AGM1_HUMAN
ID AGM1_HUMAN Reviewed; 542 AA.
AC O95394; B2RB65; B4DX94; D6RF12; E1P547; E9PF86; Q5JWR4; Q96J46; Q9H8G5;
AC Q9NS94; Q9NTT6; Q9UFV5; Q9UIY2;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Phosphoacetylglucosamine mutase {ECO:0000305};
DE Short=PAGM;
DE EC=5.4.2.3 {ECO:0000269|PubMed:24589341, ECO:0000269|PubMed:24698316, ECO:0000269|PubMed:24931394};
DE AltName: Full=Acetylglucosamine phosphomutase {ECO:0000305};
DE AltName: Full=N-acetylglucosamine-phosphate mutase {ECO:0000303|PubMed:10721701};
DE AltName: Full=Phosphoglucomutase-3 {ECO:0000312|HGNC:HGNC:8907};
DE Short=PGM 3;
GN Name=PGM3 {ECO:0000312|HGNC:HGNC:8907};
GN Synonyms=AGM1 {ECO:0000303|PubMed:11004509};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Matthijs G., Schollen E., Dierickx D.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10721701; DOI=10.1016/s0378-1119(99)00543-0;
RA Li C., Rodriguez M., Banerjee D.;
RT "Cloning and characterization of complementary DNA encoding human N-
RT acetylglucosamine-phosphate mutase protein.";
RL Gene 242:97-103(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS, ACTIVE SITE, AND
RP VARIANT ASN-466.
RX PubMed=11004509; DOI=10.1016/s0167-4781(00)00120-2;
RA Mio T., Yamada-Okabe T., Arisawa M., Yamada-Okabe H.;
RT "Functional cloning and mutational analysis of the human cDNA for
RT phosphoacetylglucosamine mutase: identification of the amino acid residues
RT essential for the catalysis.";
RL Biochim. Biophys. Acta 1492:369-376(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Placenta, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-466.
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 392-542 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INVOLVEMENT IN IMD23, VARIANTS IMD23
RP HIS-239; SER-246 AND ARG-451, AND CHARACTERIZATION OF VARIANTS IMD23
RP HIS-239; SER-246 AND ARG-451.
RX PubMed=24931394; DOI=10.1016/j.ajhg.2014.05.007;
RG Baylor-Johns Hopkins Center for Mendelian Genomics;
RA Stray-Pedersen A., Backe P.H., Sorte H.S., Moerkrid L., Chokshi N.Y.,
RA Erichsen H.C., Gambin T., Elgstoeen K.B., Bjoeraas M., Wlodarski M.W.,
RA Krueger M., Jhangiani S.N., Muzny D.M., Patel A., Raymond K.M., Sasa G.S.,
RA Krance R.A., Martinez C.A., Abraham S.M., Speckmann C., Ehl S., Hall P.,
RA Forbes L.R., Merckoll E., Westvik J., Nishimura G., Rustad C.F.,
RA Abrahamsen T.G., Roennestad A., Osnes L.T., Egeland T., Roedningen O.K.,
RA Beck C.R., Boerwinkle E.A., Gibbs R.A., Lupski J.R., Orange J.S.,
RA Lausch E., Hanson I.C.;
RT "PGM3 mutations cause a congenital disorder of glycosylation with severe
RT immunodeficiency and skeletal dysplasia.";
RL Am. J. Hum. Genet. 95:96-107(2014).
RN [18]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INVOLVEMENT IN IMD23, VARIANTS IMD23
RP GLU-297 AND GLN-501, AND CHARACTERIZATION OF VARIANTS IMD23 GLU-297 AND
RP GLN-501.
RX PubMed=24589341; DOI=10.1016/j.jaci.2014.02.013;
RA Zhang Y., Yu X., Ichikawa M., Lyons J.J., Datta S., Lamborn I.T., Jing H.,
RA Kim E.S., Biancalana M., Wolfe L.A., DiMaggio T., Matthews H.F.,
RA Kranick S.M., Stone K.D., Holland S.M., Reich D.S., Hughes J.D., Mehmet H.,
RA McElwee J., Freeman A.F., Freeze H.H., Su H.C., Milner J.D.;
RT "Autosomal recessive phosphoglucomutase 3 (PGM3) mutations link
RT glycosylation defects to atopy, immune deficiency, autoimmunity, and
RT neurocognitive impairment.";
RL J. Allergy Clin. Immunol. 133:1400-1409(2014).
RN [19]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INVOLVEMENT IN IMD23, VARIANTS IMD23
RP SER-83; GLU-340 DEL AND TYR-502, AND CHARACTERIZATION OF VARIANTS IMD23
RP SER-83; GLU-340 DEL AND TYR-502.
RX PubMed=24698316; DOI=10.1016/j.jaci.2014.02.025;
RA Sassi A., Lazaroski S., Wu G., Haslam S.M., Fliegauf M., Mellouli F.,
RA Patiroglu T., Unal E., Ozdemir M.A., Jouhadi Z., Khadir K., Ben-Khemis L.,
RA Ben-Ali M., Ben-Mustapha I., Borchani L., Pfeifer D., Jakob T., Khemiri M.,
RA Asplund A.C., Gustafsson M.O., Lundin K.E., Falk-Soerqvist E., Moens L.N.,
RA Gungor H.E., Engelhardt K.R., Dziadzio M., Stauss H., Fleckenstein B.,
RA Meier R., Prayitno K., Maul-Pavicic A., Schaffer S., Rakhmanov M.,
RA Henneke P., Kraus H., Eibel H., Koelsch U., Nadifi S., Nilsson M.,
RA Bejaoui M., Schaeffer A.A., Smith C.I., Dell A., Barbouche M.R.,
RA Grimbacher B.;
RT "Hypomorphic homozygous mutations in phosphoglucomutase 3 (PGM3) impair
RT immunity and increase serum IgE levels.";
RL J. Allergy Clin. Immunol. 133:1410-1419(2014).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62 AND SER-64, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP VARIANT ASN-466.
RX PubMed=12174217; DOI=10.1017/s0003480002001033;
RA Pang H., Koda Y., Soejima M., Kimura H.;
RT "Identification of human phosphoglucomutase 3 (PGM3) as N-
RT acetylglucosamine-phosphate mutase (AGM1).";
RL Ann. Hum. Genet. 66:139-144(2002).
CC -!- FUNCTION: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during
CC the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide
CC critical to multiple glycosylation pathways including protein N- and O-
CC glycosylation. {ECO:0000303|PubMed:24589341,
CC ECO:0000303|PubMed:24698316, ECO:0000303|PubMed:24931394}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-
CC glucosamine 6-phosphate; Xref=Rhea:RHEA:23804, ChEBI:CHEBI:57513,
CC ChEBI:CHEBI:57776; EC=5.4.2.3; Evidence={ECO:0000269|PubMed:24589341,
CC ECO:0000269|PubMed:24698316, ECO:0000269|PubMed:24931394};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9P4V2};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9P4V2};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from
CC alpha-D-glucosamine 6-phosphate (route I): step 2/2.
CC {ECO:0000303|PubMed:24589341, ECO:0000303|PubMed:24698316,
CC ECO:0000303|PubMed:24931394}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95394-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95394-3; Sequence=VSP_047320;
CC Name=3;
CC IsoId=O95394-4; Sequence=VSP_047319;
CC -!- TISSUE SPECIFICITY: Found in many tissues except lung. Relatively high
CC expression in pancreas, heart, liver, and placenta, and relatively low
CC expression in brain, skeletal muscle and kidney.
CC {ECO:0000269|PubMed:10721701}.
CC -!- DISEASE: Immunodeficiency 23 (IMD23) [MIM:615816]: A primary
CC immunodeficiency syndrome characterized by recurrent respiratory and
CC skin infections beginning in early childhood, severe atopy, increased
CC serum IgE, and developmental delay or cognitive impairment of varying
CC severity. {ECO:0000269|PubMed:24589341, ECO:0000269|PubMed:24698316,
CC ECO:0000269|PubMed:24931394}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14652.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF102265; AAC72409.1; -; mRNA.
DR EMBL; AF180371; AAD55097.1; -; mRNA.
DR EMBL; AB032081; BAB00613.1; -; mRNA.
DR EMBL; AK023709; BAB14652.1; ALT_INIT; mRNA.
DR EMBL; AK301867; BAG63306.1; -; mRNA.
DR EMBL; AK314512; BAG37112.1; -; mRNA.
DR EMBL; AL049699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48670.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48671.1; -; Genomic_DNA.
DR EMBL; BC001258; AAH01258.1; -; mRNA.
DR EMBL; AL117443; CAB55928.1; -; mRNA.
DR CCDS; CCDS4997.1; -. [O95394-1]
DR CCDS; CCDS56435.1; -. [O95394-3]
DR CCDS; CCDS56436.1; -. [O95394-4]
DR PIR; T17238; T17238.
DR RefSeq; NP_001186846.1; NM_001199917.1. [O95394-4]
DR RefSeq; NP_001186848.1; NM_001199919.1. [O95394-3]
DR RefSeq; NP_056414.1; NM_015599.2. [O95394-1]
DR RefSeq; XP_016866425.1; XM_017010936.1.
DR AlphaFoldDB; O95394; -.
DR SMR; O95394; -.
DR BioGRID; 111257; 55.
DR IntAct; O95394; 7.
DR MINT; O95394; -.
DR STRING; 9606.ENSP00000425809; -.
DR GlyGen; O95394; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95394; -.
DR MetOSite; O95394; -.
DR PhosphoSitePlus; O95394; -.
DR BioMuta; PGM3; -.
DR EPD; O95394; -.
DR jPOST; O95394; -.
DR MassIVE; O95394; -.
DR MaxQB; O95394; -.
DR PaxDb; O95394; -.
DR PeptideAtlas; O95394; -.
DR PRIDE; O95394; -.
DR ProteomicsDB; 14425; -.
DR ProteomicsDB; 20051; -.
DR ProteomicsDB; 50845; -. [O95394-1]
DR Antibodypedia; 31667; 279 antibodies from 24 providers.
DR DNASU; 5238; -.
DR Ensembl; ENST00000506587.5; ENSP00000425809.1; ENSG00000013375.16. [O95394-4]
DR Ensembl; ENST00000512866.5; ENSP00000421565.1; ENSG00000013375.16. [O95394-3]
DR Ensembl; ENST00000513973.6; ENSP00000424874.1; ENSG00000013375.16. [O95394-1]
DR GeneID; 5238; -.
DR KEGG; hsa:5238; -.
DR MANE-Select; ENST00000513973.6; ENSP00000424874.1; NM_015599.3; NP_056414.1.
DR UCSC; uc003pju.3; human. [O95394-1]
DR CTD; 5238; -.
DR DisGeNET; 5238; -.
DR GeneCards; PGM3; -.
DR GeneReviews; PGM3; -.
DR HGNC; HGNC:8907; PGM3.
DR HPA; ENSG00000013375; Low tissue specificity.
DR MalaCards; PGM3; -.
DR MIM; 172100; gene.
DR MIM; 615816; phenotype.
DR neXtProt; NX_O95394; -.
DR OpenTargets; ENSG00000013375; -.
DR Orphanet; 443811; PGM3-CDG.
DR PharmGKB; PA33244; -.
DR VEuPathDB; HostDB:ENSG00000013375; -.
DR eggNOG; KOG2537; Eukaryota.
DR GeneTree; ENSGT00390000000509; -.
DR HOGENOM; CLU_022890_1_0_1; -.
DR InParanoid; O95394; -.
DR OMA; WEAYATK; -.
DR OrthoDB; 345441at2759; -.
DR PhylomeDB; O95394; -.
DR TreeFam; TF105670; -.
DR BioCyc; MetaCyc:HS00347-MON; -.
DR BRENDA; 5.4.2.3; 2681.
DR PathwayCommons; O95394; -.
DR Reactome; R-HSA-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR SABIO-RK; O95394; -.
DR SignaLink; O95394; -.
DR UniPathway; UPA00113; UER00530.
DR BioGRID-ORCS; 5238; 156 hits in 1077 CRISPR screens.
DR ChiTaRS; PGM3; human.
DR GeneWiki; Phosphoglucomutase_3; -.
DR GenomeRNAi; 5238; -.
DR Pharos; O95394; Tbio.
DR PRO; PR:O95394; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O95394; protein.
DR Bgee; ENSG00000013375; Expressed in body of pancreas and 183 other tissues.
DR ExpressionAtlas; O95394; baseline and differential.
DR Genevisible; O95394; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006041; P:glucosamine metabolic process; NAS:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; IMP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IMP:UniProtKB.
DR CDD; cd03086; PGM3; 1.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR016657; PAGM.
DR Pfam; PF02878; PGM_PMM_I; 2.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PIRSF; PIRSF016408; PAGM; 1.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Carbohydrate metabolism;
KW Disease variant; Isomerase; Magnesium; Metal-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..542
FT /note="Phosphoacetylglucosamine mutase"
FT /id="PRO_0000148013"
FT ACT_SITE 64
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000303|PubMed:11004509"
FT BINDING 64
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 370..372
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 496..500
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT BINDING 505
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9P4V2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1
FT /note="M -> MGGEWGQSAICPESAQEWTYQVGQHLVDM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047319"
FT VAR_SEQ 542
FT /note="F -> YKAAETTHNINNAFGPGTANEHTVP (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047320"
FT VARIANT 83
FT /note="L -> S (in IMD23; decreased phosphoacetylglucosamine
FT mutase activity; no effect on protein abundance;
FT dbSNP:rs267608260)"
FT /evidence="ECO:0000269|PubMed:24698316"
FT /id="VAR_071359"
FT VARIANT 239
FT /note="D -> H (in IMD23; decreased phosphoacetylglucosamine
FT mutase activity; dbSNP:rs869312886)"
FT /evidence="ECO:0000269|PubMed:24931394"
FT /id="VAR_071360"
FT VARIANT 246
FT /note="N -> S (in IMD23; loss of phosphoacetylglucosamine
FT mutase activity; dbSNP:rs587777562)"
FT /evidence="ECO:0000269|PubMed:24931394"
FT /id="VAR_071361"
FT VARIANT 297
FT /note="D -> E (in IMD23; decreased phosphoacetylglucosamine
FT mutase activity; decreased protein abundance;
FT dbSNP:rs587777415)"
FT /evidence="ECO:0000269|PubMed:24589341"
FT /id="VAR_071362"
FT VARIANT 340
FT /note="Missing (in IMD23; decreased
FT phosphoacetylglucosamine mutase activity; decreased protein
FT abundance)"
FT /evidence="ECO:0000269|PubMed:24698316"
FT /id="VAR_071363"
FT VARIANT 451
FT /note="Q -> R (in IMD23; decreased phosphoacetylglucosamine
FT mutase activity; dbSNP:rs587777565)"
FT /evidence="ECO:0000269|PubMed:24931394"
FT /id="VAR_071364"
FT VARIANT 466
FT /note="D -> N (in allele PGM3*2; dbSNP:rs473267)"
FT /evidence="ECO:0000269|PubMed:11004509,
FT ECO:0000269|PubMed:12174217, ECO:0000269|PubMed:15489334"
FT /id="VAR_013489"
FT VARIANT 501
FT /note="E -> Q (in IMD23; decreased phosphoacetylglucosamine
FT mutase activity; no effect on protein abundance;
FT dbSNP:rs587777413)"
FT /evidence="ECO:0000269|PubMed:24589341"
FT /id="VAR_071365"
FT VARIANT 502
FT /note="D -> Y (in IMD23; decreased phosphoacetylglucosamine
FT mutase activity; no effect on protein abundance;
FT dbSNP:rs267608261)"
FT /evidence="ECO:0000303|PubMed:24698316"
FT /id="VAR_071366"
FT MUTAGEN 64
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11004509"
FT MUTAGEN 65
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11004509"
FT MUTAGEN 278
FT /note="D->A,E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11004509"
FT MUTAGEN 281
FT /note="R->A,K: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11004509"
FT CONFLICT 5
FT /note="A -> V (in Ref. 4; BAG63306)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="D -> G (in Ref. 4; BAG63306)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 59852 MW; 6A4FBCD99A2154A9 CRC64;
MDLGAITKYS ALHAKPNGLI LQYGTAGFRT KAEHLDHVMF RMGLLAVLRS KQTKSTIGVM
VTASHNPEED NGVKLVDPLG EMLAPSWEEH ATCLANAEEQ DMQRVLIDIS EKEAVNLQQD
AFVVIGRDTR PSSEKLSQSV IDGVTVLGGQ FHDYGLLTTP QLHYMVYCRN TGGRYGKATI
EGYYQKLSKA FVELTKQASC SGDEYRSLKV DCANGIGALK LREMEHYFSQ GLSVQLFNDG
SKGKLNHLCG ADFVKSHQKP PQGMEIKSNE RCCSFDGDAD RIVYYYHDAD GHFHLIDGDK
IATLISSFLK ELLVEIGESL NIGVVQTAYA NGSSTRYLEE VMKVPVYCTK TGVKHLHHKA
QEFDIGVYFE ANGHGTALFS TAVEMKIKQS AEQLEDKKRK AAKMLENIID LFNQAAGDAI
SDMLVIEAIL ALKGLTVQQW DALYTDLPNR QLKVQVADRR VISTTDAERQ AVTPPGLQEA
INDLVKKYKL SRAFVRPSGT EDVVRVYAEA DSQESADHLA HEVSLAVFQL AGGIGERPQP
GF
