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O75688

- PPM1B_HUMAN

UniProt

O75688 - PPM1B_HUMAN

Protein

Protein phosphatase 1B

Gene

PPM1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-172'. 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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi60 – 601Manganese 1By similarity
    Metal bindingi60 – 601Manganese 2By similarity
    Metal bindingi61 – 611Manganese 1; via carbonyl oxygenBy similarity
    Metal bindingi243 – 2431Manganese 2By similarity
    Metal bindingi286 – 2861Manganese 2By similarity

    GO - Molecular functioni

    1. magnesium ion binding Source: InterPro
    2. manganese ion binding Source: InterPro
    3. protein binding Source: UniProtKB
    4. protein serine/threonine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: Reactome
    2. negative regulation of defense response to virus Source: UniProtKB
    3. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    4. negative regulation of interferon-beta production Source: UniProtKB
    5. negative regulation of NF-kappaB import into nucleus Source: UniProtKB
    6. N-terminal protein myristoylation Source: UniProtKB
    7. peptidyl-threonine dephosphorylation Source: UniProtKB
    8. protein dephosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein phosphatase 1B (EC:3.1.3.16)
    Alternative name(s):
    Protein phosphatase 2C isoform beta
    Short name:
    PP2C-beta
    Gene namesi
    Name:PPM1B
    Synonyms:PP2CB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:9276. PPM1B.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. 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

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti163693. 2p21 microdeletion syndrome.
    PharmGKBiPA33604.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 479478Protein phosphatase 1BPRO_0000057746Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Cross-linki12 – 12Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)
    Cross-linki142 – 142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)

    Post-translational modificationi

    Isgylation negatively regulates its activity.1 Publication
    N-myristoylation is essential for the recognition of its substrates for dephosphorylation.By similarity

    Keywords - PTMi

    Isopeptide bond, Lipoprotein, Myristate, Ubl conjugation

    Proteomic databases

    MaxQBiO75688.
    PaxDbiO75688.
    PRIDEiO75688.

    PTM databases

    PhosphoSiteiO75688.

    Expressioni

    Tissue specificityi

    Highly expressed in heart and skeletal muscle.

    Gene expression databases

    ArrayExpressiO75688.
    BgeeiO75688.
    CleanExiHS_PPM1B.
    GenevestigatoriO75688.

    Organism-specific databases

    HPAiHPA016745.

    Interactioni

    Subunit structurei

    Monomer By similarity. Interacts with PAK6. Interacts with the phosphorylated form of IKBKB/IKKB.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARRB1P494074EBI-1047039,EBI-743313
    ARRB2P321214EBI-1047039,EBI-714559
    ISG15P051612EBI-1047039,EBI-746466

    Protein-protein interaction databases

    BioGridi111490. 35 interactions.
    IntActiO75688. 12 interactions.
    MINTiMINT-2841839.
    STRINGi9606.ENSP00000282412.

    Structurei

    Secondary structure

    1
    479
    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
    Turni83 – 853
    Helixi99 – 11820
    Turni121 – 1233
    Beta strandi134 – 1396
    Beta strandi141 – 15111
    Beta strandi153 – 1586
    Beta strandi161 – 1655
    Helixi174 – 1829
    Turni193 – 1953
    Helixi205 – 2073
    Helixi215 – 2173
    Beta strandi218 – 2214
    Beta strandi225 – 2306
    Beta strandi235 – 2417
    Helixi243 – 2464
    Helixi251 – 26212
    Helixi268 – 28114
    Beta strandi288 – 2947

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2P8EX-ray1.82A/B2-297[»]
    ProteinModelPortaliO75688.
    SMRiO75688. Positions 4-295.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75688.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PP2C family.Curated

    Phylogenomic databases

    eggNOGiCOG0631.
    HOGENOMiHOG000233895.
    HOVERGENiHBG053647.
    InParanoidiO75688.
    KOiK04461.
    OMAiVMISPEH.
    PhylomeDBiO75688.
    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 (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. Align

    Note: Additional isoforms seem to exist.

    Isoform Beta-1 (identifier: O75688-1) [UniParc]FASTAAdd to Basket

    Also known as: Beta-X, PPM1B2

    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

    MGAFLDKPKT EKHNAHGAGN GLRYGLSSMQ GWRVEMEDAH TAVVGIPHGL    50
    EDWSFFAVYD GHAGSRVANY CSTHLLEHIT TNEDFRAAGK SGSALELSVE 100
    NVKNGIRTGF LKIDEYMRNF SDLRNGMDRS GSTAVGVMIS PKHIYFINCG 150
    DSRAVLYRNG QVCFSTQDHK PCNPREKERI QNAGGSVMIQ RVNGSLAVSR 200
    ALGDYDYKCV DGKGPTEQLV SPEPEVYEIL RAEEDEFIIL ACDGIWDVMS 250
    NEELCEYVKS RLEVSDDLEN VCNWVVDTCL HKGSRDNMSI VLVCFSNAPK 300
    VSDEAVKKDS ELDKHLESRV EEIMEKSGEE GMPDLAHVMR ILSAENIPNL 350
    PPGGGLAGKR NVIEAVYSRL NPHRESDGAS DEAEESGSQG KLVEALRQMR 400
    INHRGNYRQL LEEMLTSYRL AKVEGEESPA EPAATATSSN SDAGNPVTMQ 450
    ESHTESESGL AELDSSNEDA GTKMSGEKI 479
    Length:479
    Mass (Da):52,643
    Last modified:November 1, 1998 - v1
    Checksum:iA3A5797AD263DFBD
    GO
    Isoform Beta-2 (identifier: O75688-2) [UniParc]FASTAAdd to Basket

    Also known as: PPM1B1

    The sequence of this isoform differs from the canonical sequence as follows:
         379-387: ASDEAEESG → GAGDLEDPW
         388-479: Missing.

    Show »
    Length:387
    Mass (Da):42,771
    Checksum:i56A644A4E5E2B12B
    GO
    Isoform Beta-X (identifier: O75688-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-287: Missing.

    Show »
    Length:193
    Mass (Da):20,884
    Checksum:iE655DD15842CA329
    GO
    Isoform 4 (identifier: O75688-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         379-380: AS → QK
         381-387: Missing.
         388-479: Missing.

    Show »
    Length:380
    Mass (Da):42,086
    Checksum:iE5C00B5FF4278013
    GO
    Isoform 5 (identifier: O75688-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         322-327: EIMEKS → GKTNAF
         328-380: Missing.
         381-387: Missing.
         388-479: Missing.

    Show »
    Length:327
    Mass (Da):36,313
    Checksum:iE38A263FCF7F1692
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 287286Missing in isoform Beta-X. 1 PublicationVSP_041085Add
    BLAST
    Alternative sequencei322 – 3276EIMEKS → GKTNAF in isoform 5. 1 PublicationVSP_043641
    Alternative sequencei328 – 38053Missing in isoform 5. 1 PublicationVSP_043642Add
    BLAST
    Alternative sequencei379 – 3879ASDEAEESG → GAGDLEDPW in isoform Beta-2. 4 PublicationsVSP_005087
    Alternative sequencei379 – 3802AS → QK in isoform 4. 1 PublicationVSP_043643
    Alternative sequencei381 – 3877Missing in isoform 4 and isoform 5. 1 PublicationVSP_043644
    Alternative sequencei388 – 47992Missing in isoform Beta-2, isoform 4 and isoform 5. 4 PublicationsVSP_005088Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ005801 mRNA. Translation: CAA06704.1.
    AF294792 mRNA. Translation: AAG02232.1.
    AJ271832 mRNA. Translation: CAC27992.1.
    AJ271835 mRNA. Translation: CAC27993.1.
    DQ023508 mRNA. Translation: AAY89639.1.
    DQ023509 mRNA. Translation: AAY89640.1.
    DQ023510 mRNA. Translation: AAY89641.1.
    AF136972 mRNA. Translation: AAG49433.1.
    AL833035 mRNA. Translation: CAH56319.1.
    AC013717 Genomic DNA. Translation: AAX88954.1.
    AC019129 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAX00282.1.
    CH471053 Genomic DNA. Translation: EAX00283.1.
    BC012002 mRNA. Translation: AAH12002.1.
    BC064381 mRNA. Translation: AAH64381.1.
    CCDSiCCDS1816.1. [O75688-2]
    CCDS1817.1. [O75688-1]
    CCDS46271.1. [O75688-4]
    CCDS46272.1. [O75688-5]
    RefSeqiNP_001028728.1. NM_001033556.1. [O75688-5]
    NP_001028729.1. NM_001033557.1. [O75688-4]
    NP_002697.1. NM_002706.4. [O75688-1]
    NP_808907.1. NM_177968.2. [O75688-2]
    NP_808908.1. NM_177969.2.
    UniGeneiHs.416769.

    Genome annotation databases

    EnsembliENST00000282412; ENSP00000282412; ENSG00000138032. [O75688-1]
    ENST00000345249; ENSP00000326089; ENSG00000138032. [O75688-3]
    ENST00000378551; ENSP00000367813; ENSG00000138032. [O75688-2]
    ENST00000409432; ENSP00000387287; ENSG00000138032. [O75688-4]
    GeneIDi5495.
    KEGGihsa:5495.
    UCSCiuc002rts.3. human. [O75688-5]
    uc002rtt.3. human. [O75688-1]
    uc002rtu.3. human. [O75688-4]
    uc002rtv.3. human. [O75688-3]
    uc002rtw.3. human. [O75688-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ005801 mRNA. Translation: CAA06704.1 .
    AF294792 mRNA. Translation: AAG02232.1 .
    AJ271832 mRNA. Translation: CAC27992.1 .
    AJ271835 mRNA. Translation: CAC27993.1 .
    DQ023508 mRNA. Translation: AAY89639.1 .
    DQ023509 mRNA. Translation: AAY89640.1 .
    DQ023510 mRNA. Translation: AAY89641.1 .
    AF136972 mRNA. Translation: AAG49433.1 .
    AL833035 mRNA. Translation: CAH56319.1 .
    AC013717 Genomic DNA. Translation: AAX88954.1 .
    AC019129 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAX00282.1 .
    CH471053 Genomic DNA. Translation: EAX00283.1 .
    BC012002 mRNA. Translation: AAH12002.1 .
    BC064381 mRNA. Translation: AAH64381.1 .
    CCDSi CCDS1816.1. [O75688-2 ]
    CCDS1817.1. [O75688-1 ]
    CCDS46271.1. [O75688-4 ]
    CCDS46272.1. [O75688-5 ]
    RefSeqi NP_001028728.1. NM_001033556.1. [O75688-5 ]
    NP_001028729.1. NM_001033557.1. [O75688-4 ]
    NP_002697.1. NM_002706.4. [O75688-1 ]
    NP_808907.1. NM_177968.2. [O75688-2 ]
    NP_808908.1. NM_177969.2.
    UniGenei Hs.416769.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2P8E X-ray 1.82 A/B 2-297 [» ]
    ProteinModelPortali O75688.
    SMRi O75688. Positions 4-295.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111490. 35 interactions.
    IntActi O75688. 12 interactions.
    MINTi MINT-2841839.
    STRINGi 9606.ENSP00000282412.

    Chemistry

    BindingDBi O75688.
    ChEMBLi CHEMBL2845.

    PTM databases

    PhosphoSitei O75688.

    Proteomic databases

    MaxQBi O75688.
    PaxDbi O75688.
    PRIDEi O75688.

    Protocols and materials databases

    DNASUi 5495.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000282412 ; ENSP00000282412 ; ENSG00000138032 . [O75688-1 ]
    ENST00000345249 ; ENSP00000326089 ; ENSG00000138032 . [O75688-3 ]
    ENST00000378551 ; ENSP00000367813 ; ENSG00000138032 . [O75688-2 ]
    ENST00000409432 ; ENSP00000387287 ; ENSG00000138032 . [O75688-4 ]
    GeneIDi 5495.
    KEGGi hsa:5495.
    UCSCi uc002rts.3. human. [O75688-5 ]
    uc002rtt.3. human. [O75688-1 ]
    uc002rtu.3. human. [O75688-4 ]
    uc002rtv.3. human. [O75688-3 ]
    uc002rtw.3. human. [O75688-2 ]

    Organism-specific databases

    CTDi 5495.
    GeneCardsi GC02P044307.
    HGNCi HGNC:9276. PPM1B.
    HPAi HPA016745.
    MIMi 603770. gene.
    neXtProti NX_O75688.
    Orphaneti 163693. 2p21 microdeletion syndrome.
    PharmGKBi PA33604.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0631.
    HOGENOMi HOG000233895.
    HOVERGENi HBG053647.
    InParanoidi O75688.
    KOi K04461.
    OMAi VMISPEH.
    PhylomeDBi O75688.
    TreeFami TF313590.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.

    Miscellaneous databases

    EvolutionaryTracei O75688.
    GeneWikii PPM1B.
    GenomeRNAii 5495.
    NextBioi 21250.
    PROi O75688.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75688.
    Bgeei O75688.
    CleanExi HS_PPM1B.
    Genevestigatori O75688.

    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. "The cloning expression and tissue distribution of human PP2Cbeta."
      Marely A.E., Kline A., Crabtree G., Sullivan J.E., Beri R.K.
      FEBS Lett. 431:121-124(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1).
      Tissue: Liver.
    2. "Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2Calpha and beta2 isoforms."
      Cheng A., Kaldis P., Solomon M.J.
      J. Biol. Chem. 275:34744-34749(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2).
    3. "Protein phosphatase 1B. Cloning and characterization of two major transcripts generated by alternative use of 3' exons."
      Seroussi E., Shani N., Hayut A., Faier S., Ben-Meir D., Divinski I., Smorodinsky N.I., Lavi S.
      Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-1 AND BETA-2).
    4. "The 2p21 deletion syndrome: characterization of the transcription content."
      Parvari R., Gonen Y., Alshafee I., Buriakovsky S., Regev K., Hershkovitz E.
      Genomics 86:195-211(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-2; 4 AND 5).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
      Tissue: Adrenal gland.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1).
      Tissue: Stomach.
    7. "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].
    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] (ISOFORMS BETA-1 AND BETA-X).
      Tissue: Brain and Urinary bladder.
    10. "Negative regulation of protein phosphatase 2Cbeta by ISG15 conjugation."
      Takeuchi T., Kobayashi T., Tamura S., Yokosawa H.
      FEBS Lett. 580:4521-4526(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISGYLATION AT LYS-12 AND LYS-142.
    11. "Increased PAK6 expression in prostate cancer and identification of PAK6 associated proteins."
      Kaur R., Yuan X., Lu M.L., Balk S.P.
      Prostate 68:1510-1516(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAK6.
    12. "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.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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.
    15. "PPM1B negatively regulates antiviral response via dephosphorylating TBK1."
      Zhao Y., Liang L., Fan Y., Sun S., An L., Shi Z., Cheng J., Jia W., Sun W., Mori-Akiyama Y., Zhang H., Fu S., Yang J.
      Cell. Signal. 24:2197-2204(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 2-297.

    Entry informationi

    Entry nameiPPM1B_HUMAN
    AccessioniPrimary (citable) accession number: O75688
    Secondary accession number(s): Q461Q2
    , Q4J6C1, Q4J6C2, Q658R4, Q96ER6, Q9HAY8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 152 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 2
      Human chromosome 2: 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