PPP1CB

PPP1CB

Identifiers

PPP1CB, HEL-S-80p, PP-1B, PP1B, PP1beta, PPP1CD, protein phosphatase 1 catalytic subunit beta, NSLH2, PPP1beta, PP1c, MP

External IDs

OMIM: 600590 MGI: 104871 HomoloGene: 37659 GeneCards: PPP1CB

Gene location (Human)

Chr.	Chromosome 2 (human)^[1]

Band	2p23.2	Start	28,751,640 bp^[1]
Band	2p23.2	End	28,802,940 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 5 (mouse)^[2]

Band	5\|5 B1	Start	32,616,187 bp^[2]
Band	5\|5 B1	End	32,674,777 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

Achilles tendon

amniotic fluid

popliteal artery

ascending aorta

caput epididymis

ganglionic eminence

gastric mucosa

parotid gland

gastrocnemius muscle

left coronary artery

Top expressed in

blood

atrium

pineal gland

olfactory tubercle

ventral tegmental area

medial vestibular nucleus

cerebellar vermis

parotid gland

atrioventricular valve

intercostal muscle

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

Species

Human

Mouse

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 Mb

Chr 5: 32.62 – 32.67 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000213639 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000014956 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ "Entrez Gene: PPP1CB protein phosphatase 1, catalytic subunit, beta isoform".
^ ^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.
^ 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.
^ 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.
^ 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.

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 t e PDB gallery
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

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This page was last edited on 9 April 2024, at 21:24

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Interactions

References

Further reading