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PPM1M_MOUSE
ID   PPM1M_MOUSE             Reviewed;         462 AA.
AC   Q8BU27; E9Q2I3; Q9CSD6; Q9CU88;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 3.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Protein phosphatase 1M {ECO:0000305};
DE            EC=3.1.3.16 {ECO:0000255|PROSITE-ProRule:PRU01082};
DE   AltName: Full=Protein phosphatase 2C isoform eta;
DE            Short=PP2C-eta;
DE            Short=PP2CE;
GN   Name=Ppm1m {ECO:0000312|MGI:MGI:1915155}; Synonyms=Ppm1e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000312|EMBL:BAC40085.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAR01612.1};
RX   PubMed=14654243; DOI=10.1016/j.bbaexp.2003.09.004;
RA   Komaki K., Katsura K., Ohnishi M., Li M.G., Sasaki M., Watanabe M.,
RA   Kobayashi T., Tamura S.;
RT   "Molecular cloning of PP2Ceta, a novel member of the protein phosphatase 2C
RT   family.";
RL   Biochim. Biophys. Acta 1630:130-137(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 10-462 (ISOFORM 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Corpora quadrigemina, Head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU01082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU01082};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01082};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU01082};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000255|PROSITE-ProRule:PRU01082};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14654243}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=3;
CC         IsoId=Q8BU27-3; Sequence=Displayed;
CC       Name=1 {ECO:0000269|PubMed:14654243};
CC         IsoId=Q8BU27-1; Sequence=VSP_061129;
CC       Name=2 {ECO:0000305};
CC         IsoId=Q8BU27-2; Sequence=VSP_061128;
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in testis and
CC       lower levels in lung, kidney and brain. {ECO:0000269|PubMed:14654243}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; AY332616; AAR01612.1; -; mRNA.
DR   EMBL; AK013149; BAB28679.2; -; mRNA.
DR   EMBL; AK017245; BAB30649.1; -; mRNA.
DR   EMBL; AK046387; BAC32699.1; -; mRNA.
DR   EMBL; AK087999; BAC40085.1; -; mRNA.
DR   EMBL; AC164430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS23471.1; -. [Q8BU27-1]
DR   CCDS; CCDS23472.2; -. [Q8BU27-3]
DR   RefSeq; NP_945149.2; NM_198931.3.
DR   AlphaFoldDB; Q8BU27; -.
DR   SMR; Q8BU27; -.
DR   STRING; 10090.ENSMUSP00000117908; -.
DR   PhosphoSitePlus; Q8BU27; -.
DR   MaxQB; Q8BU27; -.
DR   PaxDb; Q8BU27; -.
DR   PRIDE; Q8BU27; -.
DR   ProteomicsDB; 291716; -. [Q8BU27-1]
DR   ProteomicsDB; 291717; -. [Q8BU27-2]
DR   ProteomicsDB; 364011; -.
DR   Antibodypedia; 31173; 172 antibodies from 24 providers.
DR   DNASU; 67905; -.
DR   GeneID; 67905; -.
DR   KEGG; mmu:67905; -.
DR   UCSC; uc012gzs.1; mouse.
DR   CTD; 132160; -.
DR   MGI; MGI:1915155; Ppm1m.
DR   VEuPathDB; HostDB:ENSMUSG00000020253; -.
DR   eggNOG; KOG1323; Eukaryota.
DR   HOGENOM; CLU_029072_2_0_1; -.
DR   InParanoid; Q8BU27; -.
DR   OMA; QATCCQI; -.
DR   OrthoDB; 601888at2759; -.
DR   PhylomeDB; Q8BU27; -.
DR   TreeFam; TF314700; -.
DR   BioGRID-ORCS; 67905; 3 hits in 74 CRISPR screens.
DR   ChiTaRS; Ppm1m; mouse.
DR   PRO; PR:Q8BU27; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q8BU27; protein.
DR   Bgee; ENSMUSG00000020253; Expressed in saccule of membranous labyrinth and 247 other tissues.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:MGI.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; -; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   PANTHER; PTHR13832; PTHR13832; 1.
DR   Pfam; PF00481; PP2C; 2.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; SSF81606; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleus; Protein phosphatase; Reference proteome.
FT   CHAIN           1..462
FT                   /note="Protein phosphatase 1M"
FT                   /id="PRO_0000057757"
FT   DOMAIN          100..452
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..28
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         127
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         127
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         128
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   VAR_SEQ         1..158
FT                   /note="MSAGWFRRRFLPGGPLPEPRPAGPRSSPVPYHRPRFLRGSGSSPGATDASRR
FT                   PDARPVRSPARGRTLPWNAGYAEVINAEKSEFNEDQAACGKLCIRRCEFGIEEDQEWLT
FT                   VCPEEFLTGHYWALFDGHGGPAAAILAANTLHSCLRRQLEAVVEGMI -> MM (in
FT                   isoform 2)"
FT                   /id="VSP_061128"
FT   VAR_SEQ         1..75
FT                   /note="MSAGWFRRRFLPGGPLPEPRPAGPRSSPVPYHRPRFLRGSGSSPGATDASRR
FT                   PDARPVRSPARGRTLPWNAGYAE -> MYVPPRTSLRVWPMLCGIR (in isoform
FT                   1)"
FT                   /id="VSP_061129"
FT   CONFLICT        10
FT                   /note="F -> V (in Ref. 2; BAB28679)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        106
FT                   /note="D -> H (in Ref. 2; BAC32699/BAB28679)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        158
FT                   /note="I -> M (in Ref. 1; AAR01612 and 2; BAC40085)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="S -> L (in Ref. 2; BAB30649)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        279
FT                   /note="F -> L (in Ref. 2; BAB30649)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   462 AA;  51204 MW;  55316E77217C5C5D CRC64;
     MSAGWFRRRF LPGGPLPEPR PAGPRSSPVP YHRPRFLRGS GSSPGATDAS RRPDARPVRS
     PARGRTLPWN AGYAEVINAE KSEFNEDQAA CGKLCIRRCE FGIEEDQEWL TVCPEEFLTG
     HYWALFDGHG GPAAAILAAN TLHSCLRRQL EAVVEGMIAP QPPMHLSGRC VCPSDPQFVE
     EKGIQAEDLV IGALENAFQE CDDVIGRELE ASGQVGGCTA LVAVFLQGKL YVANAGDSRA
     ILVRRHEIRQ LSSEFTPETE RQRIQQLAFT YPELLAGEFT RLEFPRRLKG DDLGQKVLFR
     DHHMRGWSYK RVEKSDLKYP LIHGQGRQAR LLGTLAVSRG LGDHQLRVLD TDIQLKPFLL
     SIPQVTVLDV HQLAVQEEDV VVMATDGLWD VLSNEQVALL VRSFLTGNQK DDPHRFSELA
     KMLIHNTQGK DNGATGEGQV SYDDVSVFVI PLHSQAQEGS GH
 
 
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