PP2Cγ: a human protein phosphatase with a unique acidic domain
We have cloned a novel cDNA from human skeletal muscle which encodes a protein phosphatase with a unique acidic domain. It is 34% identical to mammalian PP2Cα and PP2Cβ, and we call it PP2Cγ. It more closely resembles PP2Cs from Paramecium tetraurelia and Schizosaccharomyces pombe than mammalian PP2...
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| Veröffentlicht in: | FEBS letters 1997-08, Vol.412 (3), p.415-419 |
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| creator | Travis, Sue M Welsh, Michael J |
| description | We have cloned a novel cDNA from human skeletal muscle which encodes a protein phosphatase with a unique acidic domain. It is 34% identical to mammalian PP2Cα and PP2Cβ, and we call it PP2Cγ. It more closely resembles PP2Cs from
Paramecium tetraurelia and
Schizosaccharomyces pombe than mammalian PP2Cs. Northern blot analysis shows that PP2Cγ is widely expressed, and is most abundant in testis, skeletal muscle, and heart. Like known PP2Cs, recombinant PP2Cγ requires Mg
2+ or Mn
2+ for activity. Unlike any other known phosphatase, PP2Cγ has a highly acidic domain: 75% of the 54 residues are glutamate or aspartate. |
| doi_str_mv | 10.1016/S0014-5793(97)00837-5 |
| format | Article |
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Paramecium tetraurelia and
Schizosaccharomyces pombe than mammalian PP2Cs. Northern blot analysis shows that PP2Cγ is widely expressed, and is most abundant in testis, skeletal muscle, and heart. Like known PP2Cs, recombinant PP2Cγ requires Mg
2+ or Mn
2+ for activity. Unlike any other known phosphatase, PP2Cγ has a highly acidic domain: 75% of the 54 residues are glutamate or aspartate.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(97)00837-5</identifier><identifier>PMID: 9276438</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>acidic domain ; Amino Acid Sequence ; Animals ; cDNA ; Cloning, Molecular ; Enzyme Activation ; Humans ; Mice ; Molecular Sequence Data ; Organ Specificity ; Paramecium - enzymology ; Paramecium - genetics ; Phosphoprotein Phosphatases - chemistry ; Phosphoprotein Phosphatases - genetics ; Phosphoprotein Phosphatases - isolation & purification ; Phylogeny ; Protein Phosphatase 2 ; Protein Phosphatase 2C ; Protein phosphorylation ; Protein Structure, Tertiary ; Saccharomyces cerevisiae Proteins ; Sequence Analysis, DNA</subject><ispartof>FEBS letters, 1997-08, Vol.412 (3), p.415-419</ispartof><rights>1997 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579397008375$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9276438$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Travis, Sue M</creatorcontrib><creatorcontrib>Welsh, Michael J</creatorcontrib><title>PP2Cγ: a human protein phosphatase with a unique acidic domain</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>We have cloned a novel cDNA from human skeletal muscle which encodes a protein phosphatase with a unique acidic domain. It is 34% identical to mammalian PP2Cα and PP2Cβ, and we call it PP2Cγ. It more closely resembles PP2Cs from
Paramecium tetraurelia and
Schizosaccharomyces pombe than mammalian PP2Cs. Northern blot analysis shows that PP2Cγ is widely expressed, and is most abundant in testis, skeletal muscle, and heart. Like known PP2Cs, recombinant PP2Cγ requires Mg
2+ or Mn
2+ for activity. Unlike any other known phosphatase, PP2Cγ has a highly acidic domain: 75% of the 54 residues are glutamate or aspartate.</description><subject>acidic domain</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>cDNA</subject><subject>Cloning, Molecular</subject><subject>Enzyme Activation</subject><subject>Humans</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Organ Specificity</subject><subject>Paramecium - enzymology</subject><subject>Paramecium - genetics</subject><subject>Phosphoprotein Phosphatases - chemistry</subject><subject>Phosphoprotein Phosphatases - genetics</subject><subject>Phosphoprotein Phosphatases - isolation & purification</subject><subject>Phylogeny</subject><subject>Protein Phosphatase 2</subject><subject>Protein Phosphatase 2C</subject><subject>Protein phosphorylation</subject><subject>Protein Structure, Tertiary</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Sequence Analysis, DNA</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kNtKw0AURQdRaq1-QiFPog_RuV98KRK8QcGC-jxMZyZkpElqJlH8Lv_Db3J6wad9Dntx2GcDMEXwCkHEr18gRDRnQpELJS4hlETk7ACMkRQkJ5TLQzD-R47BSYzvMO0SqREYKSw4JXIMZosFLn5_bjKTVUNtmmzdtb0PSas2rivTm-izr9BXCRia8DH4zNjggs1cW5vQnIKj0qyiP9vrBLzd370Wj_n8-eGpuJ3nHnPc50hIK5hDnkJKS84MXXKHlk5RKaiEBkFYcmwdUpyXAkPEmKOlIWkSUGFHJuB8dzflSyFir-sQrV-tTOPbIWqhMBWKoQRO9-CwrL3T6y7UpvvW-4-TP9v5PqX9DL7T0QbfWO9C522vXRs0gnpTsd5WrDf9aSX0tmLNyB-E32tl</recordid><startdate>19970804</startdate><enddate>19970804</enddate><creator>Travis, Sue M</creator><creator>Welsh, Michael J</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19970804</creationdate><title>PP2Cγ: a human protein phosphatase with a unique acidic domain</title><author>Travis, Sue M ; Welsh, Michael J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e262t-178c75d1e4044f65a4b6d1bd9487480a100f62cd1966f720155d4fa32017092d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>acidic domain</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>cDNA</topic><topic>Cloning, Molecular</topic><topic>Enzyme Activation</topic><topic>Humans</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Organ Specificity</topic><topic>Paramecium - enzymology</topic><topic>Paramecium - genetics</topic><topic>Phosphoprotein Phosphatases - chemistry</topic><topic>Phosphoprotein Phosphatases - genetics</topic><topic>Phosphoprotein Phosphatases - isolation & purification</topic><topic>Phylogeny</topic><topic>Protein Phosphatase 2</topic><topic>Protein Phosphatase 2C</topic><topic>Protein phosphorylation</topic><topic>Protein Structure, Tertiary</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Sequence Analysis, DNA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Travis, Sue M</creatorcontrib><creatorcontrib>Welsh, Michael J</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Travis, Sue M</au><au>Welsh, Michael J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PP2Cγ: a human protein phosphatase with a unique acidic domain</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1997-08-04</date><risdate>1997</risdate><volume>412</volume><issue>3</issue><spage>415</spage><epage>419</epage><pages>415-419</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>We have cloned a novel cDNA from human skeletal muscle which encodes a protein phosphatase with a unique acidic domain. It is 34% identical to mammalian PP2Cα and PP2Cβ, and we call it PP2Cγ. It more closely resembles PP2Cs from
Paramecium tetraurelia and
Schizosaccharomyces pombe than mammalian PP2Cs. Northern blot analysis shows that PP2Cγ is widely expressed, and is most abundant in testis, skeletal muscle, and heart. Like known PP2Cs, recombinant PP2Cγ requires Mg
2+ or Mn
2+ for activity. Unlike any other known phosphatase, PP2Cγ has a highly acidic domain: 75% of the 54 residues are glutamate or aspartate.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9276438</pmid><doi>10.1016/S0014-5793(97)00837-5</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1997-08, Vol.412 (3), p.415-419 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Wiley Online Library Free Content; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | acidic domain Amino Acid Sequence Animals cDNA Cloning, Molecular Enzyme Activation Humans Mice Molecular Sequence Data Organ Specificity Paramecium - enzymology Paramecium - genetics Phosphoprotein Phosphatases - chemistry Phosphoprotein Phosphatases - genetics Phosphoprotein Phosphatases - isolation & purification Phylogeny Protein Phosphatase 2 Protein Phosphatase 2C Protein phosphorylation Protein Structure, Tertiary Saccharomyces cerevisiae Proteins Sequence Analysis, DNA |
| title | PP2Cγ: a human protein phosphatase with a unique acidic domain |
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