Protein-coding gene in the species Homo sapiens
PPP1R12B |
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Identifiers |
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Aliases | PPP1R12B, MYPT2, PP1bp55, protein phosphatase 1 regulatory subunit 12B |
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External IDs | OMIM: 603768; MGI: 1916417; HomoloGene: 136757; GeneCards: PPP1R12B; OMA:PPP1R12B - orthologs |
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Gene location (Human) |
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![Chromosome 1 (human)](//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Ideogram_human_chromosome_1.svg/300px-Ideogram_human_chromosome_1.svg.png) | Chr. | Chromosome 1 (human)[1] |
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| Band | 1q32.1 | Start | 202,348,699 bp[1] |
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End | 202,592,706 bp[1] |
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Gene location (Mouse) |
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![Chromosome 1 (mouse)](//upload.wikimedia.org/wikipedia/commons/thumb/f/fb/Ideogram_house_mouse_chromosome_1.svg/260px-Ideogram_house_mouse_chromosome_1.svg.png) | Chr. | Chromosome 1 (mouse)[2] |
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| Band | 1|1 E4 | Start | 134,682,396 bp[2] |
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End | 134,883,680 bp[2] |
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RNA expression pattern |
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Bgee | Human | Mouse (ortholog) |
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Top expressed in | - saphenous vein
- myocardium of left ventricle
- right coronary artery
- cardiac muscle tissue of right atrium
- right ventricle
- popliteal artery
- tibial arteries
- tail of epididymis
- thoracic aorta
- ascending aorta
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| Top expressed in | - Rostral migratory stream
- ascending aorta
- muscle of thigh
- aortic valve
- soleus muscle
- extraocular muscle
- digastric muscle
- temporal muscle
- vastus lateralis muscle
- triceps brachii muscle
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| More reference expression data |
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BioGPS | ![](//upload.wikimedia.org/wikipedia/commons/thumb/a/ab/PBB_GE_PPP1R12B_201958_s_at_fs.png/250px-PBB_GE_PPP1R12B_201958_s_at_fs.png)
![](//upload.wikimedia.org/wikipedia/commons/thumb/9/94/PBB_GE_PPP1R12B_201957_at_fs.png/250px-PBB_GE_PPP1R12B_201957_at_fs.png) | More reference expression data |
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Gene ontology |
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Molecular function | - enzyme activator activity
- protein binding
- protein kinase binding
- phosphatase regulator activity
- enzyme inhibitor activity
| Cellular component | - cytoplasm
- cytosol
- A band
- Z discdkac
- nucleoplasm
- cytoskeleton
| Biological process | - regulation of muscle contraction
- positive regulation of catalytic activity
- signal transduction
- regulation of catalytic activity
- negative regulation of catalytic activity
- G2/M transition of mitotic cell cycle
| Sources:Amigo / QuickGO |
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Orthologs |
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Species | Human | Mouse |
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Entrez | | |
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Ensembl | | |
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UniProt | | |
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RefSeq (mRNA) | NM_001167857 NM_001167858 NM_001197131 NM_002481 NM_032103
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NM_032104 NM_032105 NM_001331029 |
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NM_001081307 NM_001368827 NM_001368829 |
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RefSeq (protein) | NP_001161329 NP_001161330 NP_001184060 NP_001317958 NP_002472
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NP_115286 NP_115287 |
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NP_001074776 NP_001355756 NP_001355758 |
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Location (UCSC) | Chr 1: 202.35 – 202.59 Mb | Chr 1: 134.68 – 134.88 Mb |
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PubMed search | [3] | [4] |
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Wikidata |
View/Edit Human | View/Edit Mouse |
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Protein phosphatase 1 regulatory subunit 12B is an enzyme that in humans is encoded by the PPP1R12B gene.[5][6]
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.[6]
Interactions
PPP1R12B has been shown to interact with Interleukin 16.[7]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000077157 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000073557 – 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.
- ^ 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.
- ^ a b "Entrez Gene: PPP1R12B protein phosphatase 1, regulatory (inhibitor) subunit 12B".
- ^ 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. 278 (43). United States: 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. ISBN 978-3-540-64753-9. 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. S2CID 35052936.
- 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. S2CID 4427026.
- 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.