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P35813

- PPM1A_HUMAN

UniProt

P35813 - PPM1A_HUMAN

Protein

Protein phosphatase 1A

Gene

PPM1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Enzyme with a broad specificity. Negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling. Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB.2 Publications

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Cofactori

    Binds 2 magnesium or manganese ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi60 – 601Manganese 1
    Metal bindingi60 – 601Manganese 2
    Metal bindingi61 – 611Manganese 1; via carbonyl oxygen
    Metal bindingi239 – 2391Manganese 2
    Metal bindingi282 – 2821Manganese 2

    GO - Molecular functioni

    1. calmodulin-dependent protein phosphatase activity Source: UniProtKB
    2. magnesium ion binding Source: InterPro
    3. manganese ion binding Source: InterPro
    4. protein binding Source: UniProtKB
    5. protein serine/threonine phosphatase activity Source: UniProtKB
    6. R-SMAD binding Source: UniProtKB
    7. signal transducer activity Source: UniProtKB

    GO - Biological processi

    1. cell cycle arrest Source: Reactome
    2. dephosphorylation Source: BHF-UCL
    3. gene expression Source: Reactome
    4. insulin receptor signaling pathway Source: Reactome
    5. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    6. negative regulation of NF-kappaB import into nucleus Source: UniProtKB
    7. negative regulation of SMAD protein complex assembly Source: UniProtKB
    8. negative regulation of transcription from RNA polymerase II promoter Source: Reactome
    9. negative regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
    10. N-terminal protein myristoylation Source: UniProtKB
    11. peptidyl-threonine dephosphorylation Source: UniProtKB
    12. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    13. positive regulation of transcription, DNA-templated Source: BHF-UCL
    14. positive regulation of Wnt signaling pathway Source: BHF-UCL
    15. protein dephosphorylation Source: UniProtKB
    16. transcription, DNA-templated Source: Reactome
    17. transcription initiation from RNA polymerase II promoter Source: Reactome
    18. transforming growth factor beta receptor signaling pathway Source: Reactome
    19. Wnt signaling pathway Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_21285. Regulation of AMPK activity via LKB1.
    SignaLinkiP35813.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein phosphatase 1A (EC:3.1.3.16)
    Alternative name(s):
    Protein phosphatase 2C isoform alpha
    Short name:
    PP2C-alpha
    Protein phosphatase IA
    Gene namesi
    Name:PPM1A
    Synonyms:PPPM1A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:9275. PPM1A.

    Subcellular locationi

    Nucleus. Cytoplasmcytosol. Membrane By similarity
    Note: Weakly associates at the membrane and N-myristoylation mediates the membrane localization.By similarity

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB
    3. neuron projection Source: Ensembl
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB
    6. voltage-gated calcium channel complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi239 – 2391D → N: No effect on binding SMAD2. 1 Publication

    Organism-specific databases

    PharmGKBiPA33603.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 382381Protein phosphatase 1APRO_0000057741Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Modified residuei375 – 3751Phosphoserine1 Publication

    Post-translational modificationi

    N-myristoylation is essential for the recognition of its substrates for dephosphorylation.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein

    Proteomic databases

    MaxQBiP35813.
    PaxDbiP35813.
    PeptideAtlasiP35813.
    PRIDEiP35813.

    PTM databases

    PhosphoSiteiP35813.

    Expressioni

    Gene expression databases

    ArrayExpressiP35813.
    BgeeiP35813.
    CleanExiHS_PPM1A.
    GenevestigatoriP35813.

    Organism-specific databases

    HPAiHPA029209.

    Interactioni

    Subunit structurei

    Monomer. Interacts with SMAD2; the interaction dephosphorylates SMAD2 in its C-terminal SXS motif resulting in disruption of the SMAD2/SMAD4 complex, SMAD2 nuclear export and termination of the TGF-beta-mediated signaling. Interacts with SMAD2; the interaction dephosphorylates SMAD2 in its C-terminal SXS motif resulting in disruption of the SMAD2/SMAD4 complex, SMAD2 nuclear export and termination of the TGF-beta-mediated signaling. Interacts with the phosphorylated form of IKBKB/IKKB.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARRB1P494074EBI-989143,EBI-743313
    ARRB2P321213EBI-989143,EBI-714559
    AXIN1O151692EBI-989143,EBI-710484
    MAPK1P2848219EBI-989143,EBI-959949
    MAPK14Q165392EBI-989143,EBI-73946
    RANBP3Q9H6Z44EBI-989143,EBI-992681
    SMAD2Q157962EBI-989143,EBI-1040141

    Protein-protein interaction databases

    BioGridi111489. 12 interactions.
    IntActiP35813. 23 interactions.
    MINTiMINT-2802996.
    STRINGi9606.ENSP00000327255.

    Structurei

    Secondary structure

    1
    382
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 1911
    Beta strandi22 – 3110
    Beta strandi33 – 353
    Beta strandi38 – 469
    Turni47 – 493
    Beta strandi50 – 6314
    Helixi66 – 8015
    Helixi83 – 864
    Beta strandi88 – 914
    Helixi94 – 11825
    Beta strandi129 – 1346
    Beta strandi136 – 14611
    Beta strandi148 – 1536
    Beta strandi156 – 1605
    Helixi169 – 1779
    Turni188 – 1903
    Helixi200 – 2023
    Helixi210 – 2123
    Beta strandi213 – 2164
    Beta strandi220 – 2256
    Turni228 – 2303
    Beta strandi231 – 2377
    Helixi239 – 2424
    Helixi247 – 25812
    Helixi264 – 27714
    Beta strandi284 – 2907
    Helixi299 – 31921
    Helixi330 – 33910
    Turni347 – 3493
    Helixi350 – 3545
    Helixi355 – 36511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A6QX-ray2.00A1-382[»]
    3FXJX-ray2.50A1-382[»]
    3FXKX-ray2.10A1-382[»]
    3FXLX-ray2.30A1-382[»]
    3FXMX-ray2.50A1-382[»]
    3FXOX-ray2.50A1-382[»]
    ProteinModelPortaliP35813.
    SMRiP35813. Positions 2-368.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35813.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PP2C family.Curated

    Phylogenomic databases

    eggNOGiCOG0631.
    HOGENOMiHOG000233895.
    HOVERGENiHBG053647.
    InParanoidiP35813.
    KOiK04457.
    OMAiEVYAIER.
    OrthoDBiEOG7WMCJH.
    PhylomeDBiP35813.
    TreeFamiTF313590.

    Family and domain databases

    Gene3Di1.10.10.430. 1 hit.
    3.60.40.10. 1 hit.
    InterProiIPR001932. PP2C-like_dom.
    IPR012911. PP2C_C.
    IPR000222. PP2C_Mn2_Asp60_BS.
    IPR015655. Protein_Pase_2C.
    [Graphical view]
    PANTHERiPTHR13832. PTHR13832. 1 hit.
    PfamiPF00481. PP2C. 1 hit.
    PF07830. PP2C_C. 1 hit.
    [Graphical view]
    SMARTiSM00331. PP2C_SIG. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view]
    SUPFAMiSSF81601. SSF81601. 1 hit.
    SSF81606. SSF81606. 1 hit.
    PROSITEiPS01032. PP2C. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Alpha-1 (identifier: P35813-1) [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

    MGAFLDKPKM EKHNAQGQGN GLRYGLSSMQ GWRVEMEDAH TAVIGLPSGL    50
    ESWSFFAVYD GHAGSQVAKY CCEHLLDHIT NNQDFKGSAG APSVENVKNG 100
    IRTGFLEIDE HMRVMSEKKH GADRSGSTAV GVLISPQHTY FINCGDSRGL 150
    LCRNRKVHFF TQDHKPSNPL EKERIQNAGG SVMIQRVNGS LAVSRALGDF 200
    DYKCVHGKGP TEQLVSPEPE VHDIERSEED DQFIILACDG IWDVMGNEEL 250
    CDFVRSRLEV TDDLEKVCNE VVDTCLYKGS RDNMSVILIC FPNAPKVSPE 300
    AVKKEAELDK YLECRVEEII KKQGEGVPDL VHVMRTLASE NIPSLPPGGE 350
    LASKRNVIEA VYNRLNPYKN DDTDSTSTDD MW 382
    Length:382
    Mass (Da):42,448
    Last modified:June 1, 1994 - v1
    Checksum:iD48EF508B4A76687
    GO
    Isoform Alpha-2 (identifier: P35813-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         318-324: EIIKKQG → GGSFNKK
         325-382: Missing.

    Show »
    Length:324
    Mass (Da):35,958
    Checksum:iED58E203BB26CE00
    GO
    Isoform 3 (identifier: P35813-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MFCSGRKWVAEATICTKLMKREKRRMGKRRAKKAKREEKKKGGERRRNEKRGNQMKRMCERKKYETDLEDQDIM

    Note: No experimental confirmation available.Curated

    Show »
    Length:455
    Mass (Da):51,366
    Checksum:iCBC6E3F350D6FDBD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti342 – 3421I → T in AK097843. (PubMed:14702039)Curated
    Isoform 3 (identifier: P35813-3)
    Sequence conflicti54 – 541Q → R in AK097843. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MFCSGRKWVAEATICTKLMK REKRRMGKRRAKKAKREEKK KGGERRRNEKRGNQMKRMCE RKKYETDLEDQDIM in isoform 3. 1 PublicationVSP_045687
    Alternative sequencei318 – 3247EIIKKQG → GGSFNKK in isoform Alpha-2. 1 PublicationVSP_005085
    Alternative sequencei325 – 38258Missing in isoform Alpha-2. 1 PublicationVSP_005086Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S87759 mRNA. Translation: AAB21784.1.
    AF070670 mRNA. Translation: AAC28354.1.
    AK097843 mRNA. No translation available.
    AB451247 mRNA. Translation: BAG70061.1.
    AL132778 Genomic DNA. No translation available.
    AL157756 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW80774.1.
    BC026691 mRNA. Translation: AAH26691.1.
    BC063243 mRNA. Translation: AAH63243.1.
    CCDSiCCDS45120.1. [P35813-3]
    CCDS9744.1. [P35813-1]
    CCDS9745.1. [P35813-2]
    PIRiS22423.
    RefSeqiNP_066283.1. NM_021003.4. [P35813-1]
    NP_808820.1. NM_177951.2. [P35813-2]
    NP_808821.2. NM_177952.2. [P35813-3]
    XP_005267834.1. XM_005267777.1. [P35813-1]
    XP_005267835.1. XM_005267778.1. [P35813-1]
    XP_005267836.1. XM_005267779.1. [P35813-1]
    XP_005267837.1. XM_005267780.1. [P35813-1]
    XP_005267838.1. XM_005267781.1. [P35813-1]
    XP_006720242.1. XM_006720179.1. [P35813-1]
    XP_006720243.1. XM_006720180.1. [P35813-1]
    UniGeneiHs.130036.

    Genome annotation databases

    EnsembliENST00000325642; ENSP00000327255; ENSG00000100614. [P35813-3]
    ENST00000325658; ENSP00000314850; ENSG00000100614. [P35813-2]
    ENST00000395076; ENSP00000378514; ENSG00000100614. [P35813-1]
    GeneIDi5494.
    KEGGihsa:5494.
    UCSCiuc001xex.4. human. [P35813-2]
    uc001xey.4. human. [P35813-1]

    Polymorphism databases

    DMDMi548442.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S87759 mRNA. Translation: AAB21784.1 .
    AF070670 mRNA. Translation: AAC28354.1 .
    AK097843 mRNA. No translation available.
    AB451247 mRNA. Translation: BAG70061.1 .
    AL132778 Genomic DNA. No translation available.
    AL157756 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW80774.1 .
    BC026691 mRNA. Translation: AAH26691.1 .
    BC063243 mRNA. Translation: AAH63243.1 .
    CCDSi CCDS45120.1. [P35813-3 ]
    CCDS9744.1. [P35813-1 ]
    CCDS9745.1. [P35813-2 ]
    PIRi S22423.
    RefSeqi NP_066283.1. NM_021003.4. [P35813-1 ]
    NP_808820.1. NM_177951.2. [P35813-2 ]
    NP_808821.2. NM_177952.2. [P35813-3 ]
    XP_005267834.1. XM_005267777.1. [P35813-1 ]
    XP_005267835.1. XM_005267778.1. [P35813-1 ]
    XP_005267836.1. XM_005267779.1. [P35813-1 ]
    XP_005267837.1. XM_005267780.1. [P35813-1 ]
    XP_005267838.1. XM_005267781.1. [P35813-1 ]
    XP_006720242.1. XM_006720179.1. [P35813-1 ]
    XP_006720243.1. XM_006720180.1. [P35813-1 ]
    UniGenei Hs.130036.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A6Q X-ray 2.00 A 1-382 [» ]
    3FXJ X-ray 2.50 A 1-382 [» ]
    3FXK X-ray 2.10 A 1-382 [» ]
    3FXL X-ray 2.30 A 1-382 [» ]
    3FXM X-ray 2.50 A 1-382 [» ]
    3FXO X-ray 2.50 A 1-382 [» ]
    ProteinModelPortali P35813.
    SMRi P35813. Positions 2-368.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111489. 12 interactions.
    IntActi P35813. 23 interactions.
    MINTi MINT-2802996.
    STRINGi 9606.ENSP00000327255.

    Chemistry

    BindingDBi P35813.
    ChEMBLi CHEMBL2437.

    PTM databases

    PhosphoSitei P35813.

    Polymorphism databases

    DMDMi 548442.

    Proteomic databases

    MaxQBi P35813.
    PaxDbi P35813.
    PeptideAtlasi P35813.
    PRIDEi P35813.

    Protocols and materials databases

    DNASUi 5494.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000325642 ; ENSP00000327255 ; ENSG00000100614 . [P35813-3 ]
    ENST00000325658 ; ENSP00000314850 ; ENSG00000100614 . [P35813-2 ]
    ENST00000395076 ; ENSP00000378514 ; ENSG00000100614 . [P35813-1 ]
    GeneIDi 5494.
    KEGGi hsa:5494.
    UCSCi uc001xex.4. human. [P35813-2 ]
    uc001xey.4. human. [P35813-1 ]

    Organism-specific databases

    CTDi 5494.
    GeneCardsi GC14P060712.
    HGNCi HGNC:9275. PPM1A.
    HPAi HPA029209.
    MIMi 606108. gene.
    neXtProti NX_P35813.
    PharmGKBi PA33603.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0631.
    HOGENOMi HOG000233895.
    HOVERGENi HBG053647.
    InParanoidi P35813.
    KOi K04457.
    OMAi EVYAIER.
    OrthoDBi EOG7WMCJH.
    PhylomeDBi P35813.
    TreeFami TF313590.

    Enzyme and pathway databases

    Reactomei REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_21285. Regulation of AMPK activity via LKB1.
    SignaLinki P35813.

    Miscellaneous databases

    ChiTaRSi PPM1A. human.
    EvolutionaryTracei P35813.
    GeneWikii PPM1A.
    GenomeRNAii 5494.
    NextBioi 21242.
    PROi P35813.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35813.
    Bgeei P35813.
    CleanExi HS_PPM1A.
    Genevestigatori P35813.

    Family and domain databases

    Gene3Di 1.10.10.430. 1 hit.
    3.60.40.10. 1 hit.
    InterProi IPR001932. PP2C-like_dom.
    IPR012911. PP2C_C.
    IPR000222. PP2C_Mn2_Asp60_BS.
    IPR015655. Protein_Pase_2C.
    [Graphical view ]
    PANTHERi PTHR13832. PTHR13832. 1 hit.
    Pfami PF00481. PP2C. 1 hit.
    PF07830. PP2C_C. 1 hit.
    [Graphical view ]
    SMARTi SM00331. PP2C_SIG. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81601. SSF81601. 1 hit.
    SSF81606. SSF81606. 1 hit.
    PROSITEi PS01032. PP2C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mammalian protein serine/threonine phosphatase 2C: cDNA cloning and comparative analysis of amino acid sequences."
      Mann D.J., Campbell D.G., McGowan C.H., Cohen P.T.W.
      Biochim. Biophys. Acta 1130:100-104(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
    2. "Protein phosphatase 2Calpha inhibits the human stress-responsive p38 and JNK MAPK pathways."
      Takekawa M., Maeda T., Saito H.
      EMBO J. 17:4744-4752(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-2).
    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 3).
      Tissue: Testis.
    4. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-1).
    5. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 ALPHA-1).
      Tissue: Colon and Lung.
    8. Cited for: INTERACTION WITH SMAD2 AND SMAD3, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-239.
    9. "PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation."
      Sun W., Yu Y., Dotti G., Shen T., Tan X., Savoldo B., Pass A.K., Chu M., Zhang D., Lu X., Fu S., Lin X., Yang J.
      Cell. Signal. 21:95-102(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IKBKB.
    10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system."
      Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T.
      Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor-? pathway."
      Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.
      Cell. Signal. 24:1999-2006(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "Crystal structure of the protein serine/threonine phosphatase 2C at 2.0-A resolution."
      Das A.K., Helps N.R., Cohen P.T.W., Barford D.
      EMBO J. 15:6798-6809(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

    Entry informationi

    Entry nameiPPM1A_HUMAN
    AccessioniPrimary (citable) accession number: P35813
    Secondary accession number(s): B5BU11, J3KNM0, O75551
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 153 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3