Full text data of INPP5K
INPP5K
(PPS, SKIP)
[Confidence: low (only semi-automatic identification from reviews)]
Inositol polyphosphate 5-phosphatase K; 3.1.3.56 (Skeletal muscle and kidney-enriched inositol phosphatase)
Inositol polyphosphate 5-phosphatase K; 3.1.3.56 (Skeletal muscle and kidney-enriched inositol phosphatase)
UniProt
Q9BT40
ID INP5K_HUMAN Reviewed; 448 AA.
AC Q9BT40; B2R6I2; B2R750; D3DTH8; Q15733; Q9NPJ5; Q9P2R5;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 3.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Inositol polyphosphate 5-phosphatase K;
DE EC=3.1.3.56;
DE AltName: Full=Skeletal muscle and kidney-enriched inositol phosphatase;
GN Name=INPP5K; Synonyms=PPS, SKIP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10753883; DOI=10.1074/jbc.275.15.10870;
RA Ijuin T., Mochizuki Y., Fukami K., Funaki M., Asano T., Takenawa T.;
RT "Identification and characterization of a novel inositol polyphosphate
RT 5-phosphatase.";
RL J. Biol. Chem. 275:10870-10875(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 120-448.
RC TISSUE=Brain;
RA Nussbaum R.L.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-349; ASP-361; TRP-362 AND
RP TYR-376.
RX PubMed=12536145; DOI=10.1074/jbc.M209991200;
RA Gurung R., Tan A., Ooms L.M., McGrath M.J., Huysmans R.D.,
RA Munday A.D., Prescott M., Whisstock J.C., Mitchell C.A.;
RT "Identification of a novel domain in two mammalian inositol-
RT polyphosphate 5-phosphatases that mediates membrane ruffle
RT localization. The inositol 5-phosphatase SKIP localizes to the
RT endoplasmic reticulum and translocates to membrane ruffles following
RT epidermal growth factor stimulation.";
RL J. Biol. Chem. 278:11376-11385(2003).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-315.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Inositol 5-phosphatase which acts on inositol 1,4,5-
CC trisphosphate, inositol 1,3,4,5-tetrakisphosphate,
CC phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol
CC 3,4,5-trisphosphate. Has 6-fold higher affinity for
CC phosphatidylinositol 4,5-bisphosphate than for inositol 1,4,5-
CC trisphosphate. May negatively regulate assembly of the actin
CC cytoskeleton.
CC -!- CATALYTIC ACTIVITY: D-myo-inositol 1,4,5-trisphosphate + H(2)O =
CC myo-inositol 1,4-bisphosphate + phosphate.
CC -!- INTERACTION:
CC Q8TBB1:LNX1; NbExp=3; IntAct=EBI-749162, EBI-739832;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Note=Following
CC stimulation with EGF, translocates to membrane ruffles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BT40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BT40-2; Sequence=VSP_050612;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
CC skeletal muscle, heart and kidney.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-
CC phosphatase type II family.
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DR EMBL; AB036829; BAA92340.1; -; mRNA.
DR EMBL; AB036830; BAA92341.1; -; mRNA.
DR EMBL; AB036831; BAA92342.1; -; Genomic_DNA.
DR EMBL; AK312585; BAG35479.1; -; mRNA.
DR EMBL; AK312844; BAG35697.1; -; mRNA.
DR EMBL; CH471108; EAW90614.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90615.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90618.1; -; Genomic_DNA.
DR EMBL; BC004362; AAH04362.1; -; mRNA.
DR EMBL; U45973; AAB03214.1; -; mRNA.
DR RefSeq; NP_001129114.1; NM_001135642.1.
DR RefSeq; NP_057616.2; NM_016532.3.
DR RefSeq; NP_570122.1; NM_130766.2.
DR RefSeq; XP_005256740.1; XM_005256683.1.
DR RefSeq; XP_005256741.1; XM_005256684.1.
DR UniGene; Hs.632238; -.
DR ProteinModelPortal; Q9BT40; -.
DR SMR; Q9BT40; 20-323.
DR IntAct; Q9BT40; 13.
DR MINT; MINT-1445023; -.
DR STRING; 9606.ENSP00000254712; -.
DR PhosphoSite; Q9BT40; -.
DR DMDM; 116242791; -.
DR PaxDb; Q9BT40; -.
DR PRIDE; Q9BT40; -.
DR Ensembl; ENST00000320345; ENSP00000318476; ENSG00000132376.
DR Ensembl; ENST00000406424; ENSP00000385177; ENSG00000132376.
DR Ensembl; ENST00000421807; ENSP00000413937; ENSG00000132376.
DR GeneID; 51763; -.
DR KEGG; hsa:51763; -.
DR UCSC; uc002fsq.3; human.
DR CTD; 51763; -.
DR GeneCards; GC17M001397; -.
DR HGNC; HGNC:33882; INPP5K.
DR HPA; HPA031044; -.
DR MIM; 607875; gene.
DR neXtProt; NX_Q9BT40; -.
DR PharmGKB; PA164720951; -.
DR eggNOG; COG5411; -.
DR HOGENOM; HOG000046051; -.
DR HOVERGEN; HBG082135; -.
DR InParanoid; Q9BT40; -.
DR KO; K01106; -.
DR OMA; TEDQFLL; -.
DR PhylomeDB; Q9BT40; -.
DR BioCyc; MetaCyc:HS05626-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR GeneWiki; SKIP; -.
DR GenomeRNAi; 51763; -.
DR NextBio; 55878; -.
DR PRO; PR:Q9BT40; -.
DR ArrayExpress; Q9BT40; -.
DR Bgee; Q9BT40; -.
DR CleanEx; HS_INPP5K; -.
DR Genevestigator; Q9BT40; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0016312; F:inositol bisphosphate phosphatase activity; IDA:MGI.
DR GO; GO:0046030; F:inositol trisphosphate phosphatase activity; IDA:MGI.
DR GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0042577; F:lipid phosphatase activity; NAS:UniProtKB.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0005000; F:vasopressin receptor activity; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:MGI.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:UniProtKB.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; IDA:UniProtKB.
DR GO; GO:0035305; P:negative regulation of dephosphorylation; ISS:UniProtKB.
DR GO; GO:0010829; P:negative regulation of glucose transport; IDA:UniProtKB.
DR GO; GO:2000466; P:negative regulation of glycogen (starch) synthase activity; ISS:UniProtKB.
DR GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; IDA:UniProtKB.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling cascade; IDA:UniProtKB.
DR GO; GO:0090315; P:negative regulation of protein targeting to membrane; IDA:UniProtKB.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IDA:UniProtKB.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; ISS:UniProtKB.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
DR GO; GO:2001153; P:positive regulation of renal water transport; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; ISS:UniProtKB.
DR GO; GO:0035810; P:positive regulation of urine volume; ISS:UniProtKB.
DR GO; GO:0072661; P:protein targeting to plasma membrane; ISS:UniProtKB.
DR GO; GO:0097178; P:ruffle assembly; IDA:UniProtKB.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000300; IPPc.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Endoplasmic reticulum;
KW Hydrolase; Polymorphism; Reference proteome.
FT CHAIN 1 448 Inositol polyphosphate 5-phosphatase K.
FT /FTId=PRO_0000209727.
FT REGION 16 318 Catalytic (Potential).
FT REGION 321 448 Required for ruffle localization.
FT VAR_SEQ 1 76 Missing (in isoform 2).
FT /FTId=VSP_050612.
FT VARIANT 315 315 S -> F (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036497.
FT MUTAGEN 349 349 Y->A,F: No effect on EGF-induced ruffle
FT localization.
FT MUTAGEN 361 361 D->A: Significant decrease in EGF-induced
FT ruffle localization.
FT MUTAGEN 362 362 W->A: Significant decrease in EGF-induced
FT ruffle localization.
FT MUTAGEN 376 376 Y->A,F: No effect on EGF-induced ruffle
FT localization.
FT CONFLICT 120 120 T -> A (in Ref. 5; AAB03214).
FT CONFLICT 416 416 S -> R (in Ref. 1; BAA92340/BAA92341/
FT BAA92342 and 5; AAB03214).
FT CONFLICT 426 426 S -> R (in Ref. 1; BAA92340/BAA92341/
FT BAA92342 and 5; AAB03214).
SQ SEQUENCE 448 AA; 51090 MW; 46FAA48C6E2EEAD4 CRC64;
MSSRKLSGPK GRRLSIHVVT WNVASAAPPL DLSDLLQLNN RNLNLDIYVI GLQELNSGII
SLLSDAAFND SWSSFLMDVL SPLSFIKVSH VRMQGILLLV FAKYQHLPYI QILSTKSTPT
GLFGYWGNKG GVNICLKLYG YYVSIINCHL PPHISNNYQR LEHFDRILEM QNCEGRDIPN
ILDHDLIIWF GDMNFRIEDF GLHFVRESIK NRCYGGLWEK DQLSIAKKHD PLLREFQEGR
LLFPPTYKFD RNSNDYDTSE KKRKPAWTDR ILWRLKRQPC AGPDTPIPPA SHFSLSLRGY
SSHMTYGISD HKPVSGTFDL ELKPLVSAPL IVLMPEDLWT VENDMMVSYS STSDFPSSPW
DWIGLYKVGL RDVNDYVSYA WVGDSKVSCS DNLNQVYIDI SNIPTTEDEF LLCYYSNSLR
SVVGISRPFQ IPPGSLREDP LGEAQPQI
//
ID INP5K_HUMAN Reviewed; 448 AA.
AC Q9BT40; B2R6I2; B2R750; D3DTH8; Q15733; Q9NPJ5; Q9P2R5;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 3.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Inositol polyphosphate 5-phosphatase K;
DE EC=3.1.3.56;
DE AltName: Full=Skeletal muscle and kidney-enriched inositol phosphatase;
GN Name=INPP5K; Synonyms=PPS, SKIP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10753883; DOI=10.1074/jbc.275.15.10870;
RA Ijuin T., Mochizuki Y., Fukami K., Funaki M., Asano T., Takenawa T.;
RT "Identification and characterization of a novel inositol polyphosphate
RT 5-phosphatase.";
RL J. Biol. Chem. 275:10870-10875(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 120-448.
RC TISSUE=Brain;
RA Nussbaum R.L.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-349; ASP-361; TRP-362 AND
RP TYR-376.
RX PubMed=12536145; DOI=10.1074/jbc.M209991200;
RA Gurung R., Tan A., Ooms L.M., McGrath M.J., Huysmans R.D.,
RA Munday A.D., Prescott M., Whisstock J.C., Mitchell C.A.;
RT "Identification of a novel domain in two mammalian inositol-
RT polyphosphate 5-phosphatases that mediates membrane ruffle
RT localization. The inositol 5-phosphatase SKIP localizes to the
RT endoplasmic reticulum and translocates to membrane ruffles following
RT epidermal growth factor stimulation.";
RL J. Biol. Chem. 278:11376-11385(2003).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-315.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Inositol 5-phosphatase which acts on inositol 1,4,5-
CC trisphosphate, inositol 1,3,4,5-tetrakisphosphate,
CC phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol
CC 3,4,5-trisphosphate. Has 6-fold higher affinity for
CC phosphatidylinositol 4,5-bisphosphate than for inositol 1,4,5-
CC trisphosphate. May negatively regulate assembly of the actin
CC cytoskeleton.
CC -!- CATALYTIC ACTIVITY: D-myo-inositol 1,4,5-trisphosphate + H(2)O =
CC myo-inositol 1,4-bisphosphate + phosphate.
CC -!- INTERACTION:
CC Q8TBB1:LNX1; NbExp=3; IntAct=EBI-749162, EBI-739832;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Note=Following
CC stimulation with EGF, translocates to membrane ruffles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BT40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BT40-2; Sequence=VSP_050612;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
CC skeletal muscle, heart and kidney.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-
CC phosphatase type II family.
CC -----------------------------------------------------------------------
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DR EMBL; AB036829; BAA92340.1; -; mRNA.
DR EMBL; AB036830; BAA92341.1; -; mRNA.
DR EMBL; AB036831; BAA92342.1; -; Genomic_DNA.
DR EMBL; AK312585; BAG35479.1; -; mRNA.
DR EMBL; AK312844; BAG35697.1; -; mRNA.
DR EMBL; CH471108; EAW90614.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90615.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90618.1; -; Genomic_DNA.
DR EMBL; BC004362; AAH04362.1; -; mRNA.
DR EMBL; U45973; AAB03214.1; -; mRNA.
DR RefSeq; NP_001129114.1; NM_001135642.1.
DR RefSeq; NP_057616.2; NM_016532.3.
DR RefSeq; NP_570122.1; NM_130766.2.
DR RefSeq; XP_005256740.1; XM_005256683.1.
DR RefSeq; XP_005256741.1; XM_005256684.1.
DR UniGene; Hs.632238; -.
DR ProteinModelPortal; Q9BT40; -.
DR SMR; Q9BT40; 20-323.
DR IntAct; Q9BT40; 13.
DR MINT; MINT-1445023; -.
DR STRING; 9606.ENSP00000254712; -.
DR PhosphoSite; Q9BT40; -.
DR DMDM; 116242791; -.
DR PaxDb; Q9BT40; -.
DR PRIDE; Q9BT40; -.
DR Ensembl; ENST00000320345; ENSP00000318476; ENSG00000132376.
DR Ensembl; ENST00000406424; ENSP00000385177; ENSG00000132376.
DR Ensembl; ENST00000421807; ENSP00000413937; ENSG00000132376.
DR GeneID; 51763; -.
DR KEGG; hsa:51763; -.
DR UCSC; uc002fsq.3; human.
DR CTD; 51763; -.
DR GeneCards; GC17M001397; -.
DR HGNC; HGNC:33882; INPP5K.
DR HPA; HPA031044; -.
DR MIM; 607875; gene.
DR neXtProt; NX_Q9BT40; -.
DR PharmGKB; PA164720951; -.
DR eggNOG; COG5411; -.
DR HOGENOM; HOG000046051; -.
DR HOVERGEN; HBG082135; -.
DR InParanoid; Q9BT40; -.
DR KO; K01106; -.
DR OMA; TEDQFLL; -.
DR PhylomeDB; Q9BT40; -.
DR BioCyc; MetaCyc:HS05626-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR GeneWiki; SKIP; -.
DR GenomeRNAi; 51763; -.
DR NextBio; 55878; -.
DR PRO; PR:Q9BT40; -.
DR ArrayExpress; Q9BT40; -.
DR Bgee; Q9BT40; -.
DR CleanEx; HS_INPP5K; -.
DR Genevestigator; Q9BT40; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0016312; F:inositol bisphosphate phosphatase activity; IDA:MGI.
DR GO; GO:0046030; F:inositol trisphosphate phosphatase activity; IDA:MGI.
DR GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0042577; F:lipid phosphatase activity; NAS:UniProtKB.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0005000; F:vasopressin receptor activity; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:MGI.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:UniProtKB.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; IDA:UniProtKB.
DR GO; GO:0035305; P:negative regulation of dephosphorylation; ISS:UniProtKB.
DR GO; GO:0010829; P:negative regulation of glucose transport; IDA:UniProtKB.
DR GO; GO:2000466; P:negative regulation of glycogen (starch) synthase activity; ISS:UniProtKB.
DR GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; IDA:UniProtKB.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling cascade; IDA:UniProtKB.
DR GO; GO:0090315; P:negative regulation of protein targeting to membrane; IDA:UniProtKB.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IDA:UniProtKB.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; ISS:UniProtKB.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
DR GO; GO:2001153; P:positive regulation of renal water transport; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; ISS:UniProtKB.
DR GO; GO:0035810; P:positive regulation of urine volume; ISS:UniProtKB.
DR GO; GO:0072661; P:protein targeting to plasma membrane; ISS:UniProtKB.
DR GO; GO:0097178; P:ruffle assembly; IDA:UniProtKB.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000300; IPPc.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Endoplasmic reticulum;
KW Hydrolase; Polymorphism; Reference proteome.
FT CHAIN 1 448 Inositol polyphosphate 5-phosphatase K.
FT /FTId=PRO_0000209727.
FT REGION 16 318 Catalytic (Potential).
FT REGION 321 448 Required for ruffle localization.
FT VAR_SEQ 1 76 Missing (in isoform 2).
FT /FTId=VSP_050612.
FT VARIANT 315 315 S -> F (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036497.
FT MUTAGEN 349 349 Y->A,F: No effect on EGF-induced ruffle
FT localization.
FT MUTAGEN 361 361 D->A: Significant decrease in EGF-induced
FT ruffle localization.
FT MUTAGEN 362 362 W->A: Significant decrease in EGF-induced
FT ruffle localization.
FT MUTAGEN 376 376 Y->A,F: No effect on EGF-induced ruffle
FT localization.
FT CONFLICT 120 120 T -> A (in Ref. 5; AAB03214).
FT CONFLICT 416 416 S -> R (in Ref. 1; BAA92340/BAA92341/
FT BAA92342 and 5; AAB03214).
FT CONFLICT 426 426 S -> R (in Ref. 1; BAA92340/BAA92341/
FT BAA92342 and 5; AAB03214).
SQ SEQUENCE 448 AA; 51090 MW; 46FAA48C6E2EEAD4 CRC64;
MSSRKLSGPK GRRLSIHVVT WNVASAAPPL DLSDLLQLNN RNLNLDIYVI GLQELNSGII
SLLSDAAFND SWSSFLMDVL SPLSFIKVSH VRMQGILLLV FAKYQHLPYI QILSTKSTPT
GLFGYWGNKG GVNICLKLYG YYVSIINCHL PPHISNNYQR LEHFDRILEM QNCEGRDIPN
ILDHDLIIWF GDMNFRIEDF GLHFVRESIK NRCYGGLWEK DQLSIAKKHD PLLREFQEGR
LLFPPTYKFD RNSNDYDTSE KKRKPAWTDR ILWRLKRQPC AGPDTPIPPA SHFSLSLRGY
SSHMTYGISD HKPVSGTFDL ELKPLVSAPL IVLMPEDLWT VENDMMVSYS STSDFPSSPW
DWIGLYKVGL RDVNDYVSYA WVGDSKVSCS DNLNQVYIDI SNIPTTEDEF LLCYYSNSLR
SVVGISRPFQ IPPGSLREDP LGEAQPQI
//
MIM
607875
*RECORD*
*FIELD* NO
607875
*FIELD* TI
*607875 SKELETAL MUSCLE- AND KIDNEY-ENRICHED INOSITOL PHOSPHATASE
;;SKIP
*FIELD* TX
read more
DESCRIPTION
SKIP is a type II inositol polyphosphate 5-phosphatase that hydrolyzes
the D5 position of inositol phosphates and corresponding phospholipids.
CLONING
Using a 5-phosphatase catalytic motif-2-like sequence as probe, Ijuin et
al. (2000) cloned 3 SKIP splice variants from a human testis cDNA
library. Two variants encode a deduced 448-amino acid protein with a
calculated molecular mass of 51 kD; however, 1 of these variants has a
deletion in the C-terminal noncoding region. The third variant uses an
alternate start codon and encodes a 372-amino acid protein with a
calculated molecular mass of 43 kD. All 3 isoforms contain the conserved
catalytic motifs 1 and 2. Northern blot analysis revealed expression of
2.0- and 3.0-kb transcripts in all tissues examined, with highest
expression in heart, skeletal muscle, and kidney. Western blot analysis
revealed differential expression of endogenous SKIP proteins with
apparent molecular masses of 51 or 43 kD in several rodent cell lines
and COS-7 cells.
GENE FUNCTION
Ijuin et al. (2000) determined that recombinant SKIP expressed in insect
cells showed 5-phosphatase activity toward inositol 1,4,5-trisphosphate
(Ins(1,4,5)P3), Ins(1,3,4,5)P4, phosphatidylinositol 4,5-bisphosphate
(PtdIns(4,5,)P2), and PtdIns(3,4,5)P3. SKIP had 6-fold higher substrate
specificity for PtdIns(4,5)P2 than for Ins(1,4,5)P3. Immunolocalization
of endogenous Skip in rat neuroblastoma cells showed expression in the
cytosol and loss of actin stress fibers where Skip was concentrated.
Ijuin and Takenawa (2003) determined that ectopic expression of SKIP
inhibited phosphoinositide 3-kinase (see 601232) signaling in insulin
(176730)-stimulated Chinese hamster ovary (CHO) cells. SKIP rapidly
decreased elevated intracellular PtdIns(3,4,5)P3 levels induced by
insulin, inhibited phosphorylation of downstream insulin targets, such
as Akt (164730), and partially suppressed insulin-induced calcium
mobilization. SKIP did not alter insulin-induced phosphorylation of
mitogen-activated protein kinases (MAPKs; see 176948). Downregulation of
endogenous Skip levels by antisense oligonucleotides enhanced Akt
phosphorylation in response to insulin. Ijuin and Takenawa (2003) also
determined that SKIP inhibited GLUT4 (138190) translocation and membrane
ruffle formation in CHO cells and suppressed insulin-induced glucose
incorporation and glycogen synthesis in rat myocytes.
By immunofluorescence and subcellular fractionation of several mammalian
cell lines, Gurung et al. (2003) determined that both endogenous and
recombinant SKIP colocalized with endoplasmic reticulum (ER) marker
proteins in serum-starved cells. Following epidermal growth factor (EGF;
131530) stimulation, SKIP transiently translocated to plasma membrane
ruffles and colocalized with submembranous actin. By database searching
and mutation analysis, Gurung et al. (2003) identified a core sequence
within a 128-amino acid C-terminal domain, which they designated the
SKICH domain, that was necessary for SKIP translocation upon EGF
stimulation. Deletion of the SKICH domain did not alter resting ER
localization.
GENE STRUCTURE
Ijuin et al. (2000) determined that the SKIP gene contains 13 exons.
Alternative splicing of exons 2 and 13 result in 3 SKIP isoforms.
MAPPING
The International Radiation Hybrid Mapping consortium mapped the SKIP
gene to chromosome 17 (TMAP stSG1504).
*FIELD* RF
1. Gurung, R.; Tan, A.; Ooms, L. M.; McGrath, M. J.; Huysmans, R.
D.; Munday, A. D.; Prescott, M.; Whisstock, J. C.; Mitchell, C. A.
: Identification of a novel domain in two mammalian inositol-polyphosphate
5-phosphatases that mediates membrane ruffle localization: the inositol
5-phosphatase SKIP localizes to the endoplasmic reticulum and translocates
to membrane ruffles following epidermal growth factor stimulation. J.
Biol. Chem. 278: 11376-11385, 2003.
2. Ijuin, T.; Mochizuki, Y.; Fukami, K.; Funaki, M.; Asano, T.; Takenawa,
T.: Identification and characterization of a novel inositol polyphosphate
5-phosphatase. J. Biol. Chem. 275: 10870-10875, 2000.
3. Ijuin, T.; Takenawa, T.: SKIP negatively regulates insulin-induced
GLUT4 translocation and membrane ruffle formation. Molec. Cell. Biol. 23:
1209-1220, 2003.
*FIELD* CD
Patricia A. Hartz: 6/11/2003
*FIELD* ED
terry: 07/20/2004
mgross: 6/11/2003
*RECORD*
*FIELD* NO
607875
*FIELD* TI
*607875 SKELETAL MUSCLE- AND KIDNEY-ENRICHED INOSITOL PHOSPHATASE
;;SKIP
*FIELD* TX
read more
DESCRIPTION
SKIP is a type II inositol polyphosphate 5-phosphatase that hydrolyzes
the D5 position of inositol phosphates and corresponding phospholipids.
CLONING
Using a 5-phosphatase catalytic motif-2-like sequence as probe, Ijuin et
al. (2000) cloned 3 SKIP splice variants from a human testis cDNA
library. Two variants encode a deduced 448-amino acid protein with a
calculated molecular mass of 51 kD; however, 1 of these variants has a
deletion in the C-terminal noncoding region. The third variant uses an
alternate start codon and encodes a 372-amino acid protein with a
calculated molecular mass of 43 kD. All 3 isoforms contain the conserved
catalytic motifs 1 and 2. Northern blot analysis revealed expression of
2.0- and 3.0-kb transcripts in all tissues examined, with highest
expression in heart, skeletal muscle, and kidney. Western blot analysis
revealed differential expression of endogenous SKIP proteins with
apparent molecular masses of 51 or 43 kD in several rodent cell lines
and COS-7 cells.
GENE FUNCTION
Ijuin et al. (2000) determined that recombinant SKIP expressed in insect
cells showed 5-phosphatase activity toward inositol 1,4,5-trisphosphate
(Ins(1,4,5)P3), Ins(1,3,4,5)P4, phosphatidylinositol 4,5-bisphosphate
(PtdIns(4,5,)P2), and PtdIns(3,4,5)P3. SKIP had 6-fold higher substrate
specificity for PtdIns(4,5)P2 than for Ins(1,4,5)P3. Immunolocalization
of endogenous Skip in rat neuroblastoma cells showed expression in the
cytosol and loss of actin stress fibers where Skip was concentrated.
Ijuin and Takenawa (2003) determined that ectopic expression of SKIP
inhibited phosphoinositide 3-kinase (see 601232) signaling in insulin
(176730)-stimulated Chinese hamster ovary (CHO) cells. SKIP rapidly
decreased elevated intracellular PtdIns(3,4,5)P3 levels induced by
insulin, inhibited phosphorylation of downstream insulin targets, such
as Akt (164730), and partially suppressed insulin-induced calcium
mobilization. SKIP did not alter insulin-induced phosphorylation of
mitogen-activated protein kinases (MAPKs; see 176948). Downregulation of
endogenous Skip levels by antisense oligonucleotides enhanced Akt
phosphorylation in response to insulin. Ijuin and Takenawa (2003) also
determined that SKIP inhibited GLUT4 (138190) translocation and membrane
ruffle formation in CHO cells and suppressed insulin-induced glucose
incorporation and glycogen synthesis in rat myocytes.
By immunofluorescence and subcellular fractionation of several mammalian
cell lines, Gurung et al. (2003) determined that both endogenous and
recombinant SKIP colocalized with endoplasmic reticulum (ER) marker
proteins in serum-starved cells. Following epidermal growth factor (EGF;
131530) stimulation, SKIP transiently translocated to plasma membrane
ruffles and colocalized with submembranous actin. By database searching
and mutation analysis, Gurung et al. (2003) identified a core sequence
within a 128-amino acid C-terminal domain, which they designated the
SKICH domain, that was necessary for SKIP translocation upon EGF
stimulation. Deletion of the SKICH domain did not alter resting ER
localization.
GENE STRUCTURE
Ijuin et al. (2000) determined that the SKIP gene contains 13 exons.
Alternative splicing of exons 2 and 13 result in 3 SKIP isoforms.
MAPPING
The International Radiation Hybrid Mapping consortium mapped the SKIP
gene to chromosome 17 (TMAP stSG1504).
*FIELD* RF
1. Gurung, R.; Tan, A.; Ooms, L. M.; McGrath, M. J.; Huysmans, R.
D.; Munday, A. D.; Prescott, M.; Whisstock, J. C.; Mitchell, C. A.
: Identification of a novel domain in two mammalian inositol-polyphosphate
5-phosphatases that mediates membrane ruffle localization: the inositol
5-phosphatase SKIP localizes to the endoplasmic reticulum and translocates
to membrane ruffles following epidermal growth factor stimulation. J.
Biol. Chem. 278: 11376-11385, 2003.
2. Ijuin, T.; Mochizuki, Y.; Fukami, K.; Funaki, M.; Asano, T.; Takenawa,
T.: Identification and characterization of a novel inositol polyphosphate
5-phosphatase. J. Biol. Chem. 275: 10870-10875, 2000.
3. Ijuin, T.; Takenawa, T.: SKIP negatively regulates insulin-induced
GLUT4 translocation and membrane ruffle formation. Molec. Cell. Biol. 23:
1209-1220, 2003.
*FIELD* CD
Patricia A. Hartz: 6/11/2003
*FIELD* ED
terry: 07/20/2004
mgross: 6/11/2003