VIP1_HUMAN - dbPTM
VIP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VIP1_HUMAN
UniProt AC Q6PFW1
Protein Name Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1
Gene Name PPIP5K1
Organism Homo sapiens (Human).
Sequence Length 1433
Subcellular Localization Cytoplasm, cytosol . Cell membrane . Relocalizes to the plasma membrane upon activation of the PtdIns 3-kinase pathway.
Protein Description 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 positions 1 or 3 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates at position 1 or 3 PP-InsP5, produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Activated when cells are exposed to hyperosmotic stress..
Protein Sequence MWSLTASEGESTTAHFFLGAGDEGLGTRGIGMRPEESDSELLEDEEDEVPPEPQIIVGICAMTKKSKSKPMTQILERLCRFDYLTVVILGEDVILNEPVENWPSCHCLISFHSKGFPLDKAVAYSKLRNPFLINDLAMQYYIQDRREVYRILQEEGIDLPRYAVLNRDPARPEECNLIEGEDQVEVNGAVFPKPFVEKPVSAEDHNVYIYYPSSAGGGSQRLFRKIGSRSSVYSPESSVRKTGSYIYEEFMPTDGTDVKVYTVGPDYAHAEARKSPALDGKVERDSEGKEIRYPVMLTAMEKLVARKVCVAFKQTVCGFDLLRANGHSFVCDVNGFSFVKNSMKYYDDCAKILGNTIMRELAPQFQIPWSIPTEAEDIPIVPTTSGTMMELRCVIAIIRHGDRTPKQKMKMEVKHPRFFALFEKHGGYKTGKLKLKRPEQLQEVLDITRLLLAELEKEPGGEIEEKTGKLEQLKSVLEMYGHFSGINRKVQLTYYPHGVKASNEGQDPQRETLAPSLLLVLKWGGELTPAGRVQAEELGRAFRCMYPGGQGDYAGFPGCGLLRLHSTFRHDLKIYASDEGRVQMTAAAFAKGLLALEGELTPILVQMVKSANMNGLLDSDGDSLSSCQHRVKARLHHILQQDAPFGPEDYDQLAPTRSTSLLNSMTIIQNPVKVCDQVFALIENLTHQIRERMQDPRSVDLQLYHSETLELMLQRWSKLERDFRQKSGRYDISKIPDIYDCVKYDVQHNGSLGLQGTAELLRLSKALADVVIPQEYGISREEKLEIAVGFCLPLLRKILLDLQRTHEDESVNKLHPLCYLRYSRGVLSPGRHVRTRLYFTSESHVHSLLSVFRYGGLLDETQDAQWQRALDYLSAISELNYMTQIVIMLYEDNTQDPLSEERFHVELHFSPGVKGVEEEGSAPAGCGFRPASSENEEMKTNQGSMENLCPGKASDEPDRALQTSPQPPEGPGLPRRSPLIRNRKAGSMEVLSETSSSRPGGYRLFSSSRPPTEMKQSGLGSQCTGLFSTTVLGGSSSAPNLQDYARSHGKKLPPASLKHRDELLFVPAVKRFSVSFAKHPTNGFEGCSMVPTIYPLETLHNALSLRQVSEFLSRVCQRHTDAQAQASAALFDSMHSSQASDNPFSPPRTLHSPPLQLQQRSEKPPWYSSGPSSTVSSAGPSSPTTVDGNSQFGFSDQPSLNSHVAEEHQGLGLLQETPGSGAQELSIEGEQELFEPNQSPQVPPMETSQPYEEVSQPCQEVPDISQPCQDISEALSQPCQKVPDISQQCQENHDNGNHTCQEVPHISQPCQKSSQLCQKVSEEVCQLCLENSEEVSQPCQGVSVEVGKLVHKFHVGVGSLVQETLVEVGSPAEEIPEEVIQPYQEFSVEVGRLAQETSAINLLSQGIPEIDKPSQEFPEEIDLQAQEVPEEIN
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
126UbiquitinationDKAVAYSKLRNPFLI
HHHHHHHHHCCCCHH		38.50-
126 (in isoform 2)Ubiquitination-38.50-
230PhosphorylationFRKIGSRSSVYSPES
HHHHCCCCCCCCCHH		26.3426552605
231PhosphorylationRKIGSRSSVYSPESS
HHHCCCCCCCCCHHH		24.7826552605
233PhosphorylationIGSRSSVYSPESSVR
HCCCCCCCCCHHHCC		22.0626552605
234PhosphorylationGSRSSVYSPESSVRK
CCCCCCCCCHHHCCC		21.7526552605
237PhosphorylationSSVYSPESSVRKTGS
CCCCCCHHHCCCCCC		37.2026552605
238PhosphorylationSVYSPESSVRKTGSY
CCCCCHHHCCCCCCE		25.0326552605
241UbiquitinationSPESSVRKTGSYIYE
CCHHHCCCCCCEEEE		55.90-
241 (in isoform 2)Ubiquitination-55.90-
261PhosphorylationDGTDVKVYTVGPDYA
CCCCEEEEEECCCCH		7.0328796482
262PhosphorylationGTDVKVYTVGPDYAH
CCCEEEEEECCCCHH		23.2128796482
267PhosphorylationVYTVGPDYAHAEARK
EEEECCCCHHHHHHC		11.9228796482
274UbiquitinationYAHAEARKSPALDGK
CHHHHHHCCCCCCCC		68.77-
274 (in isoform 2)Ubiquitination-68.77-
281UbiquitinationKSPALDGKVERDSEG
CCCCCCCCEEECCCC		40.36-
293PhosphorylationSEGKEIRYPVMLTAM
CCCCCCCHHHHHHHH		13.07-
344UbiquitinationSFVKNSMKYYDDCAK
CCCCCCCCHHHHHHH		40.24-
344 (in isoform 2)Ubiquitination-40.24-
345PhosphorylationFVKNSMKYYDDCAKI
CCCCCCCHHHHHHHH		11.9529496907
346PhosphorylationVKNSMKYYDDCAKIL
CCCCCCHHHHHHHHH		10.37-
351UbiquitinationKYYDDCAKILGNTIM
CHHHHHHHHHCHHHH		44.81-
351 (in isoform 2)Ubiquitination-44.81-
457UbiquitinationLLLAELEKEPGGEIE
HHHHHHHCCCCCCHH		80.14-
475PhosphorylationGKLEQLKSVLEMYGH
CHHHHHHHHHHHHCC		40.2920068231
500UbiquitinationTYYPHGVKASNEGQD
EEECCCCCCCCCCCC		51.17-
553PhosphorylationYPGGQGDYAGFPGCG
CCCCCCCCCCCCCCC		18.5621945579
573UbiquitinationSTFRHDLKIYASDEG
CCCCCCEEEEECCCC		39.46-
573 (in isoform 2)Ubiquitination-39.46-
575PhosphorylationFRHDLKIYASDEGRV
CCCCEEEEECCCCCH		9.8528064214
585PhosphorylationDEGRVQMTAAAFAKG
CCCCHHHHHHHHHHH		8.96-
601PhosphorylationLALEGELTPILVQMV
HHHCCCCHHHHHHHH		12.18-
650PhosphorylationAPFGPEDYDQLAPTR
CCCCHHHHHHHCCCC		12.1527642862
664PhosphorylationRSTSLLNSMTIIQNP
CCCHHHHHCCCCCCH		19.7829802988
666PhosphorylationTSLLNSMTIIQNPVK
CHHHHHCCCCCCHHH		18.1029802988
698PhosphorylationERMQDPRSVDLQLYH
HHCCCCCCCCEEECC		25.9329978859
704PhosphorylationRSVDLQLYHSETLEL
CCCCEEECCHHHHHH		7.1329978859
706PhosphorylationVDLQLYHSETLELML
CCEEECCHHHHHHHH		20.7929978859
708PhosphorylationLQLYHSETLELMLQR
EEECCHHHHHHHHHH		28.6629978859
717PhosphorylationELMLQRWSKLERDFR
HHHHHHHHHHHHHHH		29.5626074081
726AcetylationLERDFRQKSGRYDIS
HHHHHHHHCCCCCHH		51.0919413330
730PhosphorylationFRQKSGRYDISKIPD
HHHHCCCCCHHHCCC		22.5819413330
739PhosphorylationISKIPDIYDCVKYDV
HHHCCCHHHHHEEEC		15.63-
764PhosphorylationTAELLRLSKALADVV
HHHHHHHHHHHHCCC		14.95-
765UbiquitinationAELLRLSKALADVVI
HHHHHHHHHHHCCCC		52.60-
765 (in isoform 2)Ubiquitination-52.60-
776PhosphorylationDVVIPQEYGISREEK
CCCCCHHHCCCHHHH		17.95-
779PhosphorylationIPQEYGISREEKLEI
CCHHHCCCHHHHHHH		29.31-
813 (in isoform 2)Ubiquitination-46.12-
817 (in isoform 4)Phosphorylation-1.7724719451
818PhosphorylationVNKLHPLCYLRYSRG
HHHHCHHHHHEECCC		3.3724719451
818 (in isoform 2)Phosphorylation-3.3724719451
818 (in isoform 3)Phosphorylation-3.3724719451
818 (in isoform 7)Phosphorylation-3.3724719451
823 (in isoform 4)Phosphorylation-19.0024719451
824PhosphorylationLCYLRYSRGVLSPGR
HHHHEECCCCCCCCC		30.2424719451
824 (in isoform 2)Phosphorylation-30.2424719451
824 (in isoform 3)Phosphorylation-30.2424719451
824 (in isoform 7)Phosphorylation-30.2424719451
828PhosphorylationRYSRGVLSPGRHVRT
EECCCCCCCCCCEEE		23.9324719451
940PhosphorylationSENEEMKTNQGSMEN
CCCHHHCCCCCCHHH		31.3128450419
944PhosphorylationEMKTNQGSMENLCPG
HHCCCCCCHHHCCCC		17.1023401153
954PhosphorylationNLCPGKASDEPDRAL
HCCCCCCCCCCCHHH		46.0928450419
963PhosphorylationEPDRALQTSPQPPEG
CCCHHHCCCCCCCCC		43.1323401153
964PhosphorylationPDRALQTSPQPPEGP
CCHHHCCCCCCCCCC		14.4730266825
977PhosphorylationGPGLPRRSPLIRNRK
CCCCCCCCCCCCCCC		25.9019060867
987PhosphorylationIRNRKAGSMEVLSET
CCCCCCCCEEEECCC		19.3423401153
992PhosphorylationAGSMEVLSETSSSRP
CCCEEEECCCCCCCC		43.9623927012
994PhosphorylationSMEVLSETSSSRPGG
CEEEECCCCCCCCCC		30.4527251275
995PhosphorylationMEVLSETSSSRPGGY
EEEECCCCCCCCCCE		23.4327251275
996PhosphorylationEVLSETSSSRPGGYR
EEECCCCCCCCCCEE		37.4730576142
997PhosphorylationVLSETSSSRPGGYRL
EECCCCCCCCCCEEC		42.1130576142
1002PhosphorylationSSSRPGGYRLFSSSR
CCCCCCCEECCCCCC		15.2830576142
1006PhosphorylationPGGYRLFSSSRPPTE
CCCEECCCCCCCCCC		31.8125106551
1007PhosphorylationGGYRLFSSSRPPTEM
CCEECCCCCCCCCCH		24.0423312004
1008PhosphorylationGYRLFSSSRPPTEMK
CEECCCCCCCCCCHH		47.8323312004
1012PhosphorylationFSSSRPPTEMKQSGL
CCCCCCCCCHHCCCC		51.9323312004
1021PhosphorylationMKQSGLGSQCTGLFS
HHCCCCCCCCCCCCE		27.4227080861
1028PhosphorylationSQCTGLFSTTVLGGS
CCCCCCCEEEECCCC		28.3627080861
1029PhosphorylationQCTGLFSTTVLGGSS
CCCCCCEEEECCCCC		17.3727080861
1030PhosphorylationCTGLFSTTVLGGSSS
CCCCCEEEECCCCCC		16.7327732954
1035PhosphorylationSTTVLGGSSSAPNLQ
EEEECCCCCCCCCHH		21.2228450419
1036PhosphorylationTTVLGGSSSAPNLQD
EEECCCCCCCCCHHH		33.5228450419
1037PhosphorylationTVLGGSSSAPNLQDY
EECCCCCCCCCHHHH		49.8229496963
1044PhosphorylationSAPNLQDYARSHGKK
CCCCHHHHHHHCCCC		7.3128450419
1056PhosphorylationGKKLPPASLKHRDEL
CCCCCHHHHCCCCEE		43.6629457462
1073PhosphorylationVPAVKRFSVSFAKHP
CCCEEEEEEEECCCC		22.3822617229
1075PhosphorylationAVKRFSVSFAKHPTN
CEEEEEEEECCCCCC		20.4922617229
1085 (in isoform 7)Phosphorylation-61.7725849741
1104PhosphorylationETLHNALSLRQVSEF
HHHHHHHHHHHHHHH		21.0624719451
1109PhosphorylationALSLRQVSEFLSRVC
HHHHHHHHHHHHHHH		17.8128111955
1113PhosphorylationRQVSEFLSRVCQRHT
HHHHHHHHHHHHHHH		28.1728111955
1120PhosphorylationSRVCQRHTDAQAQAS
HHHHHHHHHHHHHHH		34.9128111955
1127PhosphorylationTDAQAQASAALFDSM
HHHHHHHHHHHHHHH		11.2918669648
1133PhosphorylationASAALFDSMHSSQAS
HHHHHHHHHHCCCCC		15.8528111955
1136PhosphorylationALFDSMHSSQASDNP
HHHHHHHCCCCCCCC		18.5928111955
1137PhosphorylationLFDSMHSSQASDNPF
HHHHHHCCCCCCCCC		18.3222210691
1140PhosphorylationSMHSSQASDNPFSPP
HHHCCCCCCCCCCCC		30.2222210691
1145PhosphorylationQASDNPFSPPRTLHS
CCCCCCCCCCCCCCC		34.9426074081
1149PhosphorylationNPFSPPRTLHSPPLQ
CCCCCCCCCCCCCCC		34.3023401153
1152PhosphorylationSPPRTLHSPPLQLQQ
CCCCCCCCCCCCHHH		31.1823401153
1161PhosphorylationPLQLQQRSEKPPWYS
CCCHHHCCCCCCCCC		45.7126074081
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of VIP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VIP1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of VIP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CYLD_HUMANCYLDphysical
18636086
IRF3_HUMANIRF3physical
18636086
ZC3HF_HUMANZC3H15physical
22939629
ZBT8B_HUMANZBTB8Bphysical
22939629
BUD23_HUMANWBSCR22physical
22939629
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VIP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-730 AND SER-944, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1152, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND MASSSPECTROMETRY.

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