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O15305 (PMM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphomannomutase 2

Short name=PMM 2
EC=5.4.2.8
Gene names
Name:PMM2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 246245Phosphomannomutase 2
PRO_0000199694

Sites

Active site121Nucleophile By similarity
Active site141Proton donor/acceptor Potential
Binding site211Substrate By similarity
Binding site1231Substrate By similarity
Binding site1341Substrate By similarity
Binding site1411Substrate By similarity
Binding site1791Substrate By similarity
Binding site1811Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.10
Modified residue1491N6-acetyllysine By similarity

Natural variations

Natural variant91C → Y in CDG1A. Ref.19 Ref.20 Ref.24
VAR_022469
Natural variant111F → C in CDG1A. Ref.19 Ref.20
VAR_022470
Natural variant151G → E in CDG1A. Ref.23
VAR_022471
Natural variant201P → S in CDG1A; reduction of activity. Ref.24
VAR_022472
Natural variant321L → R in CDG1A. Ref.19 Ref.24
VAR_022473
Natural variant371Q → H in CDG1A; partial loss of activity. Ref.24
VAR_022474
Natural variant371Q → L.
Corresponds to variant rs2304472 [ dbSNP | Ensembl ].
VAR_022133
Natural variant421G → R. Ref.23 Ref.24
VAR_022475
Natural variant441V → A in CDG1A. Ref.19 Ref.25
VAR_006093
Natural variant441V → L in CDG1A. Ref.24
VAR_022563
Natural variant641Y → C in CDG1A. Ref.23
VAR_022476
Natural variant651D → Y in CDG1A. Ref.19 Ref.24
VAR_006094
Natural variant671V → M in CDG1A. Ref.19 Ref.20
VAR_022477
Natural variant691P → S in CDG1A. Ref.19 Ref.24
VAR_022478
Natural variant761Y → C in CDG1A. Ref.19
VAR_022479
Natural variant931E → A in CDG1A. Ref.23
VAR_022480
Natural variant1011N → K in CDG1A. Ref.19
VAR_006095
Natural variant1031C → F in CDG1A. Ref.19 Ref.24
VAR_022481
Natural variant1041L → V in CDG1A. Ref.22
VAR_012344
Natural variant1061Y → C in CDG1A. Ref.19
VAR_006096
Natural variant1081A → V in CDG1A. Ref.19 Ref.24
VAR_006097
Natural variant1131P → L in CDG1A. Ref.19 Ref.20 Ref.24
VAR_006098
Natural variant1171G → R in CDG1A; loss of activity. Ref.15 Ref.17 Ref.19 Ref.20
VAR_006099
Natural variant1191F → L in CDG1A; partial loss of activity. Ref.17 Ref.19 Ref.20 Ref.21 Ref.24
VAR_006100
Natural variant1201I → T in CDG1A. Ref.19
VAR_022482
Natural variant1231R → Q in CDG1A. Ref.19 Ref.20 Ref.24
VAR_006101
Natural variant1291V → M in CDG1A. Ref.19 Ref.20 Ref.24
Corresponds to variant rs28938475 [ dbSNP | Ensembl ].
VAR_006102
Natural variant1311P → A in CDG1A. Ref.19 Ref.24
VAR_006103
Natural variant1321I → F in CDG1A; slightly reduced activity. Ref.24
VAR_022483
Natural variant1321I → N in CDG1A. Ref.19 Ref.21
VAR_022484
Natural variant1321I → T in CDG1A. Ref.19 Ref.24
VAR_006104
Natural variant1391E → 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.18 Ref.19 Ref.24
VAR_009232
Natural variant1411R → C in CDG1A; loss of activity. Ref.24
VAR_022485
Natural variant1411R → H in CDG1A; frequent mutation; loss of activity; observed in heterozygous patients; homozygosis of this mutation is incompatible with life. Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.24
Corresponds to variant rs28936415 [ dbSNP | Ensembl ].
VAR_006105
Natural variant1441F → L in CDG1A. Ref.16
Corresponds to variant rs150719105 [ dbSNP | Ensembl ].
VAR_022486
Natural variant1481D → N in CDG1A. Ref.19 Ref.21
VAR_022487
Natural variant1511E → G in CDG1A. Ref.19
VAR_022488
Natural variant1531I → T in CDG1A. Ref.19 Ref.24
VAR_022489
Natural variant1571F → S in CDG1A. Ref.19 Ref.24
Corresponds to variant rs190521996 [ dbSNP | Ensembl ].
VAR_022490
Natural variant1621R → W in CDG1A. Ref.19 Ref.24
VAR_006106
Natural variant1721F → V in CDG1A. Ref.19 Ref.20
VAR_022491
Natural variant1751G → R in CDG1A. Ref.19 Ref.20
VAR_006107
Natural variant1761G → V in CDG1A; loss of activity. Ref.24
VAR_022492
Natural variant1771Q → H in CDG1A; partial loss of activity. Ref.24
VAR_022493
Natural variant1831F → S in CDG1A. Ref.19 Ref.20 Ref.21
VAR_022494
Natural variant1851D → G in CDG1A. Ref.19 Ref.20
VAR_022495
Natural variant1881D → G in CDG1A; severe. Ref.19
VAR_006108
Natural variant1921C → G in CDG1A; normal activity but lower affinity for alpha-D-mannose 1-phosphate. Ref.17 Ref.19 Ref.20
VAR_022496
Natural variant1951H → R in CDG1A. Ref.19
VAR_022497
Natural variant1971E → A in CDG1A. Ref.19 Ref.24
Corresponds to variant rs34258285 [ dbSNP | Ensembl ].
VAR_022498
Natural variant2061F → S in CDG1A. Ref.19
VAR_022499
Natural variant2081G → A in CDG1A. Ref.19 Ref.21
VAR_006109
Natural variant2121M → V.
Corresponds to variant rs3743808 [ dbSNP | Ensembl ].
VAR_022134
Natural variant2141G → S in CDG1A. Ref.23 Ref.24
VAR_022500
Natural variant2161N → I in CDG1A. Ref.19
Corresponds to variant rs78290141 [ dbSNP | Ensembl ].
VAR_006110
Natural variant2161N → S in CDG1A. Ref.19 Ref.20
Corresponds to variant rs78290141 [ dbSNP | Ensembl ].
VAR_022501
Natural variant2171D → E in CDG1A. Ref.19 Ref.20
VAR_022502
Natural variant2181H → L in CDG1A. Ref.19
VAR_022503
Natural variant2231D → E in CDG1A; normal activity but lower affinity for alpha-D-mannose 1-phosphate. Ref.15 Ref.17 Ref.19 Ref.20
VAR_006111
Natural variant2231D → N in CDG1A. Ref.23
VAR_022504
Natural variant2261T → S in CDG1A. Ref.19 Ref.24
VAR_022505
Natural variant2281G → C in CDG1A. Ref.19
VAR_022506
Natural variant2281G → R in CDG1A. Ref.19 Ref.20
VAR_022507
Natural variant2291Y → S in CDG1A. Ref.16 Ref.19
VAR_006112
Natural variant2311V → M in CDG1A. Ref.19 Ref.20 Ref.21 Ref.24 Ref.25
VAR_006113
Natural variant2331A → T in CDG1A; unknown pathological significance. Ref.19
VAR_006114
Natural variant2371T → M in CDG1A. Ref.19 Ref.21 Ref.24
Corresponds to variant rs80338708 [ dbSNP | Ensembl ].
VAR_006115
Natural variant2371T → R in CDG1A; loss of activity. Ref.17 Ref.19 Ref.20 Ref.24
Corresponds to variant rs80338708 [ dbSNP | Ensembl ].
VAR_022508
Natural variant2381R → G in CDG1A. Ref.19
VAR_022509
Natural variant2381R → P in CDG1A. Ref.16
VAR_006116
Natural variant2411C → S in CDG1A. Ref.19 Ref.24
VAR_022510

Secondary structure

............................................... 246
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O15305 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 29F1D5B9539B6221

FASTA24628,082
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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).
[12]"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).
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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.
[24]"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.
[25]"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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U85773 mRNA. Translation: AAC51368.1.
AF157796 expand/collapse EMBL AC list , 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.
RefSeqNP_000294.1. NM_000303.2.
UniGeneHs.625732.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AMYX-ray2.09A2-246[»]
2Q4RX-ray2.09A2-246[»]
ProteinModelPortalO15305.
SMRO15305. Positions 4-246.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111386. 3 interactions.
STRING9606.ENSP00000268261.

Chemistry

BindingDBO15305.
ChEMBLCHEMBL1741162.

PTM databases

PhosphoSiteO15305.

Proteomic databases

PaxDbO15305.
PeptideAtlasO15305.
PRIDEO15305.

Protocols and materials databases

DNASU5373.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000268261; ENSP00000268261; ENSG00000140650.
GeneID5373.
KEGGhsa:5373.
UCSCuc002czf.4. human.

Organism-specific databases

CTD5373.
GeneCardsGC16P008799.
HGNCHGNC:9115. PMM2.
HPAHPA040852.
MIM212065. phenotype.
601785. gene.
neXtProtNX_O15305.
Orphanet79318. PMM2-CDG.
PharmGKBPA33441.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0561.
HOGENOMHOG000181843.
HOVERGENHBG009971.
InParanoidO15305.
KOK17497.
OMATYCLQHV.
PhylomeDBO15305.
TreeFamTF300874.

Enzyme and pathway databases

BRENDA5.4.2.8. 2681.
ReactomeREACT_17015. Metabolism of proteins.
SABIO-RKO15305.
UniPathwayUPA00126; UER00424.

Gene expression databases

ArrayExpressO15305.
BgeeO15305.
CleanExHS_PMM2.
GenevestigatorO15305.

Family and domain databases

Gene3D3.40.50.1000. 2 hits.
InterProIPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR005002. PMM.
[Graphical view]
PANTHERPTHR10466. PTHR10466. 1 hit.
PfamPF03332. PMM. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01484. HAD-SF-IIB. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPMM2. human.
EvolutionaryTraceO15305.
GeneWikiPMM2.
GenomeRNAi5373.
NextBio20846.
PROO15305.
SOURCESearch...

Entry information

Entry namePMM2_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM