PPM1M_HUMAN
ID PPM1M_HUMAN Reviewed; 459 AA.
AC Q96MI6; B7XGB9; F8W976; Q8N8J9; Q96DB8;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein phosphatase 1M;
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; Synonyms=PPM1E;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000312|EMBL:BAB71302.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RX PubMed=19594441; DOI=10.1042/bj20090208;
RA Henmi T., Amano K., Nagaura Y., Matsumoto K., Echigo S., Tamura S.,
RA Kobayashi T.;
RT "A mechanism for the suppression of interleukin-1-induced nuclear factor
RT kappaB activation by protein phosphatase 2Ceta-2.";
RL Biochem. J. 423:71-78(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 26-459 (ISOFORM 2).
RC TISSUE=Peripheral blood, Prostate, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Uterus {ECO:0000312|EMBL:AAH09644.1};
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).
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:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=5;
CC IsoId=Q96MI6-5; Sequence=Displayed;
CC Name=1 {ECO:0000305};
CC IsoId=Q96MI6-1; Sequence=VSP_061125, VSP_061126, VSP_061127;
CC Name=2 {ECO:0000305};
CC IsoId=Q96MI6-2; Sequence=VSP_050663, VSP_050664;
CC Name=3 {ECO:0000305};
CC IsoId=Q96MI6-3; Sequence=VSP_050660, VSP_050661;
CC Name=4 {ECO:0000305};
CC IsoId=Q96MI6-4; Sequence=VSP_050659;
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AB474372; BAH03578.1; -; mRNA.
DR EMBL; AK056894; BAB71302.1; -; mRNA.
DR EMBL; AK096681; BAC04839.1; -; mRNA.
DR EMBL; AK129647; BAC85206.1; -; mRNA.
DR EMBL; AC006252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009644; AAH09644.1; -; mRNA.
DR CCDS; CCDS46840.1; -. [Q96MI6-4]
DR RefSeq; NP_001116342.1; NM_001122870.2. [Q96MI6-4]
DR RefSeq; NP_653242.3; NM_144641.3. [Q96MI6-5]
DR AlphaFoldDB; Q96MI6; -.
DR SMR; Q96MI6; -.
DR BioGRID; 126308; 64.
DR IntAct; Q96MI6; 7.
DR MINT; Q96MI6; -.
DR STRING; 9606.ENSP00000387046; -.
DR DEPOD; PPM1M; -.
DR iPTMnet; Q96MI6; -.
DR PhosphoSitePlus; Q96MI6; -.
DR BioMuta; PPM1M; -.
DR DMDM; 41688718; -.
DR MassIVE; Q96MI6; -.
DR PaxDb; Q96MI6; -.
DR PeptideAtlas; Q96MI6; -.
DR PRIDE; Q96MI6; -.
DR ProteomicsDB; 30278; -.
DR ProteomicsDB; 6316; -.
DR ProteomicsDB; 77361; -. [Q96MI6-1]
DR ProteomicsDB; 77362; -. [Q96MI6-2]
DR ProteomicsDB; 77363; -. [Q96MI6-3]
DR ProteomicsDB; 77364; -. [Q96MI6-4]
DR Antibodypedia; 31173; 172 antibodies from 24 providers.
DR DNASU; 132160; -.
DR Ensembl; ENST00000296487.8; ENSP00000296487.4; ENSG00000164088.18. [Q96MI6-1]
DR Ensembl; ENST00000323588.9; ENSP00000319894.5; ENSG00000164088.18. [Q96MI6-5]
DR Ensembl; ENST00000409502.7; ENSP00000387046.3; ENSG00000164088.18. [Q96MI6-4]
DR GeneID; 132160; -.
DR KEGG; hsa:132160; -.
DR MANE-Select; ENST00000323588.9; ENSP00000319894.5; NM_144641.4; NP_653242.3.
DR UCSC; uc003ddf.4; human. [Q96MI6-5]
DR UCSC; uc011bed.3; human.
DR CTD; 132160; -.
DR DisGeNET; 132160; -.
DR GeneCards; PPM1M; -.
DR HGNC; HGNC:26506; PPM1M.
DR HPA; ENSG00000164088; Low tissue specificity.
DR MIM; 608979; gene.
DR neXtProt; NX_Q96MI6; -.
DR OpenTargets; ENSG00000164088; -.
DR PharmGKB; PA142671151; -.
DR VEuPathDB; HostDB:ENSG00000164088; -.
DR eggNOG; KOG1323; Eukaryota.
DR GeneTree; ENSGT00940000161084; -.
DR HOGENOM; CLU_029072_2_0_1; -.
DR InParanoid; Q96MI6; -.
DR OMA; QATCCQI; -.
DR OrthoDB; 601888at2759; -.
DR PhylomeDB; Q96MI6; -.
DR TreeFam; TF314700; -.
DR PathwayCommons; Q96MI6; -.
DR SignaLink; Q96MI6; -.
DR BioGRID-ORCS; 132160; 7 hits in 1083 CRISPR screens.
DR ChiTaRS; PPM1M; human.
DR GenomeRNAi; 132160; -.
DR Pharos; Q96MI6; Tbio.
DR PRO; PR:Q96MI6; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96MI6; protein.
DR Bgee; ENSG00000164088; Expressed in granulocyte and 141 other tissues.
DR ExpressionAtlas; Q96MI6; baseline and differential.
DR Genevisible; Q96MI6; HS.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006470; P:protein dephosphorylation; ISS: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; 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..459
FT /note="Protein phosphatase 1M"
FT /id="PRO_0000057756"
FT DOMAIN 162..459
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 125
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 125
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 126
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT VAR_SEQ 1..290
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_050660"
FT VAR_SEQ 1..212
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_050659"
FT VAR_SEQ 1..161
FT /note="Missing (in isoform 1)"
FT /id="VSP_061125"
FT VAR_SEQ 266..284
FT /note="AFVYPELLAGEFTRLEFPR -> VGALGSMEAVKLQLLGPGP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_050663"
FT VAR_SEQ 285..459
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_050664"
FT VAR_SEQ 291..305
FT /note="LGQKVLFRDHHMSGW -> MGHRAWVDAGSAPGR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_050661"
FT VAR_SEQ 413..431
FT /note="FSKLAQMLIHSTQGKEDSL -> YCSCWGPAWAWVGASSKPK (in
FT isoform 1)"
FT /id="VSP_061126"
FT VAR_SEQ 432..459
FT /note="Missing (in isoform 1)"
FT /id="VSP_061127"
SQ SEQUENCE 459 AA; 51136 MW; 553B85833ADACCD7 CRC64;
MSAGWFRRRF LPGEPLPAPR PPGPHASPVP YRRPRFLRGS SSSPGAADAS RRPDSRPVRS
PARGRTLPWN AGYAEIINAE KSEFNEDQAA CGKLCIRRCE FGAEEEWLTL CPEEFLTGHY
WALFDGHGGP AAAILAANTL HSCLRRQLEA VVEGLVATQP PMHLNGRCIC PSDPQFVEEK
GIRAEDLVIG ALESAFQECD EVIGRELEAS GQMGGCTALV AVSLQGKLYM ANAGDSRAIL
VRRDEIRPLS FEFTPETERQ RIQQLAFVYP ELLAGEFTRL EFPRRLKGDD LGQKVLFRDH
HMSGWSYKRV EKSDLKYPLI HGQGRQARLL GTLAVSRGLG DHQLRVLDTN IQLKPFLLSV
PQVTVLDVDQ LELQEDDVVV MATDGLWDVL SNEQVAWLVR SFLPGNQEDP HRFSKLAQML
IHSTQGKEDS LTEEGQVSYD DVSVFVIPLH SQGQESSDH
