Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase

Gene

VIP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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 (PubMed:17412958). 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). Required for maintaining cellular integrity, normal growth and interactions with the ARP complex (PubMed:10388810). Acts as a regulator of the PHO80-PHO85 cyclin/cyclin-dependent kinase (CDK) complex, thereby regulating signaling of phosphate availability (PubMed:17412959). Required for the function of the cortical actin cytoskeleton, possibly by participating in correct F-actin localization and ensuring polarized growth (PubMed:10388810). Regulates polarized growth and modulates interphase microtubule cytoskeleton. Regulates microtubule dynamics without the requirement of microtubule plus-end tracking protein Mal3. Required for growth zone selection (By similarity).By similarity3 Publications

Catalytic activityi

ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate.1 Publication
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.1 Publication
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.1 Publication
ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei278ATPBy similarity1
Binding sitei351ATPBy similarity1
Binding sitei358ATPBy similarity1
Binding sitei377ATPBy similarity1
Binding sitei414SubstrateBy similarity1
Binding sitei428SubstrateBy similarity1
Binding sitei430ATPBy similarity1
Binding sitei475ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi402 – 405ATPBy similarity4
Nucleotide bindingi412 – 414ATPBy similarity3
Nucleotide bindingi487 – 489ATPBy similarity3

GO - Molecular functioni

  • acid phosphatase activity Source: InterPro
  • ATP binding Source: UniProtKB
  • diphosphoinositol-pentakisphosphate kinase activity Source: GO_Central
  • inositol heptakisphosphate kinase activity Source: SGD
  • inositol hexakisphosphate 1-kinase activity Source: SGD
  • inositol hexakisphosphate 3-kinase activity Source: SGD
  • inositol hexakisphosphate 4-kinase activity Source: SGD
  • inositol hexakisphosphate 5-kinase activity Source: UniProtKB-EC
  • inositol hexakisphosphate 6-kinase activity Source: SGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-224.
ReactomeiR-SCE-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
Name:VIP1
Ordered Locus Names:YLR410W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR410W.
SGDiS000004402. VIP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi487D → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi548H → A: Does not affect enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002709241 – 1146Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinaseAdd BLAST1146

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei31PhosphoserineCombined sources1
Modified residuei54PhosphoserineCombined sources1
Modified residuei77PhosphoserineCombined sources1
Modified residuei895PhosphoserineCombined sources1
Modified residuei1107PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06685.
PRIDEiQ06685.

PTM databases

iPTMnetiQ06685.

Interactioni

Protein-protein interaction databases

BioGridi31667. 201 interactors.
IntActiQ06685. 31 interactors.
MINTiMINT-2784338.

Structurei

3D structure databases

ProteinModelPortaliQ06685.
SMRiQ06685.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni197 – 198Substrate bindingBy similarity2
Regioni377 – 378Substrate bindingBy similarity2
Regioni492 – 495Substrate bindingBy similarity4
Regioni530 – 597Polyphosphoinositide-binding domainBy similarityAdd BLAST68

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

GeneTreeiENSGT00390000009048.
HOGENOMiHOG000177917.
InParanoidiQ06685.
OMAiHGEFETV.
OrthoDBiEOG092C0FUM.

Family and domain databases

CDDicd07061. HP_HAP_like. 1 hit.
Gene3Di3.30.470.20. 1 hit.
3.40.50.1240. 4 hits.
InterProiIPR013651. ATP-grasp_RimK-type.
IPR013816. ATP_grasp_subdomain_2.
IPR000560. His_Pase_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
PF08443. RimK. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 4 hits.

Sequencei

Sequence statusi: Complete.

Q06685-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGIKKEPIE SDEVPQQETK NNLPSAPSEM SPLFLNKNTQ KAMQSIAPIL
60 70 80 90 100
EGFSPKTSAS ENMSLKLPPP GIQDDHSEEN LTVHDTLQRT ISTALGNGNN
110 120 130 140 150
TNTVTTSGLK KADSESKSEA DPEGLSNSNI VNDADNINSI SKTGSPHLPQ
160 170 180 190 200
GTMDAEQTNM GTNSVPTSSA SSRKSSTSHP KPRLPKVGKI GVCAMDAKVL
210 220 230 240 250
SKPMRHILNR LIEHGEFETV IFGDKVILDE RIENWPTCDF LISFFSSGFP
260 270 280 290 300
LDKAIKYVKL RKPFIINDLI MQKILWDRRL CLQVLEAYNV PTPPRLEISR
310 320 330 340 350
DGGPRANEEL RAKLREHGVE VKPVEEPEWK MVDDDTLEVD GKTMTKPFVE
360 370 380 390 400
KPVDGEDHNI YIYYHSKNGG GGRRLFRKVG NKSSEFDPTL VHPRTEGSYI
410 420 430 440 450
YEQFMDTDNF EDVKAYTIGE NFCHAETRKS PVVDGIVRRN THGKEVRYIT
460 470 480 490 500
ELSDEEKTIA GKVSKAFSQM ICGFDLLRVS GKSYVIDVNG FSFVKDNKAY
510 520 530 540 550
YDSCANILRS TFIEAKKKMD MEKKNLPIIR EEKEQKWVFK GLAIIIRHAD
560 570 580 590 600
RTPKQKFKHS FTSPIFISLL KGHKEEVVIR NVNDLKIVLQ ALRIALDEKA
610 620 630 640 650
GNPAKIKVLA NALEKKLNFP GTKIQLKPVL NKENEVEKVQ FILKWGGEPT
660 670 680 690 700
HSAKYQATEL GEQMRQDFDL LNKSILQNIK IFSSSERRVL HTAQYWTRAL
710 720 730 740 750
FGADELGSDE ISIRKDLLDD SNAAKDLMDK VKKKLKPLLR EGKEAPPQFA
760 770 780 790 800
WPSKMPEPYL VIKRVVELMN YHKKIMDNNF AKKDVNSMQT RWCTSEDPSL
810 820 830 840 850
FKERWDKLFK EFNNAEKVDP SKISELYDTM KYDALHNRQF LENIFDPGLP
860 870 880 890 900
NEAIADELGS HSLVDRYPIN VLAKNNFKII DSHSMNNSGK NSSNSVGSLG
910 920 930 940 950
WVLESGKTST ARNPKSSSQF DEPRFMQLRE LYKLAKVLFD FICPKEYGIS
960 970 980 990 1000
DAEKLDIGLL TSLPLAKQIL NDIGDMKNRE TPACVAYFTK ESHIYTLLNI
1010 1020 1030 1040 1050
IYESGIPMRI ARNALPELDY LSQITFELYE STDASGQKSH SIRLKMSPGC
1060 1070 1080 1090 1100
HTQDPLDVQL DDRHYISCIP KISLTKHLDM DYVQQKLRNK FTRVIMPPKF
1110 1120 1130 1140
TPVNITSPNL SFQKRKTRRK SVSVEKLKRP ASSGSSSSTS VNKTLD
Length:1,146
Mass (Da):129,755
Last modified:November 1, 1996 - v1
Checksum:iD69E44EAD16490F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20162 Genomic DNA. Translation: AAB67497.1.
BK006945 Genomic DNA. Translation: DAA09710.1.
PIRiS59376.
RefSeqiNP_013514.1. NM_001182298.1.

Genome annotation databases

EnsemblFungiiYLR410W; YLR410W; YLR410W.
GeneIDi851126.
KEGGisce:YLR410W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20162 Genomic DNA. Translation: AAB67497.1.
BK006945 Genomic DNA. Translation: DAA09710.1.
PIRiS59376.
RefSeqiNP_013514.1. NM_001182298.1.

3D structure databases

ProteinModelPortaliQ06685.
SMRiQ06685.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31667. 201 interactors.
IntActiQ06685. 31 interactors.
MINTiMINT-2784338.

PTM databases

iPTMnetiQ06685.

Proteomic databases

MaxQBiQ06685.
PRIDEiQ06685.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR410W; YLR410W; YLR410W.
GeneIDi851126.
KEGGisce:YLR410W.

Organism-specific databases

EuPathDBiFungiDB:YLR410W.
SGDiS000004402. VIP1.

Phylogenomic databases

GeneTreeiENSGT00390000009048.
HOGENOMiHOG000177917.
InParanoidiQ06685.
OMAiHGEFETV.
OrthoDBiEOG092C0FUM.

Enzyme and pathway databases

BioCyciYEAST:MONOMER3O-224.
ReactomeiR-SCE-1855167. Synthesis of pyrophosphates in the cytosol.

Miscellaneous databases

PROiQ06685.

Family and domain databases

CDDicd07061. HP_HAP_like. 1 hit.
Gene3Di3.30.470.20. 1 hit.
3.40.50.1240. 4 hits.
InterProiIPR013651. ATP-grasp_RimK-type.
IPR013816. ATP_grasp_subdomain_2.
IPR000560. His_Pase_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
PF08443. RimK. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 4 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiVIP1_YEAST
AccessioniPrimary (citable) accession number: Q06685
Secondary accession number(s): D6VZ44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8810 molecules/cell in log phase SD medium.1 Publication

Caution

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

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.