VIP1_DROME - dbPTM
VIP1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VIP1_DROME
UniProt AC Q9VR59
Protein Name Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
Gene Name l(1)G0196
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1696
Subcellular Localization Cytoplasm, cytosol .
Protein Description Bifunctional inositol kinase that acts in concert with the IP6K kinases 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, may regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, and exocytosis. 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..
Protein Sequence MSYTELESGYQDISQQHQQQNPHQSQPQQRVGFYLGLQDGNGDTDFGDSNDGMDSDTSTSSSNSKQVVVGICAMAKKTQSKPMKEILTRLGEFEFIKLVTFEENVILREPVQNWPTCDCLVSFHSKGFPLEKAIEYAQLRNPFVLNNLHMQYDIQDRRRVYAILEKEGIEIPRYAVLDRDSPDPKHHELIESEDHVEVNGITFNKPFVEKPVSAEDHNIYIYYPTSAGGGSQRLFRKIGSRSSVYSPESRVRKTGSFIYEDFMPTDGTDVKVYTVGPDYAHAEARKSPALDGKVERDSEGKEIRYPVILNHSEKLISRKVCLAFKQTVCGFDLLRANGKSYVCDVNGFSFVKNSNKYYDDCAKILGNMILRELTPTLHIPWSVPFQLDDPPIVPTTFGKMMELRCVVAVIRHGDRTPKQKMKVEVRHPKFFEIFEKYDGYKLGHVKLKRPKQLQEILDIARFLLSEIHTKAHAEIEEKESKLEQLKNVLEMYGHFSGINRKVQMKYQPKGRPRGSSSDDTNLAADQPVEPSLVLILKWGGELTPAGRIQAEELGRIFRCMYPGGQGRSDYSGTQGLGLLRLHSTFRHDLKIYASDEGRVQMTAAAFAKGLLALEGELTPILVQMVKSANTNGLLDNDCDSSKYQNLAKGRLHELMQNDREFSKEDRELINPCNSKSITQALDFVKNPVDCCHHVHLLIRELLHIISIKKDDPKTKDAILYHGETWDLMRCRWEKIEKDFSTKSKLFDISKIPDIYDCIKYDLQHNQHTLQYDQAEELYIYAKNLADIVIPQEYGLTPQEKLAIGQGICSPLLRKIKGDLQRNIDEVEDEFMNRLNPHYSHGVASPQRHVRTRLYFTSESHVHSLLTVLRYGGLLNVVTDEQWRRAMDYISMVSELNYMSQIVIMLYEDPTKDPTSEERFHVELHFSPGVNCCVQKNLPPGPGFRPHSHGDNACNVSLQSSDESNPARIEEENDSNSGEEREGKKRGTSGQRSTDRSAERISPAFGFNRLELRSKQFKSKPIPIGAHHTVSGHEAMDLAKRLNEELASHQQQQNQQLRPISPDIRAVTPDCEPRSRSFEQRPTSGVCAKEPDSQVSVSVSASVSSANASTSSRRQRHSIAGQMSYMKMLGFGGFSKKMATSANSLFSTAVISGSSSAPNLRDMITVSSSGFGDVPPIRPLETLHNALSLRKLDSFLQDMILAQIFKTPTGSPPRGFSKNTLPAVSSMTLTASNQTEVVEHEPISTTVTPTFDRRGSESGSTADAHLRLLSESQCPNLDDSNTELRESLAGKMELWPQDIVKAAEDEELNLSELETKPSLDLTMEIMERGVAGIASIQPMNRDSDETMGGGVFLSVCEEQGSGSTCLTPVSFGMDLDLSMVANKGSITLSMEGFDDDEDATLSAATTPSLLADCEPRLESCYCCPSHAEAPPEVPSDDPRFGFALPVRVTQASPEHARPVRRAHDPVSPRIQKQISLFEGNAAMATGQEKTESSGSVGGGAILHASINLPAAGPHHLRQDARLRKFENLTQSTSNSNFPFESNTLKRVPMQTTKDYDNVSHTQSCINLKSGSSGVLGGSPQRQRGSDGGGVGASGVPAESREPTRVHYGRMNSTCCSASASPSPSPGALIVKERFIEPPKRGVVRGYHGKTQSMDADFLFNEFLLLPAMAPAKISFDSSDIDQASDDDSPSSSKQRHA
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
2Phosphorylation------MSYTELESG
------CCHHHHHHH		52.6619429919
3Phosphorylation-----MSYTELESGY
-----CCHHHHHHHC		18.9819429919
4Phosphorylation----MSYTELESGYQ
----CCHHHHHHHCH		43.3019429919
505AcetylationINRKVQMKYQPKGRP
CCCCCCEECCCCCCC		24.5221791702
520PhosphorylationRGSSSDDTNLAADQP
CCCCCCCCCCCCCCC		36.8029892262
642AcetylationDNDCDSSKYQNLAKG
CCCCCCHHHHHHHHH		55.6021791702
956PhosphorylationGDNACNVSLQSSDES
CCCCCCEECCCCCCC		13.4918327897
974PhosphorylationRIEEENDSNSGEERE
CCCCCCCCCCCCCCC		44.4719429919
976PhosphorylationEEENDSNSGEEREGK
CCCCCCCCCCCCCCC		52.0819429919
996PhosphorylationGQRSTDRSAERISPA
CCCCCCCCHHHHCCC		36.9722817900
1001PhosphorylationDRSAERISPAFGFNR
CCCHHHHCCCCCCCH		19.1819429919
1028PhosphorylationIPIGAHHTVSGHEAM
CCCCCCCCCCHHHHH		13.3921082442
1030PhosphorylationIGAHHTVSGHEAMDL
CCCCCCCCHHHHHHH		35.2721082442
1060PhosphorylationNQQLRPISPDIRAVT
HHHCCCCCCCHHHCC		21.1419429919
1067PhosphorylationSPDIRAVTPDCEPRS
CCCHHHCCCCCCCCC		16.6619429919
1076PhosphorylationDCEPRSRSFEQRPTS
CCCCCCCCCCCCCCC		34.0929892262
1082PhosphorylationRSFEQRPTSGVCAKE
CCCCCCCCCCCCCCC		40.0621082442
1117PhosphorylationSSRRQRHSIAGQMSY
CCHHHHHCHHHHHHH		19.1421082442
1134PhosphorylationMLGFGGFSKKMATSA
HHCCCCCCHHHCCCH		34.3419429919
1139PhosphorylationGFSKKMATSANSLFS
CCCHHHCCCHHHHHH		25.5221082442
1143PhosphorylationKMATSANSLFSTAVI
HHCCCHHHHHHEEHH		30.4329892262
1153PhosphorylationSTAVISGSSSAPNLR
HEEHHCCCCCCCCHH		17.8329892262
1154PhosphorylationTAVISGSSSAPNLRD
EEHHCCCCCCCCHHH		33.7621082442
1155PhosphorylationAVISGSSSAPNLRDM
EHHCCCCCCCCHHHC		49.8221082442
1206PhosphorylationILAQIFKTPTGSPPR
HHHHHHCCCCCCCCC		18.4819429919
1208PhosphorylationAQIFKTPTGSPPRGF
HHHHCCCCCCCCCCC		56.3719429919
1210PhosphorylationIFKTPTGSPPRGFSK
HHCCCCCCCCCCCCC		33.9219429919
1255PhosphorylationPTFDRRGSESGSTAD
CCCCCCCCCCCCCHH		27.1219429919
1257PhosphorylationFDRRGSESGSTADAH
CCCCCCCCCCCHHHH		39.4828490779
1259PhosphorylationRRGSESGSTADAHLR
CCCCCCCCCHHHHHH		29.6918511481
1260PhosphorylationRGSESGSTADAHLRL
CCCCCCCCHHHHHHH		31.8921082442
1279PhosphorylationQCPNLDDSNTELRES
CCCCCCCCCHHHHHH		45.3721082442
1281PhosphorylationPNLDDSNTELRESLA
CCCCCCCHHHHHHHC		40.1121082442
1286PhosphorylationSNTELRESLAGKMEL
CCHHHHHHHCCCCCC		19.6521082442
1562PhosphorylationDNVSHTQSCINLKSG
CCCCCCCEEEECCCC		20.3727794539
1683PhosphorylationSSDIDQASDDDSPSS
HHHCCCCCCCCCCCH		35.6227794539
1687PhosphorylationDQASDDDSPSSSKQR
CCCCCCCCCCHHHCC		33.4127794539
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_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VIP1_DROME !!
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_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TFP11_DROMEsip1physical
14605208
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VIP1_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974; SER-1001 ANDSER-1255, AND MASS SPECTROMETRY.
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1060, AND MASSSPECTROMETRY.

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