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Q15257

- PTPA_HUMAN

UniProt

Q15257 - PTPA_HUMAN

Protein

Serine/threonine-protein phosphatase 2A activator

Gene

PPP2R4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg2+ By similarity. Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg2+ (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function appears to be independent from PP2A.By similarity2 Publications

    Catalytic activityi

    Peptidylproline (omega=180) = peptidylproline (omega=0).

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi183 – 1897ATP
    Nucleotide bindingi240 – 2423ATP
    Nucleotide bindingi342 – 3432ATP

    GO - Molecular functioni

    1. ATP binding Source: HGNC
    2. peptidyl-prolyl cis-trans isomerase activity Source: RefGenome
    3. protein heterodimerization activity Source: HGNC
    4. protein homodimerization activity Source: HGNC
    5. protein phosphatase 2A binding Source: HGNC
    6. protein phosphatase type 2A regulator activity Source: HGNC
    7. protein tyrosine phosphatase activator activity Source: HGNC
    8. receptor binding Source: BHF-UCL

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. mitotic spindle organization in nucleus Source: RefGenome
    3. negative regulation of phosphoprotein phosphatase activity Source: HGNC
    4. negative regulation of protein dephosphorylation Source: HGNC
    5. positive regulation of apoptotic process Source: UniProtKB
    6. positive regulation of phosphoprotein phosphatase activity Source: HGNC
    7. positive regulation of protein dephosphorylation Source: HGNC
    8. protein folding Source: UniProtKB-KW
    9. protein peptidyl-prolyl isomerization Source: GOC
    10. regulation of phosphoprotein phosphatase activity Source: HGNC

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 2A activator (EC:5.2.1.8)
    Alternative name(s):
    PP2A, subunit B', PR53 isoform
    Phosphotyrosyl phosphatase activator
    Short name:
    PTPA
    Serine/threonine-protein phosphatase 2A regulatory subunit 4
    Serine/threonine-protein phosphatase 2A regulatory subunit B'
    Gene namesi
    Name:PPP2R4
    Synonyms:PTPA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:9308. PPP2R4.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. calcium channel complex Source: BHF-UCL
    2. cytoplasm Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: UniProtKB
    5. protein phosphatase type 2A complex Source: HGNC

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi185 – 1851D → A: Impairs ATPase activity of the PP2A(D):PPP2R4 complex; no effect on interaction with the PP2A(D) complex. 1 Publication
    Mutagenesisi239 – 2391A → D: Impairs ATPase activity of the PP2A(D):PPP2R4 complex; no effect on interaction with the PP2A(D) complex. 1 Publication
    Mutagenesisi240 – 2401G → D: Impairs ATPase activity of the PP2A(D):PPP2R4 complex; no effect on interaction with the PP2A(D) complex. 1 Publication
    Mutagenesisi244 – 2441V → D: Impairs interaction with the PP2A(D) complex. 1 Publication
    Mutagenesisi305 – 3051E → A: Abolishes interaction with the PP2A(D) complex. 1 Publication
    Mutagenesisi316 – 3161V → D: Impairs interaction with the PP2A(D) complex.
    Mutagenesisi325 – 3251G → D: Abolishes interaction with the PP2A(D) complex. 1 Publication
    Mutagenesisi329 – 3291M → D: Abolishes interaction with the PP2A(D) complex. 1 Publication
    Mutagenesisi337 – 3371K → G: Impairs interaction with the PP2A(D) complex. 1 Publication

    Organism-specific databases

    PharmGKBiPA33671.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 358357Serine/threonine-protein phosphatase 2A activatorPRO_0000071524Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ15257.
    PaxDbiQ15257.
    PRIDEiQ15257.

    2D gel databases

    OGPiQ15257.

    PTM databases

    PhosphoSiteiQ15257.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Gene expression databases

    ArrayExpressiQ15257.
    BgeeiQ15257.
    CleanExiHS_PPP2R4.
    GenevestigatoriQ15257.

    Organism-specific databases

    HPAiCAB022068.
    CAB035999.
    HPA005695.

    Interactioni

    Subunit structurei

    Associates with PP2A heterodimeric core enzyme PP2A(D), composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65 or subunit A). Interacts with PPP2CB By similarity.By similarity

    Protein-protein interaction databases

    BioGridi111516. 54 interactions.
    IntActiQ15257. 10 interactions.
    MINTiMINT-3031079.

    Structurei

    Secondary structure

    1
    358
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi34 – 407
    Helixi43 – 5816
    Turni59 – 613
    Helixi107 – 12418
    Beta strandi134 – 1363
    Helixi139 – 15618
    Helixi161 – 1666
    Helixi167 – 1759
    Turni181 – 1844
    Helixi188 – 20316
    Helixi209 – 2113
    Helixi212 – 2176
    Helixi219 – 23315
    Beta strandi237 – 2404
    Helixi243 – 2453
    Beta strandi247 – 2504
    Helixi253 – 2619
    Turni262 – 2643
    Helixi270 – 2745
    Helixi276 – 2827
    Helixi283 – 2853
    Helixi287 – 29812
    Helixi303 – 3064
    Helixi308 – 3136
    Helixi319 – 33315
    Turni334 – 3363
    Helixi338 – 3414
    Beta strandi348 – 3503
    Beta strandi352 – 3543

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2G62X-ray1.60A22-358[»]
    2HV6X-ray1.90A/B1-358[»]
    2HV7X-ray2.50A/B/C/D/E/F/G/H1-358[»]
    2IXMX-ray1.50A20-357[»]
    4LACX-ray2.82B19-358[»]
    ProteinModelPortaliQ15257.
    SMRiQ15257. Positions 23-357.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15257.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PTPA-type PPIase family.Curated

    Phylogenomic databases

    eggNOGiCOG5057.
    HOVERGENiHBG019168.
    KOiK17605.
    OrthoDBiEOG7KQ21W.
    PhylomeDBiQ15257.
    TreeFamiTF105555.

    Family and domain databases

    InterProiIPR004327. Phstyr_phstse_ac.
    [Graphical view]
    PANTHERiPTHR10012. PTHR10012. 1 hit.
    PfamiPF03095. PTPA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016325. Phstyr_phstse_ac. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: Q15257-1) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    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

    MAEGERQPPP DSSEEAPPAT QNFIIPKKEI HTVPDMGKWK RSQAYADYIG    50
    FILTLNEGVK GKKLTFEYRV SEMWNEVHEE KEQAAKQSVS CDECIPLPRA 100
    GHCAPSEAIE KLVALLNTLD RWIDETPPVD QPSRFGNKAY RTWYAKLDEE 150
    AENLVATVVP THLAAAVPEV AVYLKESVGN STRIDYGTGH EAAFAAFLCC 200
    LCKIGVLRVD DQIAIVFKVF NRYLEVMRKL QKTYRMEPAG SQGVWGLDDF 250
    QFLPFIWGSS QLIDHPYLEP RHFVDEKAVN ENHKDYMFLE CILFITEMKT 300
    GPFAEHSNQL WNISAVPSWS KVNQGLIRMY KAECLEKFPV IQHFKFGSLL 350
    PIHPVTSG 358
    Length:358
    Mass (Da):40,668
    Last modified:October 17, 2006 - v3
    Checksum:i2A962521AF5B4CF7
    GO
    Isoform 1 (identifier: Q15257-2) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    The sequence of this isoform differs from the canonical sequence as follows:
         73-107: Missing.

    Show »
    Length:323
    Mass (Da):36,775
    Checksum:iEA0D7B96FB88CC01
    GO
    Isoform 3 (identifier: Q15257-3) [UniParc]FASTAAdd to Basket

    Also known as: Delta

    The sequence of this isoform differs from the canonical sequence as follows:
         45-108: Missing.

    Show »
    Length:294
    Mass (Da):33,467
    Checksum:i12C8B0D3D96A490B
    GO
    Isoform 4 (identifier: Q15257-4) [UniParc]FASTAAdd to Basket

    Also known as: Epsilon

    The sequence of this isoform differs from the canonical sequence as follows:
         73-149: Missing.

    Show »
    Length:281
    Mass (Da):31,859
    Checksum:i9C554DF39A3436B1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti113 – 1131V → L in CAA51873. (PubMed:8195217)Curated
    Sequence conflicti113 – 1131V → L in CAA60163. (PubMed:8530035)Curated
    Sequence conflicti113 – 1131V → L in CAB77601. (PubMed:10880964)Curated
    Sequence conflicti113 – 1131V → L in CAB77602. (PubMed:10880964)Curated
    Sequence conflicti297 – 2971Missing in CAA60163. (PubMed:8530035)Curated
    Sequence conflicti297 – 2971Missing in CAB77601. (PubMed:10880964)Curated
    Sequence conflicti297 – 2971Missing in CAB77602. (PubMed:10880964)Curated
    Sequence conflicti297 – 2971Missing in CAB77603. (PubMed:10880964)Curated
    Sequence conflicti357 – 3571S → V AA sequence (PubMed:8195217)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti28 – 281K → R.
    Corresponds to variant rs17481693 [ dbSNP | Ensembl ].
    VAR_028101
    Natural varianti208 – 2081R → Q.
    Corresponds to variant rs4836639 [ dbSNP | Ensembl ].
    VAR_028102
    Natural varianti357 – 3571S → L.1 Publication
    Corresponds to variant rs2480452 [ dbSNP | Ensembl ].
    VAR_028103

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei45 – 10864Missing in isoform 3. 1 PublicationVSP_005122Add
    BLAST
    Alternative sequencei73 – 14977Missing in isoform 4. CuratedVSP_005124Add
    BLAST
    Alternative sequencei73 – 10735Missing in isoform 1. 4 PublicationsVSP_005123Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X73478 mRNA. Translation: CAA51873.1.
    X86428
    , X86429, X86430, X86432, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAA60163.1.
    X86428
    , X86429, X86430, X86431, X86432, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAB77601.1.
    X86428
    , X86429, X86432, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAB77602.1.
    X86428
    , X86429, X86430, X86434, X86435, X86436, X86437, X86438, X86439 Genomic DNA. Translation: CAB77603.1.
    AK302043 mRNA. Translation: BAG63436.1.
    BT020119 mRNA. Translation: AAV38922.1.
    AK222788 mRNA. Translation: BAD96508.1.
    AL158151 Genomic DNA. Translation: CAM14695.1.
    AL158151 Genomic DNA. Translation: CAP58847.2.
    CH471090 Genomic DNA. Translation: EAW87876.1.
    CH471090 Genomic DNA. Translation: EAW87882.1.
    BC002545 mRNA. Translation: AAH02545.1.
    BC011605 mRNA. Translation: AAH11605.1.
    CCDSiCCDS65156.1. [Q15257-3]
    CCDS6920.1. [Q15257-2]
    PIRiA54021.
    RefSeqiNP_001180326.1. NM_001193397.1.
    NP_001258761.1. NM_001271832.1. [Q15257-3]
    NP_066954.2. NM_021131.4. [Q15257-2]
    NP_821067.1. NM_178000.2. [Q15257-2]
    NP_821068.1. NM_178001.2. [Q15257-1]
    NP_821070.1. NM_178003.2. [Q15257-4]
    UniGeneiHs.400740.

    Genome annotation databases

    EnsembliENST00000337738; ENSP00000337448; ENSG00000119383. [Q15257-1]
    ENST00000355007; ENSP00000347109; ENSG00000119383. [Q15257-4]
    ENST00000357197; ENSP00000349726; ENSG00000119383. [Q15257-3]
    ENST00000358994; ENSP00000351885; ENSG00000119383. [Q15257-2]
    ENST00000393370; ENSP00000377036; ENSG00000119383. [Q15257-2]
    GeneIDi5524.
    KEGGihsa:5524.
    UCSCiuc004bxl.2. human. [Q15257-2]
    uc004bxm.2. human. [Q15257-1]
    uc004bxo.2. human. [Q15257-4]
    uc011mbp.2. human. [Q15257-3]

    Polymorphism databases

    DMDMi116242737.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X73478 mRNA. Translation: CAA51873.1 .
    X86428
    , X86429 , X86430 , X86432 , X86434 , X86435 , X86436 , X86437 , X86438 , X86439 Genomic DNA. Translation: CAA60163.1 .
    X86428
    , X86429 , X86430 , X86431 , X86432 , X86434 , X86435 , X86436 , X86437 , X86438 , X86439 Genomic DNA. Translation: CAB77601.1 .
    X86428
    , X86429 , X86432 , X86434 , X86435 , X86436 , X86437 , X86438 , X86439 Genomic DNA. Translation: CAB77602.1 .
    X86428
    , X86429 , X86430 , X86434 , X86435 , X86436 , X86437 , X86438 , X86439 Genomic DNA. Translation: CAB77603.1 .
    AK302043 mRNA. Translation: BAG63436.1 .
    BT020119 mRNA. Translation: AAV38922.1 .
    AK222788 mRNA. Translation: BAD96508.1 .
    AL158151 Genomic DNA. Translation: CAM14695.1 .
    AL158151 Genomic DNA. Translation: CAP58847.2 .
    CH471090 Genomic DNA. Translation: EAW87876.1 .
    CH471090 Genomic DNA. Translation: EAW87882.1 .
    BC002545 mRNA. Translation: AAH02545.1 .
    BC011605 mRNA. Translation: AAH11605.1 .
    CCDSi CCDS65156.1. [Q15257-3 ]
    CCDS6920.1. [Q15257-2 ]
    PIRi A54021.
    RefSeqi NP_001180326.1. NM_001193397.1.
    NP_001258761.1. NM_001271832.1. [Q15257-3 ]
    NP_066954.2. NM_021131.4. [Q15257-2 ]
    NP_821067.1. NM_178000.2. [Q15257-2 ]
    NP_821068.1. NM_178001.2. [Q15257-1 ]
    NP_821070.1. NM_178003.2. [Q15257-4 ]
    UniGenei Hs.400740.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2G62 X-ray 1.60 A 22-358 [» ]
    2HV6 X-ray 1.90 A/B 1-358 [» ]
    2HV7 X-ray 2.50 A/B/C/D/E/F/G/H 1-358 [» ]
    2IXM X-ray 1.50 A 20-357 [» ]
    4LAC X-ray 2.82 B 19-358 [» ]
    ProteinModelPortali Q15257.
    SMRi Q15257. Positions 23-357.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111516. 54 interactions.
    IntActi Q15257. 10 interactions.
    MINTi MINT-3031079.

    Chemistry

    BindingDBi Q15257.
    ChEMBLi CHEMBL2505.

    PTM databases

    PhosphoSitei Q15257.

    Polymorphism databases

    DMDMi 116242737.

    2D gel databases

    OGPi Q15257.

    Proteomic databases

    MaxQBi Q15257.
    PaxDbi Q15257.
    PRIDEi Q15257.

    Protocols and materials databases

    DNASUi 5524.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337738 ; ENSP00000337448 ; ENSG00000119383 . [Q15257-1 ]
    ENST00000355007 ; ENSP00000347109 ; ENSG00000119383 . [Q15257-4 ]
    ENST00000357197 ; ENSP00000349726 ; ENSG00000119383 . [Q15257-3 ]
    ENST00000358994 ; ENSP00000351885 ; ENSG00000119383 . [Q15257-2 ]
    ENST00000393370 ; ENSP00000377036 ; ENSG00000119383 . [Q15257-2 ]
    GeneIDi 5524.
    KEGGi hsa:5524.
    UCSCi uc004bxl.2. human. [Q15257-2 ]
    uc004bxm.2. human. [Q15257-1 ]
    uc004bxo.2. human. [Q15257-4 ]
    uc011mbp.2. human. [Q15257-3 ]

    Organism-specific databases

    CTDi 5524.
    GeneCardsi GC09P131873.
    HGNCi HGNC:9308. PPP2R4.
    HPAi CAB022068.
    CAB035999.
    HPA005695.
    MIMi 600756. gene.
    neXtProti NX_Q15257.
    PharmGKBi PA33671.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5057.
    HOVERGENi HBG019168.
    KOi K17605.
    OrthoDBi EOG7KQ21W.
    PhylomeDBi Q15257.
    TreeFami TF105555.

    Miscellaneous databases

    ChiTaRSi PPP2R4. human.
    EvolutionaryTracei Q15257.
    GeneWikii PPP2R4.
    GenomeRNAii 5524.
    NextBioi 21382.
    PROi Q15257.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15257.
    Bgeei Q15257.
    CleanExi HS_PPP2R4.
    Genevestigatori Q15257.

    Family and domain databases

    InterProi IPR004327. Phstyr_phstse_ac.
    [Graphical view ]
    PANTHERi PTHR10012. PTHR10012. 1 hit.
    Pfami PF03095. PTPA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016325. Phstyr_phstse_ac. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, expression, and characterization of PTPA, a protein that activates the tyrosyl phosphatase activity of protein phosphatase 2A."
      Cayla X., Van Hoof C., Bosch M., Waelkens E., Peeters B., Merlevede W., Goris J.
      J. Biol. Chem. 269:15668-15675(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
      Tissue: Heart.
    2. "Structure and chromosomal localization of the human gene of the phosphotyrosyl phosphatase activator (PTPA) of protein phosphatase 2A."
      Van Hoof C., Aly M., Garcia A., Cayla X., Cassiman J.-J., Merlevede W., Goris J.
      Genomics 28:261-272(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
      Tissue: Blood.
    3. "Identification and characterization of alternative splice products encoded by the human phosphotyrosyl phosphatase activator gene."
      Janssens V., van Hoof C., Martens E., de Baere I., Merlevede W., Goris J.
      Eur. J. Biochem. 267:4406-4413(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2; 3 AND 4).
    4. "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 3).
      Tissue: Testis.
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-357.
      Tissue: Liver.
    7. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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 1).
      Tissue: Placenta.
    10. "Overexpression of the cis/trans isomerase PTPA triggers caspase 3-dependent apoptosis."
      Azam S., Drobetsky E., Ramotar D.
      Apoptosis 12:1243-1255(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APOPTOSIS, SUBCELLULAR LOCATION.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "The crystal structure of a human PP2A phosphatase activator reveals a novel fold and highly conserved cleft implicated in protein-protein interactions."
      Magnusdottir A., Stenmark P., Flodin S., Nyman T., Hammarstroem M., Ehn M., Bakali H M.A., Berglund H., Nordlund P.
      J. Biol. Chem. 281:22434-22438(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 22-358.
    15. "Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity."
      Leulliot N., Vicentini G., Jordens J., Quevillon-Cheruel S., Schiltz M., Barford D., van Tilbeurgh H., Goris J.
      Mol. Cell 23:413-424(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 20-357.
    16. "Structure and mechanism of the phosphotyrosyl phosphatase activator."
      Chao Y., Xing Y., Chen Y., Xu Y., Lin Z., Li Z., Jeffrey P.D., Stock J.B., Shi Y.
      Mol. Cell 23:535-546(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), FUNCTION IN MODULATION OF PP2A SUBSTRATE SPECIFICITY, ATP-BINDING, MUTAGENESIS OF ASP-185; ALA-239; GLY-240; VAL-244; GLU-305; GLY-325; MET-329 AND LYS-337, INTERACTION WITH THE PP2A(D) COMPLEX.

    Entry informationi

    Entry nameiPTPA_HUMAN
    AccessioniPrimary (citable) accession number: Q15257
    Secondary accession number(s): A2A347
    , A9IZU4, B4DXM4, Q15258, Q53GZ3, Q5TZQ2, Q9BUK1, Q9NNZ7, Q9NNZ8, Q9NNZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 128 of the entry and version 3 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3