PPP1R12B

Protein phosphatase 1, regulatory subunit 12B
Identifiers
Symbols	PPP1R12B ; MYPT2; PP1bp55
External IDs	OMIM: 603768 MGI: 1916417 HomoloGene: 136757 ChEMBL: 2427 GeneCards: PPP1R12B Gene
EC number	3.1.3.53
Gene ontology Molecular function • protein binding • enzyme activator activity • phosphatase regulator activity Cellular component • nucleoplasm • cytosol Biological process • G2/M transition of mitotic cell cycle • mitotic cell cycle • regulation of muscle contraction • signal transduction • small GTPase mediated signal transduction • positive regulation of catalytic activity Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4660	329251
Ensembl	ENSG00000077157	ENSMUSG00000073557
UniProt	O60237	Q8BG95
RefSeq (mRNA)	NM_001167857	NM_001081307
RefSeq (protein)	NP_001161329	NP_001074776
Location (UCSC)	Chr 1: 202.35 – 202.59 Mb	Chr 1: 134.75 – 134.96 Mb
PubMed search

Protein phosphatase 1 regulatory subunit 12B is an enzyme that in humans is encoded by the PPP1R12B gene.^[1][2]

Myosin light chain phosphatase (MLCP) consists of three subunits- catalytic subunit, large subunit/myosin binding subunit (MBS) and small subunit (sm-M20). This gene is a multi-functional gene which encodes both MBS and sm-M20. MLCP regulates myosins and the dephosphorylation is enhanced by the presence of MBS. The sm-M20 is suggested to play a regulatory role in muscle contraction by binding to MBS. MBS is also encoded by another gene, myosin light chain phosphatase target subunit 1. sm-M20 shows higher binding affinity to this gene product than to myosin light chain phosphatase target subunit 2-MBS even though the two MBS proteins are highly similar. Although both MBSs increase the activity of MLCP, myosin light chain phosphatase target subunit 1-MBS is a more efficient activator. There are four alternatively spliced transcript variants described; two alter the MBS coding region and two alter the sm-M20 coding region of this gene.^[2]

Interactions

PPP1R12B has been shown to interact with Interleukin 16.^[3]

References

1. Fujioka M, Takahashi N, Odai H, Araki S, Ichikawa K, Feng J, Nakamura M, Kaibuchi K, Hartshorne DJ, Nakano T, Ito M (Jun 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.
2. "Entrez Gene: PPP1R12B protein phosphatase 1, regulatory (inhibitor) subunit 12B".
3. Bannert, Norbert; Vollhardt Karin; Asomuddinov Bakhtier; Haag Marion; König Herbert; Norley Stephen; Kurth Reinhard (Oct 2003). "PDZ Domain-mediated interaction of interleukin-16 precursor proteins with myosin phosphatase targeting subunits". J. Biol. Chem. (United States) 278 (43): 42190–9. doi:10.1074/jbc.M306669200. ISSN 0021-9258. PMID 12923170.

Further reading

• Somlyo AP, Wu X, Walker LA, Somlyo AV (1999). "Pharmacomechanical coupling: the role of calcium, G-proteins, kinases and phosphatases.". Rev. Physiol. Biochem. Pharmacol. 134: 201–34. doi:10.1007/3-540-64753-8_5. PMID 10087910.
• Seki N, Ohira M, Nagase T, et al. (1998). "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain". DNA Res. 4 (5): 345–9. doi:10.1093/dnares/4.5.345. PMID 9455484.
• Moorhead G, Johnson D, Morrice N, Cohen P (1998). "The major myosin phosphatase in skeletal muscle is a complex between the beta-isoform of protein phosphatase 1 and the MYPT2 gene product". FEBS Lett. 438 (3): 141–4. doi:10.1016/S0014-5793(98)01276-9. PMID 9827534.
• Somlyo AP (1999). "Kinases, myosin phosphatase and Rho proteins: curiouser and curiouser". J. Physiol. (Lond.) 516 (3): 630. doi:10.1111/j.1469-7793.1999.0630u.x. PMC 2269296. PMID 10200412.
• Arimura T, Suematsu N, Zhou YB, et al. (2001). "Identification, characterization, and functional analysis of heart-specific myosin light chain phosphatase small subunit". J. Biol. Chem. 276 (9): 6073–82. doi:10.1074/jbc.M008566200. PMID 11067852.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Bannert N, Vollhardt K, Asomuddinov B, et al. (2004). "PDZ Domain-mediated interaction of interleukin-16 precursor proteins with myosin phosphatase targeting subunits". J. Biol. Chem. 278 (43): 42190–9. doi:10.1074/jbc.M306669200. PMID 12923170.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Okamoto R, Kato T, Mizoguchi A, et al. (2007). "Characterization and function of MYPT2, a target subunit of myosin phosphatase in heart". Cell. Signal. 18 (9): 1408–16. doi:10.1016/j.cellsig.2005.11.001. PMID 16431080.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.