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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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei19 – 191SubstrateBy similarity
    Binding sitei23 – 231SubstrateBy similarity
    Active sitei117 – 1171Phosphoserine intermediate1 Publication
    Metal bindingi117 – 1171Magnesium; via phosphate groupBy similarity
    Binding sitei130 – 1301SubstrateBy similarity
    Metal bindingi288 – 2881Magnesium1 Publication
    Metal bindingi290 – 2901Magnesium1 Publication
    Metal bindingi292 – 2921Magnesium1 Publication
    Binding sitei357 – 3571SubstrateBy similarity
    Binding sitei389 – 3891SubstrateBy similarity
    Binding sitei515 – 5151SubstrateBy similarity

    GO - Molecular functioni

    • magnesium ion binding Source: InterPro
    • 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.
    ReactomeiR-HSA-3322077. Glycogen synthesis.
    R-HSA-5609974. Defective PGM1 causes PGM1-CDG (CDG1t).
    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 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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191T → A in CDG1T; reduces strongly phosphoglucomutase activity. 2 Publications
    VAR_071635
    Natural varianti38 – 381N → Y in CDG1T; reduces strongly solubility; increases aggregation. 2 Publications
    Corresponds to variant rs587777402 [ dbSNP | Ensembl ].
    VAR_071636
    Natural varianti41 – 411Q → R in CDG1T; reduces solubility; increases aggregation. 2 Publications
    VAR_071637
    Natural varianti62 – 621D → H in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity. 2 Publications
    Corresponds to variant rs587777403 [ dbSNP | Ensembl ].
    VAR_071638
    Natural varianti115 – 1151T → A in CDG1T; reduces mildly phosphoglucomutase activity. 3 Publications
    Corresponds to variant rs121918371 [ dbSNP | Ensembl ].
    VAR_062280
    Natural varianti121 – 1211G → R in CDG1T; there is 7% enzyme residual phosphoglucomutase activity. 3 Publications
    Corresponds to variant rs398122912 [ dbSNP | Ensembl ].
    VAR_069219
    Natural varianti263 – 2631D → G in CDG1T; reduces strongly phosphoglucomutase activity. 2 Publications
    VAR_071639
    Natural varianti263 – 2631D → Y in CDG1T; reduces strongly phosphoglucomutase activity. 2 Publications
    Corresponds to variant rs587777404 [ dbSNP | Ensembl ].
    VAR_071640
    Natural varianti291 – 2911G → R in CDG1T; reduces strongly phosphoglucomutase activity. 3 Publications
    Corresponds to variant rs772768778 [ dbSNP | Ensembl ].
    VAR_071641
    Natural varianti330 – 3301G → R in CDG1T; decreases mildly solubility. 2 Publications
    Corresponds to variant rs777164338 [ dbSNP | Ensembl ].
    VAR_071642
    Natural varianti377 – 3771E → K in CDG1T; decreases strongly solubility. 2 Publications
    VAR_071643
    Natural varianti388 – 3881E → K in CDG1T; decreases strongly solubility. 2 Publications
    VAR_071644
    Natural varianti516 – 5161L → P in CDG1T; decreases strongly solubility. 2 Publications
    Corresponds to variant rs587777401 [ dbSNP | Ensembl ].
    VAR_071645

    Keywords - Diseasei

    Congenital disorder of glycosylation, Disease mutation, Glycogen storage disease

    Organism-specific databases

    MalaCardsiPGM1.
    MIMi614921. phenotype.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 562562Phosphoglucomutase-1PRO_0000147776Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineCombined sources
    Modified residuei16 – 161N6-acetyllysineCombined sources
    Modified residuei115 – 1151PhosphothreonineBy similarity
    Modified residuei117 – 1171PhosphoserineCombined sources1 Publication
    Modified residuei134 – 1341PhosphoserineBy similarity
    Modified residuei185 – 1851PhosphothreonineCombined sources
    Modified residuei201 – 2011PhosphoserineCombined sources
    Modified residuei206 – 2061PhosphoserineCombined sources
    Modified residuei213 – 2131PhosphoserineBy similarity
    Modified residuei349 – 3491N6-acetyllysineBy similarity
    Modified residuei353 – 3531PhosphotyrosineBy similarity
    Modified residuei369 – 3691PhosphoserineBy similarity
    Modified residuei378 – 3781PhosphoserineCombined sources
    Modified residuei419 – 4191N6-succinyllysineBy similarity
    Modified residuei467 – 4671Phosphothreonine; by PAK11 Publication
    Modified residuei477 – 4771PhosphoserineBy similarity
    Modified residuei485 – 4851PhosphoserineBy similarity
    Modified residuei505 – 5051PhosphoserineCombined sources
    Modified residuei507 – 5071PhosphothreonineBy similarity
    Modified residuei509 – 5091PhosphoserineCombined sources
    Modified residuei541 – 5411PhosphoserineBy similarity
    Isoform 2 (identifier: P36871-2)
    Modified residuei1 – 11N-acetylmethionineCombined sources

    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.
    PhosphoSiteiP36871.
    SwissPalmiP36871.

    Expressioni

    Gene expression databases

    BgeeiP36871.
    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 interactions.
    DIPiDIP-60903N.
    IntActiP36871. 9 interactions.
    MINTiMINT-5001559.

    Structurei

    Secondary structure

    1
    562
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 84Combined sources
    Turni18 – 203Combined sources
    Beta strandi22 – 254Combined sources
    Helixi26 – 316Combined sources
    Beta strandi32 – 343Combined sources
    Helixi35 – 4410Combined sources
    Helixi49 – 513Combined sources
    Turni52 – 543Combined sources
    Beta strandi56 – 616Combined sources
    Helixi67 – 8014Combined sources
    Beta strandi85 – 939Combined sources
    Helixi96 – 10611Combined sources
    Beta strandi109 – 1146Combined sources
    Beta strandi125 – 1339Combined sources
    Beta strandi136 – 1383Combined sources
    Helixi141 – 15313Combined sources
    Beta strandi156 – 1594Combined sources
    Beta strandi171 – 1777Combined sources
    Beta strandi184 – 1896Combined sources
    Helixi193 – 20210Combined sources
    Helixi205 – 2128Combined sources
    Beta strandi220 – 2234Combined sources
    Beta strandi227 – 2293Combined sources
    Helixi230 – 2367Combined sources
    Turni237 – 2415Combined sources
    Helixi245 – 2473Combined sources
    Beta strandi248 – 2503Combined sources
    Helixi257 – 2593Combined sources
    Turni266 – 2694Combined sources
    Helixi270 – 2778Combined sources
    Beta strandi282 – 2876Combined sources
    Beta strandi291 – 2988Combined sources
    Helixi299 – 3013Combined sources
    Beta strandi302 – 3043Combined sources
    Helixi306 – 31510Combined sources
    Helixi316 – 3194Combined sources
    Helixi321 – 3266Combined sources
    Beta strandi331 – 3344Combined sources
    Helixi340 – 3489Combined sources
    Beta strandi352 – 3554Combined sources
    Helixi359 – 3679Combined sources
    Beta strandi372 – 3765Combined sources
    Turni377 – 3793Combined sources
    Beta strandi380 – 3834Combined sources
    Beta strandi386 – 3883Combined sources
    Helixi391 – 40515Combined sources
    Helixi409 – 42012Combined sources
    Beta strandi422 – 43312Combined sources
    Helixi435 – 45016Combined sources
    Beta strandi458 – 47316Combined sources
    Turni479 – 4813Combined sources
    Beta strandi490 – 4945Combined sources
    Beta strandi499 – 5046Combined sources
    Beta strandi512 – 52211Combined sources
    Helixi525 – 5284Combined sources
    Helixi532 – 54716Combined sources
    Helixi549 – 5535Combined sources
    Beta strandi559 – 5624Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    5EPCX-ray1.85A/B1-562[»]
    5F9CX-ray2.50A/B1-562[»]
    5HSHX-ray2.65A/B1-562[»]
    ProteinModelPortaliP36871.
    SMRiP36871. Positions 2-562.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni117 – 1182Substrate bindingBy similarity
    Regioni292 – 2932Substrate bindingBy similarity
    Regioni376 – 3783Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00390000011831.
    HOVERGENiHBG001599.
    InParanoidiP36871.
    KOiK01835.
    OMAiGIHYWAP.
    OrthoDBiEOG76472B.
    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 AAH90856.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti134 – 1341S → C in AAH67763 (PubMed:15489334).Curated

    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191T → A in CDG1T; reduces strongly phosphoglucomutase activity. 2 Publications
    VAR_071635
    Natural varianti38 – 381N → Y in CDG1T; reduces strongly solubility; increases aggregation. 2 Publications
    Corresponds to variant rs587777402 [ dbSNP | Ensembl ].
    VAR_071636
    Natural varianti41 – 411Q → R in CDG1T; reduces solubility; increases aggregation. 2 Publications
    VAR_071637
    Natural varianti62 – 621D → H in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity. 2 Publications
    Corresponds to variant rs587777403 [ dbSNP | Ensembl ].
    VAR_071638
    Natural varianti68 – 681K → M in allele PGM1*7+, allele PGM1*7-, allele PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is similar to wild-type. 2 Publications
    Corresponds to variant rs200390982 [ dbSNP | Ensembl ].
    VAR_006090
    Natural varianti88 – 881I → V.
    Corresponds to variant rs855314 [ dbSNP | Ensembl ].
    VAR_050496
    Natural varianti115 – 1151T → A in CDG1T; reduces mildly phosphoglucomutase activity. 3 Publications
    Corresponds to variant rs121918371 [ dbSNP | Ensembl ].
    VAR_062280
    Natural varianti121 – 1211G → R in CDG1T; there is 7% enzyme residual phosphoglucomutase activity. 3 Publications
    Corresponds to variant rs398122912 [ dbSNP | Ensembl ].
    VAR_069219
    Natural varianti221 – 2211R → C in allele PGM1*2+, allele PGM1*2-, allele PGM1*3+ and allele PGM1*3-; phosphoglucomutase activity is similar to wild-type. 5 Publications
    Corresponds to variant rs1126728 [ dbSNP | Ensembl ].
    VAR_006091
    Natural varianti263 – 2631D → G in CDG1T; reduces strongly phosphoglucomutase activity. 2 Publications
    VAR_071639
    Natural varianti263 – 2631D → Y in CDG1T; reduces strongly phosphoglucomutase activity. 2 Publications
    Corresponds to variant rs587777404 [ dbSNP | Ensembl ].
    VAR_071640
    Natural varianti291 – 2911G → R in CDG1T; reduces strongly phosphoglucomutase activity. 3 Publications
    Corresponds to variant rs772768778 [ dbSNP | Ensembl ].
    VAR_071641
    Natural varianti330 – 3301G → R in CDG1T; decreases mildly solubility. 2 Publications
    Corresponds to variant rs777164338 [ dbSNP | Ensembl ].
    VAR_071642
    Natural varianti377 – 3771E → K in CDG1T; decreases strongly solubility. 2 Publications
    VAR_071643
    Natural varianti388 – 3881E → K in CDG1T; decreases strongly solubility. 2 Publications
    VAR_071644
    Natural varianti420 – 4201Y → H in allele PGM1*1-, allele PGM1*2-, allele PGM1*3- and allele PGM1*7-; phosphoglucomutase activity is similar to wild-type. 6 Publications
    Corresponds to variant rs11208257 [ dbSNP | Ensembl ].
    VAR_006092
    Natural varianti501 – 5011V → I.
    Corresponds to variant rs6676290 [ dbSNP | Ensembl ].
    VAR_034380
    Natural varianti516 – 5161L → P in CDG1T; decreases strongly solubility. 2 Publications
    Corresponds to variant rs587777401 [ dbSNP | Ensembl ].
    VAR_071645

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 197197Missing in isoform 3. 1 PublicationVSP_045204Add
    BLAST
    Alternative sequencei1 – 7777MVKIV…LIARI → MSDFEEWISGTYRKMEEGPL PLLTFATAPYHDQKPGTSGL RKKTYYFEEKPCYLENFIQS IFFSIDLKDRQGSSLVVGGD GRYFNKSAIETIVQM in isoform 2. CuratedVSP_004686Add
    BLAST

    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    5EPCX-ray1.85A/B1-562[»]
    5F9CX-ray2.50A/B1-562[»]
    5HSHX-ray2.65A/B1-562[»]
    ProteinModelPortaliP36871.
    SMRiP36871. Positions 2-562.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

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

    PTM databases

    iPTMnetiP36871.
    PhosphoSiteiP36871.
    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.
    GeneCardsiPGM1.
    GeneReviewsiPGM1.
    HGNCiHGNC:8905. PGM1.
    HPAiCAB004666.
    HPA024190.
    HPA024637.
    HPA046329.
    MalaCardsiPGM1.
    MIMi171900. gene.
    614921. phenotype.
    neXtProtiNX_P36871.
    Orphaneti711. Glycogen storage disease due to phosphoglucomutase deficiency.
    319646. PGM-CDG.
    PharmGKBiPA33242.
    GenAtlasiSearch...

    Phylogenomic databases

    GeneTreeiENSGT00390000011831.
    HOVERGENiHBG001599.
    InParanoidiP36871.
    KOiK01835.
    OMAiGIHYWAP.
    OrthoDBiEOG76472B.
    PhylomeDBiP36871.
    TreeFamiTF300350.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01335-MONOMER.
    ReactomeiR-HSA-3322077. Glycogen synthesis.
    R-HSA-5609974. Defective PGM1 causes PGM1-CDG (CDG1t).
    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

    BgeeiP36871.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Phosphoglucomutase 1: complete human and rabbit mRNA sequences and direct mapping of this highly polymorphic marker on human chromosome 1."
      Whitehouse D.B., Putt W., Lovegrove J.U., Morrison K.E., Hollyoake M., Fox M.F., Hopkinson D.A., Edwards Y.H.
      Proc. Natl. Acad. Sci. U.S.A. 89:411-415(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Skeletal muscle.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS CYS-221 AND HIS-420.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT HIS-420.
      Tissue: Astrocyte and Mesangial cell.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS CYS-221 AND HIS-420.
      Tissue: Cervix, Hypothalamus, Placenta and Skin.
    6. "Phosphoglucomutase 1: a gene with two promoters and a duplicated first exon."
      Putt W., Ives J.H., Hollyoake M., Hopkinson D.A., Whitehouse D.B., Edwards Y.H.
      Biochem. J. 296:417-422(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82 (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING.
    7. "Regulation of phosphoglucomutase 1 phosphorylation and activity by a signaling kinase."
      Gururaj A., Barnes C.J., Vadlamudi R.K., Kumar R.
      Oncogene 23:8118-8127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-467, CATALYTIC ACTIVITY.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
      Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
      J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-185; SER-201; SER-206; SER-378; SER-505 AND SER-509, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    19. "Induced structural disorder as a molecular mechanism for enzyme dysfunction in phosphoglucomutase 1 deficiency."
      Stiers K.M., Kain B.N., Graham A.C., Beamer L.J.
      J. Mol. Biol. 428:1493-1505(2016) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF WILD-TYPE; VARIANT CDG1T ARG-121 AND VARIANT ARG-291 IN COMPLEX WITH MAGNESIUM, COFACTOR.
    20. "Intragenic recombination at the human phosphoglucomutase 1 locus: predictions fulfilled."
      Takahashi N., Neels J.V.
      Proc. Natl. Acad. Sci. U.S.A. 90:10725-10729(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MET-68; CYS-221 AND HIS-420.
    21. "The classical human phosphoglucomutase (PGM1) isozyme polymorphism is generated by intragenic recombination."
      March R.E., Putt W., Hollyoake M., Ives J.H., Lovegrove J.U., Hopkinson D.A., Edwards Y.H., Whitehouse D.B.
      Proc. Natl. Acad. Sci. U.S.A. 90:10730-10733(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CYS-221 AND HIS-420.
    22. Cited for: INVOLVEMENT IN CDG1T, VARIANT CDG1T ALA-115.
    23. Cited for: VARIANT CDG1T ARG-121.
    24. "A novel congenital disorder of glycosylation type without central nervous system involvement caused by mutations in the phosphoglucomutase 1 gene."
      Perez B., Medrano C., Ecay M.J., Ruiz-Sala P., Martinez-Pardo M., Ugarte M., Perez-Cerda C.
      J. Inherit. Metab. Dis. 36:535-542(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CDG1T ARG-291.
    25. Cited for: VARIANTS CDG1T ALA-19; TYR-38; ARG-41; HIS-62; ALA-115; ARG-121; TYR-263; GLY-263; ARG-291; ARG-330; LYS-377; LYS-388 AND PRO-516.
    26. "Compromised catalysis and potential folding defects in in vitro studies of missense mutants associated with hereditary phosphoglucomutase 1 deficiency."
      Lee Y., Stiers K.M., Kain B.N., Beamer L.J.
      J. Biol. Chem. 289:32010-32019(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS CDG1T ALA-19; TYR-38; ARG-41; HIS-62; ALA-115; ARG-121; GLY-263; TYR-263; ARG-291; ARG-330; LYS-377; LYS-388 AND PRO-516, VARIANTS MET-68; CYS-221 AND HIS-420, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, PHOSPHORYLATION AT SER-117, ENZYME REGULATION.

    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: July 6, 2016
    This is version 173 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.