P36871 (PGM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoglucomutase-1
Short name=PGM 1
EC=5.4.2.2

Alternative name(s):
Glucose phosphomutase 1

Gene names

Name:

PGM1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	562 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This enzyme participates in both the breakdown and synthesis of glucose.
Catalytic activity	Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit.
Subunit structure	Monomer.
Subcellular location	Isoform 1: Cytoplasm.
Polymorphism	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.
Involvement in disease	Defects in PGM1 are the cause of glycogen storage disease type 14 (GSD14) [MIM:612934]. A metabolic disorder resulting in a myopathy characterized by exercise-induced intolerance with episodes of rhabdomyolysis, normal elevation of lactate, and hyperammonemia on a forearm-exercise test. Ref.16
Sequence similarities	Belongs to the phosphohexose mutase family.
Sequence caution	The sequence AAH90856.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Glycogen storage disease
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	galactose catabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome glucose 1-phosphate metabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome glycogen biosynthetic process Inferred from Biological aspect of Ancestor. Source: RefGenome glycogen catabolic process Traceable author statement. Source: Reactome
Cellular component	actin cytoskeleton Inferred from direct assay. Source: HPA cytosol Traceable author statement. Source: Reactome
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphoglucomutase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P36871-1)

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.

Isoform 2 (identifier: P36871-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MVKIVTVKTQAYQ → MSDFEEWISGTYRKMEEGPLPLLTFATAPYH
     25-36: RVKVFQSSANYA → KTYYFEEKPCYL
     44-56: ISTVEPAQRQEAT → FFSIDLKDRQGSS
     65-77: FYMKEAIQLIARI → YFNKSAIETIVQM

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 562	561	Phosphoglucomutase-1		PRO_0000147776
Sites
	Active site	117	1	Phosphoserine intermediate By similarity
	Metal binding	117	1	Magnesium; via phosphate group By similarity
	Metal binding	288	1	Magnesium By similarity
	Metal binding	290	1	Magnesium By similarity
	Metal binding	292	1	Magnesium By similarity
Amino acid modifications
	Modified residue	16	1	N6-acetyllysine Ref.12
	Modified residue	115	1	Phosphothreonine Ref.7 Ref.9
	Modified residue	117	1	Phosphoserine Ref.7 Ref.8 Ref.9 Ref.11
	Modified residue	353	1	Phosphotyrosine Ref.10
	Modified residue	419	1	N6-acetyllysine Ref.12
Natural variations
	Alternative sequence	1 – 13	13	MVKIV…TQAYQ → MSDFEEWISGTYRKMEEGPL PLLTFATAPYH in isoform 2.		VSP_004686
	Alternative sequence	25 – 36	12	RVKVF…SANYA → KTYYFEEKPCYL in isoform 2.		VSP_004687
	Alternative sequence	44 – 56	13	ISTVE…RQEAT → FFSIDLKDRQGSS in isoform 2.		VSP_004688
	Alternative sequence	65 – 77	13	FYMKE…LIARI → YFNKSAIETIVQM in isoform 2.		VSP_004689
	Natural variant	68	1	K → M in allele PGM1*7+, allele PGM1*7-, allele PGM1*3+ and allele PGM1*3-. Ref.14		VAR_006090
	Natural variant	88	1	I → V. Corresponds to variant rs855314 [ dbSNP | Ensembl ].		VAR_050496
	Natural variant	115	1	T → A in GSD14. Ref.16		VAR_062280
	Natural variant	221	1	R → C in allele PGM1*2+, allele PGM1*2-, allele PGM1*3+ and allele PGM1*3-. Ref.2 Ref.5 Ref.14 Ref.15 Corresponds to variant rs1126728 [ dbSNP | Ensembl ].		VAR_006091
	Natural variant	420	1	Y → H in allele PGM1*1-, allele PGM1*2-, allele PGM1*3- and allele PGM1*7-. Ref.2 Ref.3 Ref.5 Ref.14 Ref.15 Corresponds to variant rs11208257 [ dbSNP | Ensembl ].		VAR_006092
	Natural variant	501	1	V → I. Corresponds to variant rs6676290 [ dbSNP | Ensembl ].		VAR_034380
Experimental info
	Sequence conflict	134	1	S → C in AAH67763. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 61A26C19107D467A	FASTA	562	61,449
	10 20 30 40 50 60 MVKIVTVKTQ AYQDQKPGTS GLRKRVKVFQ SSANYAENFI QSIISTVEPA QRQEATLVVG 70 80 90 100 110 120 GDGRFYMKEA IQLIARIAAA NGIGRLVIGQ NGILSTPAVS CIIRKIKAIG GIILTASHNP 130 140 150 160 170 180 GGPNGDFGIK FNISNGGPAP EAITDKIFQI SKTIEEYAVC PDLKVDLGVL GKQQFDLENK 190 200 210 220 230 240 FKPFTVEIVD SVEAYATMLR SIFDFSALKE LLSGPNRLKI RIDAMHGVVG PYVKKILCEE 250 260 270 280 290 300 LGAPANSAVN CVPLEDFGGH HPDPNLTYAA DLVETMKSGE HDFGAAFDGD GDRNMILGKH 310 320 330 340 350 360 GFFVNPSDSV AVIAANIFSI PYFQQTGVRG FARSMPTSGA LDRVASATKI ALYETPTGWK 370 380 390 400 410 420 FFGNLMDASK LSLCGEESFG TGSDHIREKD GLWAVLAWLS ILATRKQSVE DILKDHWQKY 430 440 450 460 470 480 GRNFFTRYDY EEVEAEGANK MMKDLEALMF DRSFVGKQFS ANDKVYTVEK ADNFEYSDPV 490 500 510 520 530 540 DGSISRNQGL RLIFTDGSRI VFRLSGTGSA GATIRLYIDS YEKDVAKINQ DPQVMLAPLI 550 560 SIALKVSQLQ ERTGRTAPTV IT
	Isoform 2 [UniParc]. Checksum: CE4F9CA4094B5139	FASTA	580	63,791
	10 20 30 40 50 60 MSDFEEWISG TYRKMEEGPL PLLTFATAPY HDQKPGTSGL RKKTYYFEEK PCYLENFIQS 70 80 90 100 110 120 IFFSIDLKDR QGSSLVVGGD GRYFNKSAIE TIVQMAAANG IGRLVIGQNG ILSTPAVSCI 130 140 150 160 170 180 IRKIKAIGGI ILTASHNPGG PNGDFGIKFN ISNGGPAPEA ITDKIFQISK TIEEYAVCPD 190 200 210 220 230 240 LKVDLGVLGK QQFDLENKFK PFTVEIVDSV EAYATMLRSI FDFSALKELL SGPNRLKIRI 250 260 270 280 290 300 DAMHGVVGPY VKKILCEELG APANSAVNCV PLEDFGGHHP DPNLTYAADL VETMKSGEHD 310 320 330 340 350 360 FGAAFDGDGD RNMILGKHGF FVNPSDSVAV IAANIFSIPY FQQTGVRGFA RSMPTSGALD 370 380 390 400 410 420 RVASATKIAL YETPTGWKFF GNLMDASKLS LCGEESFGTG SDHIREKDGL WAVLAWLSIL 430 440 450 460 470 480 ATRKQSVEDI LKDHWQKYGR NFFTRYDYEE VEAEGANKMM KDLEALMFDR SFVGKQFSAN 490 500 510 520 530 540 DKVYTVEKAD NFEYSDPVDG SISRNQGLRL IFTDGSRIVF RLSGTGSAGA TIRLYIDSYE 550 560 570 580 KDVAKINQDP QVMLAPLISI ALKVSQLQER TGRTAPTVIT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1530890] [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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-420.
[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: 16710414] [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: 15489334] [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: 8257433] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82.
[7]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115 AND SER-117, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115 AND SER-117, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-353, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, MASS SPECTROMETRY. 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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16 AND LYS-419, MASS SPECTROMETRY.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"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: 7902567] [Abstract] Cited for: VARIANTS MET-68; CYS-221 AND HIS-420.
[15]	"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: 7902568] [Abstract] Cited for: VARIANTS CYS-221 AND HIS-420.
[16]	"Muscle glycogenosis due to phosphoglucomutase 1 deficiency." Stojkovic T., Vissing J., Petit F., Piraud M., Orngreen M.C., Andersen G., Claeys K.G., Wary C., Hogrel J.Y., Laforet P. N. Engl. J. Med. 361:425-427(2009) [PubMed: 19625727] [Abstract] Cited for: VARIANT GSD14 ALA-115.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M83088 mRNA. Translation: AAA60080.1. BT006961 mRNA. Translation: AAP35607.1. 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.
IPI	IPI00217872. IPI00219526.
PIR	A41801.
RefSeq	NP_001166289.1. NM_001172818.1. NP_001166290.1. NM_001172819.1. NP_002624.2. NM_002633.2.
UniGene	Hs.1869.
3D structure databases
ProteinModelPortal	P36871.
SMR	P36871. Positions 2-562.
ModBase	Search...
Protein-protein interaction databases
IntAct	P36871. 2 interactions.
STRING	P36871.
PTM databases
PhosphoSite	P36871.
Polymorphism databases
DMDM	585670.
2D gel databases
REPRODUCTION-2DPAGE	P36871.
Proteomic databases
PRIDE	P36871.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000371084; ENSP00000360125; ENSG00000079739.
GeneID	5236.
KEGG	hsa:5236.
NMPDR	fig|9606.3.peg.1283.
UCSC	uc001dbh.1. human.
Organism-specific databases
CTD	5236.
GeneCards	GC01P064058.
H-InvDB	HIX0023140.
HGNC	HGNC:8905. PGM1.
HPA	CAB004666. HPA024190. HPA024637.
MIM	171900. gene. 612934. phenotype.
neXtProt	NX_P36871.
Orphanet	711. Glycogen storage disease type 14.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07740.
HOVERGEN	HBG001599.
InParanoid	P36871.
OMA	SIFFSID.
OrthoDB	EOG4G1MG2.
PhylomeDB	P36871.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13389.
Pathway_Interaction_DB	hif1_tfpathway. HIF-1-alpha transcription factor network.
Reactome	REACT_474. Metabolism of carbohydrates.
Gene expression databases
ArrayExpress	P36871.
Bgee	P36871.
CleanEx	HS_PGM1.
Genevestigator	P36871.
GermOnline	ENSG00000079739. Homo sapiens.
Family and domain databases
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. IPR016066. A-D-PHexomutase_CS. IPR005841. Alpha-D-phosphohexomutase_SF. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KO	K01835.
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. [Graphical view]
PRINTS	PR00509. PGMPMM.
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 2 hits.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20232.
SOURCE	Search...

Entry information

Entry name

PGM1_HUMAN

Accession

Primary (citable) accession number: P36871
Secondary accession number(s): B2R5N9 , Q16105, Q5BKZ9, Q6NW22, Q86U74, Q96J40, Q9NTY4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 126 of the entry and version 3 of the sequence. [Complete history]

Entry status

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.