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Entry version 180 (02 Jun 2021)
Sequence version 1 (01 Apr 1988)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Inositol phosphate kinase with both monophosphoinositol and diphosphoinositol polyphosphate synthase activities. Able to phosphorylate inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) on both the carbon-3 and carbon-6 positions to synthesize inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4) and inositol 1,4,5,6-tetrakisphosphate (Ins(1,4,5,6)P4), and then to subsequently phosphorylate and convert either isomer of InsP4 to inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) (PubMed:10574768, PubMed:10683435, PubMed:11311242).

Its predominant in vivo catalytic function is to convert Ins(1,4,5)P3 to Ins(1,4,5,6)P4 to Ins(1,3,4,5,6)P5 via 6- and 3-kinase activities (PubMed:15944147).

It can also use Ins(1,3,4,5,6)P5 as a substrate and act as a diphosphoinositol polyphosphate synthase to generate two different isomers of PP-InsP4 (PubMed:11311242).

Has also a role in transcription regulation. Forms a complex with ARG80, ARG81 and MCM1 (ArgR-MCM1), which coordinates the expression of arginine anabolic and catabolic genes in response to arginine. Recruits ARG80 and MCM21 to stabilize them (PubMed:3298999, PubMed:8043104, PubMed:10632874).

Neither the kinase activity nor inositol phosphates are required for the formation of ArgR-MCM1 transciptional complexes on DNA promoter elements and the control of arginine metabolism (PubMed:11119723, PubMed:10720331, PubMed:12828642, PubMed:22992733).

In contrast, only the catalytic activity is required for PHO gene repression by phosphate and for NCR gene activation in response to nitrogen availability, indicating a role for inositol pyrophosphates in these controls (PubMed:12828642).

Inositol polyphosphates may be involved in the regulation of chromatin remodeling of transcription (PubMed:12434012).

Regulates nuclear mRNA export via inositol phosphate metabolism (PubMed:10390371, PubMed:10683435).

Also has lipid kinase activity, transforming the lipid inositol phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) into phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) in the nucleus (PubMed:16123124).

Its kinase activity is necessary for the propagation of most [PSI+] prion variants (PubMed:28923943).

15 Publications

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=15.3 µM for 1D-myo-inositol 1,4,5-trisphosphate1 Publication
  2. KM=7.1 µM for 1D-myo-inositol 1,4,5-trisphosphate1 Publication
  3. KM=62 µM for 1D-myo-inositol 1,3,4,5,6-pentakisphosphate1 Publication
  4. KM=30 µM for phosphatidylinositol 4,5-bisphosphate1 Publication
  5. KM=2.1 mM for ATP1 Publication
  1. Vmax=6272 nmol/min/mg enzyme for 1D-myo-inositol 1,4,5-trisphosphate1 Publication
  2. Vmax=4.9 nmol/min/mg enzyme for 1D-myo-inositol 1,3,4,5,6-pentakisphosphate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei31ATPCombined sources1 Publication1
Binding sitei131ATPCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi271Calcium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi274CalciumCombined sources1 Publication1
Binding sitei325ATPCombined sources1 Publication1
Metal bindingi334Calcium; via carbonyl oxygenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi118 – 120ATPCombined sources1 Publication3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Transferase
Biological processArginine metabolism, Transcription, Transcription regulation
LigandATP-binding, Calcium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER3O-64

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-1855191, Synthesis of IPs in the nucleus

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P07250

Protein family/group databases

MoonProt database of moonlighting proteins

More...
MoonProti
P07250

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000958

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Inositol polyphosphate multikinaseCurated (EC:2.7.1.127, EC:2.7.1.151)
Short name:
IPMK
Alternative name(s):
Arginine metabolism regulation protein III
GLE1 synthetic lethal protein 31 Publication
Inositol polyphosphate kinase 21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ARG82
Synonyms:ARGR3, GSL31 Publication, IPK21 Publication
Ordered Locus Names:YDR173C
ORF Names:YD9395.06C
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome IV

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000002580, ARG82

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YDR173C

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Impairs nuclear mRNA export, slows cell growth, increases cellular InsP3 170-fold and decreases InsP6 100-fold.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi131D → A: Abolishes catalytic activity, but preserves its nonkinase transcription regulation functions. 2 Publications1
Mutagenesisi133K → A: Abolishes catalytic activity, but preserves its nonkinase transcription regulation functions. 2 Publications1
Mutagenesisi257 – 260SSLL → AAAA: Abolishes catalytic activity. 1 Publication4

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000668731 – 355Inositol polyphosphate multikinaseAdd BLAST355

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineCombined sources1
Modified residuei97PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P07250

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P07250

PRoteomics IDEntifications database

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PRIDEi
P07250

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P07250

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with ARG80 and MCM1.

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
32226, 45 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1152, ARGR-MCM1 transcription regulation complex

Database of interacting proteins

More...
DIPi
DIP-1242N

Protein interaction database and analysis system

More...
IntActi
P07250, 3 interactors

Molecular INTeraction database

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MINTi
P07250

STRING: functional protein association networks

More...
STRINGi
4932.YDR173C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P07250, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1355
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P07250

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P07250

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni127 – 135Substrate bindingBy similarity9
Regioni284 – 317DisorderedSequence analysisAdd BLAST34

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi284 – 304Acidic residuesSequence analysisAdd BLAST21

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1620, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000167316

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_042569_3_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P07250

Identification of Orthologs from Complete Genome Data

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OMAi
KWYGRSF

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.510.50, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005522, IPK
IPR038286, IPK_sf

The PANTHER Classification System

More...
PANTHERi
PTHR12400, PTHR12400, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03770, IPK, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF858B39E3C54E6BF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti109E → K in AAS56022 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
S05823, RGBYR3

NCBI Reference Sequences

More...
RefSeqi
NP_010458.3, NM_001180480.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YDR173C_mRNA; YDR173C; YDR173C

Database of genes from NCBI RefSeq genomes

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GeneIDi
851753

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDR173C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IEWX-ray2.00A/B1-355[»]
2IF8X-ray2.40A/B1-355[»]
SMRiP07250
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi32226, 45 interactors
ComplexPortaliCPX-1152, ARGR-MCM1 transcription regulation complex
DIPiDIP-1242N
IntActiP07250, 3 interactors
MINTiP07250
STRINGi4932.YDR173C

Chemistry databases

SwissLipidsiSLP:000000958

Protein family/group databases

MoonProtiP07250

PTM databases

iPTMnetiP07250

Proteomic databases

MaxQBiP07250
PaxDbiP07250
PRIDEiP07250

Genome annotation databases

EnsemblFungiiYDR173C_mRNA; YDR173C; YDR173C
GeneIDi851753
KEGGisce:YDR173C

Organism-specific databases

SGDiS000002580, ARG82
VEuPathDBiFungiDB:YDR173C

Phylogenomic databases

eggNOGiKOG1620, Eukaryota
GeneTreeiENSGT00940000167316
HOGENOMiCLU_042569_3_0_1
InParanoidiP07250
OMAiKWYGRSF

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-64
ReactomeiR-SCE-1855191, Synthesis of IPs in the nucleus
SABIO-RKiP07250

Miscellaneous databases

EvolutionaryTraceiP07250

Protein Ontology

More...
PROi
PR:P07250
RNActiP07250, protein

Family and domain databases

Gene3Di1.10.510.50, 1 hit
InterProiView protein in InterPro
IPR005522, IPK
IPR038286, IPK_sf
PANTHERiPTHR12400, PTHR12400, 1 hit
PfamiView protein in Pfam
PF03770, IPK, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiIPMK_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P07250
Secondary accession number(s): D6VSF5, E9P8S7
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: June 2, 2021
This is version 180 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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