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 27-MAR-2024, entry version 220. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 78. DR IntAct; O95394; 10. 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; 9606-ENSP00000425809; -. DR PeptideAtlas; O95394; -. DR ProteomicsDB; 14425; -. DR ProteomicsDB; 20051; -. DR ProteomicsDB; 50845; -. [O95394-1] DR Pumba; O95394; -. DR Antibodypedia; 31667; 304 antibodies from 25 providers. DR DNASU; 5238; -. DR Ensembl; ENST00000506587.5; ENSP00000425809.1; ENSG00000013375.17. [O95394-4] DR Ensembl; ENST00000507554.2; ENSP00000425558.2; ENSG00000013375.17. [O95394-1] DR Ensembl; ENST00000508748.6; ENSP00000424865.2; ENSG00000013375.17. [O95394-4] DR Ensembl; ENST00000512866.5; ENSP00000421565.1; ENSG00000013375.17. [O95394-3] DR Ensembl; ENST00000513973.6; ENSP00000424874.1; ENSG00000013375.17. [O95394-1] DR Ensembl; ENST00000698524.1; ENSP00000513773.1; ENSG00000013375.17. [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 AGR; HGNC:8907; -. 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; 641368; Autosomal recessive hyper-IgE syndrome due to ZNF341 deficiency. 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; 1475at2759; -. DR PhylomeDB; O95394; -. DR TreeFam; TF105670; -. DR BioCyc; MetaCyc:HS00347-MONOMER; -. 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; 168 hits in 1168 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 185 other cell types or tissues. DR ExpressionAtlas; O95394; baseline and differential. 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 Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 2. DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 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; IPR049023; AMG1_II. DR InterPro; IPR049022; AMG1_III. DR InterPro; IPR016657; PAGM. DR PANTHER; PTHR45955; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1. DR PANTHER; PTHR45955:SF1; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1. DR Pfam; PF21405; AMG1_II; 1. DR Pfam; PF21404; AMG1_III; 1. DR Pfam; PF02878; PGM_PMM_I; 2. DR Pfam; PF00408; PGM_PMM_IV; 1. DR PIRSF; PIRSF016408; PAGM; 1. DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1. DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3. DR PROSITE; PS00710; PGM_PMM; 1. DR Genevisible; O95394; HS. 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 function in FT UUDP-N-acetylglucosamine biosynthetic process; no effect on FT protein abundance; dbSNP:rs267608261)" FT /evidence="ECO:0000269|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 //