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Q06685 (VIP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:VIP1
Ordered Locus Names:YLR410W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1146 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. 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. Acts as a regulator of the PHO80-PHO85 cyclin/cyclin-dependent kinase (CDK) complex, thereby regulating signaling of phosphate availability. Required for the function of the cortical actin cytoskeleton, possibly by participating in correct F-actin localization and ensuring polarized growth. Ref.3 Ref.8 Ref.9

Catalytic activity

ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate. Ref.8

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. Ref.8

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. Ref.8

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

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton Ref.4.

Miscellaneous

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

Sequence similarities

Belongs to the histidine acid phosphatase family. VIP1 subfamily.

Caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11461146Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
PRO_0000270924

Regions

Nucleotide binding402 – 4054ATP By similarity
Nucleotide binding412 – 4143ATP By similarity
Nucleotide binding487 – 4893ATP By similarity
Region197 – 1982Substrate binding By similarity
Region377 – 3782Substrate binding By similarity
Region492 – 4954Substrate binding By similarity

Sites

Binding site2781ATP By similarity
Binding site3511ATP By similarity
Binding site3581ATP By similarity
Binding site3771ATP By similarity
Binding site4141Substrate By similarity
Binding site4281Substrate By similarity
Binding site4301ATP By similarity
Binding site4751ATP By similarity

Amino acid modifications

Modified residue311Phosphoserine Ref.10 Ref.11
Modified residue541Phosphoserine Ref.7
Modified residue771Phosphoserine Ref.10
Modified residue8951Phosphoserine Ref.11
Modified residue11071Phosphoserine Ref.11

Experimental info

Mutagenesis4871D → A: Abolishes enzyme activity. Ref.8
Mutagenesis5481H → A: Does not affect enzyme activity. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Q06685 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D69E44EAD16490F9

FASTA1,146129,755
        10         20         30         40         50         60 
MSGIKKEPIE SDEVPQQETK NNLPSAPSEM SPLFLNKNTQ KAMQSIAPIL EGFSPKTSAS 

        70         80         90        100        110        120 
ENMSLKLPPP GIQDDHSEEN LTVHDTLQRT ISTALGNGNN TNTVTTSGLK KADSESKSEA 

       130        140        150        160        170        180 
DPEGLSNSNI VNDADNINSI SKTGSPHLPQ GTMDAEQTNM GTNSVPTSSA SSRKSSTSHP 

       190        200        210        220        230        240 
KPRLPKVGKI GVCAMDAKVL SKPMRHILNR LIEHGEFETV IFGDKVILDE RIENWPTCDF 

       250        260        270        280        290        300 
LISFFSSGFP LDKAIKYVKL RKPFIINDLI MQKILWDRRL CLQVLEAYNV PTPPRLEISR 

       310        320        330        340        350        360 
DGGPRANEEL RAKLREHGVE VKPVEEPEWK MVDDDTLEVD GKTMTKPFVE KPVDGEDHNI 

       370        380        390        400        410        420 
YIYYHSKNGG GGRRLFRKVG NKSSEFDPTL VHPRTEGSYI YEQFMDTDNF EDVKAYTIGE 

       430        440        450        460        470        480 
NFCHAETRKS PVVDGIVRRN THGKEVRYIT ELSDEEKTIA GKVSKAFSQM ICGFDLLRVS 

       490        500        510        520        530        540 
GKSYVIDVNG FSFVKDNKAY YDSCANILRS TFIEAKKKMD MEKKNLPIIR EEKEQKWVFK 

       550        560        570        580        590        600 
GLAIIIRHAD RTPKQKFKHS FTSPIFISLL KGHKEEVVIR NVNDLKIVLQ ALRIALDEKA 

       610        620        630        640        650        660 
GNPAKIKVLA NALEKKLNFP GTKIQLKPVL NKENEVEKVQ FILKWGGEPT HSAKYQATEL 

       670        680        690        700        710        720 
GEQMRQDFDL LNKSILQNIK IFSSSERRVL HTAQYWTRAL FGADELGSDE ISIRKDLLDD 

       730        740        750        760        770        780 
SNAAKDLMDK VKKKLKPLLR EGKEAPPQFA WPSKMPEPYL VIKRVVELMN YHKKIMDNNF 

       790        800        810        820        830        840 
AKKDVNSMQT RWCTSEDPSL FKERWDKLFK EFNNAEKVDP SKISELYDTM KYDALHNRQF 

       850        860        870        880        890        900 
LENIFDPGLP NEAIADELGS HSLVDRYPIN VLAKNNFKII DSHSMNNSGK NSSNSVGSLG 

       910        920        930        940        950        960 
WVLESGKTST ARNPKSSSQF DEPRFMQLRE LYKLAKVLFD FICPKEYGIS DAEKLDIGLL 

       970        980        990       1000       1010       1020 
TSLPLAKQIL NDIGDMKNRE TPACVAYFTK ESHIYTLLNI IYESGIPMRI ARNALPELDY 

      1030       1040       1050       1060       1070       1080 
LSQITFELYE STDASGQKSH SIRLKMSPGC HTQDPLDVQL DDRHYISCIP KISLTKHLDM 

      1090       1100       1110       1120       1130       1140 
DYVQQKLRNK FTRVIMPPKF TPVNITSPNL SFQKRKTRRK SVSVEKLKRP ASSGSSSSTS 


VNKTLD 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Identification and characterization of Schizosaccharomyces pombe asp1(+), a gene that interacts with mutations in the Arp2/3 complex and actin."
Feoktistova A., McCollum D., Ohi R., Gould K.L.
Genetics 152:895-908(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[7]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[8]"A conserved family of enzymes that phosphorylate inositol hexakisphosphate."
Mulugu S., Bai W., Fridy P.C., Bastidas R.J., Otto J.C., Dollins D.E., Haystead T.A., Ribeiro A.A., York J.D.
Science 316:106-109(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-487 AND HIS-548.
[9]"Regulation of a cyclin-CDK-CDK inhibitor complex by inositol pyrophosphates."
Lee Y.-S., Mulugu S., York J.D., O'Shea E.K.
Science 316:109-112(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-895 AND SER-1107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U20162 Genomic DNA. Translation: AAB67497.1.
BK006945 Genomic DNA. Translation: DAA09710.1.
PIRS59376.
RefSeqNP_013514.1. NM_001182298.1.

3D structure databases

ProteinModelPortalQ06685.
SMRQ06685. Positions 190-508.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31667. 197 interactions.
IntActQ06685. 31 interactions.
MINTMINT-2784338.
STRING4932.YLR410W.

Proteomic databases

MaxQBQ06685.
PaxDbQ06685.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR410W; YLR410W; YLR410W.
GeneID851126.
KEGGsce:YLR410W.

Organism-specific databases

CYGDYLR410w.
SGDS000004402. VIP1.

Phylogenomic databases

eggNOGNOG245915.
GeneTreeENSGT00390000009048.
HOGENOMHOG000177917.
OMAYPINILA.
OrthoDBEOG7673KF.

Enzyme and pathway databases

BioCycYEAST:G3O-32472-MONOMER.
YEAST:MONOMER3O-224.

Gene expression databases

GenevestigatorQ06685.

Family and domain databases

Gene3D3.30.470.20. 1 hit.
3.40.50.1240. 4 hits.
InterProIPR013651. ATP-grasp_RimK-type.
IPR013816. ATP_grasp_subdomain_2.
IPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamPF00328. His_Phos_2. 1 hit.
PF08443. RimK. 1 hit.
[Graphical view]
SUPFAMSSF53254. SSF53254. 4 hits.
ProtoNetSearch...

Other

NextBio967860.
PROQ06685.

Entry information

Entry nameVIP1_YEAST
AccessionPrimary (citable) accession number: Q06685
Secondary accession number(s): D6VZ44
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families