Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q06685 (VIP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 92. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	VIP1
Ordered Locus Names:	YLR410W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	1146 AA.
Sequence status	Complete.
Protein existence	Evidence 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.9 Ref.10
Catalytic activity	ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate. Ref.9 ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol diphosphate tetrakisphosphate (isomeric configuration unknown). Ref.9 ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate (isomeric configuration unknown). Ref.9
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton 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.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	inositol phosphate biosynthetic process Inferred from direct assay Ref.9. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay Ref.4. Source: SGD cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acid phosphatase activity Inferred from electronic annotation. Source: InterPro diphosphoinositol-pentakisphosphate kinase activity Inferred from electronic annotation. Source: EC inositol heptakisphosphate kinase activity Inferred from direct assay Ref.9. Source: SGD inositol hexakisphosphate 1-kinase activity Inferred from direct assay PubMed 18981179. Source: SGD inositol hexakisphosphate 3-kinase activity Inferred from direct assay PubMed 18981179. Source: SGD inositol hexakisphosphate 4-kinase activity Inferred from direct assay Ref.9. Source: SGD inositol hexakisphosphate 5-kinase activity Inferred from electronic annotation. Source: EC inositol hexakisphosphate 6-kinase activity Inferred from direct assay Ref.9. Source: SGD kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1146

1146

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase

PRO_0000270924

Regions

Nucleotide binding

402 – 405

ATP By similarity

Nucleotide binding

412 – 414

ATP By similarity

Nucleotide binding

487 – 489

ATP By similarity

Region

197 – 198

Substrate binding By similarity

Region

377 – 378

Substrate binding By similarity

Region

492 – 495

Substrate binding By similarity

Sites

Binding site

278

ATP By similarity

Binding site

351

ATP By similarity

Binding site

358

ATP By similarity

Binding site

377

ATP By similarity

Binding site

414

Substrate By similarity

Binding site

428

Substrate By similarity

Binding site

430

ATP By similarity

Binding site

475

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.6 Ref.11

Modified residue

Phosphoserine Ref.7

Modified residue

Phosphoserine Ref.11

Modified residue

Phosphothreonine Ref.11

Modified residue

Phosphoserine Ref.11

Modified residue

139

Phosphoserine Ref.11

Modified residue

141

Phosphoserine Ref.11

Modified residue

143

Phosphothreonine Ref.8 Ref.11

Modified residue

145

Phosphoserine Ref.8 Ref.11

Modified residue

895

Phosphoserine Ref.11

Modified residue

1106

Phosphothreonine Ref.11

Modified residue

1107

Phosphoserine Ref.6 Ref.11

Modified residue

1137

Phosphoserine Ref.8

Modified residue

1139

Phosphothreonine Ref.8

Modified residue

1140

Phosphoserine Ref.8

Experimental info

Mutagenesis

487

D → A: Abolishes enzyme activity. Ref.9

Mutagenesis

548

H → A: Does not affect enzyme activity. Ref.9

Sequences

Sequence

Length

Mass (Da)

Tools

Q06685 [UniParc].

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

1,146

129,755

        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' referencesShow '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. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-1107, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Strain: ADR376.
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-143; SER-145; SER-1137; THR-1139 AND SER-1140, MASS SPECTROMETRY.
[9]	"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.
[10]	"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.
[11]	"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; SER-77; THR-82; SER-92; SER-139; SER-141; THR-143; SER-145; SER-895; THR-1106 AND SER-1107, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U20162 Genomic DNA. Translation: AAB67497.1. BK006945 Genomic DNA. Translation: DAA09710.1.
PIR	S59376.
RefSeq	NP_013514.1. NM_001182298.1.
3D structure databases
ProteinModelPortal	Q06685.
SMR	Q06685. Positions 190-508.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q06685. 31 interactions.
MINT	MINT-2784338.
STRING	4932.YLR410W.
Proteomic databases
PaxDb	Q06685.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR410W; YLR410W; YLR410W.
GeneID	851126.
KEGG	sce:YLR410W.
Organism-specific databases
CYGD	YLR410w.
SGD	S000004402. VIP1.
Phylogenomic databases
eggNOG	NOG245915.
GeneTree	ENSGT00390000009048.
HOGENOM	HOG000177917.
OMA	DGFPLEK.
OrthoDB	EOG403119.
Gene expression databases
Genevestigator	Q06685.
Family and domain databases
Gene3D	3.30.470.20. 1 hit.
InterPro	IPR013651. ATP-grasp_RimK-type. IPR013816. ATP_grasp_subdomain_2. IPR000560. His_Pase_superF_clade-2. [Graphical view]
Pfam	PF00328. His_Phos_2. 1 hit. PF08443. RimK. 1 hit. [Graphical view]
PROSITE	PS00616. HIS_ACID_PHOSPHAT_1. False negative. PS00778. HIS_ACID_PHOSPHAT_2. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	967860.

Entry information

Entry name

VIP1_YEAST

Accession

Primary (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:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XII

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents