O95394 (AGM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoacetylglucosamine mutase
Short name=PAGM
EC=5.4.2.3

Alternative name(s):
Acetylglucosamine phosphomutase
N-acetylglucosamine-phosphate mutase
Phosphoglucomutase-3
Short name=PGM 3

Gene names

Name:	PGM3
Synonyms:	AGM1

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	542 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Interconverts GlcNAc-6-P and GlcNAc-1-P.
Catalytic activity	N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 2/2.
Tissue specificity	Found in many tissues except lung. Relatively high expression in pancreas, heart, liver, and placenta, and relatively low expression in brain, skeletal muscle and kidney.
Sequence similarities	Belongs to the phosphohexose mutase family.
Sequence caution	The sequence BAB14652.1 differs from that shown. Reason: Erroneous initiation. The sequence CAI22635.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI42427.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	UDP-N-acetylglucosamine biosynthetic process Inferred from Biological aspect of Ancestor. Source: RefGenome dolichol-linked oligosaccharide biosynthetic process Traceable author statement. Source: Reactome embryo development ending in birth or egg hatching Inferred from Biological aspect of Ancestor. Source: RefGenome glucose 1-phosphate metabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome hemopoiesis Inferred from Biological aspect of Ancestor. Source: RefGenome post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphoacetylglucosamine mutase activity Inferred from direct assay Ref.3. Source: UniProtKB phosphoglucomutase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 542	542	Phosphoacetylglucosamine mutase		PRO_0000148013
Sites
	Active site	64	1	Phosphoserine intermediate
	Metal binding	64	1	Magnesium; via phosphate group By similarity
	Metal binding	276	1	Magnesium By similarity
	Metal binding	278	1	Magnesium By similarity
	Metal binding	280	1	Magnesium By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.10
	Modified residue	64	1	Phosphoserine Ref.9 Ref.11
Natural variations
	Natural variant	466	1	D → N in allele PGM3*2. Ref.3 Ref.7 Ref.13 Corresponds to variant rs473267 [ dbSNP | Ensembl ].		VAR_013489
Experimental info
	Mutagenesis	64	1	S → A: Loss of activity.
	Mutagenesis	65	1	H → A: Loss of activity.
	Mutagenesis	278	1	D → A or E: Loss of activity.
	Mutagenesis	281	1	R → A or K: Loss of activity.

Sequences

	Sequence		Length	Mass (Da)
	O95394 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 6A4FBCD99A2154A9	FASTA	542	59,852
	10 20 30 40 50 60 MDLGAITKYS ALHAKPNGLI LQYGTAGFRT KAEHLDHVMF RMGLLAVLRS KQTKSTIGVM 70 80 90 100 110 120 VTASHNPEED NGVKLVDPLG EMLAPSWEEH ATCLANAEEQ DMQRVLIDIS EKEAVNLQQD 130 140 150 160 170 180 AFVVIGRDTR PSSEKLSQSV IDGVTVLGGQ FHDYGLLTTP QLHYMVYCRN TGGRYGKATI 190 200 210 220 230 240 EGYYQKLSKA FVELTKQASC SGDEYRSLKV DCANGIGALK LREMEHYFSQ GLSVQLFNDG 250 260 270 280 290 300 SKGKLNHLCG ADFVKSHQKP PQGMEIKSNE RCCSFDGDAD RIVYYYHDAD GHFHLIDGDK 310 320 330 340 350 360 IATLISSFLK ELLVEIGESL NIGVVQTAYA NGSSTRYLEE VMKVPVYCTK TGVKHLHHKA 370 380 390 400 410 420 QEFDIGVYFE ANGHGTALFS TAVEMKIKQS AEQLEDKKRK AAKMLENIID LFNQAAGDAI 430 440 450 460 470 480 SDMLVIEAIL ALKGLTVQQW DALYTDLPNR QLKVQVADRR VISTTDAERQ AVTPPGLQEA 490 500 510 520 530 540 INDLVKKYKL SRAFVRPSGT EDVVRVYAEA DSQESADHLA HEVSLAVFQL AGGIGERPQP GF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Matthijs G., Schollen E., Dierickx D. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning and characterization of complementary DNA encoding human N-acetylglucosamine-phosphate mutase protein." Li C., Rodriguez M., Banerjee D. Gene 242:97-103(2000) [PubMed: 10721701] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Functional cloning and mutational analysis of the human cDNA for phosphoacetylglucosamine mutase: identification of the amino acid residues essential for the catalysis." Mio T., Yamada-Okabe T., Arisawa M., Yamada-Okabe H. Biochim. Biophys. Acta 1492:369-376(2000) [PubMed: 11004509] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS, VARIANT ASN-466.
[4]	"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]. Tissue: Placenta.
[5]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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], VARIANT ASN-466. Tissue: Placenta.
[8]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 392-542. Tissue: Testis.
[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 SER-64, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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-64, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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].
[13]	"Identification of human phosphoglucomutase 3 (PGM3) as N-acetylglucosamine-phosphate mutase (AGM1)." Pang H., Koda Y., Soejima M., Kimura H. Ann. Hum. Genet. 66:139-144(2002) [PubMed: 12174217] [Abstract] Cited for: VARIANT ASN-466.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF102265 mRNA. Translation: AAC72409.1. AF180371 mRNA. Translation: AAD55097.1. AB032081 mRNA. Translation: BAB00613.1. AK023709 mRNA. Translation: BAB14652.1. Different initiation. AK314512 mRNA. Translation: BAG37112.1. AL049699, AL121716 Genomic DNA. Translation: CAI22635.1. Sequence problems. AL121716, AL049699 Genomic DNA. Translation: CAI42427.1. Sequence problems. CH471051 Genomic DNA. Translation: EAW48670.1. CH471051 Genomic DNA. Translation: EAW48671.1. BC001258 mRNA. Translation: AAH01258.1. AL117443 mRNA. Translation: CAB55928.1.
IPI	IPI00941001.
PIR	T17238.
RefSeq	NP_001186846.1. NM_001199917.1. NP_056414.1. NM_015599.2.
UniGene	Hs.661665.
3D structure databases
ProteinModelPortal	O95394.
SMR	O95394. Positions 3-540.
ModBase	Search...
Protein-protein interaction databases
STRING	O95394.
PTM databases
PhosphoSite	O95394.
Proteomic databases
PRIDE	O95394.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000283977; ENSP00000283977; ENSG00000013375. ENST00000416472; ENSP00000412545; ENSG00000013375.
GeneID	5238.
KEGG	hsa:5238.
UCSC	uc003pjv.1. human.
Organism-specific databases
CTD	5238.
GeneCards	GC06M083876.
H-InvDB	HIX0006036.
HGNC	HGNC:8907. PGM3.
HPA	CAB004998. HPA029759. HPA029760.
MIM	172100. gene.
neXtProt	NX_O95394.
PharmGKB	PA33244.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08774.
GeneTree	ENSGT00390000000509.
HOVERGEN	HBG024321.
InParanoid	O95394.
PhylomeDB	O95394.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13179.
BRENDA	5.4.2.3. 2681.
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	O95394.
Bgee	O95394.
CleanEx	HS_PGM3.
Genevestigator	O95394.
GermOnline	ENSG00000013375. 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. IPR005843. A-D-PHexomutase_C. IPR016066. A-D-PHexomutase_CS. IPR016657. PAGM. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KO	K01836.
PANTHER	PTHR22573:SF3. PTHR22573:SF3. 1 hit.
Pfam	PF02878. PGM_PMM_I. 2 hits. PF02879. PGM_PMM_II. 1 hit. PF00408. PGM_PMM_IV. 1 hit. [Graphical view]
PIRSF	PIRSF016408. PAGM. 1 hit.
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20236.
SOURCE	Search...

Entry information

Entry name

AGM1_HUMAN

Accession

Primary (citable) accession number: O95394
Secondary accession number(s): B2RB65 , E1P547, Q5JWR4, Q96J46, Q9H8G5, Q9NS94, Q9NTT6, Q9UFV5, Q9UIY2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	May 1, 1999
Last modified:	January 25, 2012
This is version 125 of the entry and version 1 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.