PPP1CB

Protein-coding gene in the species Homo sapiens
PPP1CB
Identifiers
AliasesPPP1CB, HEL-S-80p, PP-1B, PP1B, PP1beta, PPP1CD, protein phosphatase 1 catalytic subunit beta, NSLH2, PPP1beta, PP1c, MP
External IDsOMIM: 600590; MGI: 104871; HomoloGene: 37659; GeneCards: PPP1CB; OMA:PPP1CB - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for PPP1CB
Genomic location for PPP1CB
Band2p23.2Start28,751,640 bp[1]
End28,802,940 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for PPP1CB
Genomic location for PPP1CB
Band5|5 B1Start32,616,187 bp[2]
End32,674,777 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Achilles tendon

  • amniotic fluid

  • buccal mucosa cell

  • ventricular zone

  • Descending thoracic aorta

  • popliteal artery

  • tibial arteries

  • ascending aorta

  • caput epididymis

  • ganglionic eminence
Top expressed in
  • blood

  • Gonadal ridge

  • atrium

  • lobe of cerebellum

  • pineal gland

  • olfactory tubercle

  • ventral tegmental area

  • medial vestibular nucleus

  • cerebellar vermis

  • parotid gland
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • phosphoprotein phosphatase activity
  • myosin phosphatase activity
  • phosphatase activity
  • protein serine/threonine phosphatase activity
  • metal ion binding
  • myosin-light-chain-phosphatase activity
  • protein binding
  • protein kinase binding
  • hydrolase activity
Cellular component
  • cytoplasm
  • cytosol
  • focal adhesion
  • nucleoplasm
  • protein phosphatase type 1 complex
  • glycogen granule
  • PTW/PP1 phosphatase complex
  • nucleolus
  • extracellular exosome
  • nucleus
  • plasma membrane
Biological process
  • rhythmic process
  • protein dephosphorylation
  • circadian regulation of gene expression
  • cell division
  • regulation of cell adhesion
  • G2/M transition of mitotic cell cycle
  • regulation of circadian rhythm
  • glycogen metabolic process
  • regulation of glycogen biosynthetic process
  • cell cycle
  • regulation of glycogen catabolic process
  • entrainment of circadian clock by photoperiod
  • carbohydrate metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5500

19046

Ensembl

ENSG00000213639

ENSMUSG00000014956

UniProt

P62140

P62141

RefSeq (mRNA)

NM_206877
NM_002709
NM_206876

NM_172707

RefSeq (protein)

NP_002700
NP_996759

NP_766295

Location (UCSC)Chr 2: 28.75 – 28.8 MbChr 5: 32.62 – 32.67 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Serine/threonine-protein phosphatase PP1-beta catalytic subunit is an enzyme that in humans is encoded by the PPP1CB gene.[5]

The protein encoded by this gene is one of the three catalytic subunits of protein phosphatase 1 (PP1). PP1 is a serine/threonine specific protein phosphatase known to be involved in the regulation of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. Mouse studies suggest that PP1 functions as a suppressor of learning and memory. Two alternatively spliced transcript variants encoding distinct isoforms have been observed.[6]

Interactions

PPP1CB has been shown to interact with PPP1R15A,[7][8] Nucleolin,[9] SMARCB1[7] and PPP1R9B.[10]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000213639 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000014956 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Barker HM, Brewis ND, Street AJ, Spurr NK, Cohen PT (March 1994). "Three genes for protein phosphatase 1 map to different human chromosomes: sequence, expression and gene localisation of protein serine/threonine phosphatase 1 beta (PPP1CB)". Biochim Biophys Acta. 1220 (2): 212–8. doi:10.1016/0167-4889(94)90138-4. PMID 8312365.
  6. ^ "Entrez Gene: PPP1CB protein phosphatase 1, catalytic subunit, beta isoform".
  7. ^ a b Wu DY, Tkachuck Douglas C, Roberson Rachel S, Schubach William H (August 2002). "The human SNF5/INI1 protein facilitates the function of the growth arrest and DNA damage-inducible protein (GADD34) and modulates GADD34-bound protein phosphatase-1 activity". J. Biol. Chem. 277 (31): 27706–15. doi:10.1074/jbc.M200955200. ISSN 0021-9258. PMID 12016208.
  8. ^ Connor JH, Weiser D C, Li S, Hallenbeck J M, Shenolikar S (October 2001). "Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1". Mol. Cell. Biol. 21 (20): 6841–50. doi:10.1128/MCB.21.20.6841-6850.2001. ISSN 0270-7306. PMC 99861. PMID 11564868.
  9. ^ Morimoto H, Okamura Hirohiko, Haneji Tatsuji (September 2002). "Interaction of protein phosphatase 1 delta with nucleolin in human osteoblastic cells". J. Histochem. Cytochem. 50 (9): 1187–93. doi:10.1177/002215540205000905. ISSN 0022-1554. PMID 12185196.
  10. ^ Hsieh-Wilson LC, Allen P B, Watanabe T, Nairn A C, Greengard P (April 1999). "Characterization of the neuronal targeting protein spinophilin and its interactions with protein phosphatase-1". Biochemistry. 38 (14): 4365–73. doi:10.1021/bi982900m. ISSN 0006-2960. PMID 10194355.

Further reading

  • Prochazka M, Mochizuki H, Baier LJ, et al. (1995). "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". Diabetologia. 38 (4): 461–6. doi:10.1007/BF00410284. PMID 7796987.
  • Saadat M, Kakinoki Y, Mizuno Y, et al. (1995). "Chromosomal localization of human, rat, and mouse protein phosphatase type 1 beta catalytic subunit genes (PPP1CB) by fluorescence in situ hybridization". Jpn. J. Genet. 69 (6): 697–700. doi:10.1266/jjg.69.697. PMID 7857673.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Kawabe T, Muslin AJ, Korsmeyer SJ (1997). "HOX11 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint". Nature. 385 (6615): 454–8. Bibcode:1997Natur.385..454K. doi:10.1038/385454a0. PMID 9009195. S2CID 608633.
  • Fujioka M, Takahashi N, Odai H, et al. (1998). "A new isoform of human myosin phosphatase targeting/regulatory subunit (MYPT2): cDNA cloning, tissue expression, and chromosomal mapping". Genomics. 49 (1): 59–68. doi:10.1006/geno.1998.5222. PMID 9570949.
  • Verin AD, Csortos C, Durbin SD, et al. (2000). "Characterization of the protein phosphatase 1 catalytic subunit in endothelium: involvement in contractile responses". J. Cell. Biochem. 79 (1): 113–25. doi:10.1002/1097-4644(2000)79:1<113::AID-JCB110>3.0.CO;2-9. PMID 10906760. S2CID 42857803.
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
  • Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
  • Tan I, Ng CH, Lim L, Leung T (2001). "Phosphorylation of a novel myosin binding subunit of protein phosphatase 1 reveals a conserved mechanism in the regulation of actin cytoskeleton". J. Biol. Chem. 276 (24): 21209–16. doi:10.1074/jbc.M102615200. PMID 11399775.
  • Fresu M, Bianchi M, Parsons JT, Villa-Moruzzi E (2001). "Cell-cycle-dependent association of protein phosphatase 1 and focal adhesion kinase". Biochem. J. 358 (Pt 2): 407–14. doi:10.1042/0264-6021:3580407. PMC 1222073. PMID 11513739.
  • Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. Bibcode:2002CBio...12....1A. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298. S2CID 14132033.
  • Bharucha DC, Zhou M, Nekhai S, et al. (2002). "A protein phosphatase from human T cells augments tat transactivation of the human immunodeficiency virus type 1 long-terminal repeat". Virology. 296 (1): 6–16. doi:10.1006/viro.2002.1438. PMID 12036313.
  • Ceulemans H, Vulsteke V, De Maeyer M, et al. (2003). "Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1". J. Biol. Chem. 277 (49): 47331–7. doi:10.1074/jbc.M206838200. PMID 12226088.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
  • Galey D, Becker K, Haughey N, et al. (2003). "Differential transcriptional regulation by human immunodeficiency virus type 1 and gp120 in human astrocytes". J. Neurovirol. 9 (3): 358–71. doi:10.1080/13550280390201119. PMID 12775419. S2CID 22016092.
  • Ammosova T, Jerebtsova M, Beullens M, et al. (2003). "Nuclear protein phosphatase-1 regulates HIV-1 transcription". J. Biol. Chem. 278 (34): 32189–94. doi:10.1074/jbc.M300521200. PMID 12788939.
  • Llorian M, Beullens M, Andrés I, et al. (2004). "SIPP1, a novel pre-mRNA splicing factor and interactor of protein phosphatase-1". Biochem. J. 378 (Pt 1): 229–38. doi:10.1042/BJ20030950. PMC 1223944. PMID 14640981.
  • Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
  • v
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  • 1s70: Complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (MYPT1)
    1s70: Complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (MYPT1)
  • 1u32: Crystal structure of a Protein Phosphatase-1: Calcineurin Hybrid Bound to Okadaic Acid
    1u32: Crystal structure of a Protein Phosphatase-1: Calcineurin Hybrid Bound to Okadaic Acid
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