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Protein

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase

Gene

l(1)G0196

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

Catalytic activityi

ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate.
ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate.
ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate.
ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei157ATPBy similarity1
Binding sitei210ATPBy similarity1
Binding sitei217ATPBy similarity1
Binding sitei236ATPBy similarity1
Binding sitei271SubstrateBy similarity1
Binding sitei285SubstrateBy similarity1
Binding sitei287ATPBy similarity1
Binding sitei332ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi260 – 263ATPBy similarity4
Nucleotide bindingi269 – 271ATPBy similarity3
Nucleotide bindingi344 – 346ATPBy similarity3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-1855167. Synthesis of pyrophosphates in the cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase (EC:2.7.4.21, EC:2.7.4.24)
Alternative name(s):
InsP6 and PP-IP5 kinase
Gene namesi
ORF Names:CG14616
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0027279. l(1)G0196.

Subcellular locationi

  • Cytoplasmcytosol By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003156971 – 1696Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinaseAdd BLAST1696

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei974Phosphoserine1 Publication1
Modified residuei1001Phosphoserine1 Publication1
Modified residuei1060Phosphoserine1 Publication1
Modified residuei1255Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VR59.
PRIDEiQ9VR59.

PTM databases

iPTMnetiQ9VR59.

Expressioni

Gene expression databases

BgeeiFBgn0027279.
ExpressionAtlasiQ9VR59. baseline.
GenevisibleiQ9VR59. DM.

Interactioni

Protein-protein interaction databases

BioGridi59411. 3 interactors.
DIPiDIP-21851N.
IntActiQ9VR59. 7 interactors.
MINTiMINT-1002676.
STRINGi7227.FBpp0288801.

Structurei

3D structure databases

ProteinModelPortaliQ9VR59.
SMRiQ9VR59.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni76 – 77Substrate bindingBy similarity2
Regioni236 – 237Substrate bindingBy similarity2
Regioni349 – 352Substrate bindingBy similarity4
Regioni394 – 465Polyphosphoinositide-binding domainBy similarityAdd BLAST72

Domaini

The N-terminal kinase domain produces inositol polyphosphates. The C-terminal acid phosphatase-like domain binds inositol polyphosphates and negatively regulates their accumulation. The C-terminal domain reduces the amount of inositol pyrophosphates in a dose-dependent manner in vitro.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1057. Eukaryota.
ENOG410XNSN. LUCA.
GeneTreeiENSGT00390000009048.
InParanoidiQ9VR59.
KOiK13024.
OMAiPPHADEH.
OrthoDBiEOG091G00ZU.
PhylomeDBiQ9VR59.

Family and domain databases

CDDicd07061. HP_HAP_like. 1 hit.
Gene3Di3.40.50.1240. 3 hits.
InterProiIPR033379. Acid_Pase_AS.
IPR000560. His_Pase_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 3 hits.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform I (identifier: Q9VR59-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSYTELESGY QDISQQHQQQ NPHQSQPQQR VGFYLGLQDG NGDTDFGDSN
60 70 80 90 100
DGMDSDTSTS SSNSKQVVVG ICAMAKKTQS KPMKEILTRL GEFEFIKLVT
110 120 130 140 150
FEENVILREP VQNWPTCDCL VSFHSKGFPL EKAIEYAQLR NPFVLNNLHM
160 170 180 190 200
QYDIQDRRRV YAILEKEGIE IPRYAVLDRD SPDPKHHELI ESEDHVEVNG
210 220 230 240 250
ITFNKPFVEK PVSAEDHNIY IYYPTSAGGG SQRLFRKIGS RSSVYSPESR
260 270 280 290 300
VRKTGSFIYE DFMPTDGTDV KVYTVGPDYA HAEARKSPAL DGKVERDSEG
310 320 330 340 350
KEIRYPVILN HSEKLISRKV CLAFKQTVCG FDLLRANGKS YVCDVNGFSF
360 370 380 390 400
VKNSNKYYDD CAKILGNMIL RELTPTLHIP WSVPFQLDDP PIVPTTFGKM
410 420 430 440 450
MELRCVVAVI RHGDRTPKQK MKVEVRHPKF FEIFEKYDGY KLGHVKLKRP
460 470 480 490 500
KQLQEILDIA RFLLSEIHTK AHAEIEEKES KLEQLKNVLE MYGHFSGINR
510 520 530 540 550
KVQMKYQPKG RPRGSSSDDT NLAADQPVEP SLVLILKWGG ELTPAGRIQA
560 570 580 590 600
EELGRIFRCM YPGGQGRSDY SGTQGLGLLR LHSTFRHDLK IYASDEGRVQ
610 620 630 640 650
MTAAAFAKGL LALEGELTPI LVQMVKSANT NGLLDNDCDS SKYQNLAKGR
660 670 680 690 700
LHELMQNDRE FSKEDRELIN PCNSKSITQA LDFVKNPVDC CHHVHLLIRE
710 720 730 740 750
LLHIISIKKD DPKTKDAILY HGETWDLMRC RWEKIEKDFS TKSKLFDISK
760 770 780 790 800
IPDIYDCIKY DLQHNQHTLQ YDQAEELYIY AKNLADIVIP QEYGLTPQEK
810 820 830 840 850
LAIGQGICSP LLRKIKGDLQ RNIDEVEDEF MNRLNPHYSH GVASPQRHVR
860 870 880 890 900
TRLYFTSESH VHSLLTVLRY GGLLNVVTDE QWRRAMDYIS MVSELNYMSQ
910 920 930 940 950
IVIMLYEDPT KDPTSEERFH VELHFSPGVN CCVQKNLPPG PGFRPHSHGD
960 970 980 990 1000
NACNVSLQSS DESNPARIEE ENDSNSGEER EGKKRGTSGQ RSTDRSAERI
1010 1020 1030 1040 1050
SPAFGFNRLE LRSKQFKSKP IPIGAHHTVS GHEAMDLAKR LNEELASHQQ
1060 1070 1080 1090 1100
QQNQQLRPIS PDIRAVTPDC EPRSRSFEQR PTSGVCAKEP DSQVSVSVSA
1110 1120 1130 1140 1150
SVSSANASTS SRRQRHSIAG QMSYMKMLGF GGFSKKMATS ANSLFSTAVI
1160 1170 1180 1190 1200
SGSSSAPNLR DMITVSSSGF GDVPPIRPLE TLHNALSLRK LDSFLQDMIL
1210 1220 1230 1240 1250
AQIFKTPTGS PPRGFSKNTL PAVSSMTLTA SNQTEVVEHE PISTTVTPTF
1260 1270 1280 1290 1300
DRRGSESGST ADAHLRLLSE SQCPNLDDSN TELRESLAGK MELWPQDIVK
1310 1320 1330 1340 1350
AAEDEELNLS ELETKPSLDL TMEIMERGVA GIASIQPMNR DSDETMGGGV
1360 1370 1380 1390 1400
FLSVCEEQGS GSTCLTPVSF GMDLDLSMVA NKGSITLSME GFDDDEDATL
1410 1420 1430 1440 1450
SAATTPSLLA DCEPRLESCY CCPSHAEAPP EVPSDDPRFG FALPVRVTQA
1460 1470 1480 1490 1500
SPEHARPVRR AHDPVSPRIQ KQISLFEGNA AMATGQEKTE SSGSVGGGAI
1510 1520 1530 1540 1550
LHASINLPAA GPHHLRQDAR LRKFENLTQS TSNSNFPFES NTLKRVPMQT
1560 1570 1580 1590 1600
TKDYDNVSHT QSCINLKSGS SGVLGGSPQR QRGSDGGGVG ASGVPAESRE
1610 1620 1630 1640 1650
PTRVHYGRMN STCCSASASP SPSPGALIVK ERFIEPPKRG VVRGYHGKTQ
1660 1670 1680 1690
SMDADFLFNE FLLLPAMAPA KISFDSSDID QASDDDSPSS SKQRHA
Note: No experimental confirmation available.
Length:1,696
Mass (Da):188,677
Last modified:June 16, 2009 - v2
Checksum:iBB013ECB582C96D3
GO
Isoform G (identifier: Q9VR59-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1293-1300: LWPQDIVK → QYPTEPSI
     1301-1696: Missing.

Note: No experimental confirmation available.
Show »
Length:1,300
Mass (Da):146,528
Checksum:i644A2123503DB726
GO
Isoform H (identifier: Q9VR59-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-40: SYTELESGYQ...VGFYLGLQDG → EWTWFKDWWR...DDFCYCEVCM
     266-266: D → DVYFS
     1293-1305: LWPQDIVKAAEDE → RKCRKKSVVEWQC
     1306-1696: Missing.

Note: No experimental confirmation available.
Show »
Length:1,416
Mass (Da):159,831
Checksum:i95E98D85E6F735A6
GO
Isoform J (identifier: Q9VR59-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1090-1090: P → PATETAEDTS...PSCCTKTIAT
     1293-1300: LWPQDIVK → QYPTEPSI
     1301-1696: Missing.

Note: No experimental confirmation available.
Show »
Length:1,447
Mass (Da):162,288
Checksum:i33909E1FE36F5731
GO
Isoform K (identifier: Q9VR59-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1090-1090: P → PVSSPDFGDN...PSCCTKTIAT
     1293-1300: LWPQDIVK → QYPTEPSI
     1301-1696: Missing.

Note: No experimental confirmation available.
Show »
Length:1,846
Mass (Da):204,458
Checksum:i803BD74B91DAC0EE
GO

Sequence cautioni

The sequence ABN49448 differs from that shown. Reason: Frameshift at position 735.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti329C → F in ABN49448 (Ref. 3) Curated1
Sequence conflicti734K → KN in ABN49448 (Ref. 3) Curated1
Sequence conflicti906Y → H in ABN49448 (Ref. 3) Curated1
Sequence conflicti1092S → G in AAT94524 (Ref. 3) Curated1
Sequence conflicti1116H → R in AAT94524 (Ref. 3) Curated1
Sequence conflicti1124Y → C in AAT94524 (Ref. 3) Curated1
Sequence conflicti1124Y → C in ABN49448 (Ref. 3) Curated1

RNA editingi

Edited at positions 1093, 1117 and 1121.1 Publication
Partially edited. Target of Adar.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti1093Q → R in RNA edited version. 1
Natural varianti1117S → G in RNA edited version. 1
Natural varianti1121Q → R in RNA edited version. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0306402 – 40SYTEL…GLQDG → EWTWFKDWWRLKKLRSRHQR HKKKLQATAASAEAAVTASA FLAGSGCAESGGSQDPQTNR LHSLDAVPSDGTLARRRHGS RDSLRRNRLLQRQRRSQSAA VRSHRSHDDDDDGEYGPFNV SDYEDYGPNHGSDEESDDFC YCEVCM in isoform H. 1 PublicationAdd BLAST39
Alternative sequenceiVSP_030641266D → DVYFS in isoform H. 1 Publication1
Alternative sequenceiVSP_0306431090P → PATETAEDTSMDIQPKICIG KCAPGLLTPTVTTTDILKGI RDIAPTATQTSPPTFTPSTT TTTGAAAALFDNTATMSSNR PFTNQFQSIDPTSNDAPHQH HVHQHQYQHHRKTTTTIINN TLNENHTTATITNNTTTTPS CCTKTIAT in isoform J. Curated1
Alternative sequenceiVSP_0335931090P → PVSSPDFGDNSRTRSSEFGE TCHARVGTASNSDGGGSHPR ADHRTAFQIRVTNSLSFFKI DSSTNELPLSDIDFSLHPPT PQCGPLSHKRFHILTMRRME SCDDGAELEQVRHLPQISPM ATNERPLSSCNCSSSAAQAH SHSKSLMDLAQAVVMTSPQE TGPNSEQGCDPTTAADVSVS SFDDDFQLSSSAPAILMSAH FGNRPVVASLSSMVHVTTSP SASTLQLCRDKDKALASGTS SAHSKATSNSCGQLSMAGSA PVVTENPFRFTVSSLGSAAT NTACFVGSFEPIEEQITSIV EVDSKPLQPEPQVVYNLPTV LITGTASSSELSTKLNSNIL PTVTNAFSAIDTEINDEIGI SKEVGIGTIRITNTHTPCNK ATVTRPDTKIAITTDPQTVT ATETAEDTSMDIQPKICIGK CAPGLLTPTVTTTDILKGIR DIAPTATQTSPPTFTPSTTT TTGAAAALFDNTATMSSNRP FTNQFQSIDPTSNDAPHQHH VHQHQYQHHRKTTTTIINNT LNENHTTATITNNTTTTPSC CTKTIAT in isoform K. Curated1
Alternative sequenceiVSP_0306481293 – 1305LWPQD…AAEDE → RKCRKKSVVEWQC in isoform H. 1 PublicationAdd BLAST13
Alternative sequenceiVSP_0306491293 – 1300LWPQDIVK → QYPTEPSI in isoform G, isoform J and isoform K. 1 Publication8
Alternative sequenceiVSP_0306501301 – 1696Missing in isoform G, isoform J and isoform K. 1 PublicationAdd BLAST396
Alternative sequenceiVSP_0306511306 – 1696Missing in isoform H. 1 PublicationAdd BLAST391

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAN09569.2.
AE014298 Genomic DNA. Translation: AAN09570.3.
AE014298 Genomic DNA. Translation: AAN09571.2.
AE014298 Genomic DNA. Translation: AAN09573.2.
AE014298 Genomic DNA. Translation: ABW09458.2.
BT015295 mRNA. Translation: AAT94524.1.
BT030309 mRNA. Translation: ABN49448.1. Frameshift.
RefSeqiNP_001097041.2. NM_001103571.2. [Q9VR59-7]
NP_788950.2. NM_176777.2. [Q9VR59-1]
NP_788951.2. NM_176778.2. [Q9VR59-3]
NP_788952.2. NM_176779.3. [Q9VR59-6]
NP_788953.2. NM_176780.2. [Q9VR59-5]
UniGeneiDm.237.

Genome annotation databases

EnsemblMetazoaiFBtr0299524; FBpp0288799; FBgn0027279. [Q9VR59-1]
GeneIDi33137.
KEGGidme:Dmel_CG14616.

Keywords - Coding sequence diversityi

Alternative splicing, RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAN09569.2.
AE014298 Genomic DNA. Translation: AAN09570.3.
AE014298 Genomic DNA. Translation: AAN09571.2.
AE014298 Genomic DNA. Translation: AAN09573.2.
AE014298 Genomic DNA. Translation: ABW09458.2.
BT015295 mRNA. Translation: AAT94524.1.
BT030309 mRNA. Translation: ABN49448.1. Frameshift.
RefSeqiNP_001097041.2. NM_001103571.2. [Q9VR59-7]
NP_788950.2. NM_176777.2. [Q9VR59-1]
NP_788951.2. NM_176778.2. [Q9VR59-3]
NP_788952.2. NM_176779.3. [Q9VR59-6]
NP_788953.2. NM_176780.2. [Q9VR59-5]
UniGeneiDm.237.

3D structure databases

ProteinModelPortaliQ9VR59.
SMRiQ9VR59.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59411. 3 interactors.
DIPiDIP-21851N.
IntActiQ9VR59. 7 interactors.
MINTiMINT-1002676.
STRINGi7227.FBpp0288801.

PTM databases

iPTMnetiQ9VR59.

Proteomic databases

PaxDbiQ9VR59.
PRIDEiQ9VR59.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0299524; FBpp0288799; FBgn0027279. [Q9VR59-1]
GeneIDi33137.
KEGGidme:Dmel_CG14616.

Organism-specific databases

FlyBaseiFBgn0027279. l(1)G0196.

Phylogenomic databases

eggNOGiKOG1057. Eukaryota.
ENOG410XNSN. LUCA.
GeneTreeiENSGT00390000009048.
InParanoidiQ9VR59.
KOiK13024.
OMAiPPHADEH.
OrthoDBiEOG091G00ZU.
PhylomeDBiQ9VR59.

Enzyme and pathway databases

ReactomeiR-DME-1855167. Synthesis of pyrophosphates in the cytosol.

Miscellaneous databases

GenomeRNAii33137.
PROiQ9VR59.

Gene expression databases

BgeeiFBgn0027279.
ExpressionAtlasiQ9VR59. baseline.
GenevisibleiQ9VR59. DM.

Family and domain databases

CDDicd07061. HP_HAP_like. 1 hit.
Gene3Di3.40.50.1240. 3 hits.
InterProiIPR033379. Acid_Pase_AS.
IPR000560. His_Pase_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 3 hits.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVIP1_DROME
AccessioniPrimary (citable) accession number: Q9VR59
Secondary accession number(s): A2VEZ0
, A8JUU5, Q6AWF3, Q8IQ22, Q8IQ23, Q8IQ24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 16, 2009
Last modified: November 30, 2016
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Caution

Although related to histidine acid phosphatases, it lacks the conserved active sites, suggesting that it has no phosphatase activity.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.