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Protein

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase

Gene

asp1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission 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. 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 (By similarity). 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 (PubMed:25254656).By similarity2 Publications

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.

Kineticsi

  1. KM=58.18 µM for inositol hexakisphosphate1 Publication
  1. Vmax=450.5 nmol/min/µg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei123ATPBy similarity1
Binding sitei197ATPBy similarity1
Binding sitei204ATPBy similarity1
Binding sitei223ATPBy similarity1
Binding sitei260SubstrateBy similarity1
Binding sitei274SubstrateBy similarity1
Binding sitei276ATPBy similarity1
Binding sitei321ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi248 – 251ATPBy similarity4
Nucleotide bindingi258 – 260ATPBy similarity3
Nucleotide bindingi333 – 335ATPBy similarity3

GO - Molecular functioni

GO - Biological processi

  • cortical actin cytoskeleton organization Source: PomBase
  • inositol metabolic process Source: UniProtKB
  • inositol phosphate biosynthetic process Source: PomBase
  • regulation of bipolar cell growth Source: UniProtKB
  • regulation of cell growth Source: UniProtKB
  • regulation of microtubule cytoskeleton organization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-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):
Cortical actin cytoskeleton protein asp1
InsP6 and PP-IP5 kinase
Gene namesi
Name:asp1
Synonyms:vip1
ORF Names:SPCC1672.06c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1672.06c.
PomBaseiSPCC1672.06c. asp1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Disruption phenotypei

Hypersensitive to microtubule poison thiabendazole (TBZ). Significantly increased number of interphase microtubules that depolymerize at the lateral cortex/cytoplasm and not at the cell tip. Microtubules touch the lateral cortex and become depolymerized instead of being deflected as do the microtubules of wild-type.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi333D → A: Loss of kinase activity and thus ATP-dependent production of inositol pyrophoshates. Altered interphase microtubule dynamics. Defective polarized growth. 1 Publication1
Mutagenesisi397H → A: Increased ATP-dependent production of inositol pyrophoshates. Altered interphase microtubule dynamics. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002709231 – 920Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinaseAdd BLAST920

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei19Phosphothreonine1 Publication1
Modified residuei21Phosphoserine1 Publication1
Modified residuei706Phosphoserine1 Publication1
Modified residuei720Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO74429.

PTM databases

iPTMnetiO74429.

Interactioni

Protein-protein interaction databases

BioGridi275814. 90 interactors.
MINTiMINT-4678967.

Structurei

3D structure databases

ProteinModelPortaliO74429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni42 – 43Substrate bindingBy similarity2
Regioni223 – 224Substrate bindingBy similarity2
Regioni338 – 341Substrate bindingBy similarity4
Regioni379 – 445Polyphosphoinositide-binding domainBy similarityAdd BLAST67

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.1 Publication

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000177917.
InParanoidiO74429.
OMAiHGEFETV.
OrthoDBiEOG092C0FUM.
PhylomeDBiO74429.

Family and domain databases

CDDicd07061. HP_HAP_like. 1 hit.
Gene3Di3.40.50.1240. 4 hits.
InterProiIPR013651. ATP-grasp_RimK-type.
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.

O74429-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIQNASHLTS IDTESSTRTA SPVSSIVTPT KRNVVGICAM DAKARSKPCR
60 70 80 90 100
NILNRIIAEG EFEAIVFGDN MILDEAVENW PACDYLICFY SSGFPLKKAE
110 120 130 140 150
KYVELRKPFC VNDVVFQELL WDRRLVLNIL DAIRVSTPQR LICSRDGGPK
160 170 180 190 200
INKVLEEKLR RKFGIEITEV PTPEVKMLDE DTLSVDGKII KKPYVEKPVY
210 220 230 240 250
GEDHNIYIYF PKSVGGGGRK LFRKVANKSS DYDPDLCAPR TEGSFIYEEF
260 270 280 290 300
MNVDNAEDVK VYTVGPHYSH AETRKSPVVD GIVRRNPHGK EIRFITNLSE
310 320 330 340 350
EEKNMASKIS IAFEQPVCGF DLLRVSGQSY VIDVNGWSFV KDNNDYYDNA
360 370 380 390 400
ARILKQMFHV AERHRRNRVP SVQEVLNPPP RESEAWRLKS LVGVLRHADR
410 420 430 440 450
TPKQKFKFSF TSDPFVKLLQ GHTEEVILRN EQLNSVLAAT NLATELKCED
460 470 480 490 500
INKLKQLRLA LETKKDLPGT KVQLKPAYSP EGKLLKLQLI IKWGGEFTHS
510 520 530 540 550
ARYQSKDLGE QFHKDLYIMN RDCLKDVEIY TSSERRVSAS AEIFAMAFLE
560 570 580 590 600
QETIPSDLLK VRKDLLDDSN AAKDTMDKVK KHLKSLLRVG DTARKEFTWP
610 620 630 640 650
ENMPKPCEVM QQVVQLMKYH RAVMRENFII LGPEVEQVQS RWCCNENPAL
660 670 680 690 700
FRERWEKLFS EFCDSEKADP SKVSELYDTL KYDALHNRQF LERIFTPYQY
710 720 730 740 750
LKLPQSPSLI AKEPPQRTDS NGNLVGMTGA NTNHTERPLE KLYELYDLAK
760 770 780 790 800
VLFDFVSPQE YGIEPKEKLE IGLLTSVPLL RQIIHDIKEA RDSDHASTRM
810 820 830 840 850
YFTKESHIYT LLNCILESGL PMKLPRNQIP ELDYLTQICF ELFERTNPSG
860 870 880 890 900
NKEFSVRITL SPGCYAQCPL DMNLDAKHCI SVSPRRSLTR HLDLQQFITK
910 920
TEDLCNSVHL PKRFIPVNIN
Length:920
Mass (Da):105,680
Last modified:November 1, 1998 - v1
Checksum:i507872D240110C0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA20444.1.
PIRiT41050.
RefSeqiNP_587877.1. NM_001022869.2.

Genome annotation databases

EnsemblFungiiSPCC1672.06c.1; SPCC1672.06c.1:pep; SPCC1672.06c.
GeneIDi2539244.
KEGGispo:SPCC1672.06c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA20444.1.
PIRiT41050.
RefSeqiNP_587877.1. NM_001022869.2.

3D structure databases

ProteinModelPortaliO74429.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275814. 90 interactors.
MINTiMINT-4678967.

PTM databases

iPTMnetiO74429.

Proteomic databases

MaxQBiO74429.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1672.06c.1; SPCC1672.06c.1:pep; SPCC1672.06c.
GeneIDi2539244.
KEGGispo:SPCC1672.06c.

Organism-specific databases

EuPathDBiFungiDB:SPCC1672.06c.
PomBaseiSPCC1672.06c. asp1.

Phylogenomic databases

HOGENOMiHOG000177917.
InParanoidiO74429.
OMAiHGEFETV.
OrthoDBiEOG092C0FUM.
PhylomeDBiO74429.

Enzyme and pathway databases

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

Miscellaneous databases

PROiO74429.

Family and domain databases

CDDicd07061. HP_HAP_like. 1 hit.
Gene3Di3.40.50.1240. 4 hits.
InterProiIPR013651. ATP-grasp_RimK-type.
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_SCHPO
AccessioniPrimary (citable) accession number: O74429
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1998
Last modified: November 30, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.