O15305 (PMM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphomannomutase 2
Short name=PMM 2
EC=5.4.2.8

Gene names

Name:

PMM2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	246 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions By similarity.
Catalytic activity	Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.
Pathway	Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm.
Involvement in disease	Congenital disorder of glycosylation 1A (CDG1A) [MIM:212065]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. Congenital disorder of glycosylation type 1A is an autosomal recessive disorder characterized by a severe encephalopathy with axial hypotonia, abnormal eye movement, and pronounced psychomotor retardation, as well as peripheral neuropathy, cerebellar hypoplasia, and retinitis pigmentosa. Patients show a peculiar distribution of subcutaneous fat, nipple retraction, and hypogonadism. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23
Sequence similarities	Belongs to the eukaryotic PMM family.
Biophysicochemical properties	Kinetic parameters: KM=16 µM for alpha-D-mannose 1-phosphate Ref.7 KM=13.5 µM for alpha-D-glucose 1-phosphate

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Disease	Congenital disorder of glycosylation Disease mutation
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GDP-mannose biosynthetic process Traceable author statement. Source: Reactome dolichol-linked oligosaccharide biosynthetic process Traceable author statement. Source: Reactome mannose biosynthetic process Inferred from electronic annotation. Source: InterPro post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome neuronal cell body Inferred from electronic annotation. Source: Compara
Molecular_function	phosphomannomutase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 246

246

Phosphomannomutase 2

PRO_0000199694

Sites

Active site

12

1

Nucleophile By similarity

Active site

14

1

By similarity

Active site

47

1

By similarity

Active site

189

1

By similarity

Binding site

21

1

Substrate By similarity

Binding site

123

1

Substrate By similarity

Binding site

134

1

Substrate By similarity

Binding site

141

1

Substrate By similarity

Binding site

179

1

Substrate By similarity

Binding site

181

1

Substrate By similarity

Natural variations

Natural variant

9

1

C → Y in CDG1A. Ref.17 Ref.18 Ref.22

VAR_022469

Natural variant

11

1

F → C in CDG1A. Ref.17 Ref.18

VAR_022470

Natural variant

15

1

G → E in CDG1A. Ref.21

VAR_022471

Natural variant

20

1

P → S in CDG1A; reduction of activity. Ref.22

VAR_022472

Natural variant

32

1

L → R in CDG1A. Ref.17 Ref.22

VAR_022473

Natural variant

37

1

Q → H in CDG1A; partial loss of activity. Ref.22

VAR_022474

Natural variant

37

1

Q → L.
Corresponds to variant rs2304472 [ dbSNP | Ensembl ].

VAR_022133

Natural variant

42

1

G → R. Ref.21 Ref.22

VAR_022475

Natural variant

44

1

V → A in CDG1A. Ref.17 Ref.23

VAR_006093

Natural variant

44

1

V → L in CDG1A. Ref.22

VAR_022563

Natural variant

64

1

Y → C in CDG1A. Ref.21

VAR_022476

Natural variant

65

1

D → Y in CDG1A. Ref.17 Ref.22

VAR_006094

Natural variant

67

1

V → M in CDG1A. Ref.17 Ref.18

VAR_022477

Natural variant

69

1

P → S in CDG1A. Ref.17 Ref.22

VAR_022478

Natural variant

76

1

Y → C in CDG1A. Ref.17

VAR_022479

Natural variant

93

1

E → A in CDG1A. Ref.21

VAR_022480

Natural variant

101

1

N → K in CDG1A. Ref.17

VAR_006095

Natural variant

103

1

C → F in CDG1A. Ref.17 Ref.22

VAR_022481

Natural variant

104

1

L → V in CDG1A. Ref.20

VAR_012344

Natural variant

106

1

Y → C in CDG1A. Ref.17

VAR_006096

Natural variant

108

1

A → V in CDG1A. Ref.17 Ref.22

VAR_006097

Natural variant

113

1

P → L in CDG1A. Ref.17 Ref.18 Ref.22

VAR_006098

Natural variant

117

1

G → R in CDG1A; loss of activity. Ref.13 Ref.15 Ref.17 Ref.18

VAR_006099

Natural variant

119

1

F → L in CDG1A; partial loss of activity. Ref.15 Ref.17 Ref.18 Ref.19 Ref.22

VAR_006100

Natural variant

120

1

I → T in CDG1A. Ref.17

VAR_022482

Natural variant

123

1

R → Q in CDG1A. Ref.17 Ref.18 Ref.22

VAR_006101

Natural variant

129

1

V → M in CDG1A. Ref.17 Ref.18 Ref.22
Corresponds to variant rs28938475 [ dbSNP | Ensembl ].

VAR_006102

Natural variant

131

1

P → A in CDG1A. Ref.17 Ref.22

VAR_006103

Natural variant

132

1

I → F in CDG1A; slightly reduced activity. Ref.22

VAR_022483

Natural variant

132

1

I → N in CDG1A. Ref.17 Ref.19

VAR_022484

Natural variant

132

1

I → T in CDG1A. Ref.17 Ref.22

VAR_006104

Natural variant

139

1

E → K in CDG1A; this mutation seems to disrupt a splicing enhancer sequence and thus results in most cases in a protein with exon 5 skipped; slightly reduced activity. Ref.16 Ref.17 Ref.22

VAR_009232

Natural variant

141

1

R → C in CDG1A; loss of activity. Ref.22

VAR_022485

Natural variant

141

1

R → H in CDG1A; frequent mutation; loss of activity; observed in heterozygous patients; homozygosis of this mutation is incompatible with life. Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.22
Corresponds to variant rs28936415 [ dbSNP | Ensembl ].

VAR_006105

Natural variant

144

1

F → L in CDG1A. Ref.14

VAR_022486

Natural variant

148

1

D → N in CDG1A. Ref.17 Ref.19

VAR_022487

Natural variant

151

1

E → G in CDG1A. Ref.17

VAR_022488

Natural variant

153

1

I → T in CDG1A. Ref.17 Ref.22

VAR_022489

Natural variant

157

1

F → S in CDG1A. Ref.17 Ref.22

VAR_022490

Natural variant

162

1

R → W in CDG1A. Ref.17 Ref.22

VAR_006106

Natural variant

172

1

F → V in CDG1A. Ref.17 Ref.18

VAR_022491

Natural variant

175

1

G → R in CDG1A. Ref.17 Ref.18

VAR_006107

Natural variant

176

1

G → V in CDG1A; loss of activity. Ref.22

VAR_022492

Natural variant

177

1

Q → H in CDG1A; partial loss of activity. Ref.22

VAR_022493

Natural variant

183

1

F → S in CDG1A. Ref.17 Ref.18 Ref.19

VAR_022494

Natural variant

185

1

D → G in CDG1A. Ref.17 Ref.18

VAR_022495

Natural variant

188

1

D → G in CDG1A; severe. Ref.17

VAR_006108

Natural variant

192

1

C → G in CDG1A; normal activity but lower affinity for alpha-D-mannose 1-phosphate. Ref.15 Ref.17 Ref.18

VAR_022496

Natural variant

195

1

H → R in CDG1A. Ref.17

VAR_022497

Natural variant

197

1

E → A in CDG1A. Ref.17 Ref.22
Corresponds to variant rs34258285 [ dbSNP | Ensembl ].

VAR_022498

Natural variant

206

1

F → S in CDG1A. Ref.17

VAR_022499

Natural variant

208

1

G → A in CDG1A. Ref.17 Ref.19

VAR_006109

Natural variant

212

1

M → V.
Corresponds to variant rs3743808 [ dbSNP | Ensembl ].

VAR_022134

Natural variant

214

1

G → S in CDG1A. Ref.21 Ref.22

VAR_022500

Natural variant

216

1

N → I in CDG1A. Ref.17

VAR_006110

Natural variant

216

1

N → S in CDG1A. Ref.17 Ref.18

VAR_022501

Natural variant

217

1

D → E in CDG1A. Ref.17 Ref.18

VAR_022502

Natural variant

218

1

H → L in CDG1A. Ref.17

VAR_022503

Natural variant

223

1

D → E in CDG1A; normal activity but lower affinity for alpha-D-mannose 1-phosphate. Ref.13 Ref.15 Ref.17 Ref.18

VAR_006111

Natural variant

223

1

D → N in CDG1A. Ref.21

VAR_022504

Natural variant

226

1

T → S in CDG1A. Ref.17 Ref.22

VAR_022505

Natural variant

228

1

G → C in CDG1A. Ref.17

VAR_022506

Natural variant

228

1

G → R in CDG1A. Ref.17 Ref.18

VAR_022507

Natural variant

229

1

Y → S in CDG1A. Ref.14 Ref.17

VAR_006112

Natural variant

231

1

V → M in CDG1A. Ref.17 Ref.18 Ref.19 Ref.22 Ref.23

VAR_006113

Natural variant

233

1

A → T in CDG1A; could be a rare polymorphism. Ref.17

VAR_006114

Natural variant

237

1

T → M in CDG1A. Ref.17 Ref.19 Ref.22

VAR_006115

Natural variant

237

1

T → R in CDG1A; loss of activity. Ref.15 Ref.17 Ref.18 Ref.22

VAR_022508

Natural variant

238

1

R → G in CDG1A. Ref.17

VAR_022509

Natural variant

238

1

R → P in CDG1A. Ref.14

VAR_006116

Natural variant

241

1

C → S in CDG1A. Ref.17 Ref.22

VAR_022510

Secondary structure

1

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246

Helix Strand Turn

Details...

Beta strand

6 – 14

9

Turn

15 – 17

3

Helix

26 – 35

10

Turn

36 – 38

3

Beta strand

39 – 44

6

Helix

49 – 56

8

Helix

60 – 63

4

Beta strand

65 – 69

5

Helix

70 – 72

3

Beta strand

74 – 77

4

Beta strand

80 – 84

5

Helix

87 – 91

5

Helix

93 – 109

17

Beta strand

119 – 123

5

Beta strand

126 – 129

4

Helix

138 – 151

14

Helix

153 – 164

12

Turn

165 – 167

3

Beta strand

170 – 175

6

Turn

176 – 178

3

Beta strand

179 – 184

6

Helix

189 – 195

7

Turn

196 – 198

3

Beta strand

202 – 208

7

Helix

219 – 222

4

Beta strand

226 – 230

5

Helix

234 – 244

11

Sequences

	Sequence		Length	Mass (Da)
	O15305 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 29F1D5B9539B6221	FASTA	246	28,082
	10 20 30 40 50 60 MAAPGPALCL FDVDGTLTAP RQKITKEMDD FLQKLRQKIK IGVVGGSDFE KVQEQLGNDV 70 80 90 100 110 120 VEKYDYVFPE NGLVAYKDGK LLCRQNIQSH LGEALIQDLI NYCLSYIAKI KLPKKRGTFI 130 140 150 160 170 180 EFRNGMLNVS PIGRSCSQEE RIEFYELDKK ENIRQKFVAD LRKEFAGKGL TFSIGGQISF 190 200 210 220 230 240 DVFPDGWDKR YCLRHVENDG YKTIYFFGDK TMPGGNDHEI FTDPRTMGYS VTAPEDTRRI CELLFS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mutations in PMM2, a phosphomannomutase gene on chromosome 16p13, in carbohydrate-deficient glycoprotein type I syndrome (Jaeken syndrome)." Matthijs G., Schollen E., Pardon E., Veiga-Da-Cunha M., Jaeken J., Cassiman J.-J., van Schaftingen E. Nat. Genet. 16:88-92(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS CDG1A.
[2]	Erratum Matthijs G., Schollen E., Pardon E., Veiga-Da-Cunha M., Jaeken J., Cassiman J.-J., van Schaftingen E. Nat. Genet. 16:316-316(1997)
[3]	"Comparative analysis of the phosphomannomutase genes PMM1, PMM2 and PMM2psi: the sequence variation in the processed pseudogene is a reflection of the mutations found in the functional gene." Schollen E., Pardon E., Heykants L., Renard J., Doggett N.A., Callen D.F., Cassiman J.J., Matthijs G. Hum. Mol. Genet. 7:157-164(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas.
[7]	"The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a." Silvaggi N.R., Zhang C., Lu Z., Dai J., Dunaway-Mariano D., Allen K.N. J. Biol. Chem. 281:14918-14926(2006) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"Ensemble refinement of protein crystal structures: validation and application." Levin E.J., Kondrashov D.A., Wesenberg G.E., Phillips G.N. Jr. Structure 15:1040-1052(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS).
[10]	"X-ray structure of human phosphomannomutase 2 (PMM2)." Center for eukaryotic structural genomics (CESG) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS).
[11]	"Phosphomannomutase deficiency: the molecular basis of the classical Jaeken syndrome (CDGS type Ia)." Matthijs G., Schollen E., Heykants L., Gruenewald S. Mol. Genet. Metab. 68:220-226(1999) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS CDG1A.
[12]	"Lack of homozygotes for the most frequent disease allele in carbohydrate-deficient glycoprotein syndrome type 1A." Matthijs G., Schollen E., van Schaftingen E., Cassiman J.-J., Jaeken J. Am. J. Hum. Genet. 62:542-550(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CDG1A.
[13]	"Absence of homozygosity for predominant mutations in PMM2 in Danish patients with carbohydrate-deficient glycoprotein syndrome type 1." Kjaergaard S., Skovby F., Schwartz M. Eur. J. Hum. Genet. 6:331-336(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CDG1A ARG-117 AND GLU-223.
[14]	"Missense mutations in phosphomannomutase 2 gene in two Japanese families with carbohydrate-deficient glycoprotein syndrome type 1." Kondo I., Mizugishi K., Yoneda Y., Hashimoto T., Kuwajima K., Yuasa I., Shigemoto K., Kuroda Y. Clin. Genet. 55:50-54(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CDG1A LEU-144; SER-229 AND PRO-238.
[15]	"Carbohydrate-deficient glycoprotein syndrome type 1A: expression and characterisation of wild type and mutant PMM2 in E. coli." Kjaergaard S., Skovby F., Schwartz M. Eur. J. Hum. Genet. 7:884-888(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CDG1A GLY-192, CHARACTERIZATION OF VARIANTS CDG1A ARG-117; LEU-119; HIS-141; GLY-192; GLU-223 AND ARG-237.
[16]	"Characterization of the 415G>A (E139K) PMM2 mutation in carbohydrate-deficient glycoprotein syndrome type Ia disrupting a splicing enhancer resulting in exon 5 skipping." Vuillaumier-Barrot S., Barnier A., Cuer M., Durand G., Grandchamp B., Seta N. Hum. Mutat. 14:543-544(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CDG1A LYS-139 AND HIS-141.
[17]	"Mutations in PMM2 that cause congenital disorders of glycosylation, type Ia (CDG-Ia)." Matthijs G., Schollen E., Bjursell C., Erlandson A., Freeze H., Imtiaz F., Kjaergaard S., Martinsson T., Schwartz M., Seta N., Vuillaumier-Barrot S., Westphal V., Winchester B. Hum. Mutat. 16:386-394(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CDG1A TYR-9; CYS-11; ARG-32; ALA-44; TYR-65; MET-67; SER-69; CYS-76; LYS-101; PHE-103; CYS-106; VAL-108; LEU-113; ARG-117; LEU-119; THR-120; GLN-123; MET-129; ALA-131; ASN-132; THR-132; LYS-139; HIS-141; ASN-148; GLY-151; THR-153; SER-157; TRP-162; VAL-172; ARG-175; SER-183; GLY-185; GLY-188; GLY-192; ARG-195; ALA-197; SER-206; ALA-208; ILE-216; SER-216; GLU-217; LEU-218; GLU-223; SER-226; ARG-228; CYS-228; SER-229; MET-231; THR-233; ARG-237; MET-237; GLY-238 AND SER-241.
[18]	"PMM2 mutation spectrum, including 10 novel mutations, in a large CDG type 1A family material with a focus on Scandinavian families." Bjursell C., Erlandson A., Nordling M., Nilsson S., Wahlstroem J., Stibler H., Kristiansson B., Martinsson T. Hum. Mutat. 16:395-400(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CDG1A TYR-9; CYS-11; MET-67; LEU-113; ARG-117; LEU-119; GLN-123; MET-129; HIS-141; VAL-172; ARG-175; SER-183; GLY-185; GLY-192; SER-216; GLU-217; GLU-223; ARG-228; MET-231 AND ARG-237.
[19]	"Genotypes and phenotypes of patients in the UK with carbohydrate-deficient glycoprotein syndrome type 1." Imtiaz F., Worthington V., Champion M., Beesley C., Charlwood J., Clayton P., Keir G., Mian N., Winchester B. J. Inherit. Metab. Dis. 23:162-174(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CDG1A LEU-119; ASN-132; HIS-141; ASN-148; SER-183; ALA-208; MET-231 AND MET-237.
[20]	"Functional analysis of novel mutations in a congenital disorder of glycosylation Ia patient with mixed Asian ancestry." Westphal V., Enns G.M., McCracken M.F., Freeze H.H. Mol. Genet. Metab. 73:71-76(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CDG1A VAL-104.
[21]	"DHPLC analysis as a platform for molecular diagnosis of congenital disorders of glycosylation (CDG)." Schollen E., Martens K., Geuzens E., Matthijs G. Eur. J. Hum. Genet. 10:643-648(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CDG1A GLU-15; CYS-64; ALA-93; SER-214 AND ASN-223, VARIANT ARG-42.
[22]	"A new insight into PMM2 mutations in the French population." Le Bizec C., Vuillaumier-Barrot S., Barnier A., Dupre T., Durand G., Seta N. Hum. Mutat. 25:504-505(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CDG1A TYR-9; SER-20; ARG-32; HIS-37; LEU-44; TYR-65; SER-69; PHE-103; VAL-108; LEU-113; LEU-119; GLN-123; MET-129; ALA-131; THR-132; PHE-132; LYS-139; CYS-141; HIS-141; THR-153; SER-157; TRP-162; VAL-176; HIS-177; ALA-197; SER-214; SER-226; MET-231; ARG-237; MET-237 AND SER-241, VARIANT ARG-42, CHARACTERIZATION OF VARIANTS CDG1A SER-20; HIS-37; PHE-132; LYS-139; CYS-141; HIS-141; VAL-176 AND HIS-177.
[23]	"Characterization of two unusual truncating PMM2 mutations in two CDG-Ia patients." Schollen E., Keldermans L., Foulquier F., Briones P., Chabas A., Sanchez-Valverde F., Adamowicz M., Pronicka E., Wevers R., Matthijs G. Mol. Genet. Metab. 90:408-413(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CDG1A ALA-44 AND MET-231.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U85773 mRNA. Translation: AAC51368.1.
AF157796 , AF157790, AF157791, AF157792, AF157793, AF157794, AF157795 Genomic DNA. Translation: AAD45895.1.
AK291537 mRNA. Translation: BAF84226.1.
CH471112 Genomic DNA. Translation: EAW85202.1.
CH471112 Genomic DNA. Translation: EAW85203.1.
BC008310 mRNA. Translation: AAH08310.1.

IPI

IPI00006092.

RefSeq

NP_000294.1. NM_000303.2.

UniGene

Hs.625732.
Hs.738850.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AMY	X-ray	2.09	A	2-246	[»]
2Q4R	X-ray	2.09	A	2-246	[»]

ProteinModelPortal

O15305.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000268261.

PTM databases

PhosphoSite

O15305.

Proteomic databases

PaxDb

O15305.

PeptideAtlas

O15305.

PRIDE

O15305.

Protocols and materials databases

DNASU

5373.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000268261; ENSP00000268261; ENSG00000140650.

GeneID

5373.

KEGG

hsa:5373.

UCSC

uc002czf.4. human.

Organism-specific databases

CTD

5373.

GeneCards

GC16P008799.

HGNC

HGNC:9115. PMM2.

HPA

HPA040852.

MIM

212065. phenotype.
601785. gene.

neXtProt

NX_O15305.

Orphanet

79318. CDG syndrome type Ia.

PharmGKB

PA33441.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0561.

HOGENOM

HOG000181843.

HOVERGEN

HBG009971.

InParanoid

O15305.

KO

K01840.

OMA

EFERYDK.

OrthoDB

EOG4894NB.

Enzyme and pathway databases

BRENDA

5.4.2.8. 2681.

Reactome

REACT_17015. Metabolism of proteins.

SABIO-RK

O15305.

UniPathway

UPA00126; UER00424.

Gene expression databases

ArrayExpress

O15305.

Bgee

O15305.

CleanEx

HS_PMM2.

Genevestigator

O15305.

GermOnline

ENSG00000140650. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.1000. 2 hits.

InterPro

IPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR005002. PMM.
[Graphical view]

PANTHER

PTHR10466. PTHR10466. 1 hit.

Pfam

PF03332. PMM. 1 hit.
[Graphical view]

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR01484. HAD-SF-IIB. 1 hit.

ProtoNet

Search...

Other

BindingDB

O15305.

ChEMBL

CHEMBL1741162.

ChiTaRS

PMM2. human.

EvolutionaryTrace

O15305.

GenomeRNAi

5373.

NextBio

20846.

SOURCE

Search...

Entry information

Entry name

PMM2_HUMAN

Accession

Primary (citable) accession number: O15305
Secondary accession number(s): A8K672, D3DUF3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 141 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.