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Q9Y223 (GLCNE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Alternative name(s):
UDP-GlcNAc-2-epimerase/ManAc kinase

Including the following 2 domains:

  1. UDP-N-acetylglucosamine 2-epimerase (hydrolyzing)
    EC=3.2.1.183
    Alternative name(s):
    UDP-GlcNAc-2-epimerase
    Uridine diphosphate-N-acetylglucosamine-2-epimerase
  2. N-acetylmannosamine kinase
    EC=2.7.1.60
    Alternative name(s):
    ManAc kinase
Gene names
Name:GNE
Synonyms:GLCNE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length722 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. Plays an essential role in early development By similarity. Required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. Ref.12

Catalytic activity

UDP-N-acetyl-alpha-D-glucosamine + H2O = N-acetyl-D-mannosamine + UDP.

ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-mannosamine 6-phosphate.

Enzyme regulation

Allosterically regulated Probable; feedback inhibited by cytidine monophosphate-N-acetylneuraminic acid (CMP-Neu5Ac), the end product of neuraminic acid biosynthesis. Activity is dependent on oligomerization. The monomer is inactive, whereas the dimer catalyzes only the phosphorylation of N-acetylmannosamine; the hexamer is fully active for both enzyme activities By similarity. Up-regulated after PKC-dependent phosphorylation. Ref.11

Pathway

Amino-sugar metabolism; N-acetylneuraminate biosynthesis.

Subunit structure

Homodimer and homohexamer. Ref.14 Ref.15

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Highest expression in liver and placenta. Also found in heart, brain, lung, kidney, skeletal muscle and pancreas. Isoform 1 is expressed in heart, brain, kidney, liver, placenta, lung, spleen, pancreas, skeletal muscle and colon. Isoform 2 is expressed mainly in placenta, but also in brain, kidney, liver, lung, pancreas and colon. Isoform 3 is expressed at low level in kidney, liver, placenta and colon. Ref.1 Ref.2 Ref.7

Post-translational modification

Phosphorylated by PKC By similarity.

Involvement in disease

Sialuria (SIALURIA) [MIM:269921]: In sialuria, free sialic acid accumulates in the cytoplasm and gram quantities of neuraminic acid are secreted in the urine. The metabolic defect involves lack of feedback inhibition of UDP-GlcNAc 2-epimerase by CMP-Neu5Ac, resulting in constitutive overproduction of free Neu5Ac. Clinical features include variable degrees of developmental delay, coarse facial features and hepatomegaly. Sialuria inheritance is autosomal dominant.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.11 Ref.16 Ref.17

Inclusion body myopathy 2 (IBM2) [MIM:600737]: Hereditary inclusion body myopathies are a group of neuromuscular disorders characterized by adult onset, slowly progressive distal and proximal weakness and a typical muscle pathology including rimmed vacuoles and filamentous inclusions. IBM2 is an autosomal recessive disorder affecting mainly leg muscles, but with an unusual distribution that spares the quadriceps as also observed in Nonaka myopathy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.21 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29

Nonaka myopathy (NM) [MIM:605820]: Autosomal recessive muscular disorder, allelic to inclusion body myopathy 2. It is characterized by weakness of the anterior compartment of the lower limbs with onset in early adulthood, and sparing of the quadriceps muscles. As the inclusion body myopathy, NM is histologically characterized by the presence of numerous rimmed vacuoles without inflammatory changes in muscle specimens.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19 Ref.20 Ref.22 Ref.23 Ref.28

Sequence similarities

In the N-terminal section; belongs to the UDP-N-acetylglucosamine 2-epimerase family.

In the C-terminal section; belongs to the ROK (NagC/XylR) family.

Sequence caution

The sequence BAH12414.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionHydrolase
Kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processN-acetylglucosamine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

N-acetylneuraminate biosynthetic process

Inferred from electronic annotation. Source: InterPro

N-acetylneuraminate metabolic process

Traceable author statement PubMed 9305888. Source: ProtInc

UDP-N-acetylglucosamine metabolic process

Inferred from electronic annotation. Source: InterPro

carbohydrate phosphorylation

Traceable author statement PubMed 9305888. Source: GOC

cell adhesion

Traceable author statement Ref.12. Source: ProtInc

lipopolysaccharide biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Traceable author statement PubMed 9305888. Source: ProtInc

cytosol

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

N-acylmannosamine kinase activity

Traceable author statement PubMed 9305888. Source: ProtInc

UDP-N-acetylglucosamine 2-epimerase activity

Traceable author statement Ref.2. Source: ProtInc

hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y223-1)

Also known as: GNE1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9Y223-2)

Also known as: GNE2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → METYGYLQRESCFQGPHELYFKNLSKRNKQIM
Isoform 3 (identifier: Q9Y223-3)

Also known as: GNE3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: MEKNGNNRKL...LGSHLIDDYG → MPIGDCSVAA...RGSHAFKDLI
Isoform 4 (identifier: Q9Y223-4)

The sequence of this isoform differs from the canonical sequence as follows:
     471-544: Missing.
Isoform 5 (identifier: Q9Y223-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: Missing.
     206-256: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 722722Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
PRO_0000095716

Regions

Nucleotide binding411 – 42010ATP
Nucleotide binding543 – 55210ATP
Region1 – ?UDP-N-acetylglucosamine 2-epimerase
Region406 – 722317N-acetylmannosamine kinase

Sites

Active site5171 Ref.15
Metal binding5691Zinc
Metal binding5791Zinc
Metal binding5811Zinc
Metal binding5861Zinc
Binding site4771Substrate
Binding site4891Substrate
Binding site5171Substrate
Binding site5661Substrate
Binding site5691Substrate
Binding site5881Substrate

Natural variations

Alternative sequence1 – 5959Missing in isoform 5.
VSP_043975
Alternative sequence1 – 5555MEKNG…IDDYG → MPIGDCSVAAKPRKQLLCSL FQTTLGYRARASGWKPMVIC RGSHAFKDLI in isoform 3.
VSP_041028
Alternative sequence11M → METYGYLQRESCFQGPHELY FKNLSKRNKQIM in isoform 2.
VSP_041027
Alternative sequence206 – 25651Missing in isoform 5.
VSP_043976
Alternative sequence471 – 54474Missing in isoform 4.
VSP_043474
Natural variant271P → S in IBM2. Ref.29
VAR_021771
Natural variant361P → L in IBM2. Ref.26
VAR_017945
Natural variant1321H → Q in NM. Ref.23
VAR_021772
Natural variant1621R → C in IBM2. Ref.27
VAR_021773
Natural variant1711M → V in IBM2. Ref.25
VAR_021774
Natural variant1761D → V in NM. Ref.23
Corresponds to variant rs139425890 [ dbSNP | Ensembl ].
VAR_021775
Natural variant1771R → C in NM. Ref.23
VAR_021776
Natural variant2001I → F in IBM2. Ref.26
VAR_017946
Natural variant2061G → S in IBM2; moderate phenotype with unusual involvement of quadriceps. Ref.29
VAR_021777
Natural variant2161V → A in IBM2. Ref.24
VAR_021778
Natural variant2251D → N in IBM2. Ref.18 Ref.21 Ref.26
VAR_017947
Natural variant2461R → Q in IBM2. Ref.18 Ref.21 Ref.26 Ref.29
VAR_017948
Natural variant2461R → W in IBM2. Ref.21
VAR_017949
Natural variant2631R → L in SIALURIA; strong reduction of feedback inhibition by CMP-Neu5Ac. Ref.2
VAR_017950
Natural variant2661R → Q in SIALURIA; abolishes feedback inhibition by CMP-Neu5Ac. Ref.2 Ref.16 Ref.17
VAR_017951
Natural variant2661R → W in sialuria. Ref.2
VAR_017952
Natural variant3031C → V in IBM2; requires 2 nucleotide substitutions. Ref.26
VAR_017953
Natural variant3061R → Q in NM. Ref.23
VAR_021779
Natural variant3311V → A in NM. Ref.23
VAR_021780
Natural variant3781D → Y in IBM2 and NM. Ref.23 Ref.26
VAR_017954
Natural variant4601A → V in NM and IBM2. Ref.20 Ref.21 Ref.26
VAR_017955
Natural variant4721I → T in NM. Ref.23 Ref.28
VAR_021781
Natural variant5191N → S in IBM2. Ref.29
VAR_021782
Natural variant5241A → V in IBM2. Ref.21
VAR_017956
Natural variant5281F → C in IBM2. Ref.26
VAR_017957
Natural variant5571I → T in IBM2. Ref.26
VAR_017958
Natural variant5721V → L in NM and IBM2. Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.26 Ref.28
Corresponds to variant rs121908632 [ dbSNP | Ensembl ].
VAR_017959
Natural variant5761G → E in IBM2. Ref.18 Ref.21 Ref.26
VAR_017960
Natural variant5871I → T in IBM2. Ref.26
VAR_017961
Natural variant6001A → T in IBM2. Ref.29
VAR_021783
Natural variant6301A → T in NM. Ref.23
VAR_021784
Natural variant6311A → T in IBM2. Ref.18 Ref.21 Ref.26
VAR_017962
Natural variant6311A → V in NM and IBM2. Ref.22 Ref.23 Ref.24 Ref.26
VAR_017963
Natural variant6751Y → H in IBM2. Ref.21
VAR_017964
Natural variant6961V → M in IBM2. Ref.18 Ref.21 Ref.26
Corresponds to variant rs121908627 [ dbSNP | Ensembl ].
VAR_017965
Natural variant7121M → T in IBM2. Ref.18 Ref.21 Ref.25 Ref.26
Corresponds to variant rs28937594 [ dbSNP | Ensembl ].
VAR_017966

Experimental info

Sequence conflict3381D → G in BAH12108. Ref.6
Sequence conflict3591K → R in BAH12414. Ref.6
Sequence conflict3641G → V in BAH12108. Ref.6
Sequence conflict3821P → L in BAH12108. Ref.6
Sequence conflict4981V → A in BAH12108. Ref.6
Sequence conflict5211A → V in BAH12414. Ref.6

Secondary structure

................................................. 722
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (GNE1) [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 4D7D049B06B00077

FASTA72279,275
        10         20         30         40         50         60 
MEKNGNNRKL RVCVATCNRA DYSKLAPIMF GIKTEPEFFE LDVVVLGSHL IDDYGNTYRM 

        70         80         90        100        110        120 
IEQDDFDINT RLHTIVRGED EAAMVESVGL ALVKLPDVLN RLKPDIMIVH GDRFDALALA 

       130        140        150        160        170        180 
TSAALMNIRI LHIEGGEVSG TIDDSIRHAI TKLAHYHVCC TRSAEQHLIS MCEDHDRILL 

       190        200        210        220        230        240 
AGCPSYDKLL SAKNKDYMSI IRMWLGDDVK SKDYIVALQH PVTTDIKHSI KMFELTLDAL 

       250        260        270        280        290        300 
ISFNKRTLVL FPNIDAGSKE MVRVMRKKGI EHHPNFRAVK HVPFDQFIQL VAHAGCMIGN 

       310        320        330        340        350        360 
SSCGVREVGA FGTPVINLGT RQIGRETGEN VLHVRDADTQ DKILQALHLQ FGKQYPCSKI 

       370        380        390        400        410        420 
YGDGNAVPRI LKFLKSIDLQ EPLQKKFCFP PVKENISQDI DHILETLSAL AVDLGGTNLR 

       430        440        450        460        470        480 
VAIVSMKGEI VKKYTQFNPK TYEERINLIL QMCVEAAAEA VKLNCRILGV GISTGGRVNP 

       490        500        510        520        530        540 
REGIVLHSTK LIQEWNSVDL RTPLSDTLHL PVWVDNDGNC AALAERKFGQ GKGLENFVTL 

       550        560        570        580        590        600 
ITGTGIGGGI IHQHELIHGS SFCAAELGHL VVSLDGPDCS CGSHGCIEAY ASGMALQREA 

       610        620        630        640        650        660 
KKLHDEDLLL VEGMSVPKDE AVGALHLIQA AKLGNAKAQS ILRTAGTALG LGVVNILHTM 

       670        680        690        700        710        720 
NPSLVILSGV LASHYIHIVK DVIRQQALSS VQDVDVVVSD LVDPALLGAA SMVLDYTTRR 


IY 

« Hide

Isoform 2 (GNE2) [UniParc].

Checksum: 034C9CEFB1A403DC
Show »

FASTA75383,066
Isoform 3 (GNE3) [UniParc].

Checksum: 75BFC62D575958F4
Show »

FASTA71778,579
Isoform 4 [UniParc].

Checksum: 21829292EB9597F8
Show »

FASTA64871,278
Isoform 5 [UniParc].

Checksum: B32F395B16DB782C
Show »

FASTA61266,784

References

« Hide 'large scale' references
[1]"Primary structure and expression analysis of human UDP-N-acetyl-glucosamine-2-epimerase/N-acetylmannosamine kinase, the bifunctional enzyme in neuraminic acid biosynthesis."
Lucka L., Krause M., Danker K., Reutter W., Horstkorte R.
FEBS Lett. 454:341-344(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Liver.
[2]"Mutations in the human UDP-N-acetylglucosamine 2-epimerase gene define the disease sialuria and the allosteric site of the enzyme."
Seppala R., Lehto V.-P., Gahl W.A.
Am. J. Hum. Genet. 64:1563-1569(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS SIALURIA LEU-263; GLN-266 AND TRP-266.
[3]Wang S.S., Ryll T.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Small intestine.
[4]"Organization of the human UDP-N-acetylglucosamine 2-epimerase gene and characterization of a related pseudogene; relevance for mutation detection in patients with sialuria."
Huizing M., Anikster Y., Gahl W.A.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[5]"mRNA analysis revealed splice mutation and expression alteration of GNE gene in distal myopathy with rimmed vacuoles (DMRV) patients."
Pramono Z.A.D., Lai P.S., Seah I.A.L., Ong B., Yee W.C.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[6]"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] (ISOFORMS 1 AND 5), NUCLEOTIDE SEQUENCE [MRNA] OF 24-694 (ISOFORM 3).
Tissue: Hippocampus and Tongue.
[7]"Prediction of three different isoforms of the human UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase."
Reinke S.O., Hinderlich S.
FEBS Lett. 581:3327-3331(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 37-694 (ISOFORM 3), TISSUE SPECIFICITY.
[8]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]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].
[10]"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] (ISOFORM 1).
[11]"Identification of the metabolic defect in sialuria."
Weiss P., Tietze F., Gahl W.A., Seppala R., Ashwell G.
J. Biol. Chem. 264:17635-17636(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, INVOLVEMENT IN SIALURIA.
[12]"UDP-GlcNAc 2-epimerase: a regulator of cell surface sialylation."
Keppler O.T., Hinderlich S., Langner J., Schwartz-Albiez R., Reutter W., Pawlita M.
Science 284:1372-1376(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"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].
[14]"Crystal structure of the N-acetylmannosamine kinase domain of GNE."
Tong Y., Tempel W., Nedyalkova L., Mackenzie F., Park H.W.
PLoS ONE 4:E7165-E7165(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 406-720, SUBUNIT.
[15]"Crystal structures of N-acetylmannosamine kinase provide insights into enzyme activity and inhibition."
Martinez J., Nguyen L.D., Hinderlich S., Zimmer R., Tauberger E., Reutter W., Saenger W., Fan H., Moniot S.
J. Biol. Chem. 287:13656-13665(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 406-720 IN COMPLEX WITH ADP AND N-ACETYLMANNOSAMINE, ZINC-BINDING SITES, ACTIVE SITE, SUBUNIT.
[16]"Sialuria in a Portuguese girl: clinical, biochemical, and molecular characteristics."
Ferreira H., Seppala R., Pinto R., Huizing M., Martins E., Braga A.C., Gomes L., Krasnewich D.M., Sa Miranda M.C., Gahl W.A.
Mol. Genet. Metab. 67:131-137(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SIALURIA GLN-266.
[17]"Dominant inheritance of sialuria, an inborn error of feedback inhibition."
Leroy J.G., Seppala R., Huizing M., Dacremont G., De Simpel H., Van Coster R.N., Orvisky E., Krasnewich D.M., Gahl W.A.
Am. J. Hum. Genet. 68:1419-1427(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT SIALURIA GLN-266.
[18]"The UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase gene is mutated in recessive hereditary inclusion body myopathy."
Eisenberg I., Avidan N., Potikha T., Hochner H., Chen M., Olender T., Barash M., Shemesh M., Sadeh M., Grabov-Nardini G., Shmilevich I., Friedmann A., Karpati G., Bradley W.G., Baumbach L., Lancet D., Asher E.B., Beckmann J.S., Argov Z., Mitrani-Rosenbaum S.
Nat. Genet. 29:83-87(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS IBM2 ASN-225; GLN-246; GLU-576; THR-631; MET-696 AND THR-712.
[19]"A novel mutation in the GNE gene and a linkage disequilibrium in Japanese pedigrees."
Arai A., Tanaka K., Ikeuchi T., Igarashi S., Kobayashi H., Asaka T., Date H., Saito M., Tanaka H., Kawasaki S., Uyama E., Mizusawa H., Fukuhara N., Tsuji S.
Ann. Neurol. 52:516-519(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NM LEU-572.
[20]"Nonaka myopathy is caused by mutations in the UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase gene (GNE)."
Kayashima T., Matsuo H., Satoh A., Ohta T., Yoshiura K., Matsumoto N., Nakane Y., Niikawa N., Kishino T.
J. Hum. Genet. 47:77-79(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NM VAL-460 AND LEU-572.
[21]"Four novel mutations associated with autosomal recessive inclusion body myopathy (MIM: 600737)."
Darvish D., Vahedifar P., Huo Y.
Mol. Genet. Metab. 77:252-256(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS IBM2 ASN-225; GLN-246; TRP-246; VAL-460; VAL-524; LEU-572; GLU-576; THR-631; HIS-675; MET-696 AND THR-712.
[22]"Distal myopathy with rimmed vacuoles: novel mutations in the GNE gene."
Tomimitsu H., Ishikawa K., Shimizu J., Ohkoshi N., Kanazawa I., Mizusawa H.
Neurology 59:451-454(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NM LEU-572 AND VAL-631.
[23]"Distal myopathy with rimmed vacuoles is allelic to hereditary inclusion body myopathy."
Nishino I., Noguchi S., Murayama K., Driss A., Sugie K., Oya Y., Nagata T., Chida K., Takahashi T., Takusa Y., Ohi T., Nishimiya J., Sunohara N., Ciafaloni E., Kawai M., Aoki M., Nonaka I.
Neurology 59:1689-1693(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NM GLN-132; VAL-176; CYS-177; GLN-306; ALA-331; TYR-378; THR-472; LEU-572; THR-630 AND VAL-631.
[24]"GNE mutations in an American family with quadriceps-sparing IBM and lack of mutations in s-IBM."
Vasconcelos O.M., Raju R., Dalakas M.C.
Neurology 59:1776-1779(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS IBM2 ALA-216 AND VAL-631.
[25]"An Italian family with autosomal recessive inclusion-body myopathy and mutations in the GNE gene."
Broccolini A., Pescatori M., D'Amico A., Sabino A., Silvestri G., Ricci E., Servidei S., Tonali P.A., Mirabella M.
Neurology 59:1808-1809(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS IBM2 VAL-171 AND THR-712.
[26]"Mutations spectrum of GNE in hereditary inclusion body myopathy sparing the quadriceps."
Eisenberg I., Grabov-Nardini G., Hochner H., Korner M., Sadeh M., Bertorini T., Bushby K., Castellan C., Felice K., Mendell J., Merlini L., Shilling C., Wirguin I., Argov Z., Mitrani-Rosenbaum S.
Hum. Mutat. 21:99-99(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS IBM2 LEU-36; PHE-200; ASN-225; GLN-246; VAL-303; TYR-378; VAL-460; CYS-528; THR-557; LEU-572; GLU-576; THR-587; THR-631; VAL-631; MET-696 AND THR-712.
[27]"Novel missense mutation and large deletion of GNE gene in autosomal-recessive inclusion-body myopathy."
Del Bo R., Baron P., Prelle A., Serafini M., Moggio M., Di Fonzo A., Castagni M., Bresolin N., Comi G.P.
Muscle Nerve 28:113-117(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IBM2 CYS-162.
[28]"GNE mutations causing distal myopathy with rimmed vacuoles with inflammation."
Yabe I., Higashi T., Kikuchi S., Sasaki H., Fukazawa T., Yoshida K., Tashiro K.
Neurology 61:384-386(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NM THR-472 AND LEU-572.
[29]"Novel GNE mutations in Italian families with autosomal recessive hereditary inclusion-body myopathy."
Broccolini A., Ricci E., Cassandrini D., Gliubizzi C., Bruno C., Tonoli E., Silvestri G., Pescatori M., Rodolico C., Sinicropi S., Servidei S., Zara F., Minetti C., Tonali P.A., Mirabella M.
Hum. Mutat. 23:632-632(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS IBM2 SER-27; SER-206; GLN-246; SER-519 AND THR-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ238764 mRNA. Translation: CAB42607.1.
AF051852 mRNA. Translation: AAD32251.1.
AF155663 mRNA. Translation: AAD38197.1.
AF317635 Genomic DNA. Translation: AAG31661.1.
EU093084 mRNA. Translation: ABU55403.1.
AK295562 mRNA. Translation: BAH12108.1.
AK296687 mRNA. Translation: BAH12414.1. Different initiation.
AK312539 mRNA. Translation: BAG35438.1.
AM697708 mRNA. Translation: CAM91424.1.
AM697709 mRNA. Translation: CAM91425.1.
AL158830 Genomic DNA. No translation available.
CH471071 Genomic DNA. Translation: EAW58307.1.
CH471071 Genomic DNA. Translation: EAW58309.1.
BC121179 mRNA. Translation: AAI21180.1.
CCDSCCDS47965.1. [Q9Y223-2]
CCDS55308.1. [Q9Y223-5]
CCDS55309.1. [Q9Y223-4]
CCDS6602.1. [Q9Y223-1]
RefSeqNP_001121699.1. NM_001128227.2. [Q9Y223-2]
NP_001177312.1. NM_001190383.1. [Q9Y223-4]
NP_001177313.1. NM_001190384.1. [Q9Y223-5]
NP_001177317.1. NM_001190388.1. [Q9Y223-3]
NP_005467.1. NM_005476.5. [Q9Y223-1]
UniGeneHs.5920.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YHWX-ray1.64A406-720[»]
2YHYX-ray1.82A406-720[»]
2YI1X-ray2.15A406-720[»]
3EO3X-ray2.84A/B/C406-720[»]
ProteinModelPortalQ9Y223.
SMRQ9Y223. Positions 9-376, 406-717.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115337. 9 interactions.
STRING9606.ENSP00000379839.

PTM databases

PhosphoSiteQ9Y223.

Polymorphism databases

DMDM45476991.

Proteomic databases

MaxQBQ9Y223.
PaxDbQ9Y223.
PeptideAtlasQ9Y223.
PRIDEQ9Y223.

Protocols and materials databases

DNASU10020.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377902; ENSP00000367134; ENSG00000159921. [Q9Y223-1]
ENST00000396594; ENSP00000379839; ENSG00000159921. [Q9Y223-2]
ENST00000447283; ENSP00000414760; ENSG00000159921. [Q9Y223-4]
ENST00000539208; ENSP00000445117; ENSG00000159921. [Q9Y223-5]
ENST00000539815; ENSP00000439155; ENSG00000159921. [Q9Y223-1]
ENST00000543356; ENSP00000437765; ENSG00000159921.
GeneID10020.
KEGGhsa:10020.
UCSCuc010mlg.3. human. [Q9Y223-4]
uc010mlh.3. human. [Q9Y223-1]
uc010mli.3. human. [Q9Y223-2]
uc011lpl.2. human. [Q9Y223-5]

Organism-specific databases

CTD10020.
GeneCardsGC09M036204.
GeneReviewsGNE.
HGNCHGNC:23657. GNE.
HPAHPA007045.
HPA027258.
MIM269921. phenotype.
600737. phenotype.
603824. gene.
605820. phenotype.
neXtProtNX_Q9Y223.
Orphanet602. Distal myopathy, Nonaka type.
3166. Sialuria.
PharmGKBPA134987566.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0381.
HOGENOMHOG000008254.
HOVERGENHBG051733.
InParanoidQ9Y223.
KOK12409.
OMALIQEWSS.
OrthoDBEOG73V6JN.
PhylomeDBQ9Y223.
TreeFamTF332239.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00630.

Gene expression databases

ArrayExpressQ9Y223.
BgeeQ9Y223.
CleanExHS_GNE.
GenevestigatorQ9Y223.

Family and domain databases

InterProIPR001312. Hexokinase.
IPR000600. ROK.
IPR020004. UDP-GlcNAc_Epase.
IPR003331. UDP_GlcNAc_Epimerase_2.
[Graphical view]
PfamPF02350. Epimerase_2. 1 hit.
PF00480. ROK. 1 hit.
[Graphical view]
PRINTSPR00475. HEXOKINASE.
TIGRFAMsTIGR03568. NeuC_NnaA. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGNE. human.
EvolutionaryTraceQ9Y223.
GeneWikiGNE_(gene).
GenomeRNAi10020.
NextBio35522674.
PROQ9Y223.
SOURCESearch...

Entry information

Entry nameGLCNE_HUMAN
AccessionPrimary (citable) accession number: Q9Y223
Secondary accession number(s): A6PZH2 expand/collapse secondary AC list , A6PZH3, A7UNU7, B2R6E1, B7Z372, B7Z428, D3DRP7, F5H499, H0YFA7, Q0VA94
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 123 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 9

Human chromosome 9: entries, gene names and cross-references to MIM