ID PMM2_HUMAN Reviewed; 246 AA.
AC O15305; A8K672; B7Z6R0; D3DUF3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 229.
DE RecName: Full=Phosphomannomutase 2 {ECO:0000303|PubMed:9140401};
DE Short=PMM 2 {ECO:0000303|PubMed:9140401};
DE EC=5.4.2.8 {ECO:0000269|PubMed:16540464};
GN Name=PMM2;
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), AND VARIANTS CDG1A.
RX PubMed=9140401; DOI=10.1038/ng0597-88;
RA Matthijs G., Schollen E., Pardon E., Veiga-Da-Cunha M., Jaeken J.,
RA Cassiman J.-J., van Schaftingen E.;
RT "Mutations in PMM2, a phosphomannomutase gene on chromosome 16p13, in
RT carbohydrate-deficient glycoprotein type I syndrome (Jaeken syndrome).";
RL Nat. Genet. 16:88-92(1997).
RN [2]
RP ERRATUM OF PUBMED:9140401.
RA Matthijs G., Schollen E., Pardon E., Veiga-Da-Cunha M., Jaeken J.,
RA Cassiman J.-J., van Schaftingen E.;
RL Nat. Genet. 16:316-316(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9425221; DOI=10.1093/hmg/7.2.157;
RA Schollen E., Pardon E., Heykants L., Renard J., Doggett N.A., Callen D.F.,
RA Cassiman J.J., Matthijs G.;
RT "Comparative analysis of the phosphomannomutase genes PMM1, PMM2 and
RT PMM2psi: the sequence variation in the processed pseudogene is a reflection
RT of the mutations found in the functional gene.";
RL Hum. Mol. Genet. 7:157-164(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
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=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
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).
RC TISSUE=Pancreas;
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 CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16540464; DOI=10.1074/jbc.m601505200;
RA Silvaggi N.R., Zhang C., Lu Z., Dai J., Dunaway-Mariano D., Allen K.N.;
RT "The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal
RT the structural basis of congenital disorder of glycosylation type 1a.";
RL J. Biol. Chem. 281:14918-14926(2006).
RN [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
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 [13]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS).
RX PubMed=17850744; DOI=10.1016/j.str.2007.06.019;
RA Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr.;
RT "Ensemble refinement of protein crystal structures: validation and
RT application.";
RL Structure 15:1040-1052(2007).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS).
RG Center for eukaryotic structural genomics (CESG);
RT "X-ray structure of human phosphomannomutase 2 (PMM2).";
RL Submitted (FEB-2009) to the PDB data bank.
RN [15]
RP REVIEW ON VARIANTS CDG1A.
RX PubMed=10527672; DOI=10.1006/mgme.1999.2914;
RA Matthijs G., Schollen E., Heykants L., Gruenewald S.;
RT "Phosphomannomutase deficiency: the molecular basis of the classical Jaeken
RT syndrome (CDGS type Ia).";
RL Mol. Genet. Metab. 68:220-226(1999).
RN [16]
RP VARIANTS CDG1A.
RX PubMed=9497260; DOI=10.1086/301763;
RA Matthijs G., Schollen E., van Schaftingen E., Cassiman J.-J., Jaeken J.;
RT "Lack of homozygotes for the most frequent disease allele in carbohydrate-
RT deficient glycoprotein syndrome type 1A.";
RL Am. J. Hum. Genet. 62:542-550(1998).
RN [17]
RP VARIANTS CDG1A ARG-117 AND GLU-223.
RX PubMed=9781039; DOI=10.1038/sj.ejhg.5200194;
RA Kjaergaard S., Skovby F., Schwartz M.;
RT "Absence of homozygosity for predominant mutations in PMM2 in Danish
RT patients with carbohydrate-deficient glycoprotein syndrome type 1.";
RL Eur. J. Hum. Genet. 6:331-336(1998).
RN [18]
RP VARIANTS CDG1A LEU-144; SER-229 AND PRO-238.
RX PubMed=10066032; DOI=10.1034/j.1399-0004.1999.550109.x;
RA Kondo I., Mizugishi K., Yoneda Y., Hashimoto T., Kuwajima K., Yuasa I.,
RA Shigemoto K., Kuroda Y.;
RT "Missense mutations in phosphomannomutase 2 gene in two Japanese families
RT with carbohydrate-deficient glycoprotein syndrome type 1.";
RL Clin. Genet. 55:50-54(1999).
RN [19]
RP VARIANT CDG1A GLY-192, AND CHARACTERIZATION OF VARIANTS CDG1A ARG-117;
RP LEU-119; HIS-141; GLY-192; GLU-223 AND ARG-237.
RX PubMed=10602363; DOI=10.1038/sj.ejhg.5200398;
RA Kjaergaard S., Skovby F., Schwartz M.;
RT "Carbohydrate-deficient glycoprotein syndrome type 1A: expression and
RT characterisation of wild type and mutant PMM2 in E. coli.";
RL Eur. J. Hum. Genet. 7:884-888(1999).
RN [20]
RP VARIANTS CDG1A LYS-139 AND HIS-141.
RX PubMed=10571956;
RX DOI=10.1002/(sici)1098-1004(199912)14:6<543::aid-humu17>3.0.co;2-s;
RA Vuillaumier-Barrot S., Barnier A., Cuer M., Durand G., Grandchamp B.,
RA Seta N.;
RT "Characterization of the 415G>A (E139K) PMM2 mutation in carbohydrate-
RT deficient glycoprotein syndrome type Ia disrupting a splicing enhancer
RT resulting in exon 5 skipping.";
RL Hum. Mutat. 14:543-544(1999).
RN [21]
RP VARIANTS CDG1A TYR-9; CYS-11; ARG-32; ALA-44; TYR-65; MET-67; SER-69;
RP CYS-76; LYS-101; PHE-103; CYS-106; VAL-108; LEU-113; ARG-117; LEU-119;
RP THR-120; GLN-123; MET-129; ALA-131; ASN-132; THR-132; LYS-139; HIS-141;
RP ASN-148; GLY-151; THR-153; SER-157; TRP-162; VAL-172; ARG-175; SER-183;
RP GLY-185; GLY-188; GLY-192; ARG-195; SER-206; ALA-208; ILE-216; SER-216;
RP GLU-217; LEU-218; GLU-223; SER-226; ARG-228; CYS-228; SER-229; MET-231;
RP THR-233; ARG-237; MET-237; GLY-238 AND SER-241, AND VARIANT ALA-197.
RX PubMed=11058895;
RX DOI=10.1002/1098-1004(200011)16:5<386::aid-humu2>3.0.co;2-y;
RA Matthijs G., Schollen E., Bjursell C., Erlandson A., Freeze H., Imtiaz F.,
RA Kjaergaard S., Martinsson T., Schwartz M., Seta N., Vuillaumier-Barrot S.,
RA Westphal V., Winchester B.;
RT "Mutations in PMM2 that cause congenital disorders of glycosylation, type
RT Ia (CDG-Ia).";
RL Hum. Mutat. 16:386-394(2000).
RN [22]
RP VARIANTS CDG1A TYR-9; CYS-11; MET-67; LEU-113; ARG-117; LEU-119; GLN-123;
RP MET-129; HIS-141; VAL-172; ARG-175; SER-183; GLY-185; GLY-192; SER-216;
RP GLU-217; GLU-223; ARG-228; MET-231 AND ARG-237.
RX PubMed=11058896;
RX DOI=10.1002/1098-1004(200011)16:5<395::aid-humu3>3.0.co;2-t;
RA Bjursell C., Erlandson A., Nordling M., Nilsson S., Wahlstroem J.,
RA Stibler H., Kristiansson B., Martinsson T.;
RT "PMM2 mutation spectrum, including 10 novel mutations, in a large CDG type
RT 1A family material with a focus on Scandinavian families.";
RL Hum. Mutat. 16:395-400(2000).
RN [23]
RP VARIANTS CDG1A LEU-119; ASN-132; HIS-141; ASN-148; SER-183; ALA-208;
RP MET-231 AND MET-237.
RX PubMed=10801058; DOI=10.1023/a:1005669900330;
RA Imtiaz F., Worthington V., Champion M., Beesley C., Charlwood J.,
RA Clayton P., Keir G., Mian N., Winchester B.;
RT "Genotypes and phenotypes of patients in the UK with carbohydrate-deficient
RT glycoprotein syndrome type 1.";
RL J. Inherit. Metab. Dis. 23:162-174(2000).
RN [24]
RP VARIANT CDG1A VAL-104.
RX PubMed=11350185; DOI=10.1006/mgme.2001.3174;
RA Westphal V., Enns G.M., McCracken M.F., Freeze H.H.;
RT "Functional analysis of novel mutations in a congenital disorder of
RT glycosylation Ia patient with mixed Asian ancestry.";
RL Mol. Genet. Metab. 73:71-76(2001).
RN [25]
RP VARIANTS CDG1A GLU-15; CYS-64; ALA-93; SER-214 AND ASN-223, AND VARIANT
RP ARG-42.
RX PubMed=12357336; DOI=10.1038/sj.ejhg.5200858;
RA Schollen E., Martens K., Geuzens E., Matthijs G.;
RT "DHPLC analysis as a platform for molecular diagnosis of congenital
RT disorders of glycosylation (CDG).";
RL Eur. J. Hum. Genet. 10:643-648(2002).
RN [26]
RP VARIANTS CDG1A TYR-9; SER-20; ARG-32; HIS-37; LEU-44; TYR-65; SER-69;
RP PHE-103; VAL-108; LEU-113; LEU-119; GLN-123; MET-129; ALA-131; THR-132;
RP PHE-132; LYS-139; CYS-141; HIS-141; THR-153; SER-157; TRP-162; VAL-176;
RP HIS-177; SER-214; SER-226; MET-231; ARG-237; MET-237 AND SER-241, VARIANTS
RP ARG-42 AND ALA-197, AND CHARACTERIZATION OF VARIANTS CDG1A SER-20; HIS-37;
RP PHE-132; LYS-139; CYS-141; HIS-141; VAL-176 AND HIS-177.
RX PubMed=15844218; DOI=10.1002/humu.9336;
RA Le Bizec C., Vuillaumier-Barrot S., Barnier A., Dupre T., Durand G.,
RA Seta N.;
RT "A new insight into PMM2 mutations in the French population.";
RL Hum. Mutat. 25:504-505(2005).
RN [27]
RP VARIANTS CDG1A ALA-44 AND MET-231.
RX PubMed=17307006; DOI=10.1016/j.ymgme.2007.01.003;
RA Schollen E., Keldermans L., Foulquier F., Briones P., Chabas A.,
RA Sanchez-Valverde F., Adamowicz M., Pronicka E., Wevers R., Matthijs G.;
RT "Characterization of two unusual truncating PMM2 mutations in two CDG-Ia
RT patients.";
RL Mol. Genet. Metab. 90:408-413(2007).
CC -!- FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-
CC phosphate-mannose required for a number of critical mannosyl transfer
CC reactions. {ECO:0000250|UniProtKB:Q92871}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC EC=5.4.2.8; Evidence={ECO:0000269|PubMed:16540464};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 uM for alpha-D-mannose 1-phosphate
CC {ECO:0000269|PubMed:16540464};
CC KM=13.5 uM for alpha-D-glucose 1-phosphate
CC {ECO:0000269|PubMed:16540464};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q92871}.
CC -!- INTERACTION:
CC O15305; Q96HD9: ACY3; NbExp=9; IntAct=EBI-10182608, EBI-3916242;
CC O15305; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-10182608, EBI-16439278;
CC O15305; Q9HBY8-2: SGK2; NbExp=5; IntAct=EBI-10182608, EBI-12143041;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15305-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15305-2; Sequence=VSP_056228, VSP_056229;
CC -!- DISEASE: Congenital disorder of glycosylation 1A (CDG1A) [MIM:212065]:
CC A form of congenital disorder of glycosylation, a multisystem disorder
CC caused by a defect in glycoprotein biosynthesis and characterized by
CC under-glycosylated serum glycoproteins. Congenital disorders of
CC glycosylation result in a wide variety of clinical features, such as
CC defects in the nervous system development, psychomotor retardation,
CC dysmorphic features, hypotonia, coagulation disorders, and
CC immunodeficiency. The broad spectrum of features reflects the critical
CC role of N-glycoproteins during embryonic development, differentiation,
CC and maintenance of cell functions. CDG1A is an autosomal recessive
CC disorder characterized by a severe encephalopathy with axial hypotonia,
CC abnormal eye movement, and pronounced psychomotor retardation, as well
CC as peripheral neuropathy, cerebellar hypoplasia, and retinitis
CC pigmentosa. Patients show a peculiar distribution of subcutaneous fat,
CC nipple retraction, and hypogonadism. {ECO:0000269|PubMed:10066032,
CC ECO:0000269|PubMed:10527672, ECO:0000269|PubMed:10571956,
CC ECO:0000269|PubMed:10602363, ECO:0000269|PubMed:10801058,
CC ECO:0000269|PubMed:11058895, ECO:0000269|PubMed:11058896,
CC ECO:0000269|PubMed:11350185, ECO:0000269|PubMed:12357336,
CC ECO:0000269|PubMed:15844218, ECO:0000269|PubMed:17307006,
CC ECO:0000269|PubMed:9140401, ECO:0000269|PubMed:9497260,
CC ECO:0000269|PubMed:9781039}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the eukaryotic PMM family. {ECO:0000305}.
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DR EMBL; U85773; AAC51368.1; -; mRNA.
DR EMBL; AF157796; AAD45895.1; -; Genomic_DNA.
DR EMBL; AF157790; AAD45895.1; JOINED; Genomic_DNA.
DR EMBL; AF157791; AAD45895.1; JOINED; Genomic_DNA.
DR EMBL; AF157792; AAD45895.1; JOINED; Genomic_DNA.
DR EMBL; AF157793; AAD45895.1; JOINED; Genomic_DNA.
DR EMBL; AF157794; AAD45895.1; JOINED; Genomic_DNA.
DR EMBL; AF157795; AAD45895.1; JOINED; Genomic_DNA.
DR EMBL; AK291537; BAF84226.1; -; mRNA.
DR EMBL; AK300785; BAH13346.1; -; mRNA.
DR EMBL; AC012173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85200.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85201.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85202.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85203.1; -; Genomic_DNA.
DR EMBL; BC008310; AAH08310.1; -; mRNA.
DR CCDS; CCDS10536.1; -. [O15305-1]
DR RefSeq; NP_000294.1; NM_000303.2. [O15305-1]
DR PDB; 2AMY; X-ray; 2.09 A; A=2-246.
DR PDB; 2Q4R; X-ray; 2.09 A; A=2-246.
DR PDB; 7O0C; X-ray; 2.80 A; A/B=1-246.
DR PDB; 7O1B; X-ray; 3.08 A; A/B=1-246.
DR PDB; 7O4G; X-ray; 2.66 A; A/B=1-246.
DR PDB; 7O58; X-ray; 1.97 A; A/B=1-246.
DR PDB; 7O5Z; X-ray; 2.07 A; A/B=1-246.
DR PDBsum; 2AMY; -.
DR PDBsum; 2Q4R; -.
DR PDBsum; 7O0C; -.
DR PDBsum; 7O1B; -.
DR PDBsum; 7O4G; -.
DR PDBsum; 7O58; -.
DR PDBsum; 7O5Z; -.
DR AlphaFoldDB; O15305; -.
DR SMR; O15305; -.
DR BioGRID; 111386; 55.
DR IntAct; O15305; 20.
DR MINT; O15305; -.
DR STRING; 9606.ENSP00000268261; -.
DR BindingDB; O15305; -.
DR ChEMBL; CHEMBL1741162; -.
DR GlyGen; O15305; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15305; -.
DR MetOSite; O15305; -.
DR PhosphoSitePlus; O15305; -.
DR BioMuta; PMM2; -.
DR EPD; O15305; -.
DR jPOST; O15305; -.
DR MassIVE; O15305; -.
DR MaxQB; O15305; -.
DR PaxDb; 9606-ENSP00000268261; -.
DR PeptideAtlas; O15305; -.
DR ProteomicsDB; 48574; -. [O15305-1]
DR ProteomicsDB; 6798; -.
DR Pumba; O15305; -.
DR Antibodypedia; 24552; 240 antibodies from 30 providers.
DR DNASU; 5373; -.
DR Ensembl; ENST00000268261.9; ENSP00000268261.4; ENSG00000140650.13. [O15305-1]
DR Ensembl; ENST00000566604.5; ENSP00000456774.1; ENSG00000140650.13. [O15305-2]
DR Ensembl; ENST00000683274.1; ENSP00000507262.1; ENSG00000140650.13. [O15305-2]
DR GeneID; 5373; -.
DR KEGG; hsa:5373; -.
DR MANE-Select; ENST00000268261.9; ENSP00000268261.4; NM_000303.3; NP_000294.1.
DR UCSC; uc002czf.5; human. [O15305-1]
DR AGR; HGNC:9115; -.
DR CTD; 5373; -.
DR DisGeNET; 5373; -.
DR GeneCards; PMM2; -.
DR GeneReviews; PMM2; -.
DR HGNC; HGNC:9115; PMM2.
DR HPA; ENSG00000140650; Low tissue specificity.
DR MalaCards; PMM2; -.
DR MIM; 212065; phenotype.
DR MIM; 601785; gene.
DR neXtProt; NX_O15305; -.
DR OpenTargets; ENSG00000140650; -.
DR Orphanet; 79318; PMM2-CDG.
DR PharmGKB; PA33441; -.
DR VEuPathDB; HostDB:ENSG00000140650; -.
DR eggNOG; KOG3189; Eukaryota.
DR GeneTree; ENSGT00390000002918; -.
DR HOGENOM; CLU_065642_1_1_1; -.
DR InParanoid; O15305; -.
DR OMA; ISHRVYT; -.
DR OrthoDB; 167037at2759; -.
DR PhylomeDB; O15305; -.
DR TreeFam; TF300874; -.
DR BRENDA; 5.4.2.8; 2681.
DR PathwayCommons; O15305; -.
DR Reactome; R-HSA-4043911; Defective PMM2 causes PMM2-CDG.
DR Reactome; R-HSA-446205; Synthesis of GDP-mannose.
DR SABIO-RK; O15305; -.
DR SignaLink; O15305; -.
DR UniPathway; UPA00126; UER00424.
DR BioGRID-ORCS; 5373; 170 hits in 1176 CRISPR screens.
DR ChiTaRS; PMM2; human.
DR EvolutionaryTrace; O15305; -.
DR GeneWiki; PMM2; -.
DR GenomeRNAi; 5373; -.
DR Pharos; O15305; Tchem.
DR PRO; PR:O15305; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O15305; Protein.
DR Bgee; ENSG00000140650; Expressed in body of pancreas and 102 other cell types or tissues.
DR ExpressionAtlas; O15305; baseline and differential.
DR Genevisible; O15305; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004615; F:phosphomannomutase activity; IBA:GO_Central.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; TAS:Reactome.
DR GO; GO:0006013; P:mannose metabolic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; TAS:ProtInc.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR CDD; cd02585; HAD_PMM; 1.
DR Gene3D; 3.30.1240.20; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005002; PMM.
DR InterPro; IPR043169; PMM_cap.
DR NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR PANTHER; PTHR10466; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR10466:SF2; PHOSPHOMANNOMUTASE 2; 1.
DR Pfam; PF03332; PMM; 1.
DR SFLD; SFLDF00445; alpha-phosphomannomutase; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW Congenital disorder of glycosylation; Cytoplasm; Disease variant;
KW Isomerase; Magnesium; Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..246
FT /note="Phosphomannomutase 2"
FT /id="PRO_0000199694"
FT ACT_SITE 12
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT ACT_SITE 14
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 21
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 123
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 134
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 141
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 179
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 181
FT /ligand="alpha-D-mannose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58409"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 209
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P31353"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 223
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q92871"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 149
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2M7"
FT VAR_SEQ 117..119
FT /note="GTF -> KKI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056228"
FT VAR_SEQ 120..246
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056229"
FT VARIANT 9
FT /note="C -> Y (in CDG1A; dbSNP:rs104894532)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:11058896, ECO:0000269|PubMed:15844218"
FT /id="VAR_022469"
FT VARIANT 11
FT /note="F -> C (in CDG1A)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:11058896"
FT /id="VAR_022470"
FT VARIANT 15
FT /note="G -> E (in CDG1A)"
FT /evidence="ECO:0000269|PubMed:12357336"
FT /id="VAR_022471"
FT VARIANT 20
FT /note="P -> S (in CDG1A; reduction of activity;
FT dbSNP:rs949271895)"
FT /evidence="ECO:0000269|PubMed:15844218"
FT /id="VAR_022472"
FT VARIANT 32
FT /note="L -> R (in CDG1A; dbSNP:rs104894533)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_022473"
FT VARIANT 37
FT /note="Q -> H (in CDG1A; partial loss of activity)"
FT /evidence="ECO:0000269|PubMed:15844218"
FT /id="VAR_022474"
FT VARIANT 37
FT /note="Q -> L (in dbSNP:rs2304472)"
FT /id="VAR_022133"
FT VARIANT 42
FT /note="G -> R (in dbSNP:rs755402538)"
FT /evidence="ECO:0000269|PubMed:12357336,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_022475"
FT VARIANT 44
FT /note="V -> A (in CDG1A; dbSNP:rs104894534)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:17307006"
FT /id="VAR_006093"
FT VARIANT 44
FT /note="V -> L (in CDG1A)"
FT /evidence="ECO:0000269|PubMed:15844218"
FT /id="VAR_022563"
FT VARIANT 64
FT /note="Y -> C (in CDG1A)"
FT /evidence="ECO:0000269|PubMed:12357336"
FT /id="VAR_022476"
FT VARIANT 65
FT /note="D -> Y (in CDG1A; dbSNP:rs104894527)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_006094"
FT VARIANT 67
FT /note="V -> M (in CDG1A; dbSNP:rs1318611010)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:11058896"
FT /id="VAR_022477"
FT VARIANT 69
FT /note="P -> S (in CDG1A; dbSNP:rs769648248)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_022478"
FT VARIANT 76
FT /note="Y -> C (in CDG1A; dbSNP:rs1440183322)"
FT /evidence="ECO:0000269|PubMed:11058895"
FT /id="VAR_022479"
FT VARIANT 93
FT /note="E -> A (in CDG1A)"
FT /evidence="ECO:0000269|PubMed:12357336"
FT /id="VAR_022480"
FT VARIANT 101
FT /note="N -> K (in CDG1A; dbSNP:rs769839273)"
FT /evidence="ECO:0000269|PubMed:11058895"
FT /id="VAR_006095"
FT VARIANT 103
FT /note="C -> F (in CDG1A)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_022481"
FT VARIANT 104
FT /note="L -> V (in CDG1A; dbSNP:rs770458492)"
FT /evidence="ECO:0000269|PubMed:11350185"
FT /id="VAR_012344"
FT VARIANT 106
FT /note="Y -> C (in CDG1A; dbSNP:rs387906824)"
FT /evidence="ECO:0000269|PubMed:11058895"
FT /id="VAR_006096"
FT VARIANT 108
FT /note="A -> V (in CDG1A; dbSNP:rs200503569)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_006097"
FT VARIANT 113
FT /note="P -> L (in CDG1A; dbSNP:rs80338700)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:11058896, ECO:0000269|PubMed:15844218"
FT /id="VAR_006098"
FT VARIANT 117
FT /note="G -> R (in CDG1A; loss of activity;
FT dbSNP:rs104894530)"
FT /evidence="ECO:0000269|PubMed:10602363,
FT ECO:0000269|PubMed:11058895, ECO:0000269|PubMed:11058896,
FT ECO:0000269|PubMed:9781039"
FT /id="VAR_006099"
FT VARIANT 119
FT /note="F -> L (in CDG1A; partial loss of activity;
FT dbSNP:rs80338701)"
FT /evidence="ECO:0000269|PubMed:10602363,
FT ECO:0000269|PubMed:10801058, ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:11058896, ECO:0000269|PubMed:15844218"
FT /id="VAR_006100"
FT VARIANT 120
FT /note="I -> T (in CDG1A; dbSNP:rs368582085)"
FT /evidence="ECO:0000269|PubMed:11058895"
FT /id="VAR_022482"
FT VARIANT 123
FT /note="R -> Q (in CDG1A; dbSNP:rs141498002)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:11058896, ECO:0000269|PubMed:15844218"
FT /id="VAR_006101"
FT VARIANT 129
FT /note="V -> M (in CDG1A; dbSNP:rs104894525)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:11058896, ECO:0000269|PubMed:15844218"
FT /id="VAR_006102"
FT VARIANT 131
FT /note="P -> A (in CDG1A; dbSNP:rs1274547742)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_006103"
FT VARIANT 132
FT /note="I -> F (in CDG1A; slightly reduced activity;
FT dbSNP:rs753632453)"
FT /evidence="ECO:0000269|PubMed:15844218"
FT /id="VAR_022483"
FT VARIANT 132
FT /note="I -> N (in CDG1A)"
FT /evidence="ECO:0000269|PubMed:10801058,
FT ECO:0000269|PubMed:11058895"
FT /id="VAR_022484"
FT VARIANT 132
FT /note="I -> T (in CDG1A; dbSNP:rs80338702)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_006104"
FT VARIANT 139
FT /note="E -> K (in CDG1A; this mutation seems to disrupt a
FT splicing enhancer sequence and thus results in most cases
FT in a protein with exon 5 skipped; slightly reduced
FT activity; dbSNP:rs80338703)"
FT /evidence="ECO:0000269|PubMed:10571956,
FT ECO:0000269|PubMed:11058895, ECO:0000269|PubMed:15844218"
FT /id="VAR_009232"
FT VARIANT 141
FT /note="R -> C (in CDG1A; loss of activity;
FT dbSNP:rs746610168)"
FT /evidence="ECO:0000269|PubMed:15844218"
FT /id="VAR_022485"
FT VARIANT 141
FT /note="R -> H (in CDG1A; frequent mutation; loss of
FT activity; observed in heterozygous patients; homozygosis of
FT this mutation is incompatible with life; dbSNP:rs28936415)"
FT /evidence="ECO:0000269|PubMed:10571956,
FT ECO:0000269|PubMed:10602363, ECO:0000269|PubMed:10801058,
FT ECO:0000269|PubMed:11058895, ECO:0000269|PubMed:11058896,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_006105"
FT VARIANT 144
FT /note="F -> L (in CDG1A; dbSNP:rs150719105)"
FT /evidence="ECO:0000269|PubMed:10066032"
FT /id="VAR_022486"
FT VARIANT 148
FT /note="D -> N (in CDG1A; dbSNP:rs148032587)"
FT /evidence="ECO:0000269|PubMed:10801058,
FT ECO:0000269|PubMed:11058895"
FT /id="VAR_022487"
FT VARIANT 151
FT /note="E -> G (in CDG1A)"
FT /evidence="ECO:0000269|PubMed:11058895"
FT /id="VAR_022488"
FT VARIANT 153
FT /note="I -> T (in CDG1A; dbSNP:rs150577656)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_022489"
FT VARIANT 157
FT /note="F -> S (in CDG1A; dbSNP:rs190521996)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_022490"
FT VARIANT 162
FT /note="R -> W (in CDG1A; dbSNP:rs104894526)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_006106"
FT VARIANT 172
FT /note="F -> V (in CDG1A)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:11058896"
FT /id="VAR_022491"
FT VARIANT 175
FT /note="G -> R (in CDG1A; dbSNP:rs941830625)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:11058896"
FT /id="VAR_006107"
FT VARIANT 176
FT /note="G -> V (in CDG1A; loss of activity)"
FT /evidence="ECO:0000269|PubMed:15844218"
FT /id="VAR_022492"
FT VARIANT 177
FT /note="Q -> H (in CDG1A; partial loss of activity)"
FT /evidence="ECO:0000269|PubMed:15844218"
FT /id="VAR_022493"
FT VARIANT 183
FT /note="F -> S (in CDG1A; dbSNP:rs780581250)"
FT /evidence="ECO:0000269|PubMed:10801058,
FT ECO:0000269|PubMed:11058895, ECO:0000269|PubMed:11058896"
FT /id="VAR_022494"
FT VARIANT 185
FT /note="D -> G (in CDG1A; dbSNP:rs1386173214)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:11058896"
FT /id="VAR_022495"
FT VARIANT 188
FT /note="D -> G (in CDG1A; severe; dbSNP:rs80338704)"
FT /evidence="ECO:0000269|PubMed:11058895"
FT /id="VAR_006108"
FT VARIANT 192
FT /note="C -> G (in CDG1A; normal activity but lower affinity
FT for alpha-D-mannose 1-phosphate)"
FT /evidence="ECO:0000269|PubMed:10602363,
FT ECO:0000269|PubMed:11058895, ECO:0000269|PubMed:11058896"
FT /id="VAR_022496"
FT VARIANT 195
FT /note="H -> R (in CDG1A; dbSNP:rs1596489887)"
FT /evidence="ECO:0000269|PubMed:11058895"
FT /id="VAR_022497"
FT VARIANT 197
FT /note="E -> A (in dbSNP:rs34258285)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_022498"
FT VARIANT 206
FT /note="F -> S (in CDG1A)"
FT /evidence="ECO:0000269|PubMed:11058895"
FT /id="VAR_022499"
FT VARIANT 208
FT /note="G -> A (in CDG1A; dbSNP:rs398123309)"
FT /evidence="ECO:0000269|PubMed:10801058,
FT ECO:0000269|PubMed:11058895"
FT /id="VAR_006109"
FT VARIANT 212
FT /note="M -> V (in dbSNP:rs3743808)"
FT /id="VAR_022134"
FT VARIANT 214
FT /note="G -> S (in CDG1A; dbSNP:rs1555453238)"
FT /evidence="ECO:0000269|PubMed:12357336,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_022500"
FT VARIANT 216
FT /note="N -> I (in CDG1A; dbSNP:rs78290141)"
FT /evidence="ECO:0000269|PubMed:11058895"
FT /id="VAR_006110"
FT VARIANT 216
FT /note="N -> S (in CDG1A; dbSNP:rs78290141)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:11058896"
FT /id="VAR_022501"
FT VARIANT 217
FT /note="D -> E (in CDG1A; dbSNP:rs752614554)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:11058896"
FT /id="VAR_022502"
FT VARIANT 218
FT /note="H -> L (in CDG1A; dbSNP:rs80338705)"
FT /evidence="ECO:0000269|PubMed:11058895"
FT /id="VAR_022503"
FT VARIANT 223
FT /note="D -> E (in CDG1A; normal activity but lower affinity
FT for alpha-D-mannose 1-phosphate; dbSNP:rs104894531)"
FT /evidence="ECO:0000269|PubMed:10602363,
FT ECO:0000269|PubMed:11058895, ECO:0000269|PubMed:11058896,
FT ECO:0000269|PubMed:9781039"
FT /id="VAR_006111"
FT VARIANT 223
FT /note="D -> N (in CDG1A; dbSNP:rs201960869)"
FT /evidence="ECO:0000269|PubMed:12357336"
FT /id="VAR_022504"
FT VARIANT 226
FT /note="T -> S (in CDG1A; dbSNP:rs80338706)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_022505"
FT VARIANT 228
FT /note="G -> C (in CDG1A; dbSNP:rs558826439)"
FT /evidence="ECO:0000269|PubMed:11058895"
FT /id="VAR_022506"
FT VARIANT 228
FT /note="G -> R (in CDG1A; dbSNP:rs558826439)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:11058896"
FT /id="VAR_022507"
FT VARIANT 229
FT /note="Y -> S (in CDG1A; dbSNP:rs398123311)"
FT /evidence="ECO:0000269|PubMed:10066032,
FT ECO:0000269|PubMed:11058895"
FT /id="VAR_006112"
FT VARIANT 231
FT /note="V -> M (in CDG1A; dbSNP:rs80338707)"
FT /evidence="ECO:0000269|PubMed:10801058,
FT ECO:0000269|PubMed:11058895, ECO:0000269|PubMed:11058896,
FT ECO:0000269|PubMed:15844218, ECO:0000269|PubMed:17307006"
FT /id="VAR_006113"
FT VARIANT 233
FT /note="A -> T (in CDG1A; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:11058895"
FT /id="VAR_006114"
FT VARIANT 237
FT /note="T -> M (in CDG1A; dbSNP:rs80338708)"
FT /evidence="ECO:0000269|PubMed:10801058,
FT ECO:0000269|PubMed:11058895, ECO:0000269|PubMed:15844218"
FT /id="VAR_006115"
FT VARIANT 237
FT /note="T -> R (in CDG1A; loss of activity;
FT dbSNP:rs80338708)"
FT /evidence="ECO:0000269|PubMed:10602363,
FT ECO:0000269|PubMed:11058895, ECO:0000269|PubMed:11058896,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_022508"
FT VARIANT 238
FT /note="R -> G (in CDG1A)"
FT /evidence="ECO:0000269|PubMed:11058895"
FT /id="VAR_022509"
FT VARIANT 238
FT /note="R -> P (in CDG1A; dbSNP:rs151319324)"
FT /evidence="ECO:0000269|PubMed:10066032"
FT /id="VAR_006116"
FT VARIANT 241
FT /note="C -> S (in CDG1A; dbSNP:rs80338709)"
FT /evidence="ECO:0000269|PubMed:11058895,
FT ECO:0000269|PubMed:15844218"
FT /id="VAR_022510"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:7O58"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:7O58"
FT HELIX 26..36
FT /evidence="ECO:0007829|PDB:7O58"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:7O58"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:7O58"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:7O58"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:7O58"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:7O58"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:2AMY"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:2AMY"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:7O58"
FT HELIX 93..109
FT /evidence="ECO:0007829|PDB:7O58"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:7O58"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:7O58"
FT HELIX 138..151
FT /evidence="ECO:0007829|PDB:7O58"
FT HELIX 153..164
FT /evidence="ECO:0007829|PDB:7O58"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:7O58"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:7O58"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:7O58"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:7O58"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:7O58"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:7O58"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:7O58"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:7O58"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:7O58"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:7O58"
SQ SEQUENCE 246 AA; 28082 MW; 29F1D5B9539B6221 CRC64;
MAAPGPALCL FDVDGTLTAP RQKITKEMDD FLQKLRQKIK IGVVGGSDFE KVQEQLGNDV
VEKYDYVFPE NGLVAYKDGK LLCRQNIQSH LGEALIQDLI NYCLSYIAKI KLPKKRGTFI
EFRNGMLNVS PIGRSCSQEE RIEFYELDKK ENIRQKFVAD LRKEFAGKGL TFSIGGQISF
DVFPDGWDKR YCLRHVENDG YKTIYFFGDK TMPGGNDHEI FTDPRTMGYS VTAPEDTRRI
CELLFS
//
