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{{Infobox_gene}}
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'''Protein phosphatase 1 regulatory subunit 12B''' is an [[enzyme]] that in humans is encoded by the ''PPP1R12B'' [[gene]].<ref name="pmid9570949">{{cite journal |vauthors=Fujioka M, Takahashi N, Odai H, Araki S, Ichikawa K, Feng J, Nakamura M, Kaibuchi K, Hartshorne DJ, Nakano T, Ito M | title = A new isoform of human myosin phosphatase targeting/regulatory subunit (MYPT2): cDNA cloning, tissue expression, and chromosomal mapping | journal = Genomics | volume = 49 | issue = 1 | pages = 59–68 |date=Jun 1998 | pmid = 9570949 | pmc =  | doi = 10.1006/geno.1998.5222 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PPP1R12B protein phosphatase 1, regulatory (inhibitor) subunit 12B| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4660| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Protein phosphatase 1, regulatory (inhibitor) subunit 12B
| HGNCid = 7619
| Symbol = PPP1R12B
| AltSymbols =; MGC131980; MGC87886; MYPT2
| OMIM = 603768
| ECnumber = 
| Homologene = 23754
| MGIid = 1916417
| GeneAtlas_image1 = PBB_GE_PPP1R12B_201957_at_tn.png
| GeneAtlas_image2 = PBB_GE_PPP1R12B_201958_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008047 |text = enzyme activator activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006937 |text = regulation of muscle contraction}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4660
    | Hs_Ensembl = ENSG00000077157
    | Hs_RefseqProtein = NP_002472
    | Hs_RefseqmRNA = NM_002481
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 200584443
    | Hs_GenLoc_end = 200824320
    | Hs_Uniprot = O60237
    | Mm_EntrezGene = 329251
    | Mm_Ensembl = ENSMUSG00000073557
    | Mm_RefseqmRNA = XM_136178
    | Mm_RefseqProtein = XP_136178
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 136692379
    | Mm_GenLoc_end = 136772339
    | Mm_Uniprot = Q8BG95
  }}
}}
'''Protein phosphatase 1, regulatory (inhibitor) subunit 12B''', also known as '''PPP1R12B''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PPP1R12B protein phosphatase 1, regulatory (inhibitor) subunit 12B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4660| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: PPP1R12B protein phosphatase 1, regulatory (inhibitor) subunit 12B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4660| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez"/>
}}
}}
==Interactions==
PPP1R12B has been shown to [[Protein-protein interaction|interact]] with [[Interleukin 16]].<ref name=pmid12923170>{{cite journal |last=Bannert |first=Norbert |authorlink= |author2=Vollhardt Karin |author3=Asomuddinov Bakhtier |author4=Haag Marion |author5=König Herbert |author6=Norley Stephen |author7=Kurth Reinhard  |date=Oct 2003 |title=PDZ Domain-mediated interaction of interleukin-16 precursor proteins with myosin phosphatase targeting subunits |journal=J. Biol. Chem. |volume=278 |issue=43 |pages=42190–9 |publisher= |location = United States| issn = 0021-9258| pmid = 12923170 |doi = 10.1074/jbc.M306669200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Somlyo AP, Wu X, Walker LA, Somlyo AV |title=Pharmacomechanical coupling: the role of calcium, G-proteins, kinases and phosphatases. |journal=Rev. Physiol. Biochem. Pharmacol. |volume=134 |issue=  |pages= 201-34 |year= 1999 |pmid= 10087910 |doi=  }}
*{{cite journal  |vauthors=Somlyo AP, Wu X, Walker LA, Somlyo AV |title=Pharmacomechanical coupling: the role of calcium, G-proteins, kinases and phosphatases. |journal=Rev. Physiol. Biochem. Pharmacol. |volume=134 |issue=  |pages= 201–34 |year= 1999 |pmid= 10087910 |doi=  10.1007/3-540-64753-8_5}}
*{{cite journal  | author=Seki N, Ohira M, Nagase T, ''et al.'' |title=Characterization of cDNA clones in size-fractionated cDNA libraries from human brain. |journal=DNA Res. |volume=4 |issue= 5 |pages= 345-9 |year= 1998 |pmid= 9455484 |doi=  }}
*{{cite journal  | author=Seki N |title=Characterization of cDNA clones in size-fractionated cDNA libraries from human brain |journal=DNA Res. |volume=4 |issue= 5 |pages= 345–9 |year= 1998 |pmid= 9455484 |doi=10.1093/dnares/4.5.345  |name-list-format=vanc| author2=Ohira M  | author3=Nagase T | display-authors=3  | last4=Ishikawa | first4=K  | last5=Miyajima  | first5=N  | last6=Nakajima  | first6=D  | last7=Nomura  | first7=N  | last8=Ohara  | first8=O  }}
*{{cite journal | author=Fujioka M, Takahashi N, Odai H, ''et al.'' |title=A new isoform of human myosin phosphatase targeting/regulatory subunit (MYPT2): cDNA cloning, tissue expression, and chromosomal mapping. |journal=Genomics |volume=49 |issue= 1 |pages= 59-68 |year= 1998 |pmid= 9570949 |doi= 10.1006/geno.1998.5222 }}
*{{cite journal  |vauthors=Moorhead G, Johnson D, Morrice N, Cohen P |title=The major myosin phosphatase in skeletal muscle is a complex between the beta-isoform of protein phosphatase 1 and the MYPT2 gene product |journal=FEBS Lett. |volume=438 |issue= 3 |pages= 141–4 |year= 1998 |pmid= 9827534 |doi=10.1016/S0014-5793(98)01276-9 }}
*{{cite journal  | author=Moorhead G, Johnson D, Morrice N, Cohen P |title=The major myosin phosphatase in skeletal muscle is a complex between the beta-isoform of protein phosphatase 1 and the MYPT2 gene product. |journal=FEBS Lett. |volume=438 |issue= 3 |pages= 141-4 |year= 1998 |pmid= 9827534 |doi=  }}
*{{cite journal  | author=Somlyo AP |title=Kinases, myosin phosphatase and Rho proteins: curiouser and curiouser |journal=J. Physiol. |volume=516 |issue=  3|pages= 630 |year= 1999 |pmid= 10200412 |doi=10.1111/j.1469-7793.1999.0630u.x  | pmc=2269296 }}
*{{cite journal  | author=Somlyo AP |title=Kinases, myosin phosphatase and Rho proteins: curiouser and curiouser. |journal=J. Physiol. (Lond.) |volume=516 ( Pt 3) |issue=  |pages= 630 |year= 1999 |pmid= 10200412 |doi=  }}
*{{cite journal  | author=Arimura T |title=Identification, characterization, and functional analysis of heart-specific myosin light chain phosphatase small subunit |journal=J. Biol. Chem. |volume=276 |issue= 9 |pages= 6073–82 |year= 2001 |pmid= 11067852 |doi= 10.1074/jbc.M008566200 |name-list-format=vanc| author2=Suematsu N  | author3=Zhou YB  | display-authors=3  | last4=Nishimura  | first4=J  | last5=Satoh  | first5=S  | last6=Takeshita  | first6=A  | last7=Kanaide  | first7=H  | last8=Kimura  | first8=A }}
*{{cite journal  | author=Arimura T, Suematsu N, Zhou YB, ''et al.'' |title=Identification, characterization, and functional analysis of heart-specific myosin light chain phosphatase small subunit. |journal=J. Biol. Chem. |volume=276 |issue= 9 |pages= 6073-82 |year= 2001 |pmid= 11067852 |doi= 10.1074/jbc.M008566200 }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD |bibcode=2002PNAS...9916899M}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Bannert N |title=PDZ Domain-mediated interaction of interleukin-16 precursor proteins with myosin phosphatase targeting subunits |journal=J. Biol. Chem. |volume=278 |issue= 43 |pages= 42190–9 |year= 2004 |pmid= 12923170 |doi= 10.1074/jbc.M306669200 |name-list-format=vanc| author2=Vollhardt K  | author3=Asomuddinov B  | display-authors=3  | last4=Haag  | first4=M  | last5=König  | first5=H  | last6=Norley  | first6=S  | last7=Kurth  | first7=R }}
*{{cite journal  | author=Bannert N, Vollhardt K, Asomuddinov B, ''et al.'' |title=PDZ Domain-mediated interaction of interleukin-16 precursor proteins with myosin phosphatase targeting subunits. |journal=J. Biol. Chem. |volume=278 |issue= 43 |pages= 42190-9 |year= 2004 |pmid= 12923170 |doi= 10.1074/jbc.M306669200 }}
*{{cite journal  | author=Gerhard DS |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Rual JF |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |name-list-format=vanc| author2=Venkatesan K  | author3=Hao T  | display-authors=3  | last4=Hirozane-Kishikawa  | first4=Tomoko  | last5=Dricot  | first5=Amélie  | last6=Li  | first6=Ning  | last7=Berriz  | first7=Gabriel F.  | last8=Gibbons  | first8=Francis D.  | last9=Dreze  | first9=Matija |bibcode=2005Natur.437.1173R}}
*{{cite journal  | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | author=Okamoto R |title=Characterization and function of MYPT2, a target subunit of myosin phosphatase in heart |journal=Cell. Signal. |volume=18 |issue= 9 |pages= 1408–16 |year= 2007 |pmid= 16431080 |doi= 10.1016/j.cellsig.2005.11.001 |name-list-format=vanc| author2=Kato T  | author3=Mizoguchi A  | display-authors=3  | last4=Takahashi  | first4=N  | last5=Nakakuki  | first5=T  | last6=Mizutani  | first6=H  | last7=Isaka  | first7=N  | last8=Imanakayoshida  | first8=K  | last9=Kaibuchi  | first9=K }}
*{{cite journal  | author=Okamoto R, Kato T, Mizoguchi A, ''et al.'' |title=Characterization and function of MYPT2, a target subunit of myosin phosphatase in heart. |journal=Cell. Signal. |volume=18 |issue= 9 |pages= 1408-16 |year= 2007 |pmid= 16431080 |doi= 10.1016/j.cellsig.2005.11.001 }}
*{{cite journal  | author=Gregory SG |title=The DNA sequence and biological annotation of human chromosome 1 |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 |name-list-format=vanc| author2=Barlow KF  | author3=McLay KE  | display-authors=3  | last4=Kaul  | first4=R.  | last5=Swarbreck  | first5=D.  | last6=Dunham  | first6=A.  | last7=Scott  | first7=C. E.  | last8=Howe  | first8=K. L.  | last9=Woodfine  | first9=K. |bibcode=2006Natur.441..315G}}
*{{cite journal  | author=Gregory SG, Barlow KF, McLay KE, ''et al.'' |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315-21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
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Latest revision as of 19:48, 25 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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. ↑ 2.0 2.1 "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



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