dbPTM

VIP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VIP2_HUMAN
UniProt AC	O43314
Protein Name	Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2
Gene Name	PPIP5K2
Organism	Homo sapiens (Human).
Sequence Length	1243
Subcellular Localization	Cytoplasm, cytosol .
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..
Protein Sequence	MSEAPRFFVGPEDTEINPGNYRHFFHHADEDDEEEDDSPPERQIVVGICSMAKKSKSKPMKEILERISLFKYITVVVFEEEVILNEPVENWPLCDCLISFHSKGFPLDKAVAYAKLRNPFVINDLNMQYLIQDRREVYSILQAEGILLPRYAILNRDPNNPKECNLIEGEDHVEVNGEVFQKPFVEKPVSAEDHNVYIYYPTSAGGGSQRLFRKIGSRSSVYSPESNVRKTGSYIYEEFMPTDGTDVKVYTVGPDYAHAEARKSPALDGKVERDSEGKEVRYPVILNAREKLIAWKVCLAFKQTVCGFDLLRANGQSYVCDVNGFSFVKNSMKYYDDCAKILGNIVMRELAPQFHIPWSIPLEAEDIPIVPTTSGTMMELRCVIAVIRHGDRTPKQKMKMEVRHQKFFDLFEKCDGYKSGKLKLKKPKQLQEVLDIARQLLMELGQNNDSEIEENKPKLEQLKTVLEMYGHFSGINRKVQLTYLPHGCPKTSSEEEDSRREEPSLLLVLKWGGELTPAGRVQAEELGRAFRCMYPGGQGDYAGFPGCGLLRLHSTYRHDLKIYASDEGRVQMTAAAFAKGLLALEGELTPILVQMVKSANMNGLLDSDSDSLSSCQQRVKARLHEILQKDRDFTAEDYEKLTPSGSISLIKSMHLIKNPVKTCDKVYSLIQSLTSQIRHRMEDPKSSDIQLYHSETLELMLRRWSKLEKDFKTKNGRYDISKIPDIYDCIKYDVQHNGSLKLENTMELYRLSKALADIVIPQEYGITKAEKLEIAKGYCTPLVRKIRSDLQRTQDDDTVNKLHPVYSRGVLSPERHVRTRLYFTSESHVHSLLSILRYGALCNESKDEQWKRAMDYLNVVNELNYMTQIVIMLYEDPNKDLSSEERFHVELHFSPGAKGCEEDKNLPSGYGYRPASRENEGRRPFKIDNDDEPHTSKRDEVDRAVILFKPMVSEPIHIHRKSPLPRSRKTATNDEESPLSVSSPEGTGTWLHYTSGVGTGRRRRRSGEQITSSPVSPKSLAFTSSIFGSWQQVVSENANYLRTPRTLVEQKQNPTVGSHCAGLFSTSVLGGSSSAPNLQDYARTHRKKLTSSGCIDDATRGSAVKRFSISFARHPTNGFELYSMVPSICPLETLHNALSLKQVDEFLASIASPSSDVPRKTAEISSTALRSSPIMRKKVSLNTYTPAKILPTPPATLKSTKASSKPATSGPSSAVVPNTSSRKKNITSKTETHEHKKNTGKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	FFVGPEDTEINPGNY EECCCCCCCCCCCCC	36.78	-
21	Phosphorylation	TEINPGNYRHFFHHA CCCCCCCCCCEEECC	16.04	29978859
38	Phosphorylation	DDEEEDDSPPERQIV CCCCCCCCCCHHHHH	55.46	20201521
50	Phosphorylation	QIVVGICSMAKKSKS HHHHHHHHHHHHCCC	21.61	25278378
55	Phosphorylation	ICSMAKKSKSKPMKE HHHHHHHCCCCCHHH	41.26	25278378
61	Acetylation	KSKSKPMKEILERIS HCCCCCHHHHHHHHH	50.56	18586523
68	Phosphorylation	KEILERISLFKYITV HHHHHHHHHHHEEEE	33.69	24719451
115	Ubiquitination	DKAVAYAKLRNPFVI HHHHHHHHHCCCEEE	34.99	-
219	Phosphorylation	FRKIGSRSSVYSPES HHHHCCCCCCCCCCC	26.34	27732954
220	Phosphorylation	RKIGSRSSVYSPESN HHHCCCCCCCCCCCC	24.78	27732954
222	Phosphorylation	IGSRSSVYSPESNVR HCCCCCCCCCCCCCC	22.06	26852163
223	Phosphorylation	GSRSSVYSPESNVRK CCCCCCCCCCCCCCC	21.75	28985074
226	Phosphorylation	SSVYSPESNVRKTGS CCCCCCCCCCCCCCC	43.97	26852163
230	Ubiquitination	SPESNVRKTGSYIYE CCCCCCCCCCCEEEE	53.61	-
248	Acetylation	PTDGTDVKVYTVGPD CCCCCCEEEEEECCC	32.13	20167786
250	Phosphorylation	DGTDVKVYTVGPDYA CCCCEEEEEECCCCH	7.03	28796482
251	Phosphorylation	GTDVKVYTVGPDYAH CCCEEEEEECCCCHH	23.21	28796482
256	Phosphorylation	VYTVGPDYAHAEARK EEEECCCCHHHHHHC	11.92	28796482
263	Ubiquitination	YAHAEARKSPALDGK CHHHHHHCCCCCCCC	68.77	-
270	Acetylation	KSPALDGKVERDSEG CCCCCCCCEEECCCC	40.36	20167786
270	Ubiquitination	KSPALDGKVERDSEG CCCCCCCCEEECCCC	40.36	-
333	Ubiquitination	SFVKNSMKYYDDCAK EEECCCCCHHHHHHH	40.24	-
334	Phosphorylation	FVKNSMKYYDDCAKI EECCCCCHHHHHHHH	11.95	29496907
335	Phosphorylation	VKNSMKYYDDCAKIL ECCCCCHHHHHHHHH	10.37	-
406	Ubiquitination	KMEVRHQKFFDLFEK HHHHHHHHHHHHHHH	41.70	-
482	Phosphorylation	INRKVQLTYLPHGCP CCCEEEEEECCCCCC	13.11	28634298
483	Phosphorylation	NRKVQLTYLPHGCPK CCEEEEEECCCCCCC	27.16	23927012
491	Phosphorylation	LPHGCPKTSSEEEDS CCCCCCCCCCHHHHH	23.72	23401153
492	Phosphorylation	PHGCPKTSSEEEDSR CCCCCCCCCHHHHHH	41.71	30266825
493	Phosphorylation	HGCPKTSSEEEDSRR CCCCCCCCHHHHHHC	55.01	23401153
498	Phosphorylation	TSSEEEDSRREEPSL CCCHHHHHHCCCCCE	36.20	23927012
504	Phosphorylation	DSRREEPSLLLVLKW HHHCCCCCEEEEEEE	34.62	23898821
541	Phosphorylation	YPGGQGDYAGFPGCG CCCCCCCCCCCCCCC	18.56	21945579
561	Ubiquitination	STYRHDLKIYASDEG CEECCEEEEEECCCC	39.46	-
563	Phosphorylation	YRHDLKIYASDEGRV ECCEEEEEECCCCCH	9.85	28064214
573	Phosphorylation	DEGRVQMTAAAFAKG CCCCHHHHHHHHHHH	8.96	-
589	Phosphorylation	LALEGELTPILVQMV HHHCCCCHHHHHHHH	12.18	-
629	Ubiquitination	RLHEILQKDRDFTAE HHHHHHHHCCCCCHH	51.81	-
640	Ubiquitination	FTAEDYEKLTPSGSI CCHHHHHHCCCCCCH	51.97	-
646	Phosphorylation	EKLTPSGSISLIKSM HHCCCCCCHHHHHHH	17.22	27067055
648	Phosphorylation	LTPSGSISLIKSMHL CCCCCCHHHHHHHHH	26.24	24719451
672	Phosphorylation	KVYSLIQSLTSQIRH HHHHHHHHHHHHHHH	26.99	21955146
674	Phosphorylation	YSLIQSLTSQIRHRM HHHHHHHHHHHHHHC	24.67	21955146
675	Phosphorylation	SLIQSLTSQIRHRME HHHHHHHHHHHHHCC	28.98	21955146
686	Phosphorylation	HRMEDPKSSDIQLYH HHCCCCCCCCCEEEC	38.33	20068231
687	Phosphorylation	RMEDPKSSDIQLYHS HCCCCCCCCCEEECH	44.88	20068231
692	Phosphorylation	KSSDIQLYHSETLEL CCCCCEEECHHHHHH	6.21	20068231
694	Phosphorylation	SDIQLYHSETLELML CCCEEECHHHHHHHH	20.79	20068231
696	Phosphorylation	IQLYHSETLELMLRR CEEECHHHHHHHHHH	28.66	20068231
705	Phosphorylation	ELMLRRWSKLEKDFK HHHHHHHHHHHHHHC	26.08	20068231
727	Phosphorylation	ISKIPDIYDCIKYDV HHHCCCHHHHHCCCC	16.49	23917254
732	Phosphorylation	DIYDCIKYDVQHNGS CHHHHHCCCCCCCCC	11.05	24114839
739	Phosphorylation	YDVQHNGSLKLENTM CCCCCCCCEEEECHH	27.87	24114839
768	Ubiquitination	PQEYGITKAEKLEIA CHHHCCCHHHHHHHH	53.26	-
778	Phosphorylation	KLEIAKGYCTPLVRK HHHHHCCCCHHHHHH	7.76	-
780	Phosphorylation	EIAKGYCTPLVRKIR HHHCCCCHHHHHHHH	15.92	28348404
788	Phosphorylation	PLVRKIRSDLQRTQD HHHHHHHHHHHHCCC	46.26	27067055
801	Ubiquitination	QDDDTVNKLHPVYSR CCCCHHHHCCCCCCC	43.78	-
806	Phosphorylation	VNKLHPVYSRGVLSP HHHCCCCCCCCCCCC	9.33	29978859
807	Phosphorylation	NKLHPVYSRGVLSPE HHCCCCCCCCCCCCC	23.85	29978859
812	Phosphorylation	VYSRGVLSPERHVRT CCCCCCCCCCCCCCE	23.47	24719451
822	Phosphorylation	RHVRTRLYFTSESHV CCCCEEEEECCHHHH	11.08	29083192
824	Phosphorylation	VRTRLYFTSESHVHS CCEEEEECCHHHHHH	20.30	29083192
825	Phosphorylation	RTRLYFTSESHVHSL CEEEEECCHHHHHHH	27.48	29083192
827	Phosphorylation	RLYFTSESHVHSLLS EEEECCHHHHHHHHH	30.49	29083192
831	Phosphorylation	TSESHVHSLLSILRY CCHHHHHHHHHHHHH	29.89	29083192
834	Phosphorylation	SHVHSLLSILRYGAL HHHHHHHHHHHHHHH	25.52	29083192
894	Phosphorylation	FHVELHFSPGAKGCE EEEEEEECCCCCCCC	16.21	29214152
916	Phosphorylation	GYGYRPASRENEGRR CCCCCCCCCCCCCCC	42.69	28555341
926	Ubiquitination	NEGRRPFKIDNDDEP CCCCCCCCCCCCCCC	52.40	-
949	Acetylation	DRAVILFKPMVSEPI CEEEEEEECCCCCCE	28.85	25953088
953	Phosphorylation	ILFKPMVSEPIHIHR EEEECCCCCCEEECC	31.25	28555341
962	Phosphorylation	PIHIHRKSPLPRSRK CEEECCCCCCCCCCC	31.46	27251275
977	Phosphorylation	TATNDEESPLSVSSP CCCCCCCCCCCCCCC	29.15	28450419
980	Phosphorylation	NDEESPLSVSSPEGT CCCCCCCCCCCCCCC	24.28	30576142
982	Phosphorylation	EESPLSVSSPEGTGT CCCCCCCCCCCCCCC	36.48	30576142
983	Phosphorylation	ESPLSVSSPEGTGTW CCCCCCCCCCCCCCE	25.47	28450419
987	Phosphorylation	SVSSPEGTGTWLHYT CCCCCCCCCCEEEEE	29.76	23186163
989	Phosphorylation	SSPEGTGTWLHYTSG CCCCCCCCEEEEECC	25.37	23186163
993	Phosphorylation	GTGTWLHYTSGVGTG CCCCEEEEECCCCCC	10.63	-
999	Phosphorylation	HYTSGVGTGRRRRRS EEECCCCCCCCCCCC	25.71	-
1006	Phosphorylation	TGRRRRRSGEQITSS CCCCCCCCCCCCCCC	44.89	19664994
1011	Phosphorylation	RRSGEQITSSPVSPK CCCCCCCCCCCCCHH	23.89	30266825
1012	Phosphorylation	RSGEQITSSPVSPKS CCCCCCCCCCCCHHH	33.98	30266825
1013	Phosphorylation	SGEQITSSPVSPKSL CCCCCCCCCCCHHHH	22.22	30266825
1016	Phosphorylation	QITSSPVSPKSLAFT CCCCCCCCHHHHHEE	29.96	29255136
1029	Phosphorylation	FTSSIFGSWQQVVSE EEHHHHCCHHHHHHC	15.80	24719451
1043	Phosphorylation	ENANYLRTPRTLVEQ CCCCCCCCCCCHHHC	17.96	25627689
1046	Phosphorylation	NYLRTPRTLVEQKQN CCCCCCCCHHHCCCC	36.04	22210691
1055	Phosphorylation	VEQKQNPTVGSHCAG HHCCCCCCCCHHHCC	45.08	28450419
1058	Phosphorylation	KQNPTVGSHCAGLFS CCCCCCCHHHCCHHC	15.85	28450419
1065	Phosphorylation	SHCAGLFSTSVLGGS HHHCCHHCCCCCCCC	25.47	28450419
1066	Phosphorylation	HCAGLFSTSVLGGSS HHCCHHCCCCCCCCC	18.60	26657352
1067	Phosphorylation	CAGLFSTSVLGGSSS HCCHHCCCCCCCCCC	17.72	28450419
1072	Phosphorylation	STSVLGGSSSAPNLQ CCCCCCCCCCCCCHH	21.22	28450419
1072	O-linked_Glycosylation	STSVLGGSSSAPNLQ CCCCCCCCCCCCCHH	21.22	OGP
1073	Phosphorylation	TSVLGGSSSAPNLQD CCCCCCCCCCCCHHH	33.52	21712546
1074	Phosphorylation	SVLGGSSSAPNLQDY CCCCCCCCCCCHHHH	49.82	25159151
1081	Phosphorylation	SAPNLQDYARTHRKK CCCCHHHHHHHHHHH	5.75	24043423
1090	Phosphorylation	RTHRKKLTSSGCIDD HHHHHHCCCCCCCCC	29.71	28450419
1091	Phosphorylation	THRKKLTSSGCIDDA HHHHHCCCCCCCCCC	34.86	25159151
1092	Phosphorylation	HRKKLTSSGCIDDAT HHHHCCCCCCCCCCC	32.23	28450419
1099	Phosphorylation	SGCIDDATRGSAVKR CCCCCCCCCCCCCEE	42.42	28102081
1100	Methylation	GCIDDATRGSAVKRF CCCCCCCCCCCCEEE	38.50	115488345
1102	Phosphorylation	IDDATRGSAVKRFSI CCCCCCCCCCEEEEE	26.97	28102081
1108	Phosphorylation	GSAVKRFSISFARHP CCCCEEEEEEEEECC	22.74	30266825
1110	Phosphorylation	AVKRFSISFARHPTN CCEEEEEEEEECCCC	16.20	22617229
1139	Phosphorylation	ETLHNALSLKQVDEF HHHHHHHCHHHHHHH	30.98	24719451
1149	Phosphorylation	QVDEFLASIASPSSD HHHHHHHHHCCCCCC	22.34	28348404
1151	Phosphorylation	DEFLASIASPSSDVP HHHHHHHCCCCCCCC	16.94	24719451
1152	Phosphorylation	EFLASIASPSSDVPR HHHHHHCCCCCCCCC	24.52	25159151
1159	Phosphorylation	SPSSDVPRKTAEISS CCCCCCCCCHHHCCH	49.13	24719451
1160	Ubiquitination	PSSDVPRKTAEISST CCCCCCCCHHHCCHH	46.12	-
1161	Phosphorylation	SSDVPRKTAEISSTA CCCCCCCHHHCCHHH	30.70	23403867
1164	Phosphorylation	VPRKTAEISSTALRS CCCCHHHCCHHHHHC	3.50	24719451
1165	Phosphorylation	PRKTAEISSTALRSS CCCHHHCCHHHHHCC	17.09	23401153
1166	Phosphorylation	RKTAEISSTALRSSP CCHHHCCHHHHHCCC	24.30	23401153
1167	Phosphorylation	KTAEISSTALRSSPI CHHHCCHHHHHCCCC	23.95	23401153
1171	Phosphorylation	ISSTALRSSPIMRKK CCHHHHHCCCCCCCC	41.12	23401153
1172	Phosphorylation	SSTALRSSPIMRKKV CHHHHHCCCCCCCCC	16.41	25159151
1180	Phosphorylation	PIMRKKVSLNTYTPA CCCCCCCCCCCCCCC	25.45	25159151
1183	Phosphorylation	RKKVSLNTYTPAKIL CCCCCCCCCCCCCCC	33.78	28796482
1184	Phosphorylation	KKVSLNTYTPAKILP CCCCCCCCCCCCCCC	15.06	28796482
1185	Phosphorylation	KVSLNTYTPAKILPT CCCCCCCCCCCCCCC	18.09	25159151
1192	Phosphorylation	TPAKILPTPPATLKS CCCCCCCCCCCCCCC	38.16	21815630
1196	Phosphorylation	ILPTPPATLKSTKAS CCCCCCCCCCCCCCC	40.26	26074081
1198	Methylation	PTPPATLKSTKASSK CCCCCCCCCCCCCCC	52.29	115975521
1198	Phosphorylation	PTPPATLKSTKASSK CCCCCCCCCCCCCCC	52.29	24719451
1199	Phosphorylation	TPPATLKSTKASSKP CCCCCCCCCCCCCCC	37.95	26074081
1200	Phosphorylation	PPATLKSTKASSKPA CCCCCCCCCCCCCCC	29.10	26074081
1201	Methylation	PATLKSTKASSKPAT CCCCCCCCCCCCCCC	54.05	115975527
1209	O-linked_Glycosylation	ASSKPATSGPSSAVV CCCCCCCCCCCCCCC	51.30	31492838
1219	Phosphorylation	SSAVVPNTSSRKKNI CCCCCCCCCCCCCCC	23.24	25262027
1220	Phosphorylation	SAVVPNTSSRKKNIT CCCCCCCCCCCCCCC	34.48	25262027
1221	Phosphorylation	AVVPNTSSRKKNITS CCCCCCCCCCCCCCC	46.19	25627689

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 VIP2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of VIP2_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 VIP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WDR74_HUMAN	WDR74	physical	22939629
WDR6_HUMAN	WDR6	physical	22939629
ZC3HF_HUMAN	ZC3H15	physical	22939629
ZBT8B_HUMAN	ZBTB8B	physical	22939629
LUZP1_HUMAN	LUZP1	physical	27173435

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 VIP2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-1006, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-1006; SER-1016AND SER-1172, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504, AND MASSSPECTROMETRY.	17924679 [Abstract]
"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-38, AND MASSSPECTROMETRY.	17081983 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1185, AND MASSSPECTROMETRY.	16964243 [Abstract]