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P62140

- PP1B_HUMAN

UniProt

P62140 - PP1B_HUMAN

Protein

Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Gene

PPP1CB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E.2 Publications

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.
    [Myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate.

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Enzyme regulationi

    Inhibited by the toxins okadaic acid, tautomycin and microcystin Leu-Arg By similarity. The phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress.By similarity1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi63 – 631Manganese 1By similarity
    Metal bindingi65 – 651Manganese 1By similarity
    Metal bindingi91 – 911Manganese 1By similarity
    Metal bindingi91 – 911Manganese 2By similarity
    Metal bindingi123 – 1231Manganese 2By similarity
    Active sitei124 – 1241Proton donorBy similarity
    Metal bindingi172 – 1721Manganese 2By similarity
    Metal bindingi247 – 2471Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. myosin-light-chain-phosphatase activity Source: UniProtKB
    3. myosin phosphatase activity Source: UniProtKB
    4. phosphatase activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein kinase binding Source: UniProtKB

    GO - Biological processi

    1. cell division Source: UniProtKB-KW
    2. circadian regulation of gene expression Source: UniProtKB
    3. entrainment of circadian clock by photoperiod Source: UniProtKB
    4. G2/M transition of mitotic cell cycle Source: Reactome
    5. glycogen metabolic process Source: UniProtKB-KW
    6. mitotic cell cycle Source: Reactome
    7. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
    8. protein dephosphorylation Source: UniProtKB
    9. regulation of cell adhesion Source: UniProtKB
    10. regulation of circadian rhythm Source: UniProtKB
    11. small molecule metabolic process Source: Reactome
    12. transforming growth factor beta receptor signaling pathway Source: Reactome
    13. triglyceride catabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Biological rhythms, Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase PP1-beta catalytic subunit (EC:3.1.3.16, EC:3.1.3.53)
    Short name:
    PP-1B
    Short name:
    PPP1CD
    Gene namesi
    Name:PPP1CB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:9282. PPP1CB.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication. Nucleusnucleoplasm 1 Publication. Nucleusnucleolus 1 Publication
    Note: Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. MLL5-L complex Source: UniProtKB
    4. nucleolus Source: UniProtKB-SubCell
    5. nucleoplasm Source: Reactome
    6. nucleus Source: UniProt
    7. PTW/PP1 phosphatase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33610.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 327326Serine/threonine-protein phosphatase PP1-beta catalytic subunitPRO_0000058779Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei316 – 3161Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP62140.
    PaxDbiP62140.
    PRIDEiP62140.

    2D gel databases

    OGPiP37140.

    PTM databases

    PhosphoSiteiP62140.

    Expressioni

    Gene expression databases

    ArrayExpressiP62140.
    BgeeiP62140.
    CleanExiHS_PPP1CB.
    GenevestigatoriP62140.

    Organism-specific databases

    HPAiCAB022558.

    Interactioni

    Subunit structurei

    PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. The targeting or regulatory subunits determine the substrate specificity of PP1. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Part of a complex containing PPP1R15B, PP1 and NCK1/2 By similarity. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R7 and PPP1R12C. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Interacts with PPP1R16B. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with TRIM28; the interaction is weak. Interacts with PPP1R12A and NUAK1; the interaction is direct.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRCA1P383983EBI-352350,EBI-349905
    ClockO087852EBI-352350,EBI-79859From a different organism.

    Protein-protein interaction databases

    BioGridi111494. 60 interactions.
    IntActiP62140. 35 interactions.
    MINTiMINT-208135.
    STRINGi9606.ENSP00000296122.

    Structurei

    3D structure databases

    ProteinModelPortaliP62140.
    SMRiP62140. Positions 1-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172697.
    HOVERGENiHBG000216.
    InParanoidiP62140.
    KOiK06269.
    OMAiPDLQGME.
    PhylomeDBiP62140.
    TreeFamiTF354243.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 1 hit.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P62140-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI    50
    LLELEAPLKI CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL 100
    ETICLLLAYK IKYPENFFLL RGNHECASIN RIYGFYDECK RRFNIKLWKT 150
    FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ SMEQIRRIMR PTDVPDTGLL 200
    CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL DLICRAHQVV 250
    EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK 300
    KAKYQYGGLN SGRPVTPPRT ANPPKKR 327
    Length:327
    Mass (Da):37,187
    Last modified:January 23, 2007 - v3
    Checksum:iE8356022E9B94ECD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 511L → P in AAV38549. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80910 mRNA. Translation: CAA56870.1.
    U11005
    , U10998, U10999, U11000, U11001, U11002, U11003, U11004 Genomic DNA. Translation: AAA85093.1.
    AF092905 mRNA. Translation: AAF01137.1.
    CR542263 mRNA. Translation: CAG47059.1.
    CR542285 mRNA. Translation: CAG47080.1.
    BT019744 mRNA. Translation: AAV38549.1.
    AK312329 mRNA. Translation: BAG35251.1.
    BX647970 mRNA. No translation available.
    AC097724 Genomic DNA. Translation: AAY24124.1.
    CH471053 Genomic DNA. Translation: EAX00527.1.
    CH471053 Genomic DNA. Translation: EAX00528.1.
    CH471053 Genomic DNA. Translation: EAX00529.1.
    CH471053 Genomic DNA. Translation: EAX00530.1.
    BC002697 mRNA. Translation: AAH02697.1.
    BC012045 mRNA. Translation: AAH12045.1.
    CCDSiCCDS33169.1.
    PIRiS41052.
    RefSeqiNP_002700.1. NM_002709.2.
    NP_996759.1. NM_206876.1.
    UniGeneiHs.702907.

    Genome annotation databases

    EnsembliENST00000296122; ENSP00000296122; ENSG00000213639.
    ENST00000358506; ENSP00000351298; ENSG00000213639.
    ENST00000395366; ENSP00000378769; ENSG00000213639.
    GeneIDi5500.
    KEGGihsa:5500.
    UCSCiuc002rmg.3. human.

    Polymorphism databases

    DMDMi49065814.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    The things we forget - Issue 32 of March 2003

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80910 mRNA. Translation: CAA56870.1 .
    U11005
    , U10998 , U10999 , U11000 , U11001 , U11002 , U11003 , U11004 Genomic DNA. Translation: AAA85093.1 .
    AF092905 mRNA. Translation: AAF01137.1 .
    CR542263 mRNA. Translation: CAG47059.1 .
    CR542285 mRNA. Translation: CAG47080.1 .
    BT019744 mRNA. Translation: AAV38549.1 .
    AK312329 mRNA. Translation: BAG35251.1 .
    BX647970 mRNA. No translation available.
    AC097724 Genomic DNA. Translation: AAY24124.1 .
    CH471053 Genomic DNA. Translation: EAX00527.1 .
    CH471053 Genomic DNA. Translation: EAX00528.1 .
    CH471053 Genomic DNA. Translation: EAX00529.1 .
    CH471053 Genomic DNA. Translation: EAX00530.1 .
    BC002697 mRNA. Translation: AAH02697.1 .
    BC012045 mRNA. Translation: AAH12045.1 .
    CCDSi CCDS33169.1.
    PIRi S41052.
    RefSeqi NP_002700.1. NM_002709.2.
    NP_996759.1. NM_206876.1.
    UniGenei Hs.702907.

    3D structure databases

    ProteinModelPortali P62140.
    SMRi P62140. Positions 1-308.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111494. 60 interactions.
    IntActi P62140. 35 interactions.
    MINTi MINT-208135.
    STRINGi 9606.ENSP00000296122.

    Chemistry

    BindingDBi P62140.

    PTM databases

    PhosphoSitei P62140.

    Polymorphism databases

    DMDMi 49065814.

    2D gel databases

    OGPi P37140.

    Proteomic databases

    MaxQBi P62140.
    PaxDbi P62140.
    PRIDEi P62140.

    Protocols and materials databases

    DNASUi 5500.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296122 ; ENSP00000296122 ; ENSG00000213639 .
    ENST00000358506 ; ENSP00000351298 ; ENSG00000213639 .
    ENST00000395366 ; ENSP00000378769 ; ENSG00000213639 .
    GeneIDi 5500.
    KEGGi hsa:5500.
    UCSCi uc002rmg.3. human.

    Organism-specific databases

    CTDi 5500.
    GeneCardsi GC02P028974.
    HGNCi HGNC:9282. PPP1CB.
    HPAi CAB022558.
    MIMi 600590. gene.
    neXtProti NX_P62140.
    PharmGKBi PA33610.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172697.
    HOVERGENi HBG000216.
    InParanoidi P62140.
    KOi K06269.
    OMAi PDLQGME.
    PhylomeDBi P62140.
    TreeFami TF354243.

    Enzyme and pathway databases

    Reactomei REACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_494. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

    Miscellaneous databases

    ChiTaRSi PPP1CB. human.
    GeneWikii PPP1CB.
    GenomeRNAii 5500.
    NextBioi 21280.
    PROi P62140.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62140.
    Bgeei P62140.
    CleanExi HS_PPP1CB.
    Genevestigatori P62140.

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PRINTSi PR00114. STPHPHTASE.
    SMARTi SM00156. PP2Ac. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 1 hit.
    PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Three genes for protein phosphatase 1 map to different human chromosomes: sequence, expression and gene localisation of protein serine/threonine phosphatase 1 beta (PPP1CB)."
      Barker H.M., Brewis N.D., Street A.J., Spurr N.K., Cohen P.T.W.
      Biochim. Biophys. Acta 1220:212-218(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular and linkage analysis of type-1 protein phosphatase catalytic beta-subunit gene: lack of evidence for its major role in insulin resistance in Pima Indians."
      Prochazka M., Mochizuki H., Baier L.J., Cohen P.T.W., Bogardus C.
      Diabetologia 38:461-466(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Characterization of the protein phosphatase 1 catalytic subunit in endothelium: involvement in contractile responses."
      Verin A.D., Csortos C., Durbin S.D., Aydanyan A., Wang P., Patterson C.E., Garcia J.G.
      J. Cell. Biochem. 79:113-125(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Umbilical vein.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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].
    6. "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].
      Tissue: Cerebellum.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Endometrium.
    8. "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].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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].
      Tissue: Uterus.
    11. "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 2-14, ACETYLATION AT ALA-2.
      Tissue: Platelet.
    12. "Phosphorylation of a novel myosin binding subunit of protein phosphatase 1 reveals a conserved mechanism in the regulation of actin cytoskeleton."
      Tan I., Ng C.H., Lim L., Leung T.
      J. Biol. Chem. 276:21209-21216(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R12C.
    13. "Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells."
      Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.
      J. Cell Sci. 114:4219-4228(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1."
      Connor J.H., Weiser D.C., Li S., Hallenbeck J.M., Shenolikar S.
      Mol. Cell. Biol. 21:6841-6850(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R15A.
    15. "Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1."
      Ceulemans H., Vulsteke V., De Maeyer M., Tatchell K., Stalmans W., Bollen M.
      J. Biol. Chem. 277:47331-47337(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R7.
    16. "A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress."
      Boyce M., Bryant K.F., Jousse C., Long K., Harding H.P., Scheuner D., Kaufman R.J., Ma D., Coen D.M., Ron D., Yuan J.
      Science 307:935-939(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    17. "TIMAP is a positive regulator of pulmonary endothelial barrier function."
      Csortos C., Czikora I., Bogatcheva N.V., Adyshev D.M., Poirier C., Olah G., Verin A.D.
      Am. J. Physiol. 295:L440-L450(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R16B.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis."
      Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S.
      Nature 459:455-459(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL5-L COMPLEX.
    20. "Identification and characterization of a novel human PP1 phosphatase complex."
      Lee J.H., You J., Dobrota E., Skalnik D.G.
      J. Biol. Chem. 285:24466-24476(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, INTERACTION WITH PPP1R8.
    21. "New roles for the LKB1-NUAK pathway in controlling myosin phosphatase complexes and cell adhesion."
      Zagorska A., Deak M., Campbell D.G., Banerjee S., Hirano M., Aizawa S., Prescott A.R., Alessi D.R.
      Sci. Signal. 3:RA25-RA25(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NUAK1 AND PPP1R12A.
    22. "SUMOylation of the transcriptional co-repressor KAP1 is regulated by the serine and threonine phosphatase PP1."
      Li X., Lin H.H., Chen H., Xu X., Shih H.M., Ann D.K.
      Sci. Signal. 3:RA32-RA32(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM28.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Protein phosphatase 1 (PP1) is a post-translational regulator of the mammalian circadian clock."
      Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.
      PLoS ONE 6:E21325-E21325(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN CLOCK.
    25. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPP1B_HUMAN
    AccessioniPrimary (citable) accession number: P62140
    Secondary accession number(s): B2R5V4
    , D6W565, P37140, Q5U087, Q6FG45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 127 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

    Complete proteome, Direct protein sequencing, 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3