Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protein phosphatase 1K, mitochondrial (EC 3.1.3.16) (PP2C domain-containing protein phosphatase 1K) (PP2C-like mitochondrial protein) (PP2C-type mitochondrial phosphoprotein phosphatase) (PTMP) (Protein phosphatase 2C isoform kappa) (PP2C-kappa)

 PPM1K_HUMAN             Reviewed;         372 AA.
Q8N3J5; B2RAZ1; Q05CT5; Q49AB5; Q4W5E6; Q56AN8; Q8IUZ7; Q8IXG7;
Q8ND70; Q96NT4;
20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
25-OCT-2017, entry version 130.
RecName: Full=Protein phosphatase 1K, mitochondrial;
EC=3.1.3.16;
AltName: Full=PP2C domain-containing protein phosphatase 1K;
AltName: Full=PP2C-like mitochondrial protein;
AltName: Full=PP2C-type mitochondrial phosphoprotein phosphatase;
Short=PTMP;
AltName: Full=Protein phosphatase 2C isoform kappa;
Short=PP2C-kappa;
Flags: Precursor;
Name=PPM1K; Synonyms=PP2CM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TRANSIT PEPTIDE CLEAVAGE SITE, AND MUTAGENESIS OF ASP-298.
PubMed=17374715; DOI=10.1101/gad.1499107;
Lu G., Ren S., Korge P., Choi J., Dong Y., Weiss J., Koehler C.,
Chen J.-N., Wang Y.;
"A novel mitochondrial matrix serine/threonine protein phosphatase
regulates the mitochondria permeability transition pore and is
essential for cellular survival and development.";
Genes Dev. 21:784-796(2007).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Mao Y., Xie Y., Dai J.;
"Cloning and characterization of a novel human PP2C gene from fetal
brain.";
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17336929; DOI=10.1016/j.bbrc.2007.02.108;
Joshi M.A., Jeoung N.H., Popov K.M., Harris R.A.;
"Identification of a novel PP2C-type mitochondrial phosphatase.";
Biochem. Biophys. Res. Commun. 356:38-44(2007).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Xu J., Stagliano N., Deponte J. III, Rodrigue-Way A., Golden S.,
Katz S., Jeyaseelan R., Donoghue M., Meyers R., Gottfried S.,
Wysong D., McGovern K., Pollman M., Breitbart R.E., Acton S.;
"Protein phosphatase 2C kappa is upregulated in heart failure and
attenuates agonist-induced cardiomyocyte hypertrophy.";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cerebellum, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Amygdala, and Lymph node;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
LYS-94.
TISSUE=Pancreas, and Testis;
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).
[10]
INVOLVEMENT IN MSUDMV.
PubMed=23086801; DOI=10.1002/humu.22242;
Oyarzabal A., Martinez-Pardo M., Merinero B., Navarrete R.,
Desviat L.R., Ugarte M., Rodriguez-Pombo P.;
"A novel regulatory defect in the branched-chain alpha-keto acid
dehydrogenase complex due to a mutation in the PPM1K gene causes a
mild variant phenotype of maple syrup urine disease.";
Hum. Mutat. 34:355-362(2013).
[11]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 89-351, AND
MAGNESIUM-BINDING.
PubMed=18058037; DOI=10.1007/s10969-007-9036-1;
Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P.,
Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S.,
Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y.,
Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R., Sali A.,
Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.;
"Structural genomics of protein phosphatases.";
J. Struct. Funct. Genomics 8:121-140(2007).
[12]
VARIANT HIS-26.
PubMed=23200863; DOI=10.1016/j.ajhg.2012.10.024;
Charlesworth G., Plagnol V., Holmstroem K.M., Bras J., Sheerin U.M.,
Preza E., Rubio-Agusti I., Ryten M., Schneider S.A., Stamelou M.,
Trabzuni D., Abramov A.Y., Bhatia K.P., Wood N.W.;
"Mutations in ANO3 cause dominant craniocervical dystonia: ion channel
implicated in pathogenesis.";
Am. J. Hum. Genet. 91:1041-1050(2012).
-!- FUNCTION: Regulates the mitochondrial permeability transition pore
and is essential for cellular survival and development.
{ECO:0000269|PubMed:17374715}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=10.7 mM for p-nitrophenylphosphate
{ECO:0000269|PubMed:17336929};
Vmax=3.6 umol/min/mg enzyme toward p-nitrophenylphosphate (at 30
degrees Celsius) {ECO:0000269|PubMed:17336929};
Vmax=4 nmol/min/mg enzyme toward branched-chain alpha-ketoacid
dehydrogenase complex (at 37 degrees Celsius)
{ECO:0000269|PubMed:17336929};
Note=Half maximal activity toward p-nitrophenylphosphate
achieved with 3.7 mM of manganese ions.;
-!- INTERACTION:
Q13490:BIRC2; NbExp=5; IntAct=EBI-3923368, EBI-514538;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:17336929, ECO:0000269|PubMed:17374715}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8N3J5-1; Sequence=Displayed;
Name=2;
IsoId=Q8N3J5-2; Sequence=VSP_023158, VSP_023159;
Name=3;
IsoId=Q8N3J5-3; Sequence=VSP_023156, VSP_023157;
-!- DISEASE: Maple syrup urine disease, mild variant (MSUDMV)
[MIM:615135]: A mild form of maple syrup urine disease, a
metabolic disorder due to an enzyme defect in the catabolic
pathway of the branched-chain amino acids leucine, isoleucine, and
valine. Accumulation of these 3 amino acids and their
corresponding keto acids leads to encephalopathy and progressive
neurodegeneration. Clinical features include mental and physical
retardation, feeding problems, and a maple syrup odor to the
urine. The keto acids of the branched-chain amino acids are
present in the urine. If untreated, maple syrup urine disease can
lead to seizures, coma, and death. The disease is often classified
by its pattern of signs and symptoms. The most common and severe
form of the disease is the classic type, which becomes apparent
soon after birth. Variant forms of the disorder become apparent
later in infancy or childhood and are typically milder, but they
still involve developmental delay and other medical problems if
not treated. MSUDMV is characterized by increased plasma levels of
branched-chain amino acids (BCAA) apparent at birth. Treatment
with a low-protein diet free of BCAA can result in normal
psychomotor development and lack of metabolic episodes.
{ECO:0000269|PubMed:23086801}. Note=The gene represented in this
entry is involved in disease pathogenesis.
-!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
-!- CAUTION: PubMed:18058037 has crystallized PPM1K in the presence of
magnesium ions. However, PubMed:17336929 reported that no activity
toward p-nitrophenylphosphate was seen in the absence of manganese
ions and magnesium could not substitute for manganese.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY157615; AAO17296.1; -; mRNA.
EMBL; AF351614; AAN76514.1; -; mRNA.
EMBL; AY994097; AAX77016.1; -; mRNA.
EMBL; AY435431; AAR06213.1; -; mRNA.
EMBL; AK054678; BAB70790.1; -; mRNA.
EMBL; AK314417; BAG37038.1; -; mRNA.
EMBL; AL834167; CAD38869.2; -; mRNA.
EMBL; AL834271; CAD38946.1; -; mRNA.
EMBL; AC107067; AAY41021.1; -; Genomic_DNA.
EMBL; AC108213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471057; EAX06016.1; -; Genomic_DNA.
EMBL; BC020850; AAH20850.1; ALT_TERM; mRNA.
EMBL; BC037552; AAH37552.1; -; mRNA.
EMBL; BC041350; AAH41350.1; -; mRNA.
CCDS; CCDS3629.1; -. [Q8N3J5-1]
RefSeq; NP_689755.3; NM_152542.4. [Q8N3J5-1]
RefSeq; XP_006714174.1; XM_006714111.3. [Q8N3J5-1]
RefSeq; XP_016863292.1; XM_017007803.1. [Q8N3J5-1]
UniGene; Hs.43744; -.
PDB; 2IQ1; X-ray; 2.25 A; A=89-351.
PDB; 4DA1; X-ray; 2.38 A; A=84-360.
PDBsum; 2IQ1; -.
PDBsum; 4DA1; -.
ProteinModelPortal; Q8N3J5; -.
SMR; Q8N3J5; -.
BioGrid; 127472; 24.
IntAct; Q8N3J5; 9.
MINT; MINT-4725175; -.
STRING; 9606.ENSP00000295908; -.
DEPOD; Q8N3J5; -.
iPTMnet; Q8N3J5; -.
PhosphoSitePlus; Q8N3J5; -.
DMDM; 74750962; -.
PaxDb; Q8N3J5; -.
PeptideAtlas; Q8N3J5; -.
PRIDE; Q8N3J5; -.
DNASU; 152926; -.
Ensembl; ENST00000608933; ENSP00000477341; ENSG00000163644. [Q8N3J5-1]
GeneID; 152926; -.
KEGG; hsa:152926; -.
UCSC; uc003hrm.6; human. [Q8N3J5-1]
CTD; 152926; -.
DisGeNET; 152926; -.
EuPathDB; HostDB:ENSG00000163644.14; -.
GeneCards; PPM1K; -.
HGNC; HGNC:25415; PPM1K.
HPA; HPA020066; -.
HPA; HPA020862; -.
HPA; HPA023891; -.
MalaCards; PPM1K; -.
MIM; 611065; gene.
MIM; 615135; phenotype.
neXtProt; NX_Q8N3J5; -.
OpenTargets; ENSG00000163644; -.
Orphanet; 268162; Intermediate maple syrup urine disease.
PharmGKB; PA134912083; -.
eggNOG; KOG0698; Eukaryota.
eggNOG; COG0631; LUCA.
GeneTree; ENSGT00900000140907; -.
HOVERGEN; HBG096199; -.
InParanoid; Q8N3J5; -.
KO; K17505; -.
OMA; NVGCASH; -.
OrthoDB; EOG091G0A0V; -.
PhylomeDB; Q8N3J5; -.
TreeFam; TF354344; -.
BRENDA; 3.1.3.16; 2681.
Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
SIGNOR; Q8N3J5; -.
ChiTaRS; PPM1K; human.
EvolutionaryTrace; Q8N3J5; -.
GeneWiki; PPM1K; -.
GenomeRNAi; 152926; -.
PRO; PR:Q8N3J5; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000163644; -.
ExpressionAtlas; Q8N3J5; baseline and differential.
Genevisible; Q8N3J5; HS.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; TAS:Reactome.
GO; GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome.
CDD; cd00143; PP2Cc; 1.
Gene3D; 3.60.40.10; -; 1.
InterPro; IPR015655; PP2C.
InterPro; IPR000222; PP2C_BS.
InterPro; IPR036457; PPM-type_dom_sf.
InterPro; IPR001932; PPM-type_phosphatase_dom.
PANTHER; PTHR13832; PTHR13832; 1.
Pfam; PF00481; PP2C; 1.
SMART; SM00331; PP2C_SIG; 1.
SMART; SM00332; PP2Cc; 1.
SUPFAM; SSF81606; SSF81606; 1.
PROSITE; PS01032; PPM_1; 1.
PROSITE; PS51746; PPM_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Hydrolase;
Magnesium; Manganese; Metal-binding; Mitochondrion; Phosphoprotein;
Polymorphism; Protein phosphatase; Reference proteome;
Transit peptide.
TRANSIT 1 29 Mitochondrion.
{ECO:0000269|PubMed:17374715}.
CHAIN 30 372 Protein phosphatase 1K, mitochondrial.
/FTId=PRO_0000278208.
DOMAIN 94 346 PPM-type phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU01082}.
METAL 127 127 Magnesium.
METAL 128 128 Magnesium; via carbonyl oxygen.
METAL 337 337 Magnesium.
MOD_RES 248 248 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BXN7}.
VAR_SEQ 148 150 DLL -> YVQ (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_023156.
VAR_SEQ 151 372 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_023157.
VAR_SEQ 181 233 ATLLTSGTTATVALLRDGIELVVASVGDSRAILCRKGKPMK
LTIDHTPERKDE -> ENCAWSAALDLEPVDTICGASVERE
ICLILSQVKESSGSYPGLREGSHISLSH (in isoform
2). {ECO:0000303|Ref.2}.
/FTId=VSP_023158.
VAR_SEQ 234 372 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_023159.
VARIANT 26 26 R -> H (in dbSNP:rs369916009).
{ECO:0000269|PubMed:23200863}.
/FTId=VAR_069736.
VARIANT 94 94 N -> K (in dbSNP:rs17853762).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030691.
VARIANT 321 321 E -> K (in dbSNP:rs35523553).
/FTId=VAR_050621.
MUTAGEN 298 298 D->A: Loss of activity.
{ECO:0000269|PubMed:17374715}.
CONFLICT 17 17 V -> A (in Ref. 3; AAX77016).
{ECO:0000305}.
CONFLICT 194 194 L -> I (in Ref. 3; AAX77016).
{ECO:0000305}.
CONFLICT 211 211 A -> V (in Ref. 9; AAH20850).
{ECO:0000305}.
CONFLICT 264 264 I -> V (in Ref. 5; BAB70790).
{ECO:0000305}.
HELIX 92 94 {ECO:0000244|PDB:2IQ1}.
STRAND 96 100 {ECO:0000244|PDB:2IQ1}.
STRAND 103 106 {ECO:0000244|PDB:2IQ1}.
STRAND 109 115 {ECO:0000244|PDB:2IQ1}.
STRAND 117 131 {ECO:0000244|PDB:2IQ1}.
HELIX 133 149 {ECO:0000244|PDB:2IQ1}.
TURN 150 152 {ECO:0000244|PDB:2IQ1}.
HELIX 156 176 {ECO:0000244|PDB:2IQ1}.
HELIX 183 185 {ECO:0000244|PDB:2IQ1}.
STRAND 190 196 {ECO:0000244|PDB:2IQ1}.
TURN 197 199 {ECO:0000244|PDB:2IQ1}.
STRAND 200 208 {ECO:0000244|PDB:2IQ1}.
STRAND 210 215 {ECO:0000244|PDB:2IQ1}.
STRAND 218 221 {ECO:0000244|PDB:2IQ1}.
HELIX 231 239 {ECO:0000244|PDB:2IQ1}.
STRAND 244 246 {ECO:0000244|PDB:2IQ1}.
STRAND 252 254 {ECO:0000244|PDB:2IQ1}.
TURN 255 257 {ECO:0000244|PDB:2IQ1}.
HELIX 267 269 {ECO:0000244|PDB:2IQ1}.
TURN 270 273 {ECO:0000244|PDB:2IQ1}.
STRAND 279 284 {ECO:0000244|PDB:2IQ1}.
TURN 287 289 {ECO:0000244|PDB:2IQ1}.
STRAND 290 296 {ECO:0000244|PDB:2IQ1}.
HELIX 298 301 {ECO:0000244|PDB:2IQ1}.
HELIX 306 314 {ECO:0000244|PDB:2IQ1}.
STRAND 316 318 {ECO:0000244|PDB:2IQ1}.
HELIX 319 332 {ECO:0000244|PDB:2IQ1}.
STRAND 339 345 {ECO:0000244|PDB:2IQ1}.
SEQUENCE 372 AA; 40997 MW; 9DD37EEC0EAD3313 CRC64;
MSTAALITLV RSGGNQVRRR VLLSSRLLQD DRRVTPTCHS STSEPRCSRF DPDGSGSPAT
WDNFGIWDNR IDEPILLPPS IKYGKPIPKI SLENVGCASQ IGKRKENEDR FDFAQLTDEV
LYFAVYDGHG GPAAADFCHT HMEKCIMDLL PKEKNLETLL TLAFLEIDKA FSSHARLSAD
ATLLTSGTTA TVALLRDGIE LVVASVGDSR AILCRKGKPM KLTIDHTPER KDEKERIKKC
GGFVAWNSLG QPHVNGRLAM TRSIGDLDLK TSGVIAEPET KRIKLHHADD SFLVLTTDGI
NFMVNSQEIC DFVNQCHDPN EAAHAVTEQA IQYGTEDNST AVVVPFGAWG KYKNSEINFS
FSRSFASSGR WA


Related products :

Catalog number Product name Quantity
EIAAB32079 Homo sapiens,Human,PP2C domain-containing protein phosphatase 1K,PP2C-kappa,PP2C-like mitochondrial protein,PP2CM,PP2C-type mitochondrial phosphoprotein phosphatase,PPM1K,Protein phosphatase 1K, mitoc
EIAAB32080 Mouse,Mus musculus,PP2C-kappa,Pp2cm,Ppm1k,Protein phosphatase 1K, mitochondrial,Protein phosphatase 2C isoform kappa
EIAAB32078 Bos taurus,Bovine,PP2C-kappa,PPM1K,Protein phosphatase 1K, mitochondrial,Protein phosphatase 2C isoform kappa
PP-PPM1G-050 PPM1G, Protein Phosphatase 1G, PP2CG, PPP2CG, MGC1675, MGC2870, PP2C GAMMA, EC 3.1.3.16, Protein phosphatase 2C isoform gamma, PP2C-gamma, Protein phosphatase magnesium-dependent 1 gamma, Protein phos 50
EIAAB32071 Bos taurus,Bovine,Magnesium-dependent calcium inhibitable phosphatase,MCPP,PP2C-gamma,PPM1C,PPM1G,Protein phosphatase 1B,Protein phosphatase 1G,Protein phosphatase 2C isoform gamma,Protein phosphatase
20-002-35026 PP2C-alpha (anti-human PP2C-alpha. clone p6c7) - EC 3.1.3.16; PP2C-alpha; IA; Protein phosphatase 1A Monoclonal 0.1 ml
EIAAB32061 Homo sapiens,Human,p53-induced protein phosphatase 1,PP2C-delta,PPM1D,Protein phosphatase 1D,Protein phosphatase 2C isoform delta,Protein phosphatase magnesium-dependent 1 delta,WIP1
EIAAB32062 Mouse,Mus musculus,p53-induced protein phosphatase 1,PP2C-delta,Ppm1d,Protein phosphatase 1D,Protein phosphatase 2C isoform delta,Protein phosphatase magnesium-dependent 1 delta,Wip1
EIAAB32069 Homo sapiens,Human,PP2C-gamma,PPM1C,PPM1G,Protein phosphatase 1C,Protein phosphatase 1G,Protein phosphatase 2C isoform gamma,Protein phosphatase magnesium-dependent 1 gamma
EIAAB32055 Homo sapiens,Human,PP2C-alpha,PPM1A,PPPM1A,Protein phosphatase 1A,Protein phosphatase 2C isoform alpha,Protein phosphatase IA
EIAAB32081 Homo sapiens,Human,PP2CE,PP2C-epsilon,PPM1L,Protein phosphatase 1L,Protein phosphatase 1-like,Protein phosphatase 2C isoform epsilon
EIAAB32054 Pp2c1,PP2C-alpha,Ppm1a,Pppm1a,Protein phosphatase 1A,Protein phosphatase 2C isoform alpha,Protein phosphatase IA,Rat,Rattus norvegicus
EIAAB32056 Oryctolagus cuniculus,PP2C-alpha,PPM1A,PPPM1A,Protein phosphatase 1A,Protein phosphatase 2C isoform alpha,Protein phosphatase IA,Rabbit
EIAAB32070 Fibroblast growth factor-inducible protein 13,FIN13,Fin13,Mouse,Mus musculus,PP2C-gamma,Ppm1c,Ppm1g,Protein phosphatase 1C,Protein phosphatase 1G,Protein phosphatase 2C isoform gamma,Protein phosphata
EIAAB32084 Homo sapiens,Human,PP2CE,PP2C-eta,PPM1E,PPM1M,Protein phosphatase 1M,Protein phosphatase 2C isoform eta
EIAAB32085 Mouse,Mus musculus,PP2CE,PP2C-eta,Ppm1e,Ppm1m,Protein phosphatase 1M,Protein phosphatase 2C isoform eta
EIAAB32082 Kiaa4175,Mouse,Mus musculus,PP2C-epsilon,Ppm1l,Protein phosphatase 1L,Protein phosphatase 1-like,Protein phosphatase 2C isoform epsilon
EIAAB32083 Bos taurus,Bovine,PP2CE,PP2C-epsilon,PPM1L,Protein phosphatase 1L,Protein phosphatase 1-like,Protein phosphatase 2C isoform epsilon
EIAAB32053 Mouse,Mus musculus,PP2C-alpha,Ppm1a,Pppm1a,Protein phosphatase 1A,Protein phosphatase 2C isoform alpha,Protein phosphatase IA
ARP52711_P050 PPM1M(protein phosphatase 1M (PP2C domain containing)) Isoform 4 50 µg
10-002-38048 PP2C-alpha human. His-tag - EC 3.1.3.16; PP2C-alpha; IA; Protein phosphatase 1A N_A 0.5 mg
EIAAB32060 Homo sapiens,Human,PP2CB,PP2C-beta,PPM1B,Protein phosphatase 1B,Protein phosphatase 2C isoform beta
EIAAB32076 Homo sapiens,Human,PP2C-zeta,PPM1J,PPP2CZ,Protein phosphatase 1J,Protein phosphatase 2C isoform zeta
EIAAB32058 Mouse,Mus musculus,Pp2c2,PP2C-beta,Ppm1b,Pppm1b,Protein phosphatase 1B,Protein phosphatase 2C isoform beta
EIAAB32057 Pp2c2,PP2C-beta,Ppm1b,Pppm1b,Protein phosphatase 1B,Protein phosphatase 2C isoform beta,Rat,Rattus norvegicus


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur