Q6PFW1O15082Q5HYF8Q7Z3A7Q86TE7Q86UV3Q86UV4Q86XW8Q8IZN0VIP1_HUMANInositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 12.7.4.24Diphosphoinositol pentakisphosphate kinase 1Histidine acid phosphatase domain-containing protein 2AIP6 kinaseInositol pyrophosphate synthase 1InsP6 and PP-IP5 kinase 1VIP1 homologhsVIP1PPIP5K1HISPPD2AIP6KIPS1KIAA0377VIP1Homo sapiensHumanEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomoCATSPER2, a human autosomal nonsyndromic male infertility gene.NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5)Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro.NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7)SEQUENCE REVISIONThe full-ORF clone resource of the German cDNA consortium.NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4)The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6)A probability-based approach for high-throughput protein phosphorylation analysis and site localization.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Cloning and characterization of two human VIP1-like inositol hexakisphosphate and diphosphoinositol pentakisphosphate kinases.FUNCTIONCATALYTIC ACTIVITYBIOPHYSICOCHEMICAL PROPERTIESSUBCELLULAR LOCATIONTISSUE SPECIFICITYPurification, sequencing, and molecular identification of a mammalian PP-InsP5 kinase that is activated when cells are exposed to hyperosmotic stress.FUNCTIONCATALYTIC ACTIVITYBIOPHYSICOCHEMICAL PROPERTIESSUBCELLULAR LOCATIONCombining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1152IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]A quantitative atlas of mitotic phosphorylation.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Structural analysis and detection of biological inositol pyrophosphates reveal that the family of VIP/diphosphoinositol pentakisphosphate kinases are 1/3-kinases.FUNCTIONCATALYTIC ACTIVITYReceptor-dependent compartmentalization of PPIP5K1, a kinase with a cryptic polyphosphoinositide binding domain.BIOPHYSICOCHEMICAL PROPERTIESCATALYTIC ACTIVITYSUBCELLULAR LOCATIONPOLYPHOSPHOINOSITIDE-BINDING DOMAINMUTAGENESIS OF ARG-399 AND ARG-417Toward a comprehensive characterization of a human cancer cell phosphoproteome.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-944; SER-987; SER-1037; SER-1073 AND SER-1152IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-944IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation. Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Activated when cells are exposed to hyperosmotic stress.1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ADP5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP0.12 uM for InsP60.1 uM for InsP70.03 nmol/min/mg enzyme with InsP6 as substrate0.13 nmol/min/mg enzyme with InsP7 as substrateThe catalytic efficiency is 80 folds higher for 5-PP-InsP5 (InsP7) compared to InsP6.CytoplasmCytosolCell membraneRelocalizes to the plasma membrane upon activation of the PtdIns 3-kinase pathway.Q6PFW1-11Q6PFW1-22Q6PFW1-33Q6PFW1-44Q6PFW1-55Q6PFW1-66Q6PFW1-77Widely expressed, with a higher expression in skeletal muscle, heart and brain.The C-terminal acid phosphatase-like domain binds PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the phosphatase domain of histidine acid phosphatases, it has no phosphatase activity.Belongs to the histidine acid phosphatase family. VIP1 subfamily.Extended N-terminus.Alternative splicingATP-bindingCell membraneCytoplasmKinaseMembraneNucleotide-bindingPhosphoproteinReference proteomeTransferasesubstrateATPATPATPsubstrateATPATPATPsubstratesubstrateATPATPATPsubstrateNNGYLETRFCHVGQAGLELLTSSDLPASASQSAGITGVSHRTQPDRARADGVMEVEQLPFSVEGVILVAEGAVGALPVLATMVPRHMDTMWSLTASEGESTTAHFFLGAGDEGLGTRGIGMRPEESDSELLEDEEDEVPPEPQIIVGICAMTKKSKSKPMTQILERLCRFDYLTVVILGEDVILNEPVENWPSCHCLISFHSKGFPLDKAVAYSKLRNPFLINDLAMQYYIQDRREVYRILQEEGIDLPRYAVLNRDPARPEECNLIEGEDQVEVNGAVFPKPFVEKPVSAEDHNVYIYYPSSAGGGSQRLFRKIGSRSSVYSPESSVRKTGSYIYEEFMPTDGTDVKVYTVGPDYAHAEARKSPALDGKVERDSEGKEIRYPVMLTAMEKLVARKVCVAFKQTVCGFDLLRANGHSFVCDVNGFSFVKNSMKYYDDCAKILGNTIMRELAPQFQIPWSIPTEAEDIPIVPTTSGTMMELRCVIAIIRHGDRTPKQKMKMEVKHPRFFALFEKHGGYKTGKLKLKRPEQLQEVLDITRLLLAELEKEPGGEIEEKTGKLEQLKSVLEMYGHFSGINRKVQLTYYPHGVKASNEGQDPQRETLAPSLLLVLKWGGELTPAGRVQAEELGRAFRCMYPGGQGDYAGFPGCGLLRLHSTFRHDLKIYASDEGRVQMTAAAFAKGLLALEGELTPILVQMVKSANMNGLLDSDGDSLSSCQHRVKARLHHILQQDAPFGPEDYDQLAPTRSTSLLNSMTIIQNPVKVCDQVFALIENLTHQIRERMQDPRSVDLQLYHSETLELMLQRWSKLERDFRQKSGRYDISKIPDIYDCVKYDVQHNGSLGLQGTAELLRLSKALADVVIPQEYGISREEKLEIAVGFCLPLLRKILLDLQRTHEDESVNKLHPLCYLRYSRGVLSPGRHVRTRLYFTSESHVHSLLSVFRYGGLLDETQDAQWQRALDYLSAISELNYMTQIVIMLYEDNTQDPLSEERFHVELHFSPGVKGVEEEGSAPAGCGFRPASSENEEMKTNQGSMENLCPGKASDEPDRALQTSPQPPEGPGLPRRSPLIRNRKAGSMEVLSETSSSRPGGYRLFSSSRPPTEMKQSGLGSQCTGLFSTTVLGGSSSAPNLQDYARSHGKKLPPASLKHRDELLFVPAVKRFSVSFAKHPTNGFEGCSMVPTIYPLETLHNALSLRQVSEFLSRVCQRHTDAQAQASAALFDSMHSSQASDNPFSPPRTLHSPPLQLQQRSEKPPWYSSGPSSTVSSAGPSSPTTVDGNSQFGFSDQPSLNSHVAEEHQGLGLLQETPGSGAQELSIEGEQELFEPNQSPQVPPMETSQPYEEVSQPCQEVPDISQPCQDISEALSQPCQKVPDISQQCQENHDNGNHTCQEVPHISQPCQKSSQLCQKVSEEVCQLCLENSEEVSQPCQGVSVEVGKLVHKFHVGVGSLVQETLVEVGSPAEEIPEEVIQPYQEFSVEVGRLAQETSAINLLSQGIPEIDKPSQEFPEEIDLQAQEVPEEIN
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