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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.

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei19 – 191SubstrateBy similarity
Binding sitei23 – 231SubstrateBy similarity
Active sitei117 – 1171Phosphoserine intermediateBy similarity
Metal bindingi117 – 1171Magnesium; via phosphate groupBy similarity
Binding sitei130 – 1301SubstrateBy similarity
Metal bindingi288 – 2881MagnesiumBy similarity
Metal bindingi290 – 2901MagnesiumBy similarity
Metal bindingi292 – 2921MagnesiumBy similarity
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:5.4.2.2)
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
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
VAR_071638
Natural varianti115 – 1151T → A in CDG1T; reduces mildly phosphoglucomutase activity. 3 Publications
VAR_062280
Natural varianti121 – 1211G → R in CDG1T; there is 7% enzyme residual phosphoglucomutase activity. 3 Publications
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
VAR_071640
Natural varianti291 – 2911G → R in CDG1T; reduces strongly phosphoglucomutase activity. 3 Publications
VAR_071641
Natural varianti330 – 3301G → R in CDG1T; decreases mildly solubility. 2 Publications
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
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 sources
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.
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

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
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
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
VAR_062280
Natural varianti121 – 1211G → R in CDG1T; there is 7% enzyme residual phosphoglucomutase activity. 3 Publications
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
VAR_071640
Natural varianti291 – 2911G → R in CDG1T; reduces strongly phosphoglucomutase activity. 3 Publications
VAR_071641
Natural varianti330 – 3301G → R in CDG1T; decreases mildly solubility. 2 Publications
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
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.
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.
  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. "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.
  18. "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.
  19. "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.
  20. Cited for: INVOLVEMENT IN CDG1T, VARIANT CDG1T ALA-115.
  21. Cited for: VARIANT CDG1T ARG-121.
  22. "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.
  23. 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.
  24. "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.

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: June 8, 2016
This is version 172 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.