(data stored in ACNUC30567 zone)

HOGENOM: MOUSE5_PE2300

ID   MOUSE5_PE2300                        STANDARD;      PRT;   323 AA.
AC   MOUSE5_PE2300; P63087; O09186; O09189; P37139; Q64679;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Serine/threonine-protein phosphatase PP1-gamma catalytic
DE   subunit; Short=PP-1G; EC=3.1.3 16;AltName: Full=Protein phosphatase 1C
DE   catalytic subunit; (MOUSE5.PE2300).
GN   Name=Ppp1cc;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE5.PE2300.
CC       Mus musculus chromosome 5 NCBIM37  sequence 1..152537259 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:PP1G_MOUSE
CC   -!- FUNCTION: Protein phosphatase 1 (PP1) is essential for cell
CC       division, and participates in the regulation of glycogen
CC       metabolism, muscle contractility and protein synthesis. Involved
CC       in regulation of ionic conductances and long-term synaptic
CC       plasticity. May play an important role in dephosphorylating
CC       substrates such as the postsynaptic density-associated
CC       Ca(2+)/calmodulin dependent protein kinase II. Component of the
CC       PTW/PP1 phosphatase complex, which plays a role in the control of
CC       chromatin structure and cell cycle progression during the
CC       transition from mitosis into interphase (By similarity).
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
CC   -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or
CC       PPP1CC, which is folded into its native form by inhibitor 2 and
CC       glycogen synthetase kinase 3, and then complexed to one or several
CC       targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C
CC       mediate binding to myosin. PPP1R3A, PPP1R3B, PPP1R3C and PPP1R3D
CC       mediate binding to glycogen. Component of the MLL5-L complex, at
CC       least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB
CC       and OGT. Interacts with PPP1R3B, PPP1R7 and CDCA2 (By similarity).
CC       Isoform gamma-2 interacts with SPZ1. This interaction can prevent
CC       SPZ1 binding to the E-box and inhibits PPP1CC activity. PPP1R15A
CC       and PPP1R15B mediate binding to EIF2S1. Part of a complex
CC       containing PPP1R15B, PP1 and NCK1/2. Interacts with IKFZ1; the
CC       interaction targets PPP1CC to pericentromeric heterochromatin,
CC       dephosphorylates IKAROS, stabilizes it and prevents it from
CC       degradation. Interacts with NOM1 and PPP1R8. Component of the
CC       PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4,
CC       WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R8.
CC       Interacts with NEK2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Nucleus, nucleolus (By similarity). Cleavage furrow
CC       (By similarity). Nucleus, nucleolus (By similarity). Nucleus,
CC       nucleoplasm (By similarity). Chromosome, centromere, kinetochore
CC       (By similarity). Nucleus speckle (By similarity). Midbody (By
CC       similarity). Note=Rapidly exchanges between the nucleolar,
CC       nucleoplasmic and cytoplasmic compartments. Highly mobile in cells
CC       and can be relocalized through interaction with targeting
CC       subunits. In the presence of PPP1R8 relocalizes from the nucleolus
CC       to nuclear speckles. Shows a dynamic targeting to specific sites
CC       throughout the cell cycle. Highly concentrated in nucleoli of
CC       interphase cells and localizes at kinetochores early in mitosis.
CC       Relocalization to chromosome-containing regions occurs at the
CC       transition from early to late anaphase. Also accumulates at the
CC       cleavage furrow and midbody by telophase. Colocalizes with SPZ1 in
CC       the nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Gamma-1;
CC         IsoId=P63087-1; Sequence=Displayed;
CC       Name=Gamma-2;
CC         IsoId=P63087-2; Sequence=VSP_005095;
CC   -!- PTM: Phosphorylated by NEK2 (By similarity).
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget -
CC       Issue 32 of March 2003;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt032.shtml";
CC   -!- GENE_FAMILY: HOG000172697 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000004455;ENSMUST00000102528;ENSMUSP00000099587.
DR   EMBL; AK076009; - ;
DR   EMBL; AK088229; - ;
DR   EMBL; AK147131; - ;
DR   EMBL; AK152422; - ;
DR   EMBL; AK152625; - ;
DR   EMBL; AK153363; - ;
DR   EMBL; AK169336; - ;
DR   EMBL; BC010613; - ;
DR   EMBL; BC021646; - ;
DR   EMBL; BC085496; - ;
DR   EMBL; CH466529; - ;
DR   EMBL; CH466531; - ;
DR   EMBL; D85137; - ;
DR   EMBL; M27071; - ;
DR   EMBL; U53271; - ;
DR   EMBL; U53272; - ;
DR   EMBL; U53273; - ;
DR   EMBL; U53275; - ;
DR   EMBL; U53276; - ;
DR   EMBL; U53456; - ;
DR   UniProtKB/Swiss-Prot; P63087; O09186; O09189; P37139; Q64679; -.
DR   EMBL; M27071; AAA37526.1; -; mRNA.
DR   EMBL; U53456; AAC53383.1; -; mRNA.
DR   EMBL; U53276; AAC53384.1; -; Genomic_DNA.
DR   EMBL; U53271; AAC53384.1; JOINED; Genomic_DNA.
DR   EMBL; U53272; AAC53384.1; JOINED; Genomic_DNA.
DR   EMBL; U53273; AAC53384.1; JOINED; Genomic_DNA.
DR   EMBL; U53275; AAC53384.1; JOINED; Genomic_DNA.
DR   EMBL; U53276; AAC53385.1; -; Genomic_DNA.
DR   EMBL; U53271; AAC53385.1; JOINED; Genomic_DNA.
DR   EMBL; U53272; AAC53385.1; JOINED; Genomic_DNA.
DR   EMBL; U53273; AAC53385.1; JOINED; Genomic_DNA.
DR   EMBL; U53275; AAC53385.1; JOINED; Genomic_DNA.
DR   EMBL; D85137; BAA19729.1; -; mRNA.
DR   EMBL; BC010613; AAH10613.1; -; mRNA.
DR   EMBL; BC021646; AAH21646.1; -; mRNA.
DR   EMBL; BC085496; AAH85496.1; -; mRNA.
DR   IPI; IPI00123862; -.
DR   IPI; IPI00227773; -.
DR   PIR; C32550; C32550.
DR   RefSeq; NP_038664.2; NM_013636.3.
DR   UniGene; Mm.280784; -.
DR   ProteinModelPortal; P63087; -.
DR   SMR; P63087; 6-299.
DR   IntAct; P63087; 24.
DR   STRING; P63087; -.
DR   PhosphoSite; P63087; -.
DR   PRIDE; P63087; -.
DR   Ensembl; ENSMUST00000086294; ENSMUSP00000083474; ENSMUSG00000004455.
DR   Ensembl; ENSMUST00000102528; ENSMUSP00000099587; ENSMUSG00000004455.
DR   GeneID; 19047; -.
DR   KEGG; mmu:19047; -.
DR   CTD; 5501; -.
DR   MGI; MGI:104872; Ppp1cc.
DR   eggNOG; roNOG09668; -.
DR   GeneTree; ENSGT00530000062911; -.
DR   OMA; VGWSEND; -.
DR   OrthoDB; EOG49GKGT; -.
DR   PhylomeDB; P63087; -.
DR   NextBio; 295513; -.
DR   ArrayExpress; P63087; -.
DR   Bgee; P63087; -.
DR   Genevestigator; P63087; -.
DR   GermOnline; ENSMUSG00000044341; Mus musculus.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR   GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IMP:MGI.
DR   InterPro; IPR004843; Metallo_PEstase_dom.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR   HOGENOMDNA; MOUSE5.PE2300; -.
KW   ENSMUSG000000044555old_1320000031; ENSMUSP000000995871old_1320000031;
KW   Q3U7K1_MOUSE; Q6ZWM8_MOUSE; AK076009; AK088229; AK147131; AK152422;
KW   AK153363; AK169336; BC010613; BC021646; BC085496; CH466529; CH466531;
KW   M27071; U53271; U53272; U53273; U53275; U53276; U53456;
KW   Acetylation; Alternative splicing; Carbohydrate metabolism;
KW   Cell cycle; Cell division; Centromere; Chromosome; Complete proteome;
KW   Cytoplasm; Direct protein sequencing; Glycogen metabolism; Hydrolase;
KW   Iron; Kinetochore; Manganese; Metal-binding; Nucleus; Phosphoprotein;
KW   Protein phosphatase; Reference proteome.
SQ   SEQUENCE   323 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MADIDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK
     ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL
     LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL
     QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD
     LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE
     KKKPNATRPV TPPRGMITKQ AKK
//

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