PPM1J_MOUSE
ID PPM1J_MOUSE Reviewed; 507 AA.
AC Q149T7; Q810X6; Q9D7H6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein phosphatase 1J;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase 2C isoform zeta;
DE Short=PP2C-zeta;
GN Name=Ppm1j; Synonyms=Ppp2cz;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH UBE2I, AND TISSUE SPECIFICITY.
RX PubMed=12633878; DOI=10.1016/s0014-5793(03)00153-4;
RA Kashiwaba M., Katsura K., Ohnishi M., Sasaki M., Tanaka H., Nishimune Y.,
RA Kobayashi T., Tamura S.;
RT "A novel protein phosphatase 2C family member (PP2Czeta) is able to
RT associate with ubiquitin conjugating enzyme 9.";
RL FEBS Lett. 538:197-202(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-507.
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-41, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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;
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;
CC -!- SUBUNIT: Interacts with UBE2I/UBC9. {ECO:0000269|PubMed:12633878}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the testicular germ
CC cells. {ECO:0000269|PubMed:12633878}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB26156.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY184802; AAO72079.1; -; mRNA.
DR EMBL; BC117498; AAI17499.1; -; mRNA.
DR EMBL; BC121788; AAI21789.1; -; mRNA.
DR EMBL; AK009235; BAB26156.1; ALT_INIT; mRNA.
DR CCDS; CCDS17703.1; -.
DR RefSeq; NP_082258.2; NM_027982.2.
DR AlphaFoldDB; Q149T7; -.
DR SMR; Q149T7; -.
DR STRING; 10090.ENSMUSP00000002298; -.
DR iPTMnet; Q149T7; -.
DR PhosphoSitePlus; Q149T7; -.
DR EPD; Q149T7; -.
DR MaxQB; Q149T7; -.
DR PaxDb; Q149T7; -.
DR PeptideAtlas; Q149T7; -.
DR PRIDE; Q149T7; -.
DR ProteomicsDB; 289382; -.
DR Antibodypedia; 33835; 86 antibodies from 21 providers.
DR DNASU; 71887; -.
DR Ensembl; ENSMUST00000002298; ENSMUSP00000002298; ENSMUSG00000002228.
DR GeneID; 71887; -.
DR KEGG; mmu:71887; -.
DR UCSC; uc008quk.1; mouse.
DR CTD; 333926; -.
DR MGI; MGI:1919137; Ppm1j.
DR VEuPathDB; HostDB:ENSMUSG00000002228; -.
DR eggNOG; KOG1323; Eukaryota.
DR GeneTree; ENSGT00940000160965; -.
DR HOGENOM; CLU_029072_0_0_1; -.
DR InParanoid; Q149T7; -.
DR OMA; TAFTQMD; -.
DR OrthoDB; 601888at2759; -.
DR PhylomeDB; Q149T7; -.
DR TreeFam; TF314700; -.
DR BioGRID-ORCS; 71887; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q149T7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q149T7; protein.
DR Bgee; ENSMUSG00000002228; Expressed in lumbar dorsal root ganglion and 94 other tissues.
DR Genevisible; Q149T7; MM.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
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; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..507
FT /note="Protein phosphatase 1J"
FT /id="PRO_0000289059"
FT DOMAIN 103..499
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JR12"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JR12"
FT CONFLICT 5
FT /note="V -> A (in Ref. 1; AAO72079)"
FT /evidence="ECO:0000305"
FT CONFLICT 61..62
FT /note="Missing (in Ref. 1; AAO72079)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="G -> GET (in Ref. 1; AAO72079)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 55550 MW; 4754E503AA8A7FE2 CRC64;
MLNRVRSAVA HLVSSGGTSS QRSKSPDLPN ATSAPPAAQE TPKSSREKPG NQVGAPQKTA
ETTVSFSRPT FLQLSPGGLR RADDHAGRAV QSPPDTGRRL PWSTGYAEVI NAGKSRHNED
QACCEVVYVE SRRSRSVTGV SREPSHNQGF CFYYWGLFDG HAGGGAAEMA SRLLHRHIRE
QLKDLVEILK DPLPPPLCLP STPGTPGAPS PSQLVSPQSC WSPQKEVTHD SLIVGAIENA
FHLMDEQMAR ERRGHQVEGG CCALVVLYLL GKMYVANAGD SRAIIVRNGE IIPMSREFTP
ETERQRLQLL GFLKPELLGS EFTHLEFPRR VQPKELGQRM LYRDQNMTGW AYKKIEVEDL
RFPLVCGEGK KARVMATIGV TRGLGDHNLK VCSSTLSIKP FLSCFPEVRV YDLTQYEHCP
DDVLVLGTDG LWDVTNDSEV AATVDRVLSS YEPNDPSRYT ALAQALVLGA RGIPRDRGWR
LPNNKLGSGD DISVFVIPLG GPGSSYS
