PPM1H_RAT
ID PPM1H_RAT Reviewed; 513 AA.
AC Q5M821;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein phosphatase 1H;
DE EC=3.1.3.16;
GN Name=Ppm1h;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal
CC for proteasomal degradation. {ECO:0000250|UniProtKB:Q9ULR3}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULR3}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9ULR3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Named isoforms=2.;
CC Name=1;
CC IsoId=Q5M821-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5M821-2; Sequence=VSP_025123, VSP_025124;
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH88307.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABR03055580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03055960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03056001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03056562; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03058099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03058942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC088307; AAH88307.1; ALT_INIT; mRNA.
DR RefSeq; NP_001258008.1; NM_001271079.2. [Q5M821-1]
DR AlphaFoldDB; Q5M821; -.
DR SMR; Q5M821; -.
DR STRING; 10116.ENSRNOP00000005798; -.
DR iPTMnet; Q5M821; -.
DR PhosphoSitePlus; Q5M821; -.
DR PaxDb; Q5M821; -.
DR PRIDE; Q5M821; -.
DR Ensembl; ENSRNOT00000005798; ENSRNOP00000005798; ENSRNOG00000004314. [Q5M821-1]
DR Ensembl; ENSRNOT00000066381; ENSRNOP00000061506; ENSRNOG00000004314. [Q5M821-2]
DR GeneID; 314897; -.
DR KEGG; rno:314897; -.
DR CTD; 57460; -.
DR RGD; 1309528; Ppm1h.
DR eggNOG; KOG1323; Eukaryota.
DR GeneTree; ENSGT00940000160095; -.
DR HOGENOM; CLU_029072_2_0_1; -.
DR InParanoid; Q5M821; -.
DR OMA; KEHVEWT; -.
DR OrthoDB; 601888at2759; -.
DR PhylomeDB; Q5M821; -.
DR TreeFam; TF314700; -.
DR PRO; PR:Q5M821; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004314; Expressed in kidney and 20 other tissues.
DR ExpressionAtlas; Q5M821; baseline and differential.
DR Genevisible; Q5M821; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
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 Alternative splicing; Cytoplasm; Hydrolase; Methylation; Nucleus;
KW Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..513
FT /note="Protein phosphatase 1H"
FT /id="PRO_0000286605"
FT DOMAIN 77..506
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 110..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UYC0"
FT MOD_RES 113
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULR3"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULR3"
FT MOD_RES 212
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3UYC0"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULR3"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULR3"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULR3"
FT VAR_SEQ 1..319
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025123"
FT VAR_SEQ 320..357
FT /note="MQPHLLGNEFTHLEFPRRVQRKELGKKMLYRDFNMTGW -> MEEFRYKYVP
FT WSSEIQQEGGGMRATVSTRKKTASEMIR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025124"
SQ SEQUENCE 513 AA; 56380 MW; 4CA4B69E70C106FD CRC64;
MLTRVKSAVA NFMGGIMAGS SGSEHGGSGC GGSDLPLRFP YGRPEFLGLS QDEVECSADH
IARPILILKE TRRLPWATGY AEVINAGKST HNEDQASCEV LTVKKKVGTI TSTPNRNSKR
RSSLPNGEGL QLKENSESEG ISCHYWSLFD GHAGSGAAVV ASRLLQHHIT QQLQDIVEIL
KNSAILPPTC LGEEPESTPA HGRTLTRAAS LRGGVGAPGS PSTPPTRFFT EKKIPHECLV
IGALESAFKE MDLQIERERS AYNISGGCTA LIVVCLLGKL YVANAGDSRA IIIRNGEIIP
MSSEFTPETE RQRLQYLAFM QPHLLGNEFT HLEFPRRVQR KELGKKMLYR DFNMTGWAYK
TIEDDDLKFP LIYGEGKKAR VMATIGVTRG LGDHDLKVHD SNIYIKPFLS SAPEVRVYDL
SKYEHGADDV LILATDGLWD VLSNEEVAEA ITQFLPNCDP DDPHRYTLAA QDLVMRARGV
LKDRGWRISN DRLGSGDDIS VYVIPLIHGN KLS
