CPPED_HUMAN
ID CPPED_HUMAN Reviewed; 314 AA.
AC Q9BRF8; B4DQ68; Q6MZY9; Q9H9M9; Q9NUT6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Serine/threonine-protein phosphatase CPPED1;
DE EC=3.1.3.16;
DE AltName: Full=Calcineurin-like phosphoesterase domain-containing protein 1;
DE AltName: Full=Complete S-transactivated protein 1;
GN Name=CPPED1; Synonyms=CSTP1;
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 [MRNA] (ISOFORM 1), VARIANTS ASP-19 AND ARG-241, AND
RP INDUCTION.
RX PubMed=15991289; DOI=10.3748/wjg.v11.i25.3893;
RA Bai G.-Q., Liu Y., Cheng J., Zhang S.-L., Yue Y.-F., Huang Y.-P.,
RA Zhang L.-Y.;
RT "Transactivating effect of complete S protein of hepatitis B virus and
RT cloning of genes transactivated by complete S protein using suppression
RT subtractive hybridization technique.";
RL World J. Gastroenterol. 11:3893-3898(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP ASP-19 AND ARG-241.
RC TISSUE=Placenta;
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 MRNA] (ISOFORM 2), AND VARIANT ARG-241.
RC TISSUE=Small intestine;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ASP-19 AND
RP ARG-241.
RC TISSUE=Placenta;
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=23939394; DOI=10.2337/db13-0830;
RA Vaittinen M., Kaminska D., Kakela P., Eskelinen M., Kolehmainen M.,
RA Pihlajamaki J., Uusitupa M., Pulkkinen L.;
RT "Downregulation of CPPED1 expression improves glucose metabolism in vitro
RT in adipocytes.";
RL Diabetes 62:3747-3750(2013).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-294, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=23799035; DOI=10.1371/journal.pone.0065679;
RA Zhuo D.X., Zhang X.W., Jin B., Zhang Z., Xie B.S., Wu C.L., Gong K.,
RA Mao Z.B.;
RT "CSTP1, a novel protein phosphatase, blocks cell cycle, promotes cell
RT apoptosis, and suppresses tumor growth of bladder cancer by directly
RT dephosphorylating Akt at Ser473 site.";
RL PLoS ONE 8:E65679-E65679(2013).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-241, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Protein phosphatase that dephosphorylates AKT family kinase
CC specifically at 'Ser-473', blocking cell cycle progression and
CC promoting cell apoptosis. May play an inhibitory role in glucose uptake
CC by adipocytes. {ECO:0000269|PubMed:23799035,
CC ECO:0000269|PubMed:23939394}.
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 Evidence={ECO:0000269|PubMed:23799035};
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 Evidence={ECO:0000269|PubMed:23799035};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23799035}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BRF8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRF8-2; Sequence=VSP_031658;
CC Name=3;
CC IsoId=Q9BRF8-3; Sequence=VSP_055218, VSP_055219;
CC -!- TISSUE SPECIFICITY: Expressed in subcutaneous adipose tissue.
CC {ECO:0000269|PubMed:23939394}.
CC -!- DEVELOPMENTAL STAGE: Expression levels are slightly decreased in
CC subcutaneous adipose tissue following weight loss. Expression levels
CC may be not affected by preadipocyte differentiation.
CC {ECO:0000269|PubMed:23939394}.
CC -!- INDUCTION: Transactivated by the large envelope protein of the
CC hepatitis B virus (HBV). {ECO:0000269|PubMed:15991289}.
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. CPPED1
CC family. {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; AY553877; AAS64575.1; -; mRNA.
DR EMBL; AK002013; BAA92034.1; -; mRNA.
DR EMBL; AK022710; BAB14194.1; -; mRNA.
DR EMBL; AK298662; BAG60830.1; -; mRNA.
DR EMBL; BX640805; CAE45887.1; -; mRNA.
DR EMBL; AC010333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006289; AAH06289.1; -; mRNA.
DR CCDS; CCDS42119.1; -. [Q9BRF8-2]
DR CCDS; CCDS42120.1; -. [Q9BRF8-1]
DR RefSeq; NP_001092925.1; NM_001099455.1. [Q9BRF8-2]
DR RefSeq; NP_060810.2; NM_018340.2. [Q9BRF8-1]
DR AlphaFoldDB; Q9BRF8; -.
DR SMR; Q9BRF8; -.
DR BioGRID; 120595; 12.
DR IntAct; Q9BRF8; 4.
DR MINT; Q9BRF8; -.
DR STRING; 9606.ENSP00000371193; -.
DR DEPOD; CPPED1; -.
DR GlyGen; Q9BRF8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BRF8; -.
DR MetOSite; Q9BRF8; -.
DR PhosphoSitePlus; Q9BRF8; -.
DR BioMuta; CPPED1; -.
DR DMDM; 317373448; -.
DR EPD; Q9BRF8; -.
DR jPOST; Q9BRF8; -.
DR MassIVE; Q9BRF8; -.
DR MaxQB; Q9BRF8; -.
DR PaxDb; Q9BRF8; -.
DR PeptideAtlas; Q9BRF8; -.
DR PRIDE; Q9BRF8; -.
DR ProteomicsDB; 78760; -. [Q9BRF8-1]
DR ProteomicsDB; 78761; -. [Q9BRF8-2]
DR Antibodypedia; 24789; 144 antibodies from 23 providers.
DR DNASU; 55313; -.
DR Ensembl; ENST00000261660.4; ENSP00000261660.4; ENSG00000103381.12. [Q9BRF8-3]
DR Ensembl; ENST00000381774.9; ENSP00000371193.4; ENSG00000103381.12. [Q9BRF8-1]
DR Ensembl; ENST00000433677.6; ENSP00000411127.2; ENSG00000103381.12. [Q9BRF8-2]
DR GeneID; 55313; -.
DR KEGG; hsa:55313; -.
DR MANE-Select; ENST00000381774.9; ENSP00000371193.4; NM_018340.3; NP_060810.2.
DR UCSC; uc002dca.5; human. [Q9BRF8-1]
DR CTD; 55313; -.
DR DisGeNET; 55313; -.
DR GeneCards; CPPED1; -.
DR HGNC; HGNC:25632; CPPED1.
DR HPA; ENSG00000103381; Low tissue specificity.
DR MIM; 615603; gene.
DR neXtProt; NX_Q9BRF8; -.
DR OpenTargets; ENSG00000103381; -.
DR PharmGKB; PA164718110; -.
DR VEuPathDB; HostDB:ENSG00000103381; -.
DR eggNOG; KOG1378; Eukaryota.
DR GeneTree; ENSGT00390000008676; -.
DR HOGENOM; CLU_077151_0_0_1; -.
DR InParanoid; Q9BRF8; -.
DR OMA; YENPSKC; -.
DR OrthoDB; 908967at2759; -.
DR PhylomeDB; Q9BRF8; -.
DR TreeFam; TF329406; -.
DR PathwayCommons; Q9BRF8; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q9BRF8; -.
DR BioGRID-ORCS; 55313; 7 hits in 1076 CRISPR screens.
DR ChiTaRS; CPPED1; human.
DR GenomeRNAi; 55313; -.
DR Pharos; Q9BRF8; Tbio.
DR PRO; PR:Q9BRF8; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9BRF8; protein.
DR Bgee; ENSG00000103381; Expressed in monocyte and 181 other tissues.
DR Genevisible; Q9BRF8; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07395; MPP_CSTP1; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041867; MPP_CSTP1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Metal-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..314
FT /note="Serine/threonine-protein phosphatase CPPED1"
FT /id="PRO_0000320556"
FT REGION 47..250
FT /note="Catalytic"
FT BINDING 53
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 97..238
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_031658"
FT VAR_SEQ 97..122
FT /note="GKPWRTEQTEDLKRVLRAVDRAIPLV -> AGQRPPRAPSRGGHRRENCSPI
FT LQSR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055218"
FT VAR_SEQ 123..314
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055219"
FT VARIANT 19
FT /note="A -> D (in dbSNP:rs3748976)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15991289"
FT /id="VAR_039204"
FT VARIANT 86
FT /note="V -> I (in dbSNP:rs3748980)"
FT /id="VAR_039205"
FT VARIANT 241
FT /note="K -> R (in dbSNP:rs1713480)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15991289,
FT ECO:0000269|PubMed:17974005, ECO:0007744|PubMed:21269460"
FT /id="VAR_039206"
FT VARIANT 290
FT /note="H -> P (in dbSNP:rs11645068)"
FT /id="VAR_039207"
FT CONFLICT 47
FT /note="K -> R (in Ref. 3; CAE45887)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="K -> E (in Ref. 2; BAA92034)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="D -> Y (in Ref. 2; BAB14194)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="K -> E (in Ref. 2; BAA92034)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 35548 MW; D2DC770103053DA7 CRC64;
MSAAEAGGVF HRARGRTLAA FPAEKESEWK GPFYFILGAD PQFGLIKAWS TGDCDNGGDE
WEQEIRLTEQ AVQAINKLNP KPKFFVLCGD LIHAMPGKPW RTEQTEDLKR VLRAVDRAIP
LVLVSGNHDI GNTPTAETVE EFCRTWGDDY FSFWVGGVLF LVLNSQFYEN PSKCPSLKQA
QDQWLDEQLS IARQRHCQHA IVFQHIPLFL ESIDEDDDYY FNLSKSTRKK LADKFIHAGV
KVVFSGHYHR NAGGTYQNLD MVVSSAIGCQ LGRDPHGLRV VVVTAEKIVH RYYSLDELSE
KGIEDDLMDL IKKK
