PPP1R12B

Protein phosphatase 1 regulatory subunit 12B is an enzyme that in humans is encoded by the PPP1R12B gene.[3][4]

PPP1R12B
Identifiers
Aliases	PPP1R12B, MYPT2, PP1bp55, protein phosphatase 1 regulatory subunit 12B
External IDs	OMIM: 603768 HomoloGene: 136757 GeneCards: PPP1R12B
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q32.1 Start 202,348,699 bp[1] End 202,592,706 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0010577 enzyme activator activity • GO:0001948 protein binding • protein kinase binding • phosphatase regulator activity • GO:0048551 enzyme inhibitor activity Cellular component • cytoplasm • cytosol • A band • Z disc • nucleoplasm • cytoskeleton Biological process • regulation of muscle contraction • GO:0048554 positive regulation of catalytic activity • signal transduction • GO:0048552 regulation of catalytic activity • GO:0048553 negative regulation of catalytic activity • G2/M transition of mitotic cell cycle Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	4660	n/a
Ensembl	ENSG00000077157	n/a
UniProt	O60237	n/a
RefSeq (mRNA)	NM_001167857 NM_001167858 NM_001197131 NM_002481 NM_032103 NM_032104 NM_032105 NM_001331029	n/a
RefSeq (protein)	NP_001161329 NP_001161330 NP_001184060 NP_001317958 NP_002472 NP_115286 NP_115287	n/a
Location (UCSC)	Chr 1: 202.35 – 202.59 Mb	n/a
PubMed search	[2]	n/a
Wikidata
View/Edit Human

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.[4]

Interactions

PPP1R12B has been shown to interact with Interleukin 16.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000077157 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. 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.
4. "Entrez Gene: PPP1R12B protein phosphatase 1, regulatory (inhibitor) subunit 12B".
5. 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. 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2005Natur.437.1173R. 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. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.