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Serine/threonine-protein phosphatase 5 (PP5) (EC 3.1.3.16) (Protein phosphatase T) (PPT)

 PPP5_RAT                Reviewed;         499 AA.
P53042;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
20-JUN-2018, entry version 154.
RecName: Full=Serine/threonine-protein phosphatase 5;
Short=PP5;
EC=3.1.3.16;
AltName: Full=Protein phosphatase T;
Short=PPT;
Name=Ppp5c;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Testis;
PubMed=8077208;
Becker W., Kentrup H., Klumpp S., Schultz J.E., Joost H.G.;
"Molecular cloning of a protein serine/threonine phosphatase
containing a putative regulatory tetratricopeptide repeat domain.";
J. Biol. Chem. 269:22586-22592(1994).
[2]
FUNCTION AS PHOSPHATASE, ENZYME REGULATION, AND MUTAGENESIS OF GLU-29;
LYS-32; GLU-56; ILE-63; ARG-74; GLU-76; CYS-77; TYR-80; LYS-97 AND
ARG-101.
PubMed=11523989; DOI=10.1021/bi010999i;
Kang H., Sayner S.L., Gross K.L., Russell L.C., Chinkers M.;
"Identification of amino acids in the tetratricopeptide repeat and C-
terminal domains of protein phosphatase 5 involved in autoinhibition
and lipid activation.";
Biochemistry 40:10485-10490(2001).
[3]
COFACTOR, ENZYME REGULATION, AND CATALYTIC ACTIVITY.
PubMed=11969423; DOI=10.1021/bi016090h;
Ramsey A.J., Chinkers M.;
"Identification of potential physiological activators of protein
phosphatase 5.";
Biochemistry 41:5625-5632(2002).
[4]
FUNCTION AS PHOSPHATASE, INTERACTION WITH GNA12 AND GNA13, AND
SUBCELLULAR LOCATION.
PubMed=12176367; DOI=10.1016/S0960-9822(02)01034-5;
Yamaguchi Y., Katoh H., Mori K., Negishi M.;
"Galpha(12) and Galpha(13) interact with Ser/Thr protein phosphatase
type 5 and stimulate its phosphatase activity.";
Curr. Biol. 12:1353-1358(2002).
[5]
FUNCTION IN DEPHOSPHORYLATING MAPT, BIOPHYSICOCHEMICAL PROPERTIES, AND
TISSUE SPECIFICITY.
PubMed=15546861; DOI=10.1074/jbc.M410775200;
Liu F., Iqbal K., Grundke-Iqbal I., Rossie S., Gong C.X.;
"Dephosphorylation of tau by protein phosphatase 5: impairment in
Alzheimer's disease.";
J. Biol. Chem. 280:1790-1796(2005).
[6]
FUNCTION IN MAPK SIGNALING.
PubMed=16892053; DOI=10.1038/ncb1465;
von Kriegsheim A., Pitt A., Grindlay G.J., Kolch W., Dhillon A.S.;
"Regulation of the Raf-MEK-ERK pathway by protein phosphatase 5.";
Nat. Cell Biol. 8:1011-1016(2006).
[7]
FUNCTION IN RAC1 SIGNALING, ENZYME REGULATION, INTERACTION WITH RAC1,
AND MUTAGENESIS OF LYS-93; LYS-126 AND TYR-451.
PubMed=16549782; DOI=10.1073/pnas.0600080103;
Gentile S., Darden T., Erxleben C., Romeo C., Russo A., Martin N.,
Rossie S., Armstrong D.L.;
"Rac GTPase signaling through the PP5 protein phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 103:5202-5206(2006).
[8]
INTERACTION WITH CRY1 AND CRY2.
PubMed=16790549; DOI=10.1073/pnas.0604138103;
Partch C.L., Shields K.F., Thompson C.L., Selby C.P., Sancar A.;
"Posttranslational regulation of the mammalian circadian clock by
cryptochrome and protein phosphatase 5.";
Proc. Natl. Acad. Sci. U.S.A. 103:10467-10472(2006).
[9]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 16-499 IN COMPLEX WITH
MAGNESIUM, COFACTOR, AND INTERACTION WITH HSP90AA1.
PubMed=26182372; DOI=10.1042/BSR20150042;
Haslbeck V., Drazic A., Eckl J.M., Alte F., Helmuth M., Popowicz G.,
Schmidt W., Braun F., Weiwad M., Fischer G., Gemmecker G., Sattler M.,
Striggow F., Groll M., Richter K.;
"Selective activators of protein phosphatase 5 target the
autoinhibitory mechanism.";
Biosci. Rep. 35:E00210-E00210(2015).
-!- FUNCTION: Serine/threonine-protein phosphatase that
dephosphorylates a myriad of proteins involved in different
signaling pathways including the kinases CSNK1E, ASK1/MAP3K5,
PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2,
SMAD proteins and TAU/MAPT. Implicated in wide ranging cellular
processes, including apoptosis, differentiation, DNA damage
response, cell survival, regulation of ion channels or circadian
rhythms, in response to steroid and thyroid hormones, calcium,
fatty acids, TGF-beta as well as oxidative and genotoxic stresses.
Participates in the control of DNA damage response mechanisms such
as checkpoint activation and DNA damage repair through, for
instance, the regulation ATM/ATR-signaling and dephosphorylation
of PRKDC and TP53BP1. Inhibits ASK1/MAP3K5-mediated apoptosis
induced by oxidative stress. Plays a positive role in
adipogenesis, mainly through the dephosphorylation and activation
of PPARG transactivation function. Also dephosphorylates and
inhibits the anti-adipogenic effect of NR3C1. Regulates the
circadian rhythms, through the dephosphorylation and activation of
CSNK1E. May modulate TGF-beta signaling pathway by the regulation
of SMAD3 phosphorylation and protein expression levels.
Dephosphorylates and may play a role in the regulation of
TAU/MAPT. Through their dephosphorylation, may play a role in the
regulation of ions channels such as KCNH2.
{ECO:0000269|PubMed:11523989, ECO:0000269|PubMed:12176367,
ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16549782,
ECO:0000269|PubMed:16892053}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
{ECO:0000269|PubMed:11969423}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11969423,
ECO:0000269|PubMed:26182372};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:11969423,
ECO:0000269|PubMed:26182372};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000269|PubMed:11969423, ECO:0000269|PubMed:26182372};
-!- ENZYME REGULATION: Autoinhibited. In the autoinhibited state, the
TPR domain interacts with the catalytic region and prevents
substrate access to the catalytic pocket. Allosterically activated
by various polyunsaturated fatty acids, free long-chain fatty-
acids and long-chain fatty acyl-CoA esters, arachidonic acid being
the most effective activator. HSP90A and probably RAC1, GNA12 and
GNA13 can also release the autoinhibition by the TPR repeat.
Activation by RAC1, GNA12 and GNA13 is synergistic with the one
produced by fatty acids binding. Inhibited by okadaic acid.
{ECO:0000269|PubMed:11523989, ECO:0000269|PubMed:11969423,
ECO:0000269|PubMed:16549782}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=12.1 uM for MAPT/TAU (at pH 7.4 and 30 degrees Celsius)
{ECO:0000269|PubMed:15546861};
-!- SUBUNIT: Probably forms a complex composed of chaperones HSP90 and
HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and
client protein TSC2 (By similarity). Probably forms a complex
composed of chaperones HSP90 and HSP70, co-chaperones CDC37,
PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1;
this complex does not contain co-chaperones STIP1/HOP and
PTGES3/p23 (By similarity). Part of a complex with HSP90/HSP90AA1
and steroid receptors (By similarity). Interacts (via TPR repeats)
with HSP90AA1 (via TPR repeat-binding motif) or HSPA1A/HSPA1B; the
interaction is direct and activates the phosphatase activity
(PubMed:26182372). Dissociates from HSPA1A/HSPA1B and HSP90AA1 in
response to arachidonic acid (By similarity). Interacts with CPNE1
(via VWFA domain) (By similarity). Interacts with CDC16, CDC27 (By
similarity). Interacts with KLHDC10 (via the 6 Kelch repeats);
inhibits the phosphatase activity on MAP3K5 (By similarity).
Interacts with ATM and ATR; both interactions are induced by DNA
damage and enhance ATM and ATR kinase activity (By similarity).
Interacts with RAD17; reduced by DNA damage (By similarity).
Interacts with nuclear receptors such as NR3C1/GCR and PPARG
(activated by agonist); regulates their transactivation activities
(By similarity). Interacts (via TPR repeats) with S100 proteins
S100A1, S100A2, S100A6, S100B and S100P; the interactions are
calcium-dependent, strongly activate PPP5C phosphatase activity
and compete with HSP90AA1 and MAP3K5 interactions (By similarity).
Interacts with SMAD2 and SMAD3 but not with SMAD1; decreases SMAD3
phosphorylation and protein levels (By similarity). Interacts (via
TPR repeats) with CRY1 and CRY2; the interaction with CRY2
downregulates the phosphatase activity on CSNK1E
(PubMed:16790549). Interacts (via TPR repeats) with the active
form of RAC1, GNA12 or GNA13; these interactions activate the
phosphatase activity and translocate PPP5C to the cell membrane
(PubMed:12176367, PubMed:16549782). Interacts with FLCN (By
similarity). {ECO:0000250|UniProtKB:P53041,
ECO:0000250|UniProtKB:Q60676, ECO:0000269|PubMed:12176367,
ECO:0000269|PubMed:16549782, ECO:0000269|PubMed:16790549,
ECO:0000269|PubMed:26182372}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12176367}.
Cytoplasm {ECO:0000269|PubMed:12176367}. Cell membrane
{ECO:0000250|UniProtKB:P53041}. Note=Predominantly nuclear. But
also present in the cytoplasm. Translocates from the cytoplasm to
the plasma membrane in a RAC1-dependent manner.
{ECO:0000250|UniProtKB:P53041}.
-!- TISSUE SPECIFICITY: Predominantly found in brain and, in lower
levels, in testis, but was nearly undetectable in spleen, lung,
skeletal muscle, kidney and liver. {ECO:0000269|PubMed:15546861}.
-!- PTM: Activated by at least two different proteolytic cleavages
producing a 56 kDa and a 50 kDa form. {ECO:0000250}.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-5 (PP-T)
subfamily. {ECO:0000305}.
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EMBL; X77237; CAA54454.1; -; mRNA.
PIR; A55346; A55346.
RefSeq; NP_113917.1; NM_031729.1.
UniGene; Rn.6107; -.
PDB; 4JA7; X-ray; 2.00 A; A=16-499.
PDB; 4JA9; X-ray; 2.30 A; A=16-499.
PDBsum; 4JA7; -.
PDBsum; 4JA9; -.
ProteinModelPortal; P53042; -.
SMR; P53042; -.
DIP; DIP-61212N; -.
IntAct; P53042; 2.
STRING; 10116.ENSRNOP00000023078; -.
iPTMnet; P53042; -.
PhosphoSitePlus; P53042; -.
SwissPalm; P53042; -.
PaxDb; P53042; -.
PRIDE; P53042; -.
Ensembl; ENSRNOT00000023078; ENSRNOP00000023078; ENSRNOG00000016907.
GeneID; 65179; -.
KEGG; rno:65179; -.
UCSC; RGD:68415; rat.
CTD; 5536; -.
RGD; 68415; Ppp5c.
eggNOG; KOG0376; Eukaryota.
eggNOG; COG0639; LUCA.
GeneTree; ENSGT00530000063173; -.
HOGENOM; HOG000172698; -.
HOVERGEN; HBG000216; -.
InParanoid; P53042; -.
KO; K04460; -.
OMA; LYPNHFF; -.
OrthoDB; EOG091G0589; -.
PhylomeDB; P53042; -.
TreeFam; TF105562; -.
BRENDA; 3.1.3.16; 5301.
Reactome; R-RNO-5675221; Negative regulation of MAPK pathway.
Reactome; R-RNO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-RNO-8939211; ESR-mediated signaling.
SABIO-RK; P53042; -.
PRO; PR:P53042; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000016907; -.
Genevisible; P53042; RN.
GO; GO:0071944; C:cell periphery; IDA:RGD.
GO; GO:0101031; C:chaperone complex; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:1990635; C:proximal dendrite; IDA:RGD.
GO; GO:0043531; F:ADP binding; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:Ensembl.
GO; GO:0001965; F:G-protein alpha-subunit binding; IDA:RGD.
GO; GO:0031072; F:heat shock protein binding; IPI:RGD.
GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008017; F:microtubule binding; IDA:RGD.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:ARUK-UCL.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0071276; P:cellular response to cadmium ion; IEP:RGD.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
GO; GO:0016576; P:histone dephosphorylation; IDA:RGD.
GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:RGD.
GO; GO:2000324; P:positive regulation of glucocorticoid receptor signaling pathway; IMP:RGD.
GO; GO:0051259; P:protein complex oligomerization; IDA:RGD.
GO; GO:0006470; P:protein dephosphorylation; IDA:RGD.
GO; GO:0051291; P:protein heterooligomerization; IPI:RGD.
GO; GO:1904550; P:response to arachidonic acid; IDA:ARUK-UCL.
GO; GO:0010288; P:response to lead ion; IDA:ARUK-UCL.
GO; GO:0043278; P:response to morphine; IEA:Ensembl.
Gene3D; 1.25.40.10; -; 1.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR013235; PPP_dom.
InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
InterPro; IPR011236; Ser/Thr_PPase_5.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR001440; TPR_1.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR11668:SF391; PTHR11668:SF391; 1.
Pfam; PF00149; Metallophos; 1.
Pfam; PF08321; PPP5; 1.
Pfam; PF00515; TPR_1; 1.
PRINTS; PR00114; STPHPHTASE.
SMART; SM00156; PP2Ac; 1.
SMART; SM00028; TPR; 3.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PROSITE; PS50005; TPR; 3.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell membrane; Complete proteome;
Cytoplasm; Hydrolase; Magnesium; Manganese; Membrane; Metal-binding;
Nucleus; Protein phosphatase; Reference proteome; Repeat; TPR repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P53041}.
CHAIN 2 499 Serine/threonine-protein phosphatase 5.
/FTId=PRO_0000058897.
REPEAT 28 61 TPR 1.
REPEAT 62 95 TPR 2.
REPEAT 96 129 TPR 3.
REGION 200 499 Catalytic.
REGION 303 304 Substrate binding.
{ECO:0000250|UniProtKB:P53041}.
REGION 495 499 Required for autoinhibition.
{ECO:0000269|PubMed:11523989}.
ACT_SITE 304 304 Proton donor/acceptor.
{ECO:0000250|UniProtKB:P53041}.
METAL 242 242 Magnesium 1. {ECO:0000244|PDB:4JA7,
ECO:0000269|PubMed:26182372}.
METAL 244 244 Magnesium 1; via tele nitrogen.
{ECO:0000244|PDB:4JA7,
ECO:0000269|PubMed:26182372}.
METAL 271 271 Magnesium 1. {ECO:0000244|PDB:4JA7,
ECO:0000269|PubMed:26182372}.
METAL 271 271 Magnesium 2. {ECO:0000244|PDB:4JA7,
ECO:0000244|PDB:4JA9,
ECO:0000269|PubMed:26182372}.
METAL 303 303 Magnesium 2. {ECO:0000244|PDB:4JA7,
ECO:0000244|PDB:4JA9,
ECO:0000269|PubMed:26182372}.
METAL 352 352 Magnesium 2; via tele nitrogen.
{ECO:0000244|PDB:4JA7,
ECO:0000244|PDB:4JA9,
ECO:0000269|PubMed:26182372}.
METAL 427 427 Magnesium 2; via pros nitrogen.
{ECO:0000244|PDB:4JA7,
ECO:0000244|PDB:4JA9,
ECO:0000269|PubMed:26182372}.
BINDING 244 244 Substrate.
{ECO:0000250|UniProtKB:P53041}.
BINDING 275 275 Substrate.
{ECO:0000250|UniProtKB:P53041}.
BINDING 400 400 Substrate.
{ECO:0000250|UniProtKB:P53041}.
BINDING 427 427 Substrate.
{ECO:0000250|UniProtKB:P53041}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P53041}.
MUTAGEN 29 29 E->A: No effect on phosphatase activity.
{ECO:0000269|PubMed:11523989}.
MUTAGEN 32 32 K->A: No effect on phosphatase activity.
{ECO:0000269|PubMed:11523989}.
MUTAGEN 40 40 K->A: Slightly reduces activation by
arachidonic acid.
MUTAGEN 56 56 E->A: No effect on phosphatase activity.
{ECO:0000269|PubMed:11523989}.
MUTAGEN 63 63 I->A: No effect on phosphatase activity.
{ECO:0000269|PubMed:11523989}.
MUTAGEN 74 74 R->A: No effect on phosphatase activity.
{ECO:0000269|PubMed:11523989}.
MUTAGEN 76 76 E->A: Increases basal phosphatase
activity. {ECO:0000269|PubMed:11523989}.
MUTAGEN 77 77 C->A: No effect on phosphatase activity.
{ECO:0000269|PubMed:11523989}.
MUTAGEN 80 80 Y->A: No effect on phosphatase activity.
{ECO:0000269|PubMed:11523989}.
MUTAGEN 93 93 K->E: Loss of inhibition of KCNH2 channel
stimulation.
{ECO:0000269|PubMed:16549782}.
MUTAGEN 97 97 K->A: No effect on phosphatase activity.
{ECO:0000269|PubMed:11523989}.
MUTAGEN 101 101 R->A: No effect on phosphatase activity.
{ECO:0000269|PubMed:11523989}.
MUTAGEN 126 126 K->A: Loss of inhibition of KCNH2 channel
stimulation.
{ECO:0000269|PubMed:16549782}.
MUTAGEN 451 451 Y->A: Insensitive to okadaic acid.
{ECO:0000269|PubMed:16549782}.
HELIX 24 40 {ECO:0000244|PDB:4JA7}.
HELIX 44 57 {ECO:0000244|PDB:4JA7}.
HELIX 62 74 {ECO:0000244|PDB:4JA7}.
HELIX 78 91 {ECO:0000244|PDB:4JA7}.
HELIX 96 108 {ECO:0000244|PDB:4JA7}.
HELIX 112 125 {ECO:0000244|PDB:4JA7}.
HELIX 130 148 {ECO:0000244|PDB:4JA7}.
HELIX 161 164 {ECO:0000244|PDB:4JA7}.
HELIX 167 169 {ECO:0000244|PDB:4JA7}.
HELIX 188 199 {ECO:0000244|PDB:4JA7}.
HELIX 206 221 {ECO:0000244|PDB:4JA7}.
STRAND 225 229 {ECO:0000244|PDB:4JA7}.
STRAND 236 240 {ECO:0000244|PDB:4JA7}.
HELIX 247 257 {ECO:0000244|PDB:4JA7}.
STRAND 262 264 {ECO:0000244|PDB:4JA9}.
STRAND 266 270 {ECO:0000244|PDB:4JA7}.
STRAND 273 276 {ECO:0000244|PDB:4JA7}.
HELIX 279 292 {ECO:0000244|PDB:4JA7}.
TURN 294 296 {ECO:0000244|PDB:4JA7}.
STRAND 297 300 {ECO:0000244|PDB:4JA7}.
HELIX 307 313 {ECO:0000244|PDB:4JA7}.
HELIX 315 322 {ECO:0000244|PDB:4JA7}.
HELIX 325 335 {ECO:0000244|PDB:4JA7}.
STRAND 340 344 {ECO:0000244|PDB:4JA7}.
TURN 345 347 {ECO:0000244|PDB:4JA7}.
STRAND 348 353 {ECO:0000244|PDB:4JA7}.
STRAND 357 359 {ECO:0000244|PDB:4JA9}.
HELIX 363 367 {ECO:0000244|PDB:4JA7}.
STRAND 372 374 {ECO:0000244|PDB:4JA7}.
STRAND 377 379 {ECO:0000244|PDB:4JA7}.
HELIX 380 386 {ECO:0000244|PDB:4JA7}.
STRAND 391 397 {ECO:0000244|PDB:4JA7}.
STRAND 401 406 {ECO:0000244|PDB:4JA7}.
HELIX 408 418 {ECO:0000244|PDB:4JA7}.
STRAND 422 425 {ECO:0000244|PDB:4JA7}.
STRAND 433 437 {ECO:0000244|PDB:4JA7}.
HELIX 438 440 {ECO:0000244|PDB:4JA7}.
STRAND 442 445 {ECO:0000244|PDB:4JA7}.
HELIX 451 453 {ECO:0000244|PDB:4JA7}.
STRAND 459 465 {ECO:0000244|PDB:4JA7}.
STRAND 468 476 {ECO:0000244|PDB:4JA7}.
TURN 486 489 {ECO:0000244|PDB:4JA7}.
HELIX 492 494 {ECO:0000244|PDB:4JA9}.
SEQUENCE 499 AA; 56917 MW; 720A7FB7AFC701D2 CRC64;
MAMAEGERTE CAEPPRDEPP AEGTLKRAEE LKTQANDYFK AKDYENAIKF YSQAIELNPS
NAIYYGNRSL AYLRTECYGY ALGDATRAIE LDKKYIKGYY RRAASNMALG KFRAALRDYE
TVVKVKPNDK DAKMKYQECS KIVKQKAFER AIAGDEHRRS VVDSLDIESM TIEDEYSGPK
LEDGKVTITF MKDLMQWYKD QKKLHRKCAY QILVQVKEVL CKLSTLVETT LKETEKITVC
GDTHGQFYDL LNIFELNGLP SETNPYIFNG DFVDRGSFSV EVILTLFGFK LLYPDHFHLL
RGNHETDNMN QIYGFEGEVK AKYTAQMYEL FSEVFEWLPL AQCINGKVLI MHGGLFSEDG
VTLDDIRKIE RNRQPPDSGP MCDLLWSDPQ PQNGRSVSKR GVSCQFGPDV TKAFLEENQL
DYIIRSHEVK AEGYEVAHGG RCVTVFSAPN YCDQMGNKAS YIHLQGSDLR PQFHQFTAVP
HPNVKPMAYA NTLLQLGMM


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H0473 Serine threonine-protein phosphatase 5 (PPP5C), Rat, ELISA Kit 96T
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
RPR-515 Recombinant Human Proline-Serine-Threonine Phosphatase Interacting Protein 1 5
SHCBP_MOUSE Rat ELISA Kit FOR Serine per threonine-protein phosphatase 4 catalytic subunit 96T
PGM2_HUMAN Human ELISA Kit FOR Serine per threonine-protein phosphatase with EF-hands 1 96T
H0472 Serine threonine-protein phosphatase 5 (PPP5C), Rabbit, ELISA Kit 96T
15-288-21557 Proline-serine-threonine phosphatase-interacting protein 2 - Polyclonal 0.05 mg
H0470 Serine threonine-protein phosphatase 5 (PPP5C), Human, ELISA Kit 96T
E0544h Rabbit ELISA Kit FOR Serine per threonine-protein phosphatase 2A activator 96T
CE80 Serine Threonine-Protein Phosphatase PP1-y Catalytic Subunit PPP1CC 500
E0505r Human ELISA Kit FOR Serine per threonine-protein phosphatase with EF-hands 1 96T
3BHS_CANFA Rat ELISA Kit FOR Serine per threonine-protein phosphatase 4 catalytic subunit 96T
H0511 Serine threonine-protein phosphatase with EF-hands 1 (PPEF1), Rat, ELISA Kit 96T
PA2GE_MOUSE Rabbit ELISA Kit FOR Serine per threonine-protein phosphatase 2A activator 96T
E0035m Rat ELISA Kit FOR Serine per threonine-protein phosphatase 4 catalytic subunit 96T
15-288-21557 Proline-serine-threonine phosphatase-interacting protein 2 - Polyclonal 0.1 mg
CE80 Serine Threonine-Protein Phosphatase PP1-y Catalytic Subunit PPP1CC lmg
H0471 Serine threonine-protein phosphatase 5 (PPP5C), Mouse, ELISA Kit 96T
ZN107_HUMAN Human ELISA Kit FOR Serine per threonine-protein phosphatase 6 catalytic subunit 96T
E0791h Human ELISA Kit FOR Serine per threonine-protein phosphatase 4 catalytic subunit 96T
H0411 Serine threonine-protein phosphatase 1 regulatory subunit 10 (PPP1R10), Pig, ELISA Kit 96T


 

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