PGM1

Functionⁱ

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

Catalytic activityⁱ

α-D-glucose 1-phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
α-D-glucose 6-phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.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, ACTIVITY REGULATION.
EC:
5.4.2.2
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.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.
- Ref.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, ACTIVITY REGULATION.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
α-D-glucose 1-phosphate
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=
α-D-glucose 6-phosphate
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Cofactorⁱ

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

Activity regulationⁱ

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

Kineticsⁱ

K_M=
80 µM for alpha-D-glucose 1-phosphate
1 Publication
Manual assertion based on experiment inⁱ
Ref.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, ACTIVITY REGULATION.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	19	SubstrateBy similarity	1
Binding siteⁱ	23	SubstrateBy similarity	1
Active siteⁱ	117	Phosphoserine intermediate1 Publication	1
Metal bindingⁱ	117	Magnesium; via phosphate groupBy similarity	1
Binding siteⁱ	130	SubstrateBy similarity	1
Metal bindingⁱ	288	Magnesium1 Publication	1
Metal bindingⁱ	290	Magnesium1 Publication	1
Metal bindingⁱ	292	Magnesium1 Publication	1
Binding siteⁱ	357	SubstrateBy similarity	1
Binding siteⁱ	389	SubstrateBy similarity	1
Binding siteⁱ	515	SubstrateBy similarity	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Isomerase
Biological process	Carbohydrate metabolism, Glucose metabolism
Ligand	Magnesium, Metal-binding

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS01335-MONOMER
BRENDAⁱ	5.4.2.2, 2681
PathwayCommonsⁱ	P36871
Reactomeⁱ	R-HSA-3322077, Glycogen synthesis R-HSA-5609974, Defective PGM1 causes PGM1-CDG (CDG1t) R-HSA-6798695, Neutrophil degranulation
SABIO-RKⁱ	P36871
SIGNORⁱ	P36871

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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:8905, PGM1
MIMⁱ	171900, gene
neXtProtⁱ	NX_P36871
VEuPathDBⁱ	HostDB:ENSG00000079739

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Congenital disorder of glycosylation 1T (CDG1T)6 Publications

The disease is caused by variants 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.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_071635	19	T → A in CDG1T; reduces strongly phosphoglucomutase activity. 2 PublicationsCorresponds to variant dbSNP:rs1320810473Ensembl.	1
Natural variantⁱVAR_071636	38	N → Y in CDG1T; reduces strongly solubility; increases aggregation. 2 PublicationsCorresponds to variant dbSNP:rs587777402EnsemblClinVar.	1
Natural variantⁱVAR_071637	41	Q → R in CDG1T; reduces solubility; increases aggregation. 2 PublicationsCorresponds to variant dbSNP:rs1300651770EnsemblClinVar.	1
Natural variantⁱVAR_071638	62	D → H in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity. 2 PublicationsCorresponds to variant dbSNP:rs587777403EnsemblClinVar.	1
Natural variantⁱVAR_062280	115	T → A in CDG1T; reduces mildly phosphoglucomutase activity. 3 PublicationsCorresponds to variant dbSNP:rs121918371EnsemblClinVar.	1
Natural variantⁱVAR_069219	121	G → R in CDG1T; there is 7% enzyme residual phosphoglucomutase activity. 3 PublicationsCorresponds to variant dbSNP:rs398122912EnsemblClinVar.	1
Natural variantⁱVAR_071639	263	D → G in CDG1T; reduces strongly phosphoglucomutase activity. 2 PublicationsCorresponds to variant dbSNP:rs1465877146Ensembl.	1
Natural variantⁱVAR_071640	263	D → Y in CDG1T; reduces strongly phosphoglucomutase activity. 2 PublicationsCorresponds to variant dbSNP:rs587777404EnsemblClinVar.	1
Natural variantⁱVAR_071641	291	G → R in CDG1T; reduces strongly phosphoglucomutase activity. 3 PublicationsCorresponds to variant dbSNP:rs772768778Ensembl.	1
Natural variantⁱVAR_071642	330	G → R in CDG1T; decreases mildly solubility. 2 PublicationsCorresponds to variant dbSNP:rs777164338Ensembl.	1
Natural variantⁱVAR_071643	377	E → K in CDG1T; decreases strongly solubility. 2 Publications	1
Natural variantⁱVAR_071644	388	E → K in CDG1T; decreases strongly solubility. 2 PublicationsCorresponds to variant dbSNP:rs1301021797Ensembl.	1
Natural variantⁱVAR_071645	516	L → P in CDG1T; decreases strongly solubility. 2 PublicationsCorresponds to variant dbSNP:rs587777401EnsemblClinVar.	1

Keywords - Diseaseⁱ

Congenital disorder of glycosylation, Disease variant, Glycogen storage disease

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5236
GeneReviewsⁱ	PGM1
MalaCards human disease database More...MalaCardsⁱ	PGM1
MIMⁱ	614921, phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000079739
Orphanetⁱ	319646, PGM1-CDG
PharmGKBⁱ	PA33242

Miscellaneous databases

Pharosⁱ	P36871, Tbio

Pharosⁱ

P36871, Tbio

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB02835, Alpha-D-Glucose 1,6-Bisphosphate DB04397, Alpha-D-Glucose-1-Phosphate-6-Vanadate DB06773, Human calcitonin

DrugBankⁱ

DB02835, Alpha-D-Glucose 1,6-Bisphosphate
DB04397, Alpha-D-Glucose-1-Phosphate-6-Vanadate
DB06773, Human calcitonin

Genetic variation databases

BioMutaⁱ	PGM1
DMDMⁱ	585670

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000147776	1 – 562	Phosphoglucomutase-1Add BLAST		562

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	1	N-acetylmethionineCombined sources	1
Modified residueⁱ	16	N6-acetyllysineCombined sources	1
Modified residueⁱ	115	PhosphothreonineBy similarity	1
Modified residueⁱ	117	PhosphoserineCombined sources1 Publication	1
Modified residueⁱ	134	PhosphoserineBy similarity	1
Modified residueⁱ	185	PhosphothreonineCombined sources	1
Modified residueⁱ	201	PhosphoserineCombined sources	1
Modified residueⁱ	206	PhosphoserineCombined sources	1
Modified residueⁱ	213	PhosphoserineBy similarity	1
Modified residueⁱ	349	N6-acetyllysineBy similarity	1
Modified residueⁱ	353	PhosphotyrosineBy similarity	1
Modified residueⁱ	369	PhosphoserineBy similarity	1
Modified residueⁱ	378	PhosphoserineCombined sources	1
Modified residueⁱ	419	N6-succinyllysineBy similarity	1
Modified residueⁱ	467	Phosphothreonine; by PAK11 Publication	1
Modified residueⁱ	477	PhosphoserineBy similarity	1
Modified residueⁱ	485	PhosphoserineBy similarity	1
Modified residueⁱ	505	PhosphoserineCombined sources	1
Modified residueⁱ	507	PhosphothreonineBy similarity	1
Modified residueⁱ	509	PhosphoserineCombined sources	1
Modified residueⁱ	541	PhosphoserineBy similarity	1
Isoform 2 (identifier: P36871-2)
Modified residueⁱ	1	N-acetylmethionineCombined sources	1

Post-translational modificationⁱ

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

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal More...CPTACⁱ	CPTAC-255 CPTAC-256 CPTAC-988
EPDⁱ	P36871
jPOSTⁱ	P36871
MassIVEⁱ	P36871
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P36871
PeptideAtlas More...PeptideAtlasⁱ	P36871
PRIDEⁱ	P36871
ProteomicsDBⁱ	4816 55222 [P36871-1] 55223 [P36871-2]
TopDownProteomicsⁱ	P36871-1 [P36871-1]

2D gel databases

REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	P36871

REPRODUCTION-2DPAGEⁱ

P36871

PTM databases

GlyGenⁱ	P36871, 1 site, 1 O-linked glycan (1 site)
iPTMnetⁱ	P36871
MetOSiteⁱ	P36871
PhosphoSitePlusⁱ	P36871
SwissPalmⁱ	P36871

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000079739, Expressed in skeletal muscle tissue and 246 other tissues
ExpressionAtlasⁱ	P36871, baseline and differential
Genevisibleⁱ	P36871, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000079739, Tissue enriched (skeletal)

HPAⁱ

ENSG00000079739, Tissue enriched (skeletal)

Interactionⁱ

Subunit structureⁱ

Monomer.

Binary interactionsⁱ

P36871

With	#Exp.	IntAct
TINF2 [Q9BSI4]	2	EBI-2861475,EBI-717399

Protein-protein interaction databases

BioGRIDⁱ	111256, 79 interactors
Database of interacting proteins More...DIPⁱ	DIP-60903N
IntActⁱ	P36871, 34 interactors
STRINGⁱ	9606.ENSP00000360124

Miscellaneous databases

RNActⁱ	P36871, protein

RNActⁱ

P36871, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	5 – 8	Combined sources	4
Turnⁱ	18 – 20	Combined sources	3
Beta strandⁱ	22 – 25	Combined sources	4
Helixⁱ	26 – 31	Combined sources	6
Beta strandⁱ	32 – 34	Combined sources	3
Helixⁱ	35 – 44	Combined sources	10
Helixⁱ	49 – 51	Combined sources	3
Turnⁱ	52 – 54	Combined sources	3
Beta strandⁱ	56 – 61	Combined sources	6
Helixⁱ	67 – 80	Combined sources	14
Beta strandⁱ	85 – 93	Combined sources	9
Helixⁱ	96 – 106	Combined sources	11
Beta strandⁱ	109 – 114	Combined sources	6
Beta strandⁱ	125 – 133	Combined sources	9
Beta strandⁱ	136 – 138	Combined sources	3
Helixⁱ	141 – 153	Combined sources	13
Beta strandⁱ	156 – 159	Combined sources	4
Beta strandⁱ	167 – 169	Combined sources	3
Beta strandⁱ	171 – 177	Combined sources	7
Beta strandⁱ	184 – 189	Combined sources	6
Helixⁱ	193 – 202	Combined sources	10
Helixⁱ	205 – 212	Combined sources	8
Beta strandⁱ	220 – 223	Combined sources	4
Beta strandⁱ	227 – 229	Combined sources	3
Helixⁱ	230 – 236	Combined sources	7
Turnⁱ	237 – 241	Combined sources	5
Helixⁱ	245 – 247	Combined sources	3
Beta strandⁱ	248 – 250	Combined sources	3
Helixⁱ	257 – 259	Combined sources	3
Turnⁱ	266 – 269	Combined sources	4
Helixⁱ	270 – 277	Combined sources	8
Beta strandⁱ	282 – 287	Combined sources	6
Beta strandⁱ	291 – 298	Combined sources	8
Helixⁱ	299 – 301	Combined sources	3
Beta strandⁱ	302 – 304	Combined sources	3
Helixⁱ	306 – 315	Combined sources	10
Helixⁱ	316 – 319	Combined sources	4
Helixⁱ	321 – 326	Combined sources	6
Beta strandⁱ	331 – 334	Combined sources	4
Helixⁱ	340 – 348	Combined sources	9
Beta strandⁱ	352 – 355	Combined sources	4
Helixⁱ	359 – 367	Combined sources	9
Beta strandⁱ	372 – 376	Combined sources	5
Turnⁱ	377 – 379	Combined sources	3
Beta strandⁱ	380 – 383	Combined sources	4
Beta strandⁱ	386 – 388	Combined sources	3
Helixⁱ	391 – 405	Combined sources	15
Helixⁱ	409 – 420	Combined sources	12
Beta strandⁱ	422 – 433	Combined sources	12
Helixⁱ	435 – 450	Combined sources	16
Turnⁱ	452 – 456	Combined sources	5
Beta strandⁱ	458 – 460	Combined sources	3
Beta strandⁱ	465 – 473	Combined sources	9
Turnⁱ	479 – 481	Combined sources	3
Beta strandⁱ	490 – 494	Combined sources	5
Beta strandⁱ	499 – 504	Combined sources	6
Turnⁱ	506 – 509	Combined sources	4
Beta strandⁱ	512 – 522	Combined sources	11
Turnⁱ	525 – 529	Combined sources	5
Helixⁱ	532 – 547	Combined sources	16
Helixⁱ	549 – 553	Combined sources	5
Beta strandⁱ	559 – 562	Combined sources	4

Show more details

3D structure databases

SMRⁱ	P36871
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	117 – 118	Substrate bindingBy similarity	2
Regionⁱ	292 – 293	Substrate bindingBy similarity	2
Regionⁱ	376 – 378	Substrate bindingBy similarity	3

Sequence similaritiesⁱ

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGⁱ	KOG0625, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000155542
HOGENOMⁱ	CLU_009330_0_1_1
InParanoidⁱ	P36871
OMAⁱ	DTRFMSE
Database of Orthologous Groups More...OrthoDBⁱ	446752at2759
PhylomeDBⁱ	P36871
TreeFamⁱ	TF300350

Family and domain databases

InterProⁱ	View protein in InterPro IPR005844, A-D-PHexomutase_a/b/a-I IPR016055, A-D-PHexomutase_a/b/a-I/II/III IPR005845, A-D-PHexomutase_a/b/a-II IPR005846, A-D-PHexomutase_a/b/a-III IPR005843, A-D-PHexomutase_C IPR036900, A-D-PHexomutase_C_sf IPR016066, A-D-PHexomutase_CS IPR005841, Alpha-D-phosphohexomutase_SF
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02878, PGM_PMM_I, 1 hit PF02879, PGM_PMM_II, 1 hit PF02880, PGM_PMM_III, 1 hit PF00408, PGM_PMM_IV, 1 hit
PRINTSⁱ	PR00509, PGMPMM
SUPFAMⁱ	SSF53738, SSF53738, 3 hits SSF55957, SSF55957, 1 hit
PROSITEⁱ	View protein in PROSITE PS00710, PGM_PMM, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

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

This entry has 3 described isoforms and 1 potential isoform that is computationally mapped.Show all Align All

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

This isoform has been chosen as the canonicalⁱ 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]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MSDFEEWISG TYRKMEEGPL PLLTFATAPY HDQKPGTSGL RKKTYYFEEK 
        60         70         80         90        100
PCYLENFIQS IFFSIDLKDR QGSSLVVGGD GRYFNKSAIE TIVQMAAANG 
       110        120        130        140        150
IGRLVIGQNG ILSTPAVSCI IRKIKAIGGI ILTASHNPGG PNGDFGIKFN 
       160        170        180        190        200
ISNGGPAPEA ITDKIFQISK TIEEYAVCPD LKVDLGVLGK QQFDLENKFK 
       210        220        230        240        250
PFTVEIVDSV EAYATMLRSI FDFSALKELL SGPNRLKIRI DAMHGVVGPY 
       260        270        280        290        300
VKKILCEELG APANSAVNCV PLEDFGGHHP DPNLTYAADL VETMKSGEHD 
       310        320        330        340        350
FGAAFDGDGD RNMILGKHGF FVNPSDSVAV IAANIFSIPY FQQTGVRGFA 
       360        370        380        390        400
RSMPTSGALD RVASATKIAL YETPTGWKFF GNLMDASKLS LCGEESFGTG 
       410        420        430        440        450
SDHIREKDGL WAVLAWLSIL ATRKQSVEDI LKDHWQKYGR NFFTRYDYEE 
       460        470        480        490        500
VEAEGANKMM KDLEALMFDR SFVGKQFSAN DKVYTVEKAD NFEYSDPVDG 
       510        520        530        540        550
SISRNQGLRL IFTDGSRIVF RLSGTGSAGA TIRLYIDSYE KDVAKINQDP 
       560        570        580
QVMLAPLISI ALKVSQLQER TGRTAPTVIT

Show »

Length:580

Mass (Da):63,791

Checksum:ⁱCE4F9CA4094B5139

GO

Isoform 3 (identifier: P36871-3) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MLRSIFDFSA LKELLSGPNR LKIRIDAMHG VVGPYVKKIL CEELGAPANS 
        60         70         80         90        100
AVNCVPLEDF GGHHPDPNLT YAADLVETMK SGEHDFGAAF DGDGDRNMIL 
       110        120        130        140        150
GKHGFFVNPS DSVAVIAANI FSIPYFQQTG VRGFARSMPT SGALDRVASA 
       160        170        180        190        200
TKIALYETPT GWKFFGNLMD ASKLSLCGEE SFGTGSDHIR EKDGLWAVLA 
       210        220        230        240        250
WLSILATRKQ SVEDILKDHW QKYGRNFFTR YDYEEVEAEG ANKMMKDLEA 
       260        270        280        290        300
LMFDRSFVGK QFSANDKVYT VEKADNFEYS DPVDGSISRN QGLRLIFTDG 
       310        320        330        340        350
SRIVFRLSGT GSAGATIRLY IDSYEKDVAK INQDPQVMLA PLISIALKVS 
       360 
QLQERTGRTA PTVIT

Show »

Length:365

Mass (Da):40,283

Checksum:ⁱE0696E6FD7170D62

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	A0A3B3ITK7	A0A3B3ITK7_HUMAN		Phosphoglucomutase-1 Phosphoglucomutase-1	PGM1	584	Annotation score:

Sequence cautionⁱ

The sequence AAH90856 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	134	S → C in AAH67763 (PubMed:15489334).Curated		1

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 key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_071635	19	T → A in CDG1T; reduces strongly phosphoglucomutase activity. 2 PublicationsCorresponds to variant dbSNP:rs1320810473Ensembl.	1
Natural variantⁱVAR_071636	38	N → Y in CDG1T; reduces strongly solubility; increases aggregation. 2 PublicationsCorresponds to variant dbSNP:rs587777402EnsemblClinVar.	1
Natural variantⁱVAR_071637	41	Q → R in CDG1T; reduces solubility; increases aggregation. 2 PublicationsCorresponds to variant dbSNP:rs1300651770EnsemblClinVar.	1
Natural variantⁱVAR_071638	62	D → H in CDG1T; reduces solubility; reduces strongly phosphoglucomutase activity. 2 PublicationsCorresponds to variant dbSNP:rs587777403EnsemblClinVar.	1
Natural variantⁱVAR_006090	68	K → M in allele PGM17+, allele PGM17-, allele PGM13+ and allele PGM13-; phosphoglucomutase activity is similar to wild-type. 2 PublicationsCorresponds to variant dbSNP:rs200390982Ensembl.	1
Natural variantⁱVAR_050496	88	I → V. Corresponds to variant dbSNP:rs855314EnsemblClinVar.	1
Natural variantⁱVAR_062280	115	T → A in CDG1T; reduces mildly phosphoglucomutase activity. 3 PublicationsCorresponds to variant dbSNP:rs121918371EnsemblClinVar.	1
Natural variantⁱVAR_069219	121	G → R in CDG1T; there is 7% enzyme residual phosphoglucomutase activity. 3 PublicationsCorresponds to variant dbSNP:rs398122912EnsemblClinVar.	1
Natural variantⁱVAR_006091	221	R → C in allele PGM12+, allele PGM12-, allele PGM13+ and allele PGM13-; phosphoglucomutase activity is similar to wild-type. 5 PublicationsCorresponds to variant dbSNP:rs1126728EnsemblClinVar.	1
Natural variantⁱVAR_071639	263	D → G in CDG1T; reduces strongly phosphoglucomutase activity. 2 PublicationsCorresponds to variant dbSNP:rs1465877146Ensembl.	1
Natural variantⁱVAR_071640	263	D → Y in CDG1T; reduces strongly phosphoglucomutase activity. 2 PublicationsCorresponds to variant dbSNP:rs587777404EnsemblClinVar.	1
Natural variantⁱVAR_071641	291	G → R in CDG1T; reduces strongly phosphoglucomutase activity. 3 PublicationsCorresponds to variant dbSNP:rs772768778Ensembl.	1
Natural variantⁱVAR_071642	330	G → R in CDG1T; decreases mildly solubility. 2 PublicationsCorresponds to variant dbSNP:rs777164338Ensembl.	1
Natural variantⁱVAR_071643	377	E → K in CDG1T; decreases strongly solubility. 2 Publications	1
Natural variantⁱVAR_071644	388	E → K in CDG1T; decreases strongly solubility. 2 PublicationsCorresponds to variant dbSNP:rs1301021797Ensembl.	1
Natural variantⁱVAR_006092	420	Y → H in allele PGM11-, allele PGM12-, allele PGM13- and allele PGM17-; phosphoglucomutase activity is similar to wild-type. 6 PublicationsCorresponds to variant dbSNP:rs11208257EnsemblClinVar.	1
Natural variantⁱVAR_034380	501	V → I. Corresponds to variant dbSNP:rs6676290EnsemblClinVar.	1
Natural variantⁱVAR_071645	516	L → P in CDG1T; decreases strongly solubility. 2 PublicationsCorresponds to variant dbSNP:rs587777401EnsemblClinVar.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_045204	1 – 197	Missing in isoform 3. 1 PublicationAdd BLAST		197
Alternative sequenceⁱVSP_004686	1 – 77	MVKIV…LIARI → MSDFEEWISGTYRKMEEGPL PLLTFATAPYHDQKPGTSGL RKKTYYFEEKPCYLENFIQS IFFSIDLKDRQGSSLVVGGD GRYFNKSAIETIVQM in isoform 2. CuratedAdd BLAST		77

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 No translation available. 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS53323.1 [P36871-2] CCDS53324.1 [P36871-3] CCDS625.1 [P36871-1]
PIRⁱ	A41801 S39397
NCBI Reference Sequences More...RefSeqⁱ	NP_001166289.1, NM_001172818.1 [P36871-2] NP_001166290.1, NM_001172819.1 [P36871-3] NP_002624.2, NM_002633.2 [P36871-1]

Genome annotation databases

Ensemblⁱ	ENST00000371083; ENSP00000360124; ENSG00000079739 [P36871-2] ENST00000371084; ENSP00000360125; ENSG00000079739 [P36871-1] ENST00000540265; ENSP00000443449; ENSG00000079739 [P36871-3]
GeneIDⁱ	5236
KEGGⁱ	hsa:5236
UCSC genome browser More...UCSCⁱ	uc001dbh.5, human [P36871-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P36871	Isoform 3 of Phosphoglucomutase-1		HUMAN		365	UniRef90_P36871
Phosphoglucomutase 1		URSMA		563
Phosphoglucomutase 1		AILME		562
phosphoglucomutase-1 isoform X2		Ursus arctos horribilis		562
Phosphoglucomutase-1-like protein		MICFL		562
+19

Protein	Similar proteins		Species	Score	Length	Source
P36871	Phosphoglucomutase-1		MOUSE		562	UniRef50_P36871
Isoform 3 of Phosphoglucomutase-1		HUMAN		365
Phosphoglucomutase 1		URSMA		563
Phosphoglucomutase 1		AILME		562
phosphoglucomutase-1 isoform X2		Ursus arctos horribilis		562
+446

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 No translation available. 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
CCDSⁱ	CCDS53323.1 [P36871-2] CCDS53324.1 [P36871-3] CCDS625.1 [P36871-1]
PIRⁱ	A41801 S39397
RefSeqⁱ	NP_001166289.1, NM_001172818.1 [P36871-2] NP_001166290.1, NM_001172819.1 [P36871-3] NP_002624.2, NM_002633.2 [P36871-1]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	5EPC	X-ray	1.85	A/B	1-562	[»]
	5F9C	X-ray	2.50	A/B	1-562	[»]
	5HSH	X-ray	2.65	A/B	1-562	[»]
	5JN5	X-ray	1.75	A/B	1-562	[»]
	5TR2	X-ray	2.50	A/B	1-562	[»]
	5VBI	X-ray	1.75	A/B	1-562	[»]
	5VEC	X-ray	2.20	A/B	1-562	[»]
	5VG7	X-ray	1.95	A/B	1-562	[»]
	5VIN	X-ray	2.60	A/B	1-562	[»]
	6SNO	X-ray	2.70	A	2-562	[»]
	6SNP	X-ray	2.75	A	2-562	[»]
	6SNQ	X-ray	2.70	A	2-562	[»]
	6UIQ	X-ray	2.30	A/B	1-562	[»]
	6UO6	X-ray	2.15	A/B	1-562	[»]
SMRⁱ	P36871
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	111256, 79 interactors
DIPⁱ	DIP-60903N
IntActⁱ	P36871, 34 interactors
STRINGⁱ	9606.ENSP00000360124

Chemistry databases

DrugBankⁱ	DB02835, Alpha-D-Glucose 1,6-Bisphosphate DB04397, Alpha-D-Glucose-1-Phosphate-6-Vanadate DB06773, Human calcitonin

DrugBankⁱ

DB02835, Alpha-D-Glucose 1,6-Bisphosphate
DB04397, Alpha-D-Glucose-1-Phosphate-6-Vanadate
DB06773, Human calcitonin

PTM databases

GlyGenⁱ	P36871, 1 site, 1 O-linked glycan (1 site)
iPTMnetⁱ	P36871
MetOSiteⁱ	P36871
PhosphoSitePlusⁱ	P36871
SwissPalmⁱ	P36871

Genetic variation databases

BioMutaⁱ	PGM1
DMDMⁱ	585670

2D gel databases

REPRODUCTION-2DPAGEⁱ	P36871

REPRODUCTION-2DPAGEⁱ

P36871

Proteomic databases

CPTACⁱ	CPTAC-255 CPTAC-256 CPTAC-988
EPDⁱ	P36871
jPOSTⁱ	P36871
MassIVEⁱ	P36871
MaxQBⁱ	P36871
PeptideAtlasⁱ	P36871
PRIDEⁱ	P36871
ProteomicsDBⁱ	4816 55222 [P36871-1] 55223 [P36871-2]
TopDownProteomicsⁱ	P36871-1 [P36871-1]

Protocols and materials databases

Antibodypediaⁱ	3314, 237 antibodies
The DNASU plasmid repository More...DNASUⁱ	5236

Genome annotation databases

Ensemblⁱ	ENST00000371083; ENSP00000360124; ENSG00000079739 [P36871-2] ENST00000371084; ENSP00000360125; ENSG00000079739 [P36871-1] ENST00000540265; ENSP00000443449; ENSG00000079739 [P36871-3]
GeneIDⁱ	5236
KEGGⁱ	hsa:5236
UCSCⁱ	uc001dbh.5, human [P36871-1]

Organism-specific databases

CTDⁱ	5236
DisGeNETⁱ	5236
GeneCardsⁱ	PGM1
GeneReviewsⁱ	PGM1
HGNCⁱ	HGNC:8905, PGM1
HPAⁱ	ENSG00000079739, Tissue enriched (skeletal)
MalaCardsⁱ	PGM1
MIMⁱ	171900, gene 614921, phenotype
neXtProtⁱ	NX_P36871
OpenTargetsⁱ	ENSG00000079739
Orphanetⁱ	319646, PGM1-CDG
PharmGKBⁱ	PA33242
VEuPathDBⁱ	HostDB:ENSG00000079739
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0625, Eukaryota
GeneTreeⁱ	ENSGT00940000155542
HOGENOMⁱ	CLU_009330_0_1_1
InParanoidⁱ	P36871
OMAⁱ	DTRFMSE
OrthoDBⁱ	446752at2759
PhylomeDBⁱ	P36871
TreeFamⁱ	TF300350

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS01335-MONOMER
BRENDAⁱ	5.4.2.2, 2681
PathwayCommonsⁱ	P36871
Reactomeⁱ	R-HSA-3322077, Glycogen synthesis R-HSA-5609974, Defective PGM1 causes PGM1-CDG (CDG1t) R-HSA-6798695, Neutrophil degranulation
SABIO-RKⁱ	P36871
SIGNORⁱ	P36871

Miscellaneous databases

BioGRID-ORCSⁱ	5236, 5 hits in 1011 CRISPR screens
ChiTaRSⁱ	PGM1, human
GeneWikiⁱ	PGM1
GenomeRNAiⁱ	5236
Pharosⁱ	P36871, Tbio
Protein Ontology More...PROⁱ	PR:P36871
RNActⁱ	P36871, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000079739, Expressed in skeletal muscle tissue and 246 other tissues
ExpressionAtlasⁱ	P36871, baseline and differential
Genevisibleⁱ	P36871, HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR005844, A-D-PHexomutase_a/b/a-I IPR016055, A-D-PHexomutase_a/b/a-I/II/III IPR005845, A-D-PHexomutase_a/b/a-II IPR005846, A-D-PHexomutase_a/b/a-III IPR005843, A-D-PHexomutase_C IPR036900, A-D-PHexomutase_C_sf IPR016066, A-D-PHexomutase_CS IPR005841, Alpha-D-phosphohexomutase_SF
Pfamⁱ	View protein in Pfam PF02878, PGM_PMM_I, 1 hit PF02879, PGM_PMM_II, 1 hit PF02880, PGM_PMM_III, 1 hit PF00408, PGM_PMM_IV, 1 hit
PRINTSⁱ	PR00509, PGMPMM
SUPFAMⁱ	SSF53738, SSF53738, 3 hits SSF55957, SSF55957, 1 hit
PROSITEⁱ	View protein in PROSITE PS00710, PGM_PMM, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PGM1_HUMAN
Accessionⁱ	P36871Primary (citable) accession number: P36871 Secondary accession number(s): B2R5N9 Q9NTY4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
	Last sequence update:	January 23, 2007
	Last modified:	September 29, 2021
	This is version 211 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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, Reference proteome

Documents

Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM
Human entries with genetic variants
List of human entries with genetic variants
Human variants curated from literature reports
Index of human variants curated from literature reports
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

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UniProtKB - P36871 (PGM1_HUMAN)

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Phosphoglucomutase-1

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

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

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

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GO - Biological processi

Enzyme and pathway databases

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

Organism-specific databases

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

Cytoplasm and Cytosol

Cytosol

Extracellular region or secreted

Other locations

Keywords - Cellular componenti

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

Keywords - Diseasei

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

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

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

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

Gene expression databases

Organism-specific databases

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

P36871

Protein-protein interaction databases

Miscellaneous databases

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

Secondary structure

3D structure databases

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

Region

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

Phylogenomic databases

Family and domain databases

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

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

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Genetic variation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

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Gene expression databases

Family and domain databases

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

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ