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PMM2_HUMAN
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   03-AUG-2022, entry version 220.
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; 34.
DR   IntAct; O15305; 18.
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; O15305; -.
DR   PeptideAtlas; O15305; -.
DR   PRIDE; O15305; -.
DR   ProteomicsDB; 48574; -. [O15305-1]
DR   ProteomicsDB; 6798; -.
DR   Antibodypedia; 24552; 226 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   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; VCPIGRQ; -.
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; 159 hits in 1084 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 101 other 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; -; 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   PANTHER; PTHR10466; PTHR10466; 1.
DR   Pfam; PF03332; PMM; 1.
DR   SFLD; SFLDF00445; alpha-phosphomannomutase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 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:rs398123312)"
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; unknown pathological
FT                   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          6..14
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   TURN            15..17
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   HELIX           26..35
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   TURN            36..38
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   STRAND          39..44
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   HELIX           49..56
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   HELIX           60..63
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   STRAND          65..69
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:2AMY"
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:2AMY"
FT   HELIX           93..109
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   STRAND          119..123
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   STRAND          126..129
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   HELIX           138..151
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   HELIX           153..164
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   TURN            165..167
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   STRAND          170..175
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   TURN            176..178
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   STRAND          179..184
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   HELIX           189..195
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   TURN            196..198
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   STRAND          202..208
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   HELIX           219..222
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   STRAND          226..230
FT                   /evidence="ECO:0007829|PDB:2AMY"
FT   HELIX           234..244
FT                   /evidence="ECO:0007829|PDB:2AMY"
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
 
 
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