Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P37012 (PGM2_YEAST)

Entry version 179 (17 Jun 2020)
Sequence version 1 (01 Jun 1994)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Phosphoglucomutase 2

Gene

PGM2

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

Major phosphoglucomutase isozyme that catalyzes the reversible interconversion of glucose 1-phosphate and glucose 6-phosphate (PubMed:5784209). Constitutes about 80-90% of the phosphoglucomutase activity in the cell (PubMed:14264884, PubMed:5231755). Key enzyme in hexose metabolism. The forward reaction is an essential step in the energy metabolism of galactose since the product of the galactose pathway enzymes in yeast is glucose 1-phosphate. The reverse reaction is an essential step for biosynthesis when carbon sources other than galactose are the energy source because glucose 1-phosphate is the starting point for the synthesis of UDP-glucose, which acts as a precursor for the synthesis of oligosaccharides and trehalose (PubMed:14264884).2 Publications

Miscellaneous

Present with 3790 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

Mg2+2 Publications, Zn2+2 PublicationsNote: Binds 1 magnesium ion per subunit. Can also use Zn2+ as cofactor.2 Publications

<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=2.24 µM for alpha-D-glucose 1,6-diphosphate1 Publication
  2. KM=23.4 µM for alpha-D-glucose 1-phosphate1 Publication
  3. KM=26 µM for alpha-D-glucose 1-phosphate1 Publication
  4. KM=530 µM for D-ribose 1-phosphate1 Publication
  1. Vmax=33.7 µmol/min/mg enzyme for alpha-D-glucose 1-phosphate1 Publication
  2. Vmax=0.32 µmol/min/mg enzyme for D-ribose 1-phosphate1 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 sitei20SubstrateBy similarity1
Binding sitei24SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei119Phosphoserine intermediateBy similarity1
<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 bindingi119Magnesium; via phosphate groupBy similarity1
Binding sitei132SubstrateBy similarity1
Metal bindingi290MagnesiumBy similarity1
Metal bindingi292MagnesiumBy similarity1
Metal bindingi294MagnesiumBy similarity1
Binding sitei359SubstrateBy similarity1
Binding sitei391SubstrateBy similarity1
Binding sitei522SubstrateBy similarity1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionIsomerase
Biological processCarbohydrate metabolism, Glucose metabolism
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:YMR105C-MONOMER
YEAST:YMR105C-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P37012

<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:
Phosphoglucomutase 21 Publication (EC:5.4.2.23 Publications)
Short name:
PGM 21 Publication
Alternative name(s):
D-glucose-1,6-diphosphate:D-glucose-1-phosphate phosphotransferase1 Publication
Glucose phosphomutase 2
<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:PGM21 Publication
Synonyms:GA-51 Publication, GAL51 Publication
Ordered Locus Names:YMR105CImported
ORF Names:YM9718.04C
<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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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 XIII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		FungiDB:YMR105C

Saccharomyces Genome Database

More...SGDi		S000004711 PGM2

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<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

Blocks galactose utilization, but does not impair growth on glucose.1 Publication

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00001477972 – 569Phosphoglucomutase 2Add BLAST568

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 residuei2N-acetylserineCombined sources1
Modified residuei111PhosphothreonineCombined sources1
Modified residuei117PhosphothreonineCombined sources1
Modified residuei119PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

O-glycosylated with mannose residues (By similarity). Substrate of UDP-glucose--glycoprotein glucose phosphotransferase, linking glucose in a phosphodiester linkage to O-linked mannose (PubMed:8385141, PubMed:7929458).By similarity2 Publications

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P37012

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

More...PaxDbi		P37012

PRoteomics IDEntifications database

More...PRIDEi		P37012

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P37012

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced in response to galactose and severely repressed in response to glucose.1 Publication

<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

Monomer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		35280, 122 interactors

Database of interacting proteins

More...DIPi		DIP-6499N

Protein interaction database and analysis system

More...IntActi		P37012, 28 interactors

Molecular INTeraction database

More...MINTi		P37012

STRING: functional protein association networks

More...STRINGi		4932.YMR105C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P37012 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

3D structure databases

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

More...SMRi		P37012

Database of comparative protein structure models

More...ModBasei		Search...

<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>Regioni119 – 120Substrate bindingBy similarity2
Regioni294 – 295Substrate bindingBy similarity2
Regioni378 – 380Substrate bindingBy similarity3

<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

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

Ensembl GeneTree

More...GeneTreei		ENSGT00940000173602

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_009330_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P37012

KEGG Orthology (KO)

More...KOi		K01835

Identification of Orthologs from Complete Genome Data

More...OMAi		DIYKIYA

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR005844 A-D-PHexomutase_a/b/a-I
IPR016055 A-D-PHexomutase_a/b/a-I/II/III
IPR005845 A-D-PHexomutase_a/b/a-II
IPR005846 A-D-PHexomutase_a/b/a-III
IPR005843 A-D-PHexomutase_C
IPR036900 A-D-PHexomutase_C_sf
IPR016066 A-D-PHexomutase_CS
IPR005841 Alpha-D-phosphohexomutase_SF

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02878 PGM_PMM_I, 1 hit
PF02879 PGM_PMM_II, 1 hit
PF02880 PGM_PMM_III, 1 hit
PF00408 PGM_PMM_IV, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00509 PGMPMM

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53738 SSF53738, 3 hits
SSF55957 SSF55957, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00710 PGM_PMM, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P37012-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSFQIETVPT KPYEDQKPGT SGLRKKTKVF KDEPNYTENF IQSIMEAIPE 
        60         70         80         90        100
GSKGATLVVG GDGRYYNDVI LHKIAAIGAA NGIKKLVIGQ HGLLSTPAAS 
       110        120        130        140        150
HIMRTYEEKC TGGIILTASH NPGGPENDMG IKYNLSNGGP APESVTNAIW 
       160        170        180        190        200
EISKKLTSYK IIKDFPELDL GTIGKNKKYG PLLVDIIDIT KDYVNFLKEI 
       210        220        230        240        250
FDFDLIKKFI DNQRSTKNWK LLFDSMNGVT GPYGKAIFVD EFGLPADEVL 
       260        270        280        290        300
QNWHPSPDFG GMHPDPNLTY ASSLVKRVDR EKIEFGAASD GDGDRNMIYG 
       310        320        330        340        350
YGPSFVSPGD SVAIIAEYAA EIPYFAKQGI YGLARSFPTS GAIDRVAKAH 
       360        370        380        390        400
GLNCYEVPTG WKFFCALFDA KKLSICGEES FGTGSNHVRE KDGVWAIMAW 
       410        420        430        440        450
LNILAIYNKH HPENEASIKT IQNEFWAKYG RTFFTRYDFE KVETEKANKI 
       460        470        480        490        500
VDQLRAYVTK SGVVNSAFPA DESLKVTDCG DFSYTDLDGS VSDHQGLYVK 
       510        520        530        540        550
LSNGARFVLR LSGTGSSGAT IRLYIEKYCD DKSQYQKTAE EYLKPIINSV 
       560 
IKFLNFKQVL GTEEPTVRT
Length:569
Mass (Da):63,089
Last modified:June 1, 1994 - 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:i45B78AFF8197645E
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 conflicti27T → G AA sequence (PubMed:8385141).Curated1
Sequence conflicti32D → G AA sequence (PubMed:8385141).Curated1
Sequence conflicti272S → A AA sequence (PubMed:8385141).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X74823 Genomic DNA Translation: CAA52820.1
U09499 Genomic DNA Translation: AAA91282.1
Z49702 Genomic DNA Translation: CAA89741.1
AY723853 Genomic DNA Translation: AAU09770.1
BK006946 Genomic DNA Translation: DAA10001.1

Protein sequence database of the Protein Information Resource

More...PIRi		S41200

NCBI Reference Sequences

More...RefSeqi		NP_013823.1, NM_001182605.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YMR105C_mRNA; YMR105C; YMR105C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		855131

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YMR105C

<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
X74823 Genomic DNA Translation: CAA52820.1
U09499 Genomic DNA Translation: AAA91282.1
Z49702 Genomic DNA Translation: CAA89741.1
AY723853 Genomic DNA Translation: AAU09770.1
BK006946 Genomic DNA Translation: DAA10001.1
PIRiS41200
RefSeqiNP_013823.1, NM_001182605.1

3D structure databases

SMRiP37012
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi35280, 122 interactors
DIPiDIP-6499N
IntActiP37012, 28 interactors
MINTiP37012
STRINGi4932.YMR105C

PTM databases

iPTMnetiP37012

Proteomic databases

MaxQBiP37012
PaxDbiP37012
PRIDEiP37012

Genome annotation databases

EnsemblFungiiYMR105C_mRNA; YMR105C; YMR105C
GeneIDi855131
KEGGisce:YMR105C

Organism-specific databases

EuPathDBiFungiDB:YMR105C
SGDiS000004711 PGM2

Phylogenomic databases

GeneTreeiENSGT00940000173602
HOGENOMiCLU_009330_0_1_1
InParanoidiP37012
KOiK01835
OMAiDIYKIYA

Enzyme and pathway databases

BioCyciMetaCyc:YMR105C-MONOMER
YEAST:YMR105C-MONOMER
SABIO-RKiP37012

Miscellaneous databases

Protein Ontology

More...PROi		PR:P37012
RNActiP37012 protein

Family and domain databases

InterProiView protein in InterPro
IPR005844 A-D-PHexomutase_a/b/a-I
IPR016055 A-D-PHexomutase_a/b/a-I/II/III
IPR005845 A-D-PHexomutase_a/b/a-II
IPR005846 A-D-PHexomutase_a/b/a-III
IPR005843 A-D-PHexomutase_C
IPR036900 A-D-PHexomutase_C_sf
IPR016066 A-D-PHexomutase_CS
IPR005841 Alpha-D-phosphohexomutase_SF
PfamiView protein in Pfam
PF02878 PGM_PMM_I, 1 hit
PF02879 PGM_PMM_II, 1 hit
PF02880 PGM_PMM_III, 1 hit
PF00408 PGM_PMM_IV, 1 hit
PRINTSiPR00509 PGMPMM
SUPFAMiSSF53738 SSF53738, 3 hits
SSF55957 SSF55957, 1 hit
PROSITEiView protein in PROSITE
PS00710 PGM_PMM, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiPGM2_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: P37012
Secondary accession number(s): D6VZS7
<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: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 17, 2020
This is version 179 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

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again