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Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (PP-1G) (EC 3.1.3.16) (Protein phosphatase 1C catalytic subunit)

 PP1G_HUMAN              Reviewed;         323 AA.
P36873;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
25-OCT-2017, entry version 207.
RecName: Full=Serine/threonine-protein phosphatase PP1-gamma catalytic subunit;
Short=PP-1G;
EC=3.1.3.16;
AltName: Full=Protein phosphatase 1C catalytic subunit;
Name=PPP1CC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GAMMA-1 AND GAMMA-2).
PubMed=8394140; DOI=10.1016/0167-4889(93)90014-G;
Barker H.M., Craig S.P., Spurr N.K., Cohen P.T.W.;
"Sequence of human protein serine/threonine phosphatase 1 gamma and
localization of the gene (PPP1CC) encoding it to chromosome bands
12q24.1-q24.2.";
Biochim. Biophys. Acta 1178:228-233(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 2-15; 44-60; 99-122; 151-168 AND 247-260, CLEAVAGE
OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[4]
PROTEIN SEQUENCE OF 2-15; 27-36; 44-60; 99-111; 133-141; 151-187 AND
239-260, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Bilsland A.E., Keith W.N.;
Submitted (JAN-2010) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 5-323 (ISOFORM GAMMA-1).
TISSUE=Skeletal muscle;
PubMed=8111128; DOI=10.1007/BF00360567;
Norman S.A., Mott D.M.;
"Molecular cloning and chromosomal localization of a human skeletal
muscle PP-1 gamma 1 cDNA.";
Mamm. Genome 5:41-45(1994).
[6]
INTERACTION WITH MICROCYSTIN, AND MUTAGENESIS OF CYS-273.
PubMed=7556599; DOI=10.1016/0014-5793(95)00888-G;
MacKintosh R.W., Dalby K.N., Campbell D.G., Cohen P.T.W., Cohen P.,
MacKintosh C.;
"The cyanobacterial toxin microcystin binds covalently to cysteine-273
on protein phosphatase 1.";
FEBS Lett. 371:236-240(1995).
[7]
INTERACTION WITH PPP1R3D.
PubMed=9414128; DOI=10.1016/S0014-5793(97)01385-9;
Armstrong C.G., Browne G.J., Cohen P., Cohen P.T.W.;
"PPP1R6, a novel member of the family of glycogen-targeting subunits
of protein phosphatase 1.";
FEBS Lett. 418:210-214(1997).
[8]
SUBCELLULAR LOCATION, INTERACTION WITH PPP1R8, AND MUTAGENESIS OF
HIS-125.
PubMed=11739654;
Trinkle-Mulcahy L., Sleeman J.E., Lamond A.I.;
"Dynamic targeting of protein phosphatase 1 within the nuclei of
living mammalian cells.";
J. Cell Sci. 114:4219-4228(2001).
[9]
INTERACTION WITH PPP1R15A.
PubMed=11564868; DOI=10.1128/MCB.21.20.6841-6850.2001;
Connor J.H., Weiser D.C., Li S., Hallenbeck J.M., Shenolikar S.;
"Growth arrest and DNA damage-inducible protein GADD34 assembles a
novel signaling complex containing protein phosphatase 1 and inhibitor
1.";
Mol. Cell. Biol. 21:6841-6850(2001).
[10]
INTERACTION WITH PPP1R7.
PubMed=12226088; DOI=10.1074/jbc.M206838200;
Ceulemans H., Vulsteke V., De Maeyer M., Tatchell K., Stalmans W.,
Bollen M.;
"Binding of the concave surface of the Sds22 superhelix to the alpha
4/alpha 5/alpha 6-triangle of protein phosphatase-1.";
J. Biol. Chem. 277:47331-47337(2002).
[11]
SUBCELLULAR LOCATION.
PubMed=12529430; DOI=10.1091/mbc.E02-07-0376;
Trinkle-Mulcahy L., Andrews P.D., Wickramasinghe S., Sleeman J.,
Prescott A., Lam Y.W., Lyon C., Swedlow J.R., Lamond A.I.;
"Time-lapse imaging reveals dynamic relocalization of PP1gamma
throughout the mammalian cell cycle.";
Mol. Biol. Cell 14:107-117(2003).
[12]
INTERACTION WITH NEK2, AND PHOSPHORYLATION.
PubMed=15659832; DOI=10.1196/annals.1329.059;
Fardilha M., Wu W., Sa R., Fidalgo S., Sousa C., Mota C.,
da Cruz e Silva O.A., da Cruz e Silva E.F.;
"Alternatively spliced protein variants as potential therapeutic
targets for male infertility and contraception.";
Ann. N. Y. Acad. Sci. 1030:468-478(2004).
[13]
ENZYME REGULATION.
PubMed=15705855; DOI=10.1126/science.1101902;
Boyce M., Bryant K.F., Jousse C., Long K., Harding H.P., Scheuner D.,
Kaufman R.J., Ma D., Coen D.M., Ron D., Yuan J.;
"A selective inhibitor of eIF2alpha dephosphorylation protects cells
from ER stress.";
Science 307:935-939(2005).
[14]
INTERACTION WITH CDCA2.
PubMed=16492807; DOI=10.1083/jcb.200508154;
Trinkle-Mulcahy L., Andersen J., Lam Y.W., Moorhead G., Mann M.,
Lamond A.I.;
"Repo-Man recruits PP1 gamma to chromatin and is essential for cell
viability.";
J. Cell Biol. 172:679-692(2006).
[15]
INTERACTION WITH NEK2.
PubMed=17283141; DOI=10.1158/0008-5472.CAN-06-3071;
Mi J., Guo C., Brautigan D.L., Larner J.M.;
"Protein phosphatase-1alpha regulates centrosome splitting through
Nek2.";
Cancer Res. 67:1082-1089(2007).
[16]
FUNCTION IN DEPHOSPHORYLATION OF RPS6KB1, ENZYME REGULATION,
INTERACTION WITH URI1, SUBCELLULAR LOCATION, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=17936702; DOI=10.1016/j.molcel.2007.08.010;
Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M.,
Aebersold R., Hess D., Krek W.;
"S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes
activates a negative feedback program that counters S6K1 survival
signaling.";
Mol. Cell 28:28-40(2007).
[17]
SUBCELLULAR LOCATION, AND INTERACTION WITH NOM1.
PubMed=17965019; DOI=10.1074/jbc.M706708200;
Gunawardena S.R., Ruis B.L., Meyer J.A., Kapoor M., Conklin K.F.;
"NOM1 targets protein phosphatase I to the nucleolus.";
J. Biol. Chem. 283:398-404(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
IDENTIFICATION IN THE MLL5-L COMPLEX.
PubMed=19377461; DOI=10.1038/nature07954;
Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G.,
Kitagawa H., Kato S.;
"GlcNAcylation of a histone methyltransferase in retinoic-acid-induced
granulopoiesis.";
Nature 459:455-459(2009).
[20]
IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, AND
INTERACTION WITH PPP1R8.
PubMed=20516061; DOI=10.1074/jbc.M110.109801;
Lee J.H., You J., Dobrota E., Skalnik D.G.;
"Identification and characterization of a novel human PP1 phosphatase
complex.";
J. Biol. Chem. 285:24466-24476(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
FUNCTION IN CIRCADIAN CLOCK.
PubMed=21712997; DOI=10.1371/journal.pone.0021325;
Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.;
"Protein phosphatase 1 (PP1) is a post-translational regulator of the
mammalian circadian clock.";
PLoS ONE 6:E21325-E21325(2011).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
FUNCTION, INTERACTION WITH FOXP3, AND INDUCTION.
PubMed=23396208; DOI=10.1038/nm.3085;
Nie H., Zheng Y., Li R., Guo T.B., He D., Fang L., Liu X., Xiao L.,
Chen X., Wan B., Chin Y.E., Zhang J.Z.;
"Phosphorylation of FOXP3 controls regulatory T cell function and is
inhibited by TNF-alpha in rheumatoid arthritis.";
Nat. Med. 19:322-328(2013).
[26]
INTERACTION WITH MKI67.
PubMed=24867636; DOI=10.7554/eLife.01641;
Booth D.G., Takagi M., Sanchez-Pulido L., Petfalski E., Vargiu G.,
Samejima K., Imamoto N., Ponting C.P., Tollervey D., Earnshaw W.C.,
Vagnarelli P.;
"Ki-67 is a PP1-interacting protein that organises the mitotic
chromosome periphery.";
Elife 3:E01641-E01641(2014).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[29]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS, AND ACTIVE SITE.
PubMed=7500362; DOI=10.1006/jmbi.1995.0667;
Egloff M.-P., Cohen P.T.W., Reinemer P., Barford D.;
"Crystal structure of the catalytic subunit of human protein
phosphatase 1 and its complex with tungstate.";
J. Mol. Biol. 254:942-959(1995).
[30]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MANGANESE, AND
COFACTOR.
PubMed=11535607; DOI=10.1074/jbc.M107656200;
Maynes J.T., Bateman K.S., Cherney M.M., Das A.K., Luu H.A.,
Holmes C.F., James M.N.;
"Crystal structure of the tumor-promoter okadaic acid bound to protein
phosphatase-1.";
J. Biol. Chem. 276:44078-44082(2001).
[31]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 6-298 IN COMPLEX WITH
MANGANESE, CATALYTIC ACTIVITY, AND COFACTOR.
PubMed=15280359; DOI=10.1074/jbc.M407184200;
Maynes J.T., Perreault K.R., Cherney M.M., Luu H.A., James M.N.,
Holmes C.F.;
"Crystal structure and mutagenesis of a protein phosphatase-
1:calcineurin hybrid elucidate the role of the beta12-beta13 loop in
inhibitor binding.";
J. Biol. Chem. 279:43198-43206(2004).
-!- FUNCTION: Protein phosphatase that associates with over 200
regulatory proteins to form highly specific holoenzymes which
dephosphorylate hundreds of biological targets. Protein
phosphatase 1 (PP1) is essential for cell division, and
participates in the regulation of glycogen metabolism, muscle
contractility and protein synthesis. Dephosphorylates RPS6KB1.
Involved in regulation of ionic conductances and long-term
synaptic plasticity. May play an important role in
dephosphorylating substrates such as the postsynaptic density-
associated Ca(2+)/calmodulin dependent protein kinase II.
Component of the PTW/PP1 phosphatase complex, which plays a role
in the control of chromatin structure and cell cycle progression
during the transition from mitosis into interphase. In balance
with CSNK1D and CSNK1E, determines the circadian period length,
through the regulation of the speed and rhythmicity of PER1 and
PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E.
Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-
cells (Treg) from patients with rheumatoid arthritis, thereby
inactivating FOXP3 and rendering Treg cells functionally defective
(PubMed:23396208). {ECO:0000269|PubMed:17936702,
ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:21712997,
ECO:0000269|PubMed:23396208}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
{ECO:0000269|PubMed:15280359}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:11535607,
ECO:0000269|PubMed:15280359};
Note=Binds 2 manganese ions per subunit.
{ECO:0000269|PubMed:11535607, ECO:0000269|PubMed:15280359};
-!- ENZYME REGULATION: Inactivated by binding to URI1. The phosphatase
activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically
inhibited by Salubrinal, a drug that protects cells from
endoplasmic reticulum stress. {ECO:0000269|PubMed:15705855,
ECO:0000269|PubMed:17936702}.
-!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or
PPP1CC, which is folded into its native form by inhibitor 2 and
glycogen synthetase kinase 3, and then complexed to one or several
targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C
mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B
(in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate
binding to glycogen. Interacts with cyanobacterial toxin
microcystin; disulfide-linked. Interacts with PPP1R3B and PPP1R7.
Isoform gamma-2 interacts with SPZ1 (By similarity). Component of
the MLL5-L complex, at least composed of KMT2E/MLL5, STK38,
PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with CDCA2.
PPP1R15A and PPP1R15B mediate binding to EIF2S1. Part of a complex
containing PPP1R15B, PP1 and NCK1/2. Interacts with IKFZ1; the
interaction targets PPP1CC to pericentromeric heterochromatin,
dephosphorylates IKAROS, stabilizes it and prevents it from
degradation. Interacts with PPP1R42; the interaction is direct (By
similarity). Interacts with NOM1 and PPP1R8. Component of the
PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4,
WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R8.
Interacts with isoform 1 and isoform 4 NEK2. Interacts with URI1;
the interaction is phosphorylation-dependent and occurs in a
growth factor-dependent manner. Interacts with FOXP3. Interacts
with TMEM225 (via RVxF motif) (By similarity). Interacts with
MKI67 (PubMed:24867636). {ECO:0000250|UniProtKB:P63087,
ECO:0000269|PubMed:11535607, ECO:0000269|PubMed:11564868,
ECO:0000269|PubMed:11739654, ECO:0000269|PubMed:12226088,
ECO:0000269|PubMed:15280359, ECO:0000269|PubMed:15659832,
ECO:0000269|PubMed:16492807, ECO:0000269|PubMed:17283141,
ECO:0000269|PubMed:17936702, ECO:0000269|PubMed:17965019,
ECO:0000269|PubMed:19377461, ECO:0000269|PubMed:20516061,
ECO:0000269|PubMed:23396208, ECO:0000269|PubMed:24867636,
ECO:0000269|PubMed:7556599, ECO:0000269|PubMed:9414128}.
-!- INTERACTION:
A1DRY3:-; NbExp=2; IntAct=EBI-3964623, EBI-4311408;
P38398:BRCA1; NbExp=2; IntAct=EBI-356283, EBI-349905;
O95400:CD2BP2; NbExp=3; IntAct=EBI-356283, EBI-768015;
O08785:Clock (xeno); NbExp=2; IntAct=EBI-356283, EBI-79859;
Q96S65:CSRNP1; NbExp=3; IntAct=EBI-356283, EBI-4311573;
Q9H175:CSRNP2; NbExp=5; IntAct=EBI-356283, EBI-5235958;
O15294:OGT; NbExp=11; IntAct=EBI-356283, EBI-539828;
P41236:PPP1R2; NbExp=7; IntAct=EBI-356283, EBI-1056517;
Q7Z5V6:PPP1R32; NbExp=4; IntAct=EBI-3964623, EBI-4311771;
Q15435:PPP1R7; NbExp=5; IntAct=EBI-356283, EBI-1024281;
Q96S59:RANBP9; NbExp=3; IntAct=EBI-3964623, EBI-636085;
Q5JR98:TCTEX1D4; NbExp=3; IntAct=EBI-3964623, EBI-4311709;
P04637:TP53; NbExp=2; IntAct=EBI-356289, EBI-366083;
Q13625:TP53BP2; NbExp=8; IntAct=EBI-356283, EBI-77642;
Q13625-3:TP53BP2; NbExp=3; IntAct=EBI-356283, EBI-10175039;
O94763:URI1; NbExp=17; IntAct=EBI-356283, EBI-357067;
O94763-1:URI1; NbExp=8; IntAct=EBI-356283, EBI-12590720;
O95405:ZFYVE9; NbExp=5; IntAct=EBI-356283, EBI-296817;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus.
Nucleus, nucleoplasm. Nucleus speckle. Chromosome, centromere,
kinetochore. Cleavage furrow. Midbody. Mitochondrion.
Note=Colocalizes with SPZ1 in the nucleus (By similarity).
Colocalizes with URI1 at mitochondrion. Rapidly exchanges between
the nucleolar, nucleoplasmic and cytoplasmic compartments. Highly
mobile in cells and can be relocalized through interaction with
targeting subunits. In the presence of PPP1R8 relocalizes from the
nucleolus to nuclear speckles. Shows a dynamic targeting to
specific sites throughout the cell cycle. Highly concentrated in
nucleoli of interphase cells and localizes at kinetochores early
in mitosis. Relocalization to chromosome-containing regions occurs
at the transition from early to late anaphase. Also accumulates at
the cleavage furrow and midbody by telophase. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Gamma-1;
IsoId=P36873-1; Sequence=Displayed;
Name=Gamma-2;
IsoId=P36873-2; Sequence=VSP_005094;
-!- INDUCTION: Up-regulated in synovial fluid mononuclear cells and
peripheral blood mononuclear cells from patients with rheumatoid
arthritis. {ECO:0000269|PubMed:23396208}.
-!- PTM: Phosphorylated by NEK2. {ECO:0000269|PubMed:15659832}.
-!- MISCELLANEOUS: Microcystin toxin is bound to Cys-273 through a
thioether bond.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget
- Issue 32 of March 2003;
URL="http://web.expasy.org/spotlight/back_issues/032";
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EMBL; X74008; CAA52169.1; -; mRNA.
EMBL; BC014073; AAH14073.1; -; mRNA.
EMBL; L07395; AAA19823.1; -; mRNA.
CCDS; CCDS58279.1; -. [P36873-2]
CCDS; CCDS9150.1; -. [P36873-1]
PIR; S35699; S35699.
PIR; S35700; S35700.
RefSeq; NP_001231903.1; NM_001244974.1. [P36873-2]
RefSeq; NP_002701.1; NM_002710.3. [P36873-1]
UniGene; Hs.79081; -.
PDB; 1IT6; X-ray; 2.00 A; A/B=1-323.
PDB; 1JK7; X-ray; 1.90 A; A=1-323.
PDB; 1U32; X-ray; 2.00 A; A=6-298.
PDB; 2BCD; X-ray; 2.10 A; A=1-323.
PDB; 2BDX; X-ray; 2.30 A; A=1-323.
PDB; 4UT2; X-ray; 1.96 A; A/B=1-323.
PDB; 4UT3; X-ray; 2.19 A; A/B=1-323.
PDB; 5INB; X-ray; 1.30 A; A=7-308.
PDB; 5J28; X-ray; 2.00 A; A/B=7-308.
PDBsum; 1IT6; -.
PDBsum; 1JK7; -.
PDBsum; 1U32; -.
PDBsum; 2BCD; -.
PDBsum; 2BDX; -.
PDBsum; 4UT2; -.
PDBsum; 4UT3; -.
PDBsum; 5INB; -.
PDBsum; 5J28; -.
ProteinModelPortal; P36873; -.
SMR; P36873; -.
BioGrid; 111495; 304.
DIP; DIP-749N; -.
IntAct; P36873; 232.
MINT; MINT-190765; -.
STRING; 9606.ENSP00000335084; -.
BindingDB; P36873; -.
ChEMBL; CHEMBL4438; -.
DrugBank; DB02860; Calyculin A.
DrugBank; DB04738; Motuporin.
DEPOD; P36873; -.
iPTMnet; P36873; -.
PhosphoSitePlus; P36873; -.
SwissPalm; P36873; -.
BioMuta; PPP1CC; -.
DMDM; 548573; -.
EPD; P36873; -.
MaxQB; P36873; -.
PaxDb; P36873; -.
PeptideAtlas; P36873; -.
PRIDE; P36873; -.
TopDownProteomics; P36873-1; -. [P36873-1]
TopDownProteomics; P36873-2; -. [P36873-2]
DNASU; 5501; -.
Ensembl; ENST00000335007; ENSP00000335084; ENSG00000186298. [P36873-1]
Ensembl; ENST00000340766; ENSP00000341779; ENSG00000186298. [P36873-2]
GeneID; 5501; -.
KEGG; hsa:5501; -.
UCSC; uc001tru.4; human. [P36873-1]
CTD; 5501; -.
DisGeNET; 5501; -.
EuPathDB; HostDB:ENSG00000186298.11; -.
GeneCards; PPP1CC; -.
HGNC; HGNC:9283; PPP1CC.
HPA; CAB022645; -.
MIM; 176914; gene.
neXtProt; NX_P36873; -.
OpenTargets; ENSG00000186298; -.
PharmGKB; PA33611; -.
eggNOG; ENOG410IN85; Eukaryota.
eggNOG; ENOG410XPVF; LUCA.
GeneTree; ENSGT00530000062911; -.
HOGENOM; HOG000172697; -.
HOVERGEN; HBG000216; -.
InParanoid; P36873; -.
KO; K06269; -.
OMA; HECEEIN; -.
OrthoDB; EOG091G0EKF; -.
PhylomeDB; P36873; -.
TreeFam; TF354243; -.
BRENDA; 3.1.3.16; 2681.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-163560; Triglyceride catabolism.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-68877; Mitotic Prometaphase.
SignaLink; P36873; -.
SIGNOR; P36873; -.
ChiTaRS; PPP1CC; human.
EvolutionaryTrace; P36873; -.
GeneWiki; PPP1CC; -.
GenomeRNAi; 5501; -.
PRO; PR:P36873; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000186298; -.
CleanEx; HS_PPP1CC; -.
ExpressionAtlas; P36873; baseline and differential.
Genevisible; P36873; HS.
GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IMP:UniProtKB.
GO; GO:0072357; C:PTW/PP1 phosphatase complex; IDA:UniProtKB.
GO; GO:0005521; F:lamin binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
GO; GO:0004721; F:phosphoprotein phosphatase activity; TAS:Reactome.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IDA:MGI.
GO; GO:0008157; F:protein phosphatase 1 binding; IEA:Ensembl.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
GO; GO:0006470; P:protein dephosphorylation; IMP:MGI.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IEA:Ensembl.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
InterPro; IPR031675; STPPase_N.
Pfam; PF00149; Metallophos; 1.
Pfam; PF16891; STPPase_N; 1.
PRINTS; PR00114; STPHPHTASE.
SMART; SM00156; PP2Ac; 1.
SUPFAM; SSF56300; SSF56300; 1.
PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Biological rhythms;
Carbohydrate metabolism; Cell cycle; Cell division; Centromere;
Chromosome; Complete proteome; Cytoplasm; Direct protein sequencing;
Disulfide bond; Glycogen metabolism; Hydrolase; Kinetochore;
Manganese; Metal-binding; Mitochondrion; Nucleus; Phosphoprotein;
Polymorphism; Protein phosphatase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.3, ECO:0000269|Ref.4}.
CHAIN 2 323 Serine/threonine-protein phosphatase PP1-
gamma catalytic subunit.
/FTId=PRO_0000058787.
ACT_SITE 125 125 Proton donor.
{ECO:0000269|PubMed:7500362}.
METAL 64 64 Manganese 1.
{ECO:0000269|PubMed:11535607,
ECO:0000269|PubMed:15280359}.
METAL 66 66 Manganese 1.
{ECO:0000269|PubMed:11535607,
ECO:0000269|PubMed:15280359}.
METAL 92 92 Manganese 1.
{ECO:0000269|PubMed:11535607,
ECO:0000269|PubMed:15280359}.
METAL 92 92 Manganese 2.
{ECO:0000269|PubMed:11535607,
ECO:0000269|PubMed:15280359}.
METAL 124 124 Manganese 2.
{ECO:0000269|PubMed:11535607,
ECO:0000269|PubMed:15280359}.
METAL 173 173 Manganese 2.
{ECO:0000269|PubMed:11535607,
ECO:0000269|PubMed:15280359}.
METAL 248 248 Manganese 2.
{ECO:0000269|PubMed:11535607,
ECO:0000269|PubMed:15280359}.
SITE 273 273 Inhibition by microcystin toxin binding.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.3, ECO:0000269|Ref.4}.
MOD_RES 307 307 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 311 311 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 315 323 GMITKQAKK -> VASGLNPSIQKASNYRNNTVLYE (in
isoform Gamma-2).
{ECO:0000303|PubMed:8394140}.
/FTId=VSP_005094.
VARIANT 152 152 F -> S (in dbSNP:rs11558237).
/FTId=VAR_051734.
MUTAGEN 125 125 H->A: Loss of activity.
{ECO:0000269|PubMed:11739654}.
MUTAGEN 273 273 C->A,S,L: Abolishes interaction with
microcystin toxin.
{ECO:0000269|PubMed:7556599}.
HELIX 9 17 {ECO:0000244|PDB:5INB}.
HELIX 18 21 {ECO:0000244|PDB:5INB}.
HELIX 32 48 {ECO:0000244|PDB:5INB}.
STRAND 51 55 {ECO:0000244|PDB:5INB}.
STRAND 57 62 {ECO:0000244|PDB:5INB}.
HELIX 69 79 {ECO:0000244|PDB:5INB}.
STRAND 87 89 {ECO:0000244|PDB:5INB}.
STRAND 94 98 {ECO:0000244|PDB:5INB}.
HELIX 100 113 {ECO:0000244|PDB:5INB}.
TURN 115 117 {ECO:0000244|PDB:5INB}.
STRAND 118 120 {ECO:0000244|PDB:5INB}.
HELIX 128 131 {ECO:0000244|PDB:5INB}.
TURN 132 135 {ECO:0000244|PDB:4UT3}.
HELIX 136 143 {ECO:0000244|PDB:5INB}.
HELIX 146 156 {ECO:0000244|PDB:5INB}.
STRAND 162 165 {ECO:0000244|PDB:5INB}.
TURN 166 168 {ECO:0000244|PDB:5INB}.
STRAND 169 174 {ECO:0000244|PDB:5INB}.
HELIX 183 187 {ECO:0000244|PDB:5INB}.
STRAND 197 199 {ECO:0000244|PDB:5INB}.
HELIX 200 206 {ECO:0000244|PDB:5INB}.
STRAND 214 218 {ECO:0000244|PDB:5INB}.
STRAND 222 227 {ECO:0000244|PDB:5INB}.
HELIX 229 239 {ECO:0000244|PDB:5INB}.
STRAND 243 246 {ECO:0000244|PDB:5INB}.
STRAND 254 258 {ECO:0000244|PDB:5INB}.
TURN 259 262 {ECO:0000244|PDB:5INB}.
STRAND 263 267 {ECO:0000244|PDB:5INB}.
HELIX 272 274 {ECO:0000244|PDB:5INB}.
STRAND 280 285 {ECO:0000244|PDB:5INB}.
STRAND 290 298 {ECO:0000244|PDB:5INB}.
SEQUENCE 323 AA; 36984 MW; 0EEEF0E842188536 CRC64;
MADLDKLNID 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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