PPM1N_HUMAN
ID PPM1N_HUMAN Reviewed; 430 AA.
AC Q8N819; Q6P662;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable protein phosphatase 1N;
DE EC=3.1.3.16;
GN Name=PPM1N;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain;
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;
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N819-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N819-2; Sequence=VSP_035234, VSP_035235;
CC Name=3;
CC IsoId=Q8N819-3; Sequence=VSP_035233;
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AC138534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471126; EAW57360.1; -; Genomic_DNA.
DR EMBL; AK097444; BAC05056.1; -; mRNA.
DR EMBL; BC028228; AAH28228.1; -; mRNA.
DR EMBL; BC062452; AAH62452.1; -; mRNA.
DR CCDS; CCDS46115.1; -. [Q8N819-1]
DR RefSeq; NP_001073870.1; NM_001080401.1. [Q8N819-1]
DR AlphaFoldDB; Q8N819; -.
DR SMR; Q8N819; -.
DR BioGRID; 127077; 2.
DR IntAct; Q8N819; 1.
DR STRING; 9606.ENSP00000397050; -.
DR DEPOD; PPM1N; -.
DR BioMuta; PPM1N; -.
DR DMDM; 205829293; -.
DR MassIVE; Q8N819; -.
DR PaxDb; Q8N819; -.
DR PeptideAtlas; Q8N819; -.
DR PRIDE; Q8N819; -.
DR ProteomicsDB; 72364; -. [Q8N819-1]
DR ProteomicsDB; 72365; -. [Q8N819-2]
DR Antibodypedia; 31351; 9 antibodies from 6 providers.
DR DNASU; 147699; -.
DR Ensembl; ENST00000396735.6; ENSP00000379961.2; ENSG00000213889.11. [Q8N819-3]
DR Ensembl; ENST00000396737.6; ENSP00000379963.1; ENSG00000213889.11. [Q8N819-3]
DR Ensembl; ENST00000401705.5; ENSP00000384318.1; ENSG00000213889.11. [Q8N819-3]
DR Ensembl; ENST00000451287.7; ENSP00000397050.2; ENSG00000213889.11. [Q8N819-1]
DR GeneID; 147699; -.
DR KEGG; hsa:147699; -.
DR MANE-Select; ENST00000451287.7; ENSP00000397050.2; NM_001080401.2; NP_001073870.1.
DR UCSC; uc002pce.4; human. [Q8N819-1]
DR CTD; 147699; -.
DR DisGeNET; 147699; -.
DR GeneCards; PPM1N; -.
DR HGNC; HGNC:26845; PPM1N.
DR HPA; ENSG00000213889; Tissue enriched (skeletal).
DR neXtProt; NX_Q8N819; -.
DR OpenTargets; ENSG00000213889; -.
DR PharmGKB; PA165394107; -.
DR VEuPathDB; HostDB:ENSG00000213889; -.
DR eggNOG; KOG0697; Eukaryota.
DR GeneTree; ENSGT00940000162694; -.
DR HOGENOM; CLU_146811_0_0_1; -.
DR InParanoid; Q8N819; -.
DR OMA; LWTACKK; -.
DR OrthoDB; 957254at2759; -.
DR PhylomeDB; Q8N819; -.
DR PathwayCommons; Q8N819; -.
DR SignaLink; Q8N819; -.
DR BioGRID-ORCS; 147699; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; PPM1N; human.
DR GenomeRNAi; 147699; -.
DR Pharos; Q8N819; Tdark.
DR PRO; PR:Q8N819; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8N819; protein.
DR Bgee; ENSG00000213889; Expressed in monocyte and 94 other tissues.
DR ExpressionAtlas; Q8N819; baseline and differential.
DR Genevisible; Q8N819; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 1.10.10.430; -; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR012911; PP2C_C.
DR InterPro; IPR036580; PP2C_C_sf.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR Pfam; PF00481; PP2C; 1.
DR Pfam; PF07830; PP2C_C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81601; SSF81601; 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 Protein phosphatase; Reference proteome.
FT CHAIN 1..430
FT /note="Probable protein phosphatase 1N"
FT /id="PRO_0000349231"
FT DOMAIN 66..326
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 16..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..318
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035233"
FT VAR_SEQ 1..78
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_035234"
FT VAR_SEQ 314..430
FT /note="GSLDNMTCILVCFPGAPRPSEEAIRRELALDAALGCRIAELCASAQKPPSLN
FT TVFRTLASEDIPDLPPGGGLDCKATVIAEVYSQICQVSEECGEKGQDGAGKSNPTHLGS
FT ALDMEA -> VLGAWRGTFGAWCSRGREPRGFGEEGFDREARVKLAKEGIGLKRRAWPE
FT VGRAKIQGRSLRDALRHGRVSGRDLRERAWSFGKGRFWVVGAGPEVLISAGRWKSR
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_035235"
SQ SEQUENCE 430 AA; 46170 MW; 297363BEB0E73F22 CRC64;
MAVLARQLQR LLWTACKKKE REKEGREEEE EEEAGRRAPE GPRSLLTAPR RAQRPHGGAE
ASGGLRFGAS AAQGWRARME DAHCTWLSLP GLPPGWALFA VLDGHGGARA ARFGARHLPG
HVLQELGPEP SEPEGVREAL RRAFLSADER LRSLWPRVET GGCTAVVLLV SPRFLYLAHC
GDSRAVLSRA GAVAFSTEDH RPLRPRERER IHAAGGTIRR RRVEGSLAVS RALGDFTYKE
APGRPPELQL VSAEPEVAAL ARQAEDEFML LASDGVWDTV SGAALAGLVA SRLRLGLAPE
LLCAQLLDTC LCKGSLDNMT CILVCFPGAP RPSEEAIRRE LALDAALGCR IAELCASAQK
PPSLNTVFRT LASEDIPDLP PGGGLDCKAT VIAEVYSQIC QVSEECGEKG QDGAGKSNPT
HLGSALDMEA
