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Polyphosphatidylinositol phosphatase INP53 (Suppressor of PMA1 protein 2) (Synaptojanin-like protein 3) [Includes: SAC1-like phosphoinositide phosphatase (EC 3.1.3.-); Phosphatidylinositol 4,5-bisphosphate 5-phosphatase (EC 3.1.3.36)]

 INP53_YEAST             Reviewed;        1107 AA.
Q12271; D6W2G8;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 135.
RecName: Full=Polyphosphatidylinositol phosphatase INP53;
AltName: Full=Suppressor of PMA1 protein 2;
AltName: Full=Synaptojanin-like protein 3;
Includes:
RecName: Full=SAC1-like phosphoinositide phosphatase;
EC=3.1.3.-;
Includes:
RecName: Full=Phosphatidylinositol 4,5-bisphosphate 5-phosphatase;
EC=3.1.3.36;
Name=INP53; Synonyms=SJL3, SOP2; OrderedLocusNames=YOR109W;
ORFNames=YOR3231w;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9200815;
DOI=10.1002/(SICI)1097-0061(19970615)13:7<655::AID-YEA120>3.0.CO;2-I;
Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
Schwager C., Paces V., Sander C., Ansorge W.;
"DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
Yeast 13:655-672(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION.
PubMed=9265642; DOI=10.1083/jcb.138.4.731;
Luo W.-J., Chang A.;
"Novel genes involved in endosomal traffic in yeast revealed by
suppression of a targeting-defective plasma membrane ATPase mutant.";
J. Cell Biol. 138:731-746(1997).
[5]
FUNCTION.
PubMed=9560389;
Stolz L.E., Huynh C.V., Thorner J., York J.D.;
"Identification and characterization of an essential family of
inositol polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene
products) in the yeast Saccharomyces cerevisiae.";
Genetics 148:1715-1729(1998).
[6]
FUNCTION.
PubMed=9788876;
Singer-Krueger B., Nemoto Y., Daniell L., Ferro-Novick S.,
De Camilli P.;
"Synaptojanin family members are implicated in endocytic membrane
traffic in yeast.";
J. Cell Sci. 111:3347-3356(1998).
[7]
FUNCTION, AND DOMAIN.
PubMed=10224048; DOI=10.1074/jbc.274.19.12990;
Guo S., Stolz L.E., Lemrow S.M., York J.D.;
"SAC1-like domains of yeast SAC1, INP52, and INP53 and of human
synaptojanin encode polyphosphoinositide phosphatases.";
J. Biol. Chem. 274:12990-12995(1999).
[8]
FUNCTION.
PubMed=10029994;
DOI=10.1002/(SICI)1097-0061(19990130)15:2<155::AID-YEA342>3.0.CO;2-U;
Saiz J.E., de Los Angeles Santos M., Vazquez de Aldana C.R.,
Revuelta J.L.;
"Disruption of six unknown open reading frames from Saccharomyces
cerevisiae reveals two genes involved in vacuolar morphogenesis and
one gene required for sporulation.";
Yeast 15:155-164(1999).
[9]
FUNCTION.
PubMed=10628971;
Bensen E.S., Costaguta G., Payne G.S.;
"Synthetic genetic interactions with temperature-sensitive clathrin in
Saccharomyces cerevisiae. Roles for synaptojanin-like Inp53p and
dynamin-related Vps1p in clathrin-dependent protein sorting at the
trans-Golgi network.";
Genetics 154:83-97(2000).
[10]
FUNCTION.
PubMed=10625610; DOI=10.1074/jbc.275.2.801;
Hughes W.E., Woscholski R., Cooke F.T., Patrick R.S., Dove S.K.,
McDonald N.Q., Parker P.J.;
"SAC1 encodes a regulated lipid phosphoinositide phosphatase, defects
in which can be suppressed by the homologous Inp52p and Inp53p
phosphatases.";
J. Biol. Chem. 275:801-808(2000).
[11]
FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
PubMed=11094088; DOI=10.1128/MCB.20.24.9376-9390.2000;
Ooms L.M., McColl B.K., Wiradjaja F., Wijayaratnam A.P.W., Gleeson P.,
Gething M.J., Sambrook J.F., Mitchell C.A.;
"The yeast inositol polyphosphate 5-phosphatases inp52p and inp53p
translocate to actin patches following hyperosmotic stress: mechanism
for regulating phosphatidylinositol 4,5-bisphosphate at plasma
membrane invaginations.";
Mol. Cell. Biol. 20:9376-9390(2000).
[12]
FUNCTION.
PubMed=11598201; DOI=10.1091/mbc.12.10.3175;
Ha S.-A., Bunch J.T., Hama H., DeWald D.B., Nothwehr S.F.;
"A novel mechanism for localizing membrane proteins to yeast trans-
Golgi network requires function of synaptojanin-like protein.";
Mol. Biol. Cell 12:3175-3190(2001).
[13]
INTERACTION WITH BSP1.
PubMed=12606027; DOI=10.1016/S0014-5793(03)00067-X;
Wicky S., Frischmuth S., Singer-Krueger B.;
"Bsp1p/Ypr171p is an adapter that directly links some synaptojanin
family members to the cortical actin cytoskeleton in yeast.";
FEBS Lett. 537:35-41(2003).
[14]
FUNCTION, DOMAINS, MUTAGENESIS OF CYS-421; CYS-424; ARG-427; ASP-746
AND ASN-748, AND INTERACTION WITH CHC1.
PubMed=12686590; DOI=10.1091/mbc.E02-10-0686;
Ha S.-A., Torabinejad J., DeWald D.B., Wenk M.R., Lucast L.,
De Camilli P., Newitt R.A., Aebersold R., Nothwehr S.F.;
"The synaptojanin-like protein Inp53/Sjl3 functions with clathrin in a
yeast TGN-to-endosome pathway distinct from the GGA protein-dependent
pathway.";
Mol. Biol. Cell 14:1319-1333(2003).
[15]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[16]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[17]
FUNCTION.
PubMed=15169871; DOI=10.1091/mbc.E04-03-0209;
Parrish W.R., Stefan C.J., Emr S.D.;
"Essential role for the myotubularin-related phosphatase Ymr1p and the
synaptojanin-like phosphatases Sjl2p and Sjl3p in regulation of
phosphatidylinositol 3-phosphate in yeast.";
Mol. Biol. Cell 15:3567-3579(2004).
[18]
FUNCTION.
PubMed=15691741; DOI=10.1016/j.femsyr.2004.09.007;
Nguyen P.H., Hasek J., Kohlwein S.D., Romero C., Choi J.H.,
Vancura A.;
"Interaction of Pik1p and Sjl proteins in membrane trafficking.";
FEMS Yeast Res. 5:363-371(2005).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1105, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1035, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-986 AND THR-1105, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[22]
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).
-!- FUNCTION: Dephosphorylates a number of phosphatidylinositols (PIs)
like phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), but
also phosphatidylinositol 3-phosphate (PtdIns(3)P),
phosphatidylinositol 4-phosphate (PtdIns(4)P), and
phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Controls
the cellular levels and subcellular distribution of
phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-
bisphosphate. Plays an essential role in a TGN (trans Golgi
network)-to-early endosome pathway. Involved in clathrin-mediated
protein sorting at the TGN. {ECO:0000269|PubMed:10029994,
ECO:0000269|PubMed:10224048, ECO:0000269|PubMed:10625610,
ECO:0000269|PubMed:10628971, ECO:0000269|PubMed:11094088,
ECO:0000269|PubMed:11598201, ECO:0000269|PubMed:12686590,
ECO:0000269|PubMed:15169871, ECO:0000269|PubMed:15691741,
ECO:0000269|PubMed:9265642, ECO:0000269|PubMed:9560389,
ECO:0000269|PubMed:9788876}.
-!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 4-phosphate
+ phosphate.
-!- SUBUNIT: Interacts with BSP1 and CHC1.
{ECO:0000269|PubMed:12606027, ECO:0000269|PubMed:12686590}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11094088,
ECO:0000269|PubMed:14562095}. Note=Cytoplasmic punctate
structures. Hyperosmotic stress causes translocation to actin
patches.
-!- DOMAIN: The SAC1 domain is capable of hydrolyzing
phosphatidylinositol 3-phosphate (PtdIns(3)P),
phosphatidylinositol 4-phosphate (PtdIns(4)P), and
phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
-!- DOMAIN: The 5-phosphatase domain (residues 568 to 856) selectively
removes the phosphate group at the 5' position of inositol of
phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2).
-!- DOMAIN: The C-terminal proline-rich domain is required for the
function and associates with clathrin heavy chain CHC1.
-!- MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the synaptojanin family. {ECO:0000305}.
-!- SIMILARITY: In the central section; belongs to the inositol 1,4,5-
trisphosphate 5-phosphatase family. {ECO:0000305}.
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EMBL; X94335; CAA64029.1; -; Genomic_DNA.
EMBL; Z75017; CAA99307.1; -; Genomic_DNA.
EMBL; BK006948; DAA10884.1; -; Genomic_DNA.
PIR; S61667; S61667.
RefSeq; NP_014752.3; NM_001183528.3.
ProteinModelPortal; Q12271; -.
SMR; Q12271; -.
BioGrid; 34505; 298.
DIP; DIP-2555N; -.
IntAct; Q12271; 14.
MINT; MINT-4502837; -.
STRING; 4932.YOR109W; -.
iPTMnet; Q12271; -.
MaxQB; Q12271; -.
PRIDE; Q12271; -.
EnsemblFungi; YOR109W; YOR109W; YOR109W.
GeneID; 854276; -.
KEGG; sce:YOR109W; -.
EuPathDB; FungiDB:YOR109W; -.
SGD; S000005635; INP53.
GeneTree; ENSGT00760000119075; -.
HOGENOM; HOG000179717; -.
InParanoid; Q12271; -.
KO; K20279; -.
OMA; IMGIAGN; -.
OrthoDB; EOG092C1610; -.
BioCyc; YEAST:YOR109W-MONOMER; -.
Reactome; R-SCE-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-SCE-1660514; Synthesis of PIPs at the Golgi membrane.
Reactome; R-SCE-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
Reactome; R-SCE-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-SCE-194840; Rho GTPase cycle.
Reactome; R-SCE-202424; Downstream TCR signaling.
PRO; PR:Q12271; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0030479; C:actin cortical patch; IDA:SGD.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0016020; C:membrane; IDA:SGD.
GO; GO:0043813; F:phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity; IDA:SGD.
GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IDA:SGD.
GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:SGD.
GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; IDA:SGD.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:SGD.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
Gene3D; 3.60.10.10; -; 1.
InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
InterPro; IPR005135; Endo/exonuclease/phosphatase.
InterPro; IPR000300; IPPc.
InterPro; IPR002013; SAC_dom.
Pfam; PF03372; Exo_endo_phos; 1.
Pfam; PF02383; Syja_N; 1.
SMART; SM00128; IPPc; 1.
SUPFAM; SSF56219; SSF56219; 1.
PROSITE; PS50275; SAC; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Endocytosis; Hydrolase; Phosphoprotein;
Protein transport; Reference proteome; Transport.
CHAIN 1 1107 Polyphosphatidylinositol phosphatase
INP53.
/FTId=PRO_0000268681.
DOMAIN 142 482 SAC. {ECO:0000255|PROSITE-
ProRule:PRU00183}.
COMPBIAS 957 989 Pro-rich.
MOD_RES 497 497 Phosphoserine.
{ECO:0000250|UniProtKB:P50942}.
MOD_RES 986 986 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 1035 1035 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 1105 1105 Phosphothreonine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MUTAGEN 421 421 C->A: Reduces hydrolysis of PtdIns(4)P;
when associated with A-424 and A-427.
{ECO:0000269|PubMed:12686590}.
MUTAGEN 424 424 C->A: Reduces hydrolysis of PtdIns(4)P;
when associated with A-421 and A-427.
{ECO:0000269|PubMed:12686590}.
MUTAGEN 427 427 R->A: Reduces hydrolysis of PtdIns(4)P;
when associated with A-421 and A-424.
{ECO:0000269|PubMed:12686590}.
MUTAGEN 746 746 D->A: Abolishes hydrolysis of
PtdIns(4,5)P2; when associated with A-
748. {ECO:0000269|PubMed:12686590}.
MUTAGEN 748 748 N->A: Abolishes hydrolysis of
PtdIns(4,5)P2; when associated with A-
746. {ECO:0000269|PubMed:12686590}.
SEQUENCE 1107 AA; 124577 MW; 1E024F15085261EA CRC64;
MIIFVSEEPE RRLAIVSNLY ALVLKPVGKK PSDKPLCAIE LLQKNDLKKY GFKRLTSHEI
FGVIGLIEVN GLLFVGAITG KSKVAQPCPG ETVNKIFAVD FFCLNDNSWD FIEIDSSGYP
VLPETASTEY QDALPKHPCY ELKKLLSNGS FYYSSDFDLT STLQHRGYGQ HSLSTDTYEE
EYMWNSFLMQ EMITYRDHLD TNLKQILDDE GFLTTVIRGF AETFVSYVKK LKVALTIISK
QSWKRAGTRF NARGVDDEAN VANFVETEFI MYSSQYCYAF TQIRGSIPVF WEQGTSLINP
RVQITRSFEA TQPVFDKHIM KSVEKYGPVH VVNLLSTKSS EIELSKRYKE HLTHSKKLNF
NKDIFLTEFD FHKETSQEGF SGVRKLIPLI LDSLLSSGYY SYDVREKKNI SEQHGIFRTN
CLDCLDRTNL AQQIISLAAF RTFLEDFRLI SSNSFIDDDD FVSKHNTLWA DHGDQISQIY
TGTNALKSSF SRKGKMSLAG ALSDATKSVS RIYINNFMDK EKQQNIDTLL GRLPYQKAVQ
LYDPVNEYVS TKLQSMSDKF TSTSNINLLI GSFNVNGATK KVDLSKWLFP IGEKFKPDIV
VLGLQEVIEL SAGSILNADY SKSSFWENLV GDCLNQYDDK YLLLRVEQMT SLLILFFVKA
DKAKYVKQVE GATKKTGFRG MAGNKGAVSI RFEYGATSFC FVNSHLAAGA TNVEERRSDY
ESIVRGITFT RTKMIPHHDS IFWLGDMNYR INLPNEDVRR ELLNQEEGYI DKLLHFDQLT
LGINSGSVFE GFKEPTLKFR PTYKYDPGTG TYDSSEKERT PSWTDRIIYK GENLLPLSYS
DAPIMISDHR PVYAAYRAKI TFVDDKERLS LKKRLFTEYK QEHPEEPGSL ISDLLSLDLD
NKSTDGFKSS SESSLLDIDP IMAQPTASSV ASSSPVSSAS ASLQPVRTQN SSQSRTPIKK
PVLRPPPPPA HKSVSAPAPS TSKEKSPTPQ TSTASLSSVT KNIQENKPLA QNRRIPPPGF
SQNILTPKST SNLASPMSSK VDLYNSASES TRSAQDARQQ TPTAFAASRD VNGQPEALLG
DENPIEPEEK AKLNHMTLDS WQPLTPK


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EIAAB38291 Inositol polyphosphate phosphatase-like protein 1,Inppl1,INPPL-1,Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2,Rat,Rattus norvegicus,SH2 domain-containing inositol phosphatase 2,SH2 domain-
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
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
EH1661 Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN Elisa Kit 96T
EIAAB12042 3ch134,Dual specificity protein phosphatase 1,Dusp1,MAP kinase phosphatase 1,Mitogen-activated protein kinase phosphatase 1,Mkp1,MKP-1,Mouse,Mus musculus,Protein-tyrosine phosphatase 3CH134,Protein-ty
EIAAB33117 FMI,Homo sapiens,hPTP-J,Human,Pancreatic carcinoma phosphatase 2,PCP2,PCP-2,Protein-tyrosine phosphatase J,Protein-tyrosine phosphatase pi,Protein-tyrosine phosphatase receptor omicron,PTP pi,PTP-J,PT
EIAAB12040 Cl100,Dual specificity protein phosphatase 1,Dusp1,MAP kinase phosphatase 1,Mitogen-activated protein kinase phosphatase 1,Mkp1,MKP-1,Protein-tyrosine phosphatase CL100,Protein-tyrosine phosphatase no
15-288-22164F Dual specificity protein phosphatase 14 - EC 3.1.3.48; EC 3.1.3.16; Mitogen-activated protein kinase phosphatase 6; MAP kinase phosphatase 6; MKP-6; MKP-1-like protein tyrosine phosphatase; MKP-L Poly 0.05 mg
15-288-22164F Dual specificity protein phosphatase 14 - EC 3.1.3.48; EC 3.1.3.16; Mitogen-activated protein kinase phosphatase 6; MAP kinase phosphatase 6; MKP-6; MKP-1-like protein tyrosine phosphatase; MKP-L Poly 0.1 mg


 

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