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O74429 (VIP1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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):
Cortical actin cytoskeleton protein asp1
InsP6 and PP-IP5 kinase
Gene names
Name:asp1
Synonyms:vip1
ORF Names:SPCC1672.06c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length920 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 By similarity. Required for the function of the cortical actin cytoskeleton, possibly by participating in correct F-actin localization and ensuring polarized growth. Ref.2

Catalytic activity

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.

Subcellular location

Cytoplasm. Nucleus. Cytoplasmcytoskeleton Ref.2 Ref.3.

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 componentCytoplasm
Cytoskeleton
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcortical actin cytoskeleton organization

Inferred from mutant phenotype Ref.2. Source: PomBase

establishment or maintenance of actin cytoskeleton polarity

Inferred from mutant phenotype Ref.2. Source: PomBase

inositol phosphate biosynthetic process

Inferred from sequence orthology. Source: PomBase

   Cellular_componentcytoplasm

Inferred from sequence orthology. Source: PomBase

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay Ref.3. Source: PomBase

nucleus

Inferred from direct assay Ref.3. Source: PomBase

   Molecular_functionATP 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: UniProtKB-EC

inositol heptakisphosphate kinase activity

Inferred from sequence orthology. Source: PomBase

inositol hexakisphosphate 1-kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol hexakisphosphate 3-kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol hexakisphosphate 5-kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol hexakisphosphate kinase activity

Inferred from sequence orthology. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 920920Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
PRO_0000270923

Regions

Nucleotide binding248 – 2514ATP By similarity
Nucleotide binding258 – 2603ATP By similarity
Nucleotide binding333 – 3353ATP By similarity
Region42 – 432Substrate binding By similarity
Region223 – 2242Substrate binding By similarity
Region338 – 3414Substrate binding By similarity

Sites

Binding site1231ATP By similarity
Binding site1971ATP By similarity
Binding site2041ATP By similarity
Binding site2231ATP By similarity
Binding site2601Substrate By similarity
Binding site2741Substrate By similarity
Binding site2761ATP By similarity
Binding site3211ATP By similarity

Amino acid modifications

Modified residue191Phosphothreonine Ref.4
Modified residue211Phosphoserine Ref.4
Modified residue7061Phosphoserine Ref.4
Modified residue7201Phosphoserine Ref.4

Sequences

Sequence LengthMass (Da)Tools
O74429 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 507872D240110C0A

FASTA920105,680
        10         20         30         40         50         60 
MIQNASHLTS IDTESSTRTA SPVSSIVTPT KRNVVGICAM DAKARSKPCR NILNRIIAEG 

        70         80         90        100        110        120 
EFEAIVFGDN MILDEAVENW PACDYLICFY SSGFPLKKAE KYVELRKPFC VNDVVFQELL 

       130        140        150        160        170        180 
WDRRLVLNIL DAIRVSTPQR LICSRDGGPK INKVLEEKLR RKFGIEITEV PTPEVKMLDE 

       190        200        210        220        230        240 
DTLSVDGKII KKPYVEKPVY GEDHNIYIYF PKSVGGGGRK LFRKVANKSS DYDPDLCAPR 

       250        260        270        280        290        300 
TEGSFIYEEF MNVDNAEDVK VYTVGPHYSH AETRKSPVVD GIVRRNPHGK EIRFITNLSE 

       310        320        330        340        350        360 
EEKNMASKIS IAFEQPVCGF DLLRVSGQSY VIDVNGWSFV KDNNDYYDNA ARILKQMFHV 

       370        380        390        400        410        420 
AERHRRNRVP SVQEVLNPPP RESEAWRLKS LVGVLRHADR TPKQKFKFSF TSDPFVKLLQ 

       430        440        450        460        470        480 
GHTEEVILRN EQLNSVLAAT NLATELKCED INKLKQLRLA LETKKDLPGT KVQLKPAYSP 

       490        500        510        520        530        540 
EGKLLKLQLI IKWGGEFTHS ARYQSKDLGE QFHKDLYIMN RDCLKDVEIY TSSERRVSAS 

       550        560        570        580        590        600 
AEIFAMAFLE QETIPSDLLK VRKDLLDDSN AAKDTMDKVK KHLKSLLRVG DTARKEFTWP 

       610        620        630        640        650        660 
ENMPKPCEVM QQVVQLMKYH RAVMRENFII LGPEVEQVQS RWCCNENPAL FRERWEKLFS 

       670        680        690        700        710        720 
EFCDSEKADP SKVSELYDTL KYDALHNRQF LERIFTPYQY LKLPQSPSLI AKEPPQRTDS 

       730        740        750        760        770        780 
NGNLVGMTGA NTNHTERPLE KLYELYDLAK VLFDFVSPQE YGIEPKEKLE IGLLTSVPLL 

       790        800        810        820        830        840 
RQIIHDIKEA RDSDHASTRM YFTKESHIYT LLNCILESGL PMKLPRNQIP ELDYLTQICF 

       850        860        870        880        890        900 
ELFERTNPSG NKEFSVRITL SPGCYAQCPL DMNLDAKHCI SVSPRRSLTR HLDLQQFITK 

       910        920 
TEDLCNSVHL PKRFIPVNIN 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"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, SUBCELLULAR LOCATION.
[3]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-21; SER-706 AND SER-720, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329672 Genomic DNA. Translation: CAA20444.1.
PIRT41050.
RefSeqNP_587877.1. NM_001022869.2.

3D structure databases

ProteinModelPortalO74429.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid275814. 89 interactions.
MINTMINT-4678967.
STRING4896.SPCC1672.06c-1.

Proteomic databases

MaxQBO74429.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC1672.06c.1; SPCC1672.06c.1:pep; SPCC1672.06c.
GeneID2539244.
KEGGspo:SPCC1672.06c.

Organism-specific databases

PomBaseSPCC1672.06c.

Phylogenomic databases

eggNOGNOG245915.
HOGENOMHOG000177917.
OMAIFEEDVI.
OrthoDBEOG7673KF.
PhylomeDBO74429.

Family and domain databases

Gene3D3.40.50.1240. 4 hits.
InterProIPR013651. ATP-grasp_RimK-type.
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

NextBio20800414.
PROO74429.

Entry information

Entry nameVIP1_SCHPO
AccessionPrimary (citable) accession number: O74429
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1998
Last modified: June 11, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names