQ9H2U2.

Protocols and materials databases

DNASUi27068.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341695; ENSP00000343885; ENSG00000138777. [Q9H2U2-1]
ENST00000348706; ENSP00000313061; ENSG00000138777. [Q9H2U2-3]
ENST00000354147; ENSP00000340352; ENSG00000138777. [Q9H2U2-4]
ENST00000432483; ENSP00000389957; ENSG00000138777. [Q9H2U2-6]
GeneIDi27068.
KEGGihsa:27068.
UCSCiuc003hxl.3. human. [Q9H2U2-1]
uc003hxn.3. human. [Q9H2U2-3]
uc003hxp.3. human. [Q9H2U2-4]

Organism-specific databases

CTDi27068.
GeneCardsiGC04M106290.
HGNCiHGNC:28883. PPA2.
HPAiHPA030888.
HPA031671.
HPA031672.
MIMi609988. gene.
neXtProtiNX_Q9H2U2.
PharmGKBiPA142671159.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0221.
GeneTreeiENSGT00390000017004.
HOVERGENiHBG000491.
InParanoidiQ9H2U2.
KOiK01507.
OMAiSTHQCWK.
OrthoDBiEOG7R2BKH.
PhylomeDBiQ9H2U2.
TreeFamiTF300887.

Enzyme and pathway databases

BRENDAi3.6.1.1. 2681.
ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.

Miscellaneous databases

ChiTaRSiPPA2. human.
GenomeRNAii27068.
NextBioi35533887.
PROiQ9H2U2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H2U2.
CleanExiHS_PPA2.
ExpressionAtlasiQ9H2U2. baseline and differential.
GenevisibleiQ9H2U2. HS.

Family and domain databases

Gene3Di3.90.80.10. 1 hit.
InterProiIPR008162. Pyrophosphatase.
[Graphical view]
PANTHERiPTHR10286. PTHR10286. 1 hit.
PfamiPF00719. Pyrophosphatase. 1 hit.
[Graphical view]
SUPFAMiSSF50324. SSF50324. 1 hit.
PROSITEiPS00387. PPASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiIPYR2_HUMAN
AccessioniPrimary (citable) accession number: Q9H2U2
Secondary accession number(s): B4DLP7
, F8WDN9, I6L9B6, Q4W5E9, Q6PG51, Q8TBW0, Q96E55, Q9H0T0, Q9NX37, Q9P033, Q9ULX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: October 17, 2006
Last modified: June 24, 2015
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.