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Protein

Phosphoglucomutase-1

Gene

PGM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This enzyme participates in both the breakdown and synthesis of glucose.

Catalytic activityi

Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.2 Publications

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Enzyme regulationi

Glucose-1,6-bisphosphate enhances phosphorylation of the active site Ser-117, and thereby increases enzyme activity.1 Publication

Kineticsi

  1. KM=80 µM for alpha-D-glucose 1-phosphate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei19SubstrateBy similarity1
    Binding sitei23SubstrateBy similarity1
    Active sitei117Phosphoserine intermediate1 Publication1
    Metal bindingi117Magnesium; via phosphate groupBy similarity1
    Binding sitei130SubstrateBy similarity1
    Metal bindingi288Magnesium1 Publication1
    Metal bindingi290Magnesium1 Publication1
    Metal bindingi292Magnesium1 Publication1
    Binding sitei357SubstrateBy similarity1
    Binding sitei389SubstrateBy similarity1
    Binding sitei515SubstrateBy similarity1

    GO - Molecular functioni

    • magnesium ion binding Source: UniProtKB
    • phosphoglucomutase activity Source: UniProtKB

    GO - Biological processi

    • galactose catabolic process Source: GO_Central
    • gluconeogenesis Source: UniProtKB
    • glucose metabolic process Source: UniProtKB
    • glycogen biosynthetic process Source: GO_Central
    • glycogen catabolic process Source: Reactome
    • glycolytic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01335-MONOMER.
    ZFISH:HS01335-MONOMER.
    ReactomeiR-HSA-3322077. Glycogen synthesis.
    R-HSA-6798695. Neutrophil degranulation.
    R-HSA-70221. Glycogen breakdown (glycogenolysis).
    R-HSA-70370. Galactose catabolism.
    SABIO-RKP36871.
    SIGNORiP36871.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoglucomutase-1 (EC:5.4.2.22 Publications)
    Short name:
    PGM 1
    Alternative name(s):
    Glucose phosphomutase 1
    Gene namesi
    Name:PGM1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:8905. PGM1.

    Subcellular locationi

    GO - Cellular componenti

    • actin cytoskeleton Source: HPA
    • cytoplasm Source: UniProtKB
    • cytosol Source: GO_Central
    • extracellular exosome Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Congenital disorder of glycosylation 1T (CDG1T)5 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA form of congenital disorder of glycosylation, a multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
    See also OMIM:614921
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_07163519T → A in CDG1T; reduces strongly phosphoglucomutase activity. 2 Publications1
    Natural variantiVAR_07163638N → Y in CDG1T; reduces strongly solubility; increases aggregation. 2 PublicationsCorresponds to variant rs587777402dbSNPEnsembl.1
    Natural variantiVAR_07163741Q → R in CDG1T; reduces solubility; increases aggregation. 2 Publications1
    Natural variantiVAR_07163862D → H in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity. 2 PublicationsCorresponds to variant rs587777403dbSNPEnsembl.1
    Natural variantiVAR_062280115T → A in CDG1T; reduces mildly phosphoglucomutase activity. 3 PublicationsCorresponds to variant rs121918371dbSNPEnsembl.1
    Natural variantiVAR_069219121G → R in CDG1T; there is 7% enzyme residual phosphoglucomutase activity. 3 PublicationsCorresponds to variant rs398122912dbSNPEnsembl.1
    Natural variantiVAR_071639263D → G in CDG1T; reduces strongly phosphoglucomutase activity. 2 Publications1
    Natural variantiVAR_071640263D → Y in CDG1T; reduces strongly phosphoglucomutase activity. 2 PublicationsCorresponds to variant rs587777404dbSNPEnsembl.1
    Natural variantiVAR_071641291G → R in CDG1T; reduces strongly phosphoglucomutase activity. 3 PublicationsCorresponds to variant rs772768778dbSNPEnsembl.1
    Natural variantiVAR_071642330G → R in CDG1T; decreases mildly solubility. 2 PublicationsCorresponds to variant rs777164338dbSNPEnsembl.1
    Natural variantiVAR_071643377E → K in CDG1T; decreases strongly solubility. 2 Publications1
    Natural variantiVAR_071644388E → K in CDG1T; decreases strongly solubility. 2 Publications1
    Natural variantiVAR_071645516L → P in CDG1T; decreases strongly solubility. 2 PublicationsCorresponds to variant rs587777401dbSNPEnsembl.1

    Keywords - Diseasei

    Congenital disorder of glycosylation, Disease mutation, Glycogen storage disease

    Organism-specific databases

    DisGeNETi5236.
    MalaCardsiPGM1.
    MIMi614921. phenotype.
    OpenTargetsiENSG00000079739.
    Orphaneti711. Glycogen storage disease due to phosphoglucomutase deficiency.
    319646. PGM-CDG.
    PharmGKBiPA33242.

    Polymorphism and mutation databases

    BioMutaiPGM1.
    DMDMi585670.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001477761 – 562Phosphoglucomutase-1Add BLAST562

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei1N-acetylmethionineCombined sources1
    Modified residuei16N6-acetyllysineCombined sources1
    Modified residuei115PhosphothreonineBy similarity1
    Modified residuei117PhosphoserineCombined sources1 Publication1
    Modified residuei134PhosphoserineBy similarity1
    Modified residuei185PhosphothreonineCombined sources1
    Modified residuei201PhosphoserineCombined sources1
    Modified residuei206PhosphoserineCombined sources1
    Modified residuei213PhosphoserineBy similarity1
    Modified residuei349N6-acetyllysineBy similarity1
    Modified residuei353PhosphotyrosineBy similarity1
    Modified residuei369PhosphoserineBy similarity1
    Modified residuei378PhosphoserineCombined sources1
    Modified residuei419N6-succinyllysineBy similarity1
    Modified residuei467Phosphothreonine; by PAK11 Publication1
    Modified residuei477PhosphoserineBy similarity1
    Modified residuei485PhosphoserineBy similarity1
    Modified residuei505PhosphoserineCombined sources1
    Modified residuei507PhosphothreonineBy similarity1
    Modified residuei509PhosphoserineCombined sources1
    Modified residuei541PhosphoserineBy similarity1
    Isoform 2 (identifier: P36871-2)
    Modified residuei1N-acetylmethionineCombined sources1

    Post-translational modificationi

    Phosphorylation at Thr-467 by PAK1 significantly enhances enzymatic activity.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiP36871.
    MaxQBiP36871.
    PeptideAtlasiP36871.
    PRIDEiP36871.

    2D gel databases

    REPRODUCTION-2DPAGEP36871.

    PTM databases

    iPTMnetiP36871.
    PhosphoSitePlusiP36871.
    SwissPalmiP36871.

    Expressioni

    Gene expression databases

    BgeeiENSG00000079739.
    CleanExiHS_PGM1.
    GenevisibleiP36871. HS.

    Organism-specific databases

    HPAiCAB004666.
    HPA024190.
    HPA024637.
    HPA046329.

    Interactioni

    Subunit structurei

    Monomer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TINF2Q9BSI42EBI-2861475,EBI-717399

    Protein-protein interaction databases

    BioGridi111256. 44 interactors.
    DIPiDIP-60903N.
    IntActiP36871. 9 interactors.
    MINTiMINT-5001559.

    Structurei

    Secondary structure

    1562
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 8Combined sources4
    Turni18 – 20Combined sources3
    Beta strandi22 – 25Combined sources4
    Helixi26 – 31Combined sources6
    Beta strandi32 – 34Combined sources3
    Helixi35 – 44Combined sources10
    Helixi49 – 51Combined sources3
    Turni52 – 54Combined sources3
    Beta strandi56 – 61Combined sources6
    Helixi67 – 80Combined sources14
    Beta strandi85 – 93Combined sources9
    Helixi96 – 106Combined sources11
    Beta strandi109 – 114Combined sources6
    Beta strandi125 – 133Combined sources9
    Beta strandi136 – 138Combined sources3
    Helixi141 – 153Combined sources13
    Beta strandi156 – 159Combined sources4
    Beta strandi171 – 177Combined sources7
    Beta strandi184 – 189Combined sources6
    Helixi193 – 202Combined sources10
    Helixi205 – 212Combined sources8
    Beta strandi220 – 223Combined sources4
    Beta strandi227 – 229Combined sources3
    Helixi230 – 236Combined sources7
    Turni237 – 241Combined sources5
    Helixi245 – 247Combined sources3
    Beta strandi248 – 250Combined sources3
    Helixi257 – 259Combined sources3
    Turni266 – 269Combined sources4
    Helixi270 – 277Combined sources8
    Beta strandi282 – 287Combined sources6
    Beta strandi291 – 298Combined sources8
    Helixi299 – 301Combined sources3
    Beta strandi302 – 304Combined sources3
    Helixi306 – 315Combined sources10
    Helixi316 – 319Combined sources4
    Helixi321 – 326Combined sources6
    Beta strandi331 – 334Combined sources4
    Helixi340 – 348Combined sources9
    Beta strandi352 – 355Combined sources4
    Helixi359 – 367Combined sources9
    Beta strandi372 – 376Combined sources5
    Turni377 – 379Combined sources3
    Beta strandi380 – 383Combined sources4
    Beta strandi386 – 388Combined sources3
    Helixi391 – 405Combined sources15
    Helixi409 – 420Combined sources12
    Beta strandi422 – 433Combined sources12
    Helixi435 – 450Combined sources16
    Beta strandi458 – 473Combined sources16
    Turni479 – 481Combined sources3
    Beta strandi490 – 494Combined sources5
    Beta strandi499 – 504Combined sources6
    Beta strandi512 – 522Combined sources11
    Helixi525 – 528Combined sources4
    Helixi532 – 547Combined sources16
    Helixi549 – 553Combined sources5
    Beta strandi559 – 562Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5EPCX-ray1.85A/B1-562[»]
    5F9CX-ray2.50A/B1-562[»]
    5HSHX-ray2.65A/B1-562[»]
    ProteinModelPortaliP36871.
    SMRiP36871.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni117 – 118Substrate bindingBy similarity2
    Regioni292 – 293Substrate bindingBy similarity2
    Regioni376 – 378Substrate bindingBy similarity3

    Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00390000011831.
    HOVERGENiHBG001599.
    InParanoidiP36871.
    KOiK01835.
    OMAiPAYSKGI.
    OrthoDBiEOG091G0HZ0.
    PhylomeDBiP36871.
    TreeFamiTF300350.

    Family and domain databases

    Gene3Di3.30.310.50. 1 hit.
    3.40.120.10. 3 hits.
    InterProiIPR005844. 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.
    IPR016066. A-D-PHexomutase_CS.
    IPR005841. Alpha-D-phosphohexomutase_SF.
    [Graphical view]
    PfamiPF02878. PGM_PMM_I. 1 hit.
    PF02879. PGM_PMM_II. 1 hit.
    PF02880. PGM_PMM_III. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view]
    PRINTSiPR00509. PGMPMM.
    SUPFAMiSSF53738. SSF53738. 3 hits.
    SSF55957. SSF55957. 1 hit.
    PROSITEiPS00710. PGM_PMM. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P36871-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MVKIVTVKTQ AYQDQKPGTS GLRKRVKVFQ SSANYAENFI QSIISTVEPA
    60 70 80 90 100
    QRQEATLVVG GDGRFYMKEA IQLIARIAAA NGIGRLVIGQ NGILSTPAVS
    110 120 130 140 150
    CIIRKIKAIG GIILTASHNP GGPNGDFGIK FNISNGGPAP EAITDKIFQI
    160 170 180 190 200
    SKTIEEYAVC PDLKVDLGVL GKQQFDLENK FKPFTVEIVD SVEAYATMLR
    210 220 230 240 250
    SIFDFSALKE LLSGPNRLKI RIDAMHGVVG PYVKKILCEE LGAPANSAVN
    260 270 280 290 300
    CVPLEDFGGH HPDPNLTYAA DLVETMKSGE HDFGAAFDGD GDRNMILGKH
    310 320 330 340 350
    GFFVNPSDSV AVIAANIFSI PYFQQTGVRG FARSMPTSGA LDRVASATKI
    360 370 380 390 400
    ALYETPTGWK FFGNLMDASK LSLCGEESFG TGSDHIREKD GLWAVLAWLS
    410 420 430 440 450
    ILATRKQSVE DILKDHWQKY GRNFFTRYDY EEVEAEGANK MMKDLEALMF
    460 470 480 490 500
    DRSFVGKQFS ANDKVYTVEK ADNFEYSDPV DGSISRNQGL RLIFTDGSRI
    510 520 530 540 550
    VFRLSGTGSA GATIRLYIDS YEKDVAKINQ DPQVMLAPLI SIALKVSQLQ
    560
    ERTGRTAPTV IT
    Length:562
    Mass (Da):61,449
    Last modified:January 23, 2007 - v3
    Checksum:i61A26C19107D467A
    GO
    Isoform 2 (identifier: P36871-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-77: MVKIVTVKTQ...KEAIQLIARI → MSDFEEWISG...KSAIETIVQM

    Show »
    Length:580
    Mass (Da):63,791
    Checksum:iCE4F9CA4094B5139
    GO
    Isoform 3 (identifier: P36871-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-197: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:365
    Mass (Da):40,283
    Checksum:iE0696E6FD7170D62
    GO

    Sequence cautioni

    The sequence AAH90856 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti134S → C in AAH67763 (PubMed:15489334).Curated1

    Polymorphismi

    Many polymorphic variants of PGM1 exist. 8 different alleles are known: PGM1*1+, PGM1*1-, PGM1*2+, PGM1*2-, PGM1*3+, PGM1*3-, PGM1*7+ and PGM1*7-. The sequence of PGM1*1+ is shown here.

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_07163519T → A in CDG1T; reduces strongly phosphoglucomutase activity. 2 Publications1
    Natural variantiVAR_07163638N → Y in CDG1T; reduces strongly solubility; increases aggregation. 2 PublicationsCorresponds to variant rs587777402dbSNPEnsembl.1
    Natural variantiVAR_07163741Q → R in CDG1T; reduces solubility; increases aggregation. 2 Publications1
    Natural variantiVAR_07163862D → H in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity. 2 PublicationsCorresponds to variant rs587777403dbSNPEnsembl.1
    Natural variantiVAR_00609068K → M in allele PGM1*7+, allele PGM1*7-, allele PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is similar to wild-type. 2 PublicationsCorresponds to variant rs200390982dbSNPEnsembl.1
    Natural variantiVAR_05049688I → V.Corresponds to variant rs855314dbSNPEnsembl.1
    Natural variantiVAR_062280115T → A in CDG1T; reduces mildly phosphoglucomutase activity. 3 PublicationsCorresponds to variant rs121918371dbSNPEnsembl.1
    Natural variantiVAR_069219121G → R in CDG1T; there is 7% enzyme residual phosphoglucomutase activity. 3 PublicationsCorresponds to variant rs398122912dbSNPEnsembl.1
    Natural variantiVAR_006091221R → C in allele PGM1*2+, allele PGM1*2-, allele PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is similar to wild-type. 5 PublicationsCorresponds to variant rs1126728dbSNPEnsembl.1
    Natural variantiVAR_071639263D → G in CDG1T; reduces strongly phosphoglucomutase activity. 2 Publications1
    Natural variantiVAR_071640263D → Y in CDG1T; reduces strongly phosphoglucomutase activity. 2 PublicationsCorresponds to variant rs587777404dbSNPEnsembl.1
    Natural variantiVAR_071641291G → R in CDG1T; reduces strongly phosphoglucomutase activity. 3 PublicationsCorresponds to variant rs772768778dbSNPEnsembl.1
    Natural variantiVAR_071642330G → R in CDG1T; decreases mildly solubility. 2 PublicationsCorresponds to variant rs777164338dbSNPEnsembl.1
    Natural variantiVAR_071643377E → K in CDG1T; decreases strongly solubility. 2 Publications1
    Natural variantiVAR_071644388E → K in CDG1T; decreases strongly solubility. 2 Publications1
    Natural variantiVAR_006092420Y → H in allele PGM1*1-, allele PGM1*2-, allele PGM1*3- and allele PGM1*7-; phosphoglucomutase activity is similar to wild-type. 6 PublicationsCorresponds to variant rs11208257dbSNPEnsembl.1
    Natural variantiVAR_034380501V → I.Corresponds to variant rs6676290dbSNPEnsembl.1
    Natural variantiVAR_071645516L → P in CDG1T; decreases strongly solubility. 2 PublicationsCorresponds to variant rs587777401dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0452041 – 197Missing in isoform 3. 1 PublicationAdd BLAST197
    Alternative sequenceiVSP_0046861 – 77MVKIV…LIARI → MSDFEEWISGTYRKMEEGPL PLLTFATAPYHDQKPGTSGL RKKTYYFEEKPCYLENFIQS IFFSIDLKDRQGSSLVVGGD GRYFNKSAIETIVQM in isoform 2. CuratedAdd BLAST77

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M83088 mRNA. Translation: AAA60080.1.
    BT006961 mRNA. Translation: AAP35607.1.
    AK298505 mRNA. Translation: BAG60712.1.
    AK312254 mRNA. Translation: BAG35186.1.
    AL109925 Genomic DNA. Translation: CAB92085.1.
    AL109925 Genomic DNA. Translation: CAB92086.1.
    BC001756 mRNA. Translation: AAH01756.3.
    BC019920 mRNA. Translation: AAH19920.1.
    BC067763 mRNA. Translation: AAH67763.2.
    BC090856 mRNA. Translation: AAH90856.1. Different initiation.
    S67989 Genomic DNA. Translation: AAB29177.2.
    S67998 Genomic DNA. Translation: AAB29178.1.
    CCDSiCCDS53323.1. [P36871-2]
    CCDS53324.1. [P36871-3]
    CCDS625.1. [P36871-1]
    PIRiA41801.
    S39397.
    RefSeqiNP_001166289.1. NM_001172818.1. [P36871-2]
    NP_001166290.1. NM_001172819.1. [P36871-3]
    NP_002624.2. NM_002633.2. [P36871-1]
    UniGeneiHs.1869.

    Genome annotation databases

    EnsembliENST00000371083; ENSP00000360124; ENSG00000079739. [P36871-2]
    ENST00000371084; ENSP00000360125; ENSG00000079739. [P36871-1]
    ENST00000540265; ENSP00000443449; ENSG00000079739. [P36871-3]
    GeneIDi5236.
    KEGGihsa:5236.
    UCSCiuc001dbh.5. human. [P36871-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M83088 mRNA. Translation: AAA60080.1.
    BT006961 mRNA. Translation: AAP35607.1.
    AK298505 mRNA. Translation: BAG60712.1.
    AK312254 mRNA. Translation: BAG35186.1.
    AL109925 Genomic DNA. Translation: CAB92085.1.
    AL109925 Genomic DNA. Translation: CAB92086.1.
    BC001756 mRNA. Translation: AAH01756.3.
    BC019920 mRNA. Translation: AAH19920.1.
    BC067763 mRNA. Translation: AAH67763.2.
    BC090856 mRNA. Translation: AAH90856.1. Different initiation.
    S67989 Genomic DNA. Translation: AAB29177.2.
    S67998 Genomic DNA. Translation: AAB29178.1.
    CCDSiCCDS53323.1. [P36871-2]
    CCDS53324.1. [P36871-3]
    CCDS625.1. [P36871-1]
    PIRiA41801.
    S39397.
    RefSeqiNP_001166289.1. NM_001172818.1. [P36871-2]
    NP_001166290.1. NM_001172819.1. [P36871-3]
    NP_002624.2. NM_002633.2. [P36871-1]
    UniGeneiHs.1869.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5EPCX-ray1.85A/B1-562[»]
    5F9CX-ray2.50A/B1-562[»]
    5HSHX-ray2.65A/B1-562[»]
    ProteinModelPortaliP36871.
    SMRiP36871.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi111256. 44 interactors.
    DIPiDIP-60903N.
    IntActiP36871. 9 interactors.
    MINTiMINT-5001559.

    PTM databases

    iPTMnetiP36871.
    PhosphoSitePlusiP36871.
    SwissPalmiP36871.

    Polymorphism and mutation databases

    BioMutaiPGM1.
    DMDMi585670.

    2D gel databases

    REPRODUCTION-2DPAGEP36871.

    Proteomic databases

    EPDiP36871.
    MaxQBiP36871.
    PeptideAtlasiP36871.
    PRIDEiP36871.

    Protocols and materials databases

    DNASUi5236.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000371083; ENSP00000360124; ENSG00000079739. [P36871-2]
    ENST00000371084; ENSP00000360125; ENSG00000079739. [P36871-1]
    ENST00000540265; ENSP00000443449; ENSG00000079739. [P36871-3]
    GeneIDi5236.
    KEGGihsa:5236.
    UCSCiuc001dbh.5. human. [P36871-1]

    Organism-specific databases

    CTDi5236.
    DisGeNETi5236.
    GeneCardsiPGM1.
    GeneReviewsiPGM1.
    HGNCiHGNC:8905. PGM1.
    HPAiCAB004666.
    HPA024190.
    HPA024637.
    HPA046329.
    MalaCardsiPGM1.
    MIMi171900. gene.
    614921. phenotype.
    neXtProtiNX_P36871.
    OpenTargetsiENSG00000079739.
    Orphaneti711. Glycogen storage disease due to phosphoglucomutase deficiency.
    319646. PGM-CDG.
    PharmGKBiPA33242.
    GenAtlasiSearch...

    Phylogenomic databases

    GeneTreeiENSGT00390000011831.
    HOVERGENiHBG001599.
    InParanoidiP36871.
    KOiK01835.
    OMAiPAYSKGI.
    OrthoDBiEOG091G0HZ0.
    PhylomeDBiP36871.
    TreeFamiTF300350.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01335-MONOMER.
    ZFISH:HS01335-MONOMER.
    ReactomeiR-HSA-3322077. Glycogen synthesis.
    R-HSA-6798695. Neutrophil degranulation.
    R-HSA-70221. Glycogen breakdown (glycogenolysis).
    R-HSA-70370. Galactose catabolism.
    SABIO-RKP36871.
    SIGNORiP36871.

    Miscellaneous databases

    ChiTaRSiPGM1. human.
    GeneWikiiPGM1.
    GenomeRNAii5236.
    PROiP36871.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000079739.
    CleanExiHS_PGM1.
    GenevisibleiP36871. HS.

    Family and domain databases

    Gene3Di3.30.310.50. 1 hit.
    3.40.120.10. 3 hits.
    InterProiIPR005844. 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.
    IPR016066. A-D-PHexomutase_CS.
    IPR005841. Alpha-D-phosphohexomutase_SF.
    [Graphical view]
    PfamiPF02878. PGM_PMM_I. 1 hit.
    PF02879. PGM_PMM_II. 1 hit.
    PF02880. PGM_PMM_III. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view]
    PRINTSiPR00509. PGMPMM.
    SUPFAMiSSF53738. SSF53738. 3 hits.
    SSF55957. SSF55957. 1 hit.
    PROSITEiPS00710. PGM_PMM. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPGM1_HUMAN
    AccessioniPrimary (citable) accession number: P36871
    Secondary accession number(s): B2R5N9
    , B4DPV0, Q16105, Q16106, Q5BKZ9, Q6NW22, Q86U74, Q96J40, Q9NTY4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: January 23, 2007
    Last modified: November 30, 2016
    This is version 177 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. 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.