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Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha (PIP5K1-alpha) (PtdIns(4)P-5-kinase 1 alpha) (EC 2.7.1.68) (68 kDa type I phosphatidylinositol 4-phosphate 5-kinase alpha) (Phosphatidylinositol 4-phosphate 5-kinase type I alpha) (PIP5KIalpha)

 PI51A_HUMAN             Reviewed;         562 AA.
Q99755; A8K4Q0; B4DIN0; Q99754; Q99756;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
22-NOV-2017, entry version 154.
RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha;
Short=PIP5K1-alpha;
Short=PtdIns(4)P-5-kinase 1 alpha;
EC=2.7.1.68;
AltName: Full=68 kDa type I phosphatidylinositol 4-phosphate 5-kinase alpha;
AltName: Full=Phosphatidylinositol 4-phosphate 5-kinase type I alpha;
Short=PIP5KIalpha;
Name=PIP5K1A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Fetal brain;
PubMed=8955136; DOI=10.1074/jbc.271.51.32937;
Loijens J.C., Anderson R.A.;
"Type I phosphatidylinositol-4-phosphate 5-kinases are distinct
members of this novel lipid kinase family.";
J. Biol. Chem. 271:32937-32943(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
TISSUE=Hippocampus;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Muscle;
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).
[6]
FUNCTION, AND INTERACTION WITH TUT1.
PubMed=18288197; DOI=10.1038/nature06666;
Mellman D.L., Gonzales M.L., Song C., Barlow C.A., Wang P.,
Kendziorski C., Anderson R.A.;
"A PtdIns4,5P2-regulated nuclear poly(A) polymerase controls
expression of select mRNAs.";
Nature 451:1013-1017(2008).
[7]
FUNCTION IN KERATINOCYTE DIFFERENTIATION, SUBCELLULAR LOCATION, AND
IDENTIFICATION IN A COMPLEX WITH CDH1; CTNNB1 AND CTNND1.
PubMed=19158393; DOI=10.1091/mbc.E08-07-0756;
Xie Z., Chang S.M., Pennypacker S.D., Liao E.-Y., Bikle D.D.;
"Phosphatidylinositol-4-phosphate 5-kinase 1alpha mediates
extracellular calcium-induced keratinocyte differentiation.";
Mol. Biol. Cell 20:1695-1704(2009).
[8]
FUNCTION IN CELL MIGRATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
ASP-322 AND ARG-440.
PubMed=20660631; DOI=10.1083/jcb.200911110;
Chao W.-T., Daquinag A.C., Ashcroft F., Kunz J.;
"Type I PIPK-alpha regulates directed cell migration by modulating
Rac1 plasma membrane targeting and activation.";
J. Cell Biol. 190:247-262(2010).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-
phosphate (PtdIns4P) to form phosphatidylinositol 4,5-bisphosphate
(PtdIns(4,5)P2). PtdIns(4,5)P2 is involved in a variety of
cellular processes and is the substrate to form
phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3),
another second messenger. The majority of PtdIns(4,5)P2 is thought
to occur via type I phosphatidylinositol 4-phosphate 5-kinases
given the abundance of PtdIns4P. Participates in a variety of
cellular processes such as actin cytoskeleton organization, cell
adhesion, migration and phagocytosis. Required for membrane
ruffling formation, actin organization and focal adhesion
formation during directional cell migration by controlling
integrin-induced translocation of RAC1 to the plasma membrane.
Together with PIP5K1C is required for phagocytosis, but they
regulate different types of actin remodeling at sequential steps.
Promotes particle ingestion by activating WAS that induces Arp2/3
dependent actin polymerization at the nascent phagocytic cup.
Together with PIP5K1B is required after stimulation of G-protein
coupled receptors for stable platelet adhesion. Plays a role
during calcium-induced keratinocyte differentiation. Recruited to
the plasma membrane by the E-cadherin/beta-catenin complex where
it provides the substrate PtdIns(4,5)P2 for the production of
PtdIns(3,4,5)P3, diacylglycerol and inositol 1,4,5-trisphosphate
that mobilize internal calcium and drive keratinocyte
differentiation. Together with PIP5K1C have a role during
embryogenesis. Functions also in the nucleus where acts as an
activator of TUT1 adenylyltransferase activity in nuclear
speckles, thereby regulating mRNA polyadenylation of a select set
of mRNAs. {ECO:0000269|PubMed:18288197,
ECO:0000269|PubMed:19158393, ECO:0000269|PubMed:20660631}.
-!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4-
phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
-!- SUBUNIT: Interacts with RAC1 (By similarity). Interacts with TUT1.
Forms a complex with CDH1/E-cadherin, CTNNB1/beta-catenin and
CTNND1 at the plasma membrane upon calcium stimulation.
{ECO:0000250, ECO:0000269|PubMed:18288197,
ECO:0000269|PubMed:19158393}.
-!- INTERACTION:
Q9H6E5:TUT1; NbExp=3; IntAct=EBI-726414, EBI-2511680;
-!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm {ECO:0000250}.
Nucleus speckle. Cell projection, ruffle. Note=Colocalizes with
RAC1 at actin-rich membrane ruffles. Localizes to nuclear speckles
and associates with TUT1 to regulate polyadenylation of selected
mRNAs.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=PIP5KIalpha2;
IsoId=Q99755-1; Sequence=Displayed;
Name=2; Synonyms=PIP5KIalpha3;
IsoId=Q99755-2; Sequence=VSP_016007, VSP_016008;
Name=3;
IsoId=Q99755-3; Sequence=VSP_016007;
Name=4;
IsoId=Q99755-4; Sequence=VSP_041912, VSP_041913;
-!- TISSUE SPECIFICITY: Highly expressed in heart, placenta, skeletal
muscle, kidney and pancreas. Detected at lower levels in brain,
lung and liver.
-!- CAUTION: There is confusion in the literature with
phosphatidylinositol 4-phosphate 5-kinase type I nomenclature due
to the fact that frequently mouse PIP5K1B is named
Phosphatidylinositol 4-phosphate 5-kinase type I alpha.
{ECO:0000305}.
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EMBL; U78575; AAC50910.1; -; mRNA.
EMBL; U78576; AAC50911.1; -; mRNA.
EMBL; U78577; AAC50912.1; -; mRNA.
EMBL; AK291015; BAF83704.1; -; mRNA.
EMBL; AK295691; BAG58542.1; -; mRNA.
EMBL; AL592424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53461.1; -; Genomic_DNA.
EMBL; BC007833; AAH07833.1; -; mRNA.
CCDS; CCDS44219.1; -. [Q99755-1]
CCDS; CCDS44220.1; -. [Q99755-4]
CCDS; CCDS44221.1; -. [Q99755-2]
CCDS; CCDS990.1; -. [Q99755-3]
RefSeq; NP_001129108.1; NM_001135636.1. [Q99755-4]
RefSeq; NP_001129109.1; NM_001135637.1. [Q99755-2]
RefSeq; NP_001129110.1; NM_001135638.1. [Q99755-1]
RefSeq; NP_001317618.1; NM_001330689.1.
RefSeq; NP_003548.1; NM_003557.2. [Q99755-3]
UniGene; Hs.655131; -.
UniGene; Hs.661888; -.
ProteinModelPortal; Q99755; -.
SMR; Q99755; -.
BioGrid; 113983; 53.
DIP; DIP-60649N; -.
IntAct; Q99755; 9.
MINT; MINT-1406942; -.
STRING; 9606.ENSP00000357883; -.
BindingDB; Q99755; -.
ChEMBL; CHEMBL5969; -.
GuidetoPHARMACOLOGY; 2164; -.
SwissLipids; SLP:000000553; -. [Q99755-3]
SwissLipids; SLP:000000554; -.
iPTMnet; Q99755; -.
PhosphoSitePlus; Q99755; -.
SwissPalm; Q99755; -.
BioMuta; PIP5K1A; -.
DMDM; 74752158; -.
EPD; Q99755; -.
MaxQB; Q99755; -.
PaxDb; Q99755; -.
PeptideAtlas; Q99755; -.
PRIDE; Q99755; -.
DNASU; 8394; -.
Ensembl; ENST00000349792; ENSP00000271663; ENSG00000143398. [Q99755-3]
Ensembl; ENST00000368888; ENSP00000357883; ENSG00000143398. [Q99755-1]
Ensembl; ENST00000368890; ENSP00000357885; ENSG00000143398. [Q99755-2]
Ensembl; ENST00000441902; ENSP00000415648; ENSG00000143398. [Q99755-4]
GeneID; 8394; -.
KEGG; hsa:8394; -.
UCSC; uc001exi.4; human. [Q99755-1]
CTD; 8394; -.
DisGeNET; 8394; -.
EuPathDB; HostDB:ENSG00000143398.19; -.
GeneCards; PIP5K1A; -.
HGNC; HGNC:8994; PIP5K1A.
HPA; HPA029366; -.
MIM; 603275; gene.
neXtProt; NX_Q99755; -.
OpenTargets; ENSG00000143398; -.
PharmGKB; PA33327; -.
eggNOG; KOG0229; Eukaryota.
eggNOG; COG5253; LUCA.
GeneTree; ENSGT00760000119184; -.
HOGENOM; HOG000193876; -.
HOVERGEN; HBG052818; -.
InParanoid; Q99755; -.
KO; K00889; -.
OMA; HMKYDLK; -.
OrthoDB; EOG091G0A6L; -.
PhylomeDB; Q99755; -.
TreeFam; TF319618; -.
BioCyc; MetaCyc:HS07047-MONOMER; -.
BRENDA; 2.7.1.68; 2681.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SignaLink; Q99755; -.
SIGNOR; Q99755; -.
ChiTaRS; PIP5K1A; human.
GeneWiki; PIP5K1A; -.
GenomeRNAi; 8394; -.
PMAP-CutDB; Q99755; -.
PRO; PR:Q99755; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143398; -.
CleanEx; HS_PIP5K1A; -.
ExpressionAtlas; Q99755; baseline and differential.
Genevisible; Q99755; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0052811; F:1-phosphatidylinositol-3-phosphate 4-kinase activity; TAS:Reactome.
GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; TAS:Reactome.
GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IDA:UniProtKB.
GO; GO:0052810; F:1-phosphatidylinositol-5-kinase activity; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019900; F:kinase binding; IDA:UniProtKB.
GO; GO:0052812; F:phosphatidylinositol-3,4-bisphosphate 5-kinase activity; TAS:Reactome.
GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
GO; GO:0090630; P:activation of GTPase activity; IMP:UniProtKB.
GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
GO; GO:0016477; P:cell migration; NAS:UniProtKB.
GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
GO; GO:0048041; P:focal adhesion assembly; IMP:UniProtKB.
GO; GO:0006650; P:glycerophospholipid metabolic process; TAS:ProtInc.
GO; GO:0030216; P:keratinocyte differentiation; TAS:UniProtKB.
GO; GO:0006909; P:phagocytosis; TAS:UniProtKB.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0008654; P:phospholipid biosynthetic process; IDA:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0097178; P:ruffle assembly; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 3.30.800.10; -; 1.
Gene3D; 3.30.810.10; -; 1.
InterPro; IPR023610; PInositol-4-P-5-kinase.
InterPro; IPR027483; PInositol-4-P-5-kinase_C.
InterPro; IPR002498; PInositol-4-P-5-kinase_core.
InterPro; IPR027484; PInositol-4-P-5-kinase_N.
PANTHER; PTHR23086; PTHR23086; 1.
Pfam; PF01504; PIP5K; 1.
SMART; SM00330; PIPKc; 1.
PROSITE; PS51455; PIPK; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Isopeptide bond; Kinase; Membrane;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Transferase; Ubl conjugation.
CHAIN 1 562 Phosphatidylinositol 4-phosphate 5-kinase
type-1 alpha.
/FTId=PRO_0000185456.
DOMAIN 81 449 PIPK. {ECO:0000255|PROSITE-
ProRule:PRU00781}.
MOD_RES 486 486 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 103 103 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
VAR_SEQ 30 52 ASGIKRPMASEVLEARQDSYISL -> SGIKRPMASE (in
isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8955136}.
/FTId=VSP_016007.
VAR_SEQ 41 52 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041912.
VAR_SEQ 382 410 HMGGIPARNSKGERLLLYIGIIDILQSYR -> Q (in
isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041913.
VAR_SEQ 455 504 LKPSPSKKFRSGSSFSRRAGSSGNSCITYQPSVSGEHKAQV
TTKAEVEPG -> C (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8955136}.
/FTId=VSP_016008.
MUTAGEN 322 322 D->N: Does not affect targeting of RAC1
to the plasma membrane; when associated
with Q-440.
{ECO:0000269|PubMed:20660631}.
MUTAGEN 440 440 R->Q: Does not affect targeting of RAC1
to the plasma membrane; when associated
with N-322.
{ECO:0000269|PubMed:20660631}.
CONFLICT 257 257 K -> E (in Ref. 2; BAG58542).
{ECO:0000305}.
SEQUENCE 562 AA; 62633 MW; A8F7988EB73506A0 CRC64;
MASASSGPSS SVGFSSFDPA VPSCTLSSAA SGIKRPMASE VLEARQDSYI SLVPYASGMP
IKKIGHRSVD SSGETTYKKT TSSALKGAIQ LGITHTVGSL STKPERDVLM QDFYVVESIF
FPSEGSNLTP AHHYNDFRFK TYAPVAFRYF RELFGIRPDD YLYSLCSEPL IELCSSGASG
SLFYVSSDDE FIIKTVQHKE AEFLQKLLPG YYMNLNQNPR TLLPKFYGLY CVQAGGKNIR
IVVMNNLLPR SVKMHIKYDL KGSTYKRRAS QKEREKPLPT FKDLDFLQDI PDGLFLDADM
YNALCKTLQR DCLVLQSFKI MDYSLLMSIH NIDHAQREPL SSETQYSVDT RRPAPQKALY
STAMESIQGE ARRGGTMETD DHMGGIPARN SKGERLLLYI GIIDILQSYR FVKKLEHSWK
ALVHDGDTVS VHRPGFYAER FQRFMCNTVF KKIPLKPSPS KKFRSGSSFS RRAGSSGNSC
ITYQPSVSGE HKAQVTTKAE VEPGVHLGRP DVLPQTPPLE EISEGSPIPD PSFSPLVGET
LQMLTTSTTL EKLEVAESEF TH


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EIAAB31015 68 kDa type I phosphatidylinositol-4-phosphate 5-kinase alpha,Homo sapiens,Human,Phosphatidylinositol-4-phosphate 5-kinase type I alpha,Phosphatidylinositol-4-phosphate 5-kinase type-1 alpha,PIP5K1A,P
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EIAAB31014 68 kDa type I phosphatidylinositol-4-phosphate 5-kinase,Mouse,Mus musculus,Phosphatidylinositol-4-phosphate 5-kinase type I alpha,Phosphatidylinositol-4-phosphate 5-kinase type I beta,Phosphatidylinos
EIAAB30997 1-phosphatidylinositol-5-phosphate 4-kinase 2-alpha,Chicken,Diphosphoinositide kinase 2-alpha,Gallus gallus,Phosphatidylinositol-5-phosphate 4-kinase type II alpha,Phosphatidylinositol-5-phosphate 4-k
EIAAB31018 Mouse,Mus musculus,Phosphatidylinositol-4-phosphate 5-kinase type I alpha,Phosphatidylinositol-4-phosphate 5-kinase type I beta,Phosphatidylinositol-4-phosphate 5-kinase type-1 beta,Pip5k1a,Pip5k1b,PI
EIAAB30998 1-phosphatidylinositol-5-phosphate 4-kinase 2-alpha,Diphosphoinositide kinase 2-alpha,Phosphatidylinositol-5-phosphate 4-kinase type II alpha,Phosphatidylinositol-5-phosphate 4-kinase type-2 alpha,PI(
EIAAB30995 1-phosphatidylinositol-5-phosphate 4-kinase 2-alpha,Diphosphoinositide kinase 2-alpha,Phosphatidylinositol-5-phosphate 4-kinase type II alpha,Phosphatidylinositol-5-phosphate 4-kinase type-2 alpha,PI(
EIAAB29518 Cpk,Cpk-m,Mouse,Mus musculus,p170,Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha,Phosphoinositide 3-kinase-C2-alpha,PI3K-C2-alpha,Pik3c2a,PtdIns-3-kinase C2 subunit alpha
EIAAB29519 Homo sapiens,Human,Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha,Phosphoinositide 3-kinase-C2-alpha,PI3K-C2-alpha,PIK3C2A,PtdIns-3-kinase C2 subunit alpha
EIAAB31019 Homo sapiens,Human,Phosphatidylinositol-4-phosphate 5-kinase type I beta,Phosphatidylinositol-4-phosphate 5-kinase type-1 beta,PIP5K1B,PIP5K1-beta,PIP5KIbeta,Protein STM-7,PtdIns(4)P-5-kinase 1 beta,S
EIAAB31022 Homo sapiens,Human,KIAA0589,Phosphatidylinositol-4-phosphate 5-kinase type I gamma,Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma,PIP5K1C,PIP5K1-gamma,PIP5KIgamma,PtdIns(4)P-5-kinase 1 gamma
EIAAB31021 Kiaa0589,Mouse,Mus musculus,Phosphatidylinositol-4-phosphate 5-kinase type I gamma,Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma,Pip5k1c,PIP5K1-gamma,PIP5KIgamma,PtdIns(4)P-5-kinase 1 gamma
EIAAB31020 Phosphatidylinositol-4-phosphate 5-kinase type I gamma,Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma,Pip5k1c,PIP5K1-gamma,PIP5KIgamma,PtdIns(4)P-5-kinase 1 gamma,Rat,Rattus norvegicus
EIAAB31016 Chicken,Gallus gallus,Phosphatidylinositol-4-phosphate 5-kinase type I beta,Phosphatidylinositol-4-phosphate 5-kinase type-1 beta,PIP5K1B,PIP5K1-beta,PIP5KIbeta,PtdIns(4)P-5-kinase 1 beta,RCJMB04_20j1
EIAAB29552 55 kDa type II phosphatidylinositol 4-kinase,Phosphatidylinositol 4-kinase type 2-alpha,Phosphatidylinositol 4-kinase type II-alpha,Pi4k2a,Pi4kii,Rat,Rattus norvegicus
EIAAB31006 Homo sapiens,Human,Phosphatidylinositol 4-kinase alpha,PI4KA,PI4K-alpha,PI4-kinase alpha,PIK4,PIK4CA,PtdIns-4-kinase alpha
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EIAAB31007 Bos taurus,Bovine,Phosphatidylinositol 4-kinase alpha,PI4KA,PI4K-alpha,PI4-kinase alpha,PIK4CA,PtdIns-4-kinase alpha
EIAAB31001 1-phosphatidylinositol-5-phosphate 4-kinase 2-beta,Diphosphoinositide kinase 2-beta,Mouse,Mus musculus,Phosphatidylinositol-5-phosphate 4-kinase type II beta,Phosphatidylinositol-5-phosphate 4-kinase
EIAAB29554 Homo sapiens,Human,Phosphatidylinositol 4-kinase type 2-alpha,Phosphatidylinositol 4-kinase type II-alpha,PI4K2A
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