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Protein

Inositol polyphosphate multikinase

Gene

ARG82

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

Has kinase activity and phosphorylates inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) and inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4). Has low kinase activity towards InsP6. With ARG80, ARG81 and MCM1, coordinates the expression of arginine anabolic and catabolic genes in response to arginine. Recruites ARG80 and MCM21 to stabilize them.2 Publications

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi133 – 1331Manganese1 Publication
Metal bindingi271 – 2711Calcium; via carbonyl oxygen1 Publication
Metal bindingi274 – 2741Calcium1 Publication
Metal bindingi325 – 3251Manganese1 Publication
Metal bindingi334 – 3341Calcium; via carbonyl oxygen1 Publication

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • inositol-1,3,4,5,6-pentakisphosphate kinase activity Source: SGD
  • inositol-1,4,5-trisphosphate 3-kinase activity Source: SGD
  • inositol-1,4,5-trisphosphate 6-kinase activity Source: SGD
  • inositol tetrakisphosphate 3-kinase activity Source: SGD
  • inositol tetrakisphosphate 6-kinase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW
  • phosphatidylinositol 3-kinase activity Source: SGD
  • protein binding, bridging Source: SGD

GO - Biological processi

  • arginine metabolic process Source: UniProtKB-KW
  • inositol phosphate biosynthetic process Source: SGD
  • macroautophagy Source: SGD
  • negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • phosphatidylinositol phosphorylation Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • protein stabilization Source: SGD
  • regulation of arginine metabolic process Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Arginine metabolism, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Calcium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-7707.
YEAST:G3O-29762-MONOMER.
YEAST:MONOMER3O-64.
SABIO-RKP07250.

Chemistry

SwissLipidsiSLP:000000958.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol polyphosphate multikinase (EC:2.7.1.151)
Short name:
IPMK
Alternative name(s):
Arginine metabolism regulation protein III
Gene namesi
Name:ARG82
Synonyms:ARGR3, IPK2
Ordered Locus Names:YDR173C
ORF Names:YD9395.06C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR173C.
SGDiS000002580. ARG82.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 355355Inositol polyphosphate multikinasePRO_0000066873Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei97 – 971PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP07250.

PTM databases

iPTMnetiP07250.

Interactioni

Subunit structurei

Interacts with ARG80 and MCM1.2 Publications

GO - Molecular functioni

  • protein binding, bridging Source: SGD

Protein-protein interaction databases

BioGridi32226. 36 interactions.
DIPiDIP-1242N.
IntActiP07250. 3 interactions.
MINTiMINT-2732136.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 325Combined sources
Helixi35 – 4410Combined sources
Helixi62 – 654Combined sources
Beta strandi69 – 746Combined sources
Beta strandi113 – 1186Combined sources
Turni120 – 1234Combined sources
Beta strandi125 – 13410Combined sources
Helixi145 – 15713Combined sources
Helixi159 – 1635Combined sources
Beta strandi164 – 17310Combined sources
Helixi176 – 1816Combined sources
Helixi184 – 1863Combined sources
Beta strandi194 – 1985Combined sources
Helixi200 – 2056Combined sources
Turni208 – 2103Combined sources
Helixi211 – 2199Combined sources
Helixi226 – 24924Combined sources
Beta strandi252 – 26413Combined sources
Helixi267 – 2726Combined sources
Turni273 – 2753Combined sources
Beta strandi319 – 3246Combined sources
Beta strandi329 – 3313Combined sources
Helixi339 – 35517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IEWX-ray2.00A/B1-355[»]
2IF8X-ray2.40A/B1-355[»]
ProteinModelPortaliP07250.
SMRiP07250. Positions 26-355.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07250.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni127 – 1359Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi282 – 30120Asp-rich (acidic)Add
BLAST

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000065947.
InParanoidiP07250.
KOiK00915.
OMAiKWYGRSF.
OrthoDBiEOG092C36TH.

Family and domain databases

InterProiIPR005522. IPK.
[Graphical view]
PANTHERiPTHR12400. PTHR12400. 4 hits.
PfamiPF03770. IPK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07250-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTVNNYRVL EHKAAGHDGT LTDGDGLLIF KPAFPQELEF YKAIQVRDVS
60 70 80 90 100
RRKSSADGDA PLCSWMPTYL GVLNEGAKIE QSGDAALLKI DERLSDSTDN
110 120 130 140 150
LDSIPVKSEK SKQYLVLENL LYGFSKPNIL DIKLGKTLYD SKASLEKRER
160 170 180 190 200
MKRVSETTTS GSLGFRICGM KIQKNPSVLN QLSLEYYEEE ADSDYIFINK
210 220 230 240 250
LYGRSRTDQN VSDAIELYFN NPHLSDARKH QLKKTFLKRL QLFYNTMLEE
260 270 280 290 300
EVRMISSSLL FIYEGDPERW ELLNDVDKLM RDDFIDDDDD DDDNDDDDDD
310 320 330 340 350
DAEGSSEGPK DKKTTGSLSS MSLIDFAHSE ITPGKGYDEN VIEGVETLLD

IFMKF
Length:355
Mass (Da):40,353
Last modified:April 1, 1988 - v1
Checksum:iF858B39E3C54E6BF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091E → K in AAS56022 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05328 Genomic DNA. Translation: CAA28945.1.
Z46727 Genomic DNA. Translation: CAA86678.1.
AY557696 Genomic DNA. Translation: AAS56022.1.
BK006938 Genomic DNA. Translation: DAA12015.1.
PIRiS05823. RGBYR3.
RefSeqiNP_010458.3. NM_001180480.3.

Genome annotation databases

EnsemblFungiiYDR173C; YDR173C; YDR173C.
GeneIDi851753.
KEGGisce:YDR173C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05328 Genomic DNA. Translation: CAA28945.1.
Z46727 Genomic DNA. Translation: CAA86678.1.
AY557696 Genomic DNA. Translation: AAS56022.1.
BK006938 Genomic DNA. Translation: DAA12015.1.
PIRiS05823. RGBYR3.
RefSeqiNP_010458.3. NM_001180480.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IEWX-ray2.00A/B1-355[»]
2IF8X-ray2.40A/B1-355[»]
ProteinModelPortaliP07250.
SMRiP07250. Positions 26-355.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32226. 36 interactions.
DIPiDIP-1242N.
IntActiP07250. 3 interactions.
MINTiMINT-2732136.

Chemistry

SwissLipidsiSLP:000000958.

PTM databases

iPTMnetiP07250.

Proteomic databases

MaxQBiP07250.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR173C; YDR173C; YDR173C.
GeneIDi851753.
KEGGisce:YDR173C.

Organism-specific databases

EuPathDBiFungiDB:YDR173C.
SGDiS000002580. ARG82.

Phylogenomic databases

HOGENOMiHOG000065947.
InParanoidiP07250.
KOiK00915.
OMAiKWYGRSF.
OrthoDBiEOG092C36TH.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-7707.
YEAST:G3O-29762-MONOMER.
YEAST:MONOMER3O-64.
SABIO-RKP07250.

Miscellaneous databases

EvolutionaryTraceiP07250.
PROiP07250.

Family and domain databases

InterProiIPR005522. IPK.
[Graphical view]
PANTHERiPTHR12400. PTHR12400. 4 hits.
PfamiPF03770. IPK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIPMK_YEAST
AccessioniPrimary (citable) accession number: P07250
Secondary accession number(s): D6VSF5, E9P8S7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: September 7, 2016
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

The expression of this protein is not effected by the presence of arginine.
Present with 2720 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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