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Q9Y223

- GLCNE_HUMAN

UniProt

Q9Y223 - GLCNE_HUMAN

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Protein

Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase

Gene

GNE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Catalytic activityi

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 regulationi

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.By similarity1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei477 – 4771Substrate
Binding sitei489 – 4891Substrate
Active sitei517 – 51711 Publication
Binding sitei517 – 5171Substrate
Binding sitei566 – 5661Substrate
Metal bindingi569 – 5691Zinc
Binding sitei569 – 5691Substrate
Metal bindingi579 – 5791Zinc
Metal bindingi581 – 5811Zinc
Metal bindingi586 – 5861Zinc
Binding sitei588 – 5881Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi411 – 42010ATP
Nucleotide bindingi543 – 55210ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. N-acylmannosamine kinase activity Source: ProtInc
  5. UDP-N-acetylglucosamine 2-epimerase activity Source: ProtInc

GO - Biological processi

  1. carbohydrate phosphorylation Source: GOC
  2. cell adhesion Source: ProtInc
  3. N-acetylglucosamine biosynthetic process Source: UniProtKB-UniPathway
  4. N-acetylneuraminate metabolic process Source: ProtInc
  5. UDP-N-acetylglucosamine metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Transferase

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_200874. Sialic acid metabolism.
UniPathwayiUPA00630.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Alternative name(s):
UDP-GlcNAc-2-epimerase/ManAc kinase
Including the following 2 domains:
UDP-N-acetylglucosamine 2-epimerase (hydrolyzing) (EC:3.2.1.183)
Alternative name(s):
UDP-GlcNAc-2-epimerase
Uridine diphosphate-N-acetylglucosamine-2-epimerase
N-acetylmannosamine kinase (EC:2.7.1.60)
Alternative name(s):
ManAc kinase
Gene namesi
Name:GNE
Synonyms:GLCNE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:23657. GNE.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti263 – 2631R → L in SIALURIA; strong reduction of feedback inhibition by CMP-Neu5Ac. 1 Publication
VAR_017950
Natural varianti266 – 2661R → Q in SIALURIA; abolishes feedback inhibition by CMP-Neu5Ac. 2 Publications
VAR_017951
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.7 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271P → S in IBM2. 1 Publication
VAR_021771
Natural varianti36 – 361P → L in IBM2. 1 Publication
VAR_017945
Natural varianti162 – 1621R → C in IBM2. 1 Publication
VAR_021773
Natural varianti171 – 1711M → V in IBM2. 1 Publication
VAR_021774
Natural varianti200 – 2001I → F in IBM2. 1 Publication
VAR_017946
Natural varianti206 – 2061G → S in IBM2; moderate phenotype with unusual involvement of quadriceps. 1 Publication
VAR_021777
Natural varianti216 – 2161V → A in IBM2. 1 Publication
VAR_021778
Natural varianti225 – 2251D → N in IBM2. 3 Publications
VAR_017947
Natural varianti246 – 2461R → Q in IBM2. 4 Publications
VAR_017948
Natural varianti246 – 2461R → W in IBM2. 1 Publication
VAR_017949
Natural varianti303 – 3031C → V in IBM2; requires 2 nucleotide substitutions. 1 Publication
VAR_017953
Natural varianti378 – 3781D → Y in IBM2 and NM. 2 Publications
VAR_017954
Natural varianti460 – 4601A → V in NM and IBM2. 3 Publications
VAR_017955
Natural varianti519 – 5191N → S in IBM2. 1 Publication
VAR_021782
Natural varianti524 – 5241A → V in IBM2. 1 Publication
VAR_017956
Natural varianti528 – 5281F → C in IBM2. 1 Publication
VAR_017957
Natural varianti557 – 5571I → T in IBM2. 1 Publication
VAR_017958
Natural varianti572 – 5721V → L in NM and IBM2. 7 Publications
Corresponds to variant rs121908632 [ dbSNP | Ensembl ].
VAR_017959
Natural varianti576 – 5761G → E in IBM2. 3 Publications
VAR_017960
Natural varianti587 – 5871I → T in IBM2. 1 Publication
VAR_017961
Natural varianti600 – 6001A → T in IBM2. 1 Publication
VAR_021783
Natural varianti631 – 6311A → T in IBM2. 3 Publications
VAR_017962
Natural varianti631 – 6311A → V in NM and IBM2. 4 Publications
VAR_017963
Natural varianti675 – 6751Y → H in IBM2. 1 Publication
VAR_017964
Natural varianti696 – 6961V → M in IBM2. 3 Publications
Corresponds to variant rs121908627 [ dbSNP | Ensembl ].
VAR_017965
Natural varianti712 – 7121M → T in IBM2. 4 Publications
Corresponds to variant rs28937594 [ dbSNP | Ensembl ].
VAR_017966
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.5 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti132 – 1321H → Q in NM. 1 Publication
VAR_021772
Natural varianti176 – 1761D → V in NM. 1 Publication
Corresponds to variant rs139425890 [ dbSNP | Ensembl ].
VAR_021775
Natural varianti177 – 1771R → C in NM. 1 Publication
VAR_021776
Natural varianti306 – 3061R → Q in NM. 1 Publication
VAR_021779
Natural varianti331 – 3311V → A in NM. 1 Publication
VAR_021780
Natural varianti378 – 3781D → Y in IBM2 and NM. 2 Publications
VAR_017954
Natural varianti460 – 4601A → V in NM and IBM2. 3 Publications
VAR_017955
Natural varianti472 – 4721I → T in NM. 2 Publications
VAR_021781
Natural varianti572 – 5721V → L in NM and IBM2. 7 Publications
Corresponds to variant rs121908632 [ dbSNP | Ensembl ].
VAR_017959
Natural varianti630 – 6301A → T in NM. 1 Publication
VAR_021784
Natural varianti631 – 6311A → V in NM and IBM2. 4 Publications
VAR_017963

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi269921. phenotype.
600737. phenotype.
605820. phenotype.
Orphaneti602. Distal myopathy, Nonaka type.
3166. Sialuria.
PharmGKBiPA134987566.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 722722Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinasePRO_0000095716Add
BLAST

Post-translational modificationi

Phosphorylated by PKC.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y223.
PaxDbiQ9Y223.
PeptideAtlasiQ9Y223.
PRIDEiQ9Y223.

PTM databases

PhosphoSiteiQ9Y223.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

BgeeiQ9Y223.
CleanExiHS_GNE.
GenevestigatoriQ9Y223.

Organism-specific databases

HPAiHPA007045.
HPA027258.

Interactioni

Subunit structurei

Homodimer and homohexamer.2 Publications

Protein-protein interaction databases

BioGridi115337. 13 interactions.
STRINGi9606.ENSP00000379839.

Structurei

Secondary structure

1
722
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi406 – 4149Combined sources
Beta strandi416 – 42510Combined sources
Beta strandi430 – 4378Combined sources
Helixi442 – 46221Combined sources
Beta strandi465 – 47915Combined sources
Turni480 – 4834Combined sources
Beta strandi484 – 4874Combined sources
Beta strandi492 – 4943Combined sources
Beta strandi496 – 4994Combined sources
Helixi501 – 5088Combined sources
Beta strandi512 – 5165Combined sources
Helixi517 – 52711Combined sources
Turni530 – 5334Combined sources
Beta strandi537 – 55216Combined sources
Helixi567 – 5693Combined sources
Beta strandi571 – 5744Combined sources
Beta strandi584 – 5863Combined sources
Helixi587 – 5915Combined sources
Helixi593 – 60513Combined sources
Helixi624 – 6329Combined sources
Helixi636 – 65924Combined sources
Beta strandi663 – 6697Combined sources
Helixi672 – 68615Combined sources
Helixi689 – 6913Combined sources
Beta strandi695 – 6984Combined sources
Helixi704 – 71613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YHWX-ray1.64A406-720[»]
2YHYX-ray1.82A406-720[»]
2YI1X-ray2.15A406-720[»]
3EO3X-ray2.84A/B/C406-720[»]
ProteinModelPortaliQ9Y223.
SMRiQ9Y223. Positions 9-376, 406-717.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y223.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – ?UDP-N-acetylglucosamine 2-epimerase
Regioni406 – 722317N-acetylmannosamine kinaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the UDP-N-acetylglucosamine 2-epimerase family.Curated
In the C-terminal section; belongs to the ROK (NagC/XylR) family.Curated

Phylogenomic databases

eggNOGiCOG0381.
GeneTreeiENSGT00390000017246.
HOGENOMiHOG000008254.
HOVERGENiHBG051733.
InParanoidiQ9Y223.
KOiK12409.
OMAiLIQEWSS.
OrthoDBiEOG73V6JN.
PhylomeDBiQ9Y223.
TreeFamiTF332239.

Family and domain databases

InterProiIPR001312. Hexokinase.
IPR000600. ROK.
IPR020004. UDP-GlcNAc_Epase.
IPR003331. UDP_GlcNAc_Epimerase_2.
[Graphical view]
PfamiPF02350. Epimerase_2. 1 hit.
PF00480. ROK. 1 hit.
[Graphical view]
PRINTSiPR00475. HEXOKINASE.
TIGRFAMsiTIGR03568. NeuC_NnaA. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y223-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MEKNGNNRKL RVCVATCNRA DYSKLAPIMF GIKTEPEFFE LDVVVLGSHL
60 70 80 90 100
IDDYGNTYRM IEQDDFDINT RLHTIVRGED EAAMVESVGL ALVKLPDVLN
110 120 130 140 150
RLKPDIMIVH GDRFDALALA TSAALMNIRI LHIEGGEVSG TIDDSIRHAI
160 170 180 190 200
TKLAHYHVCC TRSAEQHLIS MCEDHDRILL AGCPSYDKLL SAKNKDYMSI
210 220 230 240 250
IRMWLGDDVK SKDYIVALQH PVTTDIKHSI KMFELTLDAL ISFNKRTLVL
260 270 280 290 300
FPNIDAGSKE MVRVMRKKGI EHHPNFRAVK HVPFDQFIQL VAHAGCMIGN
310 320 330 340 350
SSCGVREVGA FGTPVINLGT RQIGRETGEN VLHVRDADTQ DKILQALHLQ
360 370 380 390 400
FGKQYPCSKI YGDGNAVPRI LKFLKSIDLQ EPLQKKFCFP PVKENISQDI
410 420 430 440 450
DHILETLSAL AVDLGGTNLR VAIVSMKGEI VKKYTQFNPK TYEERINLIL
460 470 480 490 500
QMCVEAAAEA VKLNCRILGV GISTGGRVNP REGIVLHSTK LIQEWNSVDL
510 520 530 540 550
RTPLSDTLHL PVWVDNDGNC AALAERKFGQ GKGLENFVTL ITGTGIGGGI
560 570 580 590 600
IHQHELIHGS SFCAAELGHL VVSLDGPDCS CGSHGCIEAY ASGMALQREA
610 620 630 640 650
KKLHDEDLLL VEGMSVPKDE AVGALHLIQA AKLGNAKAQS ILRTAGTALG
660 670 680 690 700
LGVVNILHTM NPSLVILSGV LASHYIHIVK DVIRQQALSS VQDVDVVVSD
710 720
LVDPALLGAA SMVLDYTTRR IY
Length:722
Mass (Da):79,275
Last modified:November 1, 1999 - v1
Checksum:i4D7D049B06B00077
GO
Isoform 2 (identifier: Q9Y223-2) [UniParc]FASTAAdd to Basket

Also known as: GNE2

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → METYGYLQRESCFQGPHELYFKNLSKRNKQIM

Show »
Length:753
Mass (Da):83,066
Checksum:i034C9CEFB1A403DC
GO
Isoform 3 (identifier: Q9Y223-3) [UniParc]FASTAAdd to Basket

Also known as: GNE3

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: MEKNGNNRKL...LGSHLIDDYG → MPIGDCSVAA...RGSHAFKDLI

Show »
Length:717
Mass (Da):78,579
Checksum:i75BFC62D575958F4
GO
Isoform 4 (identifier: Q9Y223-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     471-544: Missing.

Show »
Length:648
Mass (Da):71,278
Checksum:i21829292EB9597F8
GO
Isoform 5 (identifier: Q9Y223-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:612
Mass (Da):66,784
Checksum:iB32F395B16DB782C
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti338 – 3381D → G in BAH12108. (PubMed:14702039)Curated
Sequence conflicti359 – 3591K → R in BAH12414. (PubMed:14702039)Curated
Sequence conflicti364 – 3641G → V in BAH12108. (PubMed:14702039)Curated
Sequence conflicti382 – 3821P → L in BAH12108. (PubMed:14702039)Curated
Sequence conflicti498 – 4981V → A in BAH12108. (PubMed:14702039)Curated
Sequence conflicti521 – 5211A → V in BAH12414. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271P → S in IBM2. 1 Publication
VAR_021771
Natural varianti36 – 361P → L in IBM2. 1 Publication
VAR_017945
Natural varianti132 – 1321H → Q in NM. 1 Publication
VAR_021772
Natural varianti162 – 1621R → C in IBM2. 1 Publication
VAR_021773
Natural varianti171 – 1711M → V in IBM2. 1 Publication
VAR_021774
Natural varianti176 – 1761D → V in NM. 1 Publication
Corresponds to variant rs139425890 [ dbSNP | Ensembl ].
VAR_021775
Natural varianti177 – 1771R → C in NM. 1 Publication
VAR_021776
Natural varianti200 – 2001I → F in IBM2. 1 Publication
VAR_017946
Natural varianti206 – 2061G → S in IBM2; moderate phenotype with unusual involvement of quadriceps. 1 Publication
VAR_021777
Natural varianti216 – 2161V → A in IBM2. 1 Publication
VAR_021778
Natural varianti225 – 2251D → N in IBM2. 3 Publications
VAR_017947
Natural varianti246 – 2461R → Q in IBM2. 4 Publications
VAR_017948
Natural varianti246 – 2461R → W in IBM2. 1 Publication
VAR_017949
Natural varianti263 – 2631R → L in SIALURIA; strong reduction of feedback inhibition by CMP-Neu5Ac. 1 Publication
VAR_017950
Natural varianti266 – 2661R → Q in SIALURIA; abolishes feedback inhibition by CMP-Neu5Ac. 2 Publications
VAR_017951
Natural varianti266 – 2661R → W in sialuria. 1 Publication
VAR_017952
Natural varianti303 – 3031C → V in IBM2; requires 2 nucleotide substitutions. 1 Publication
VAR_017953
Natural varianti306 – 3061R → Q in NM. 1 Publication
VAR_021779
Natural varianti331 – 3311V → A in NM. 1 Publication
VAR_021780
Natural varianti378 – 3781D → Y in IBM2 and NM. 2 Publications
VAR_017954
Natural varianti460 – 4601A → V in NM and IBM2. 3 Publications
VAR_017955
Natural varianti472 – 4721I → T in NM. 2 Publications
VAR_021781
Natural varianti519 – 5191N → S in IBM2. 1 Publication
VAR_021782
Natural varianti524 – 5241A → V in IBM2. 1 Publication
VAR_017956
Natural varianti528 – 5281F → C in IBM2. 1 Publication
VAR_017957
Natural varianti557 – 5571I → T in IBM2. 1 Publication
VAR_017958
Natural varianti572 – 5721V → L in NM and IBM2. 7 Publications
Corresponds to variant rs121908632 [ dbSNP | Ensembl ].
VAR_017959
Natural varianti576 – 5761G → E in IBM2. 3 Publications
VAR_017960
Natural varianti587 – 5871I → T in IBM2. 1 Publication
VAR_017961
Natural varianti600 – 6001A → T in IBM2. 1 Publication
VAR_021783
Natural varianti630 – 6301A → T in NM. 1 Publication
VAR_021784
Natural varianti631 – 6311A → T in IBM2. 3 Publications
VAR_017962
Natural varianti631 – 6311A → V in NM and IBM2. 4 Publications
VAR_017963
Natural varianti675 – 6751Y → H in IBM2. 1 Publication
VAR_017964
Natural varianti696 – 6961V → M in IBM2. 3 Publications
Corresponds to variant rs121908627 [ dbSNP | Ensembl ].
VAR_017965
Natural varianti712 – 7121M → T in IBM2. 4 Publications
Corresponds to variant rs28937594 [ dbSNP | Ensembl ].
VAR_017966

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5959Missing in isoform 5. 1 PublicationVSP_043975Add
BLAST
Alternative sequencei1 – 5555MEKNG…IDDYG → MPIGDCSVAAKPRKQLLCSL FQTTLGYRARASGWKPMVIC RGSHAFKDLI in isoform 3. 2 PublicationsVSP_041028Add
BLAST
Alternative sequencei1 – 11M → METYGYLQRESCFQGPHELY FKNLSKRNKQIM in isoform 2. 1 PublicationVSP_041027
Alternative sequencei206 – 25651Missing in isoform 5. 1 PublicationVSP_043976Add
BLAST
Alternative sequencei471 – 54474Missing in isoform 4. 1 PublicationVSP_043474Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47965.1. [Q9Y223-2]
CCDS55308.1. [Q9Y223-5]
CCDS55309.1. [Q9Y223-4]
CCDS55310.1. [Q9Y223-3]
CCDS6602.1. [Q9Y223-1]
RefSeqiNP_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]
UniGeneiHs.5920.

Genome annotation databases

EnsembliENST00000377902; 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. [Q9Y223-3]
GeneIDi10020.
KEGGihsa:10020.
UCSCiuc010mlg.3. human. [Q9Y223-4]
uc010mlh.3. human. [Q9Y223-1]
uc010mli.3. human. [Q9Y223-2]
uc011lpl.2. human. [Q9Y223-5]

Polymorphism databases

DMDMi45476991.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS47965.1. [Q9Y223-2 ]
CCDS55308.1. [Q9Y223-5 ]
CCDS55309.1. [Q9Y223-4 ]
CCDS55310.1. [Q9Y223-3 ]
CCDS6602.1. [Q9Y223-1 ]
RefSeqi NP_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 ]
UniGenei Hs.5920.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YHW X-ray 1.64 A 406-720 [» ]
2YHY X-ray 1.82 A 406-720 [» ]
2YI1 X-ray 2.15 A 406-720 [» ]
3EO3 X-ray 2.84 A/B/C 406-720 [» ]
ProteinModelPortali Q9Y223.
SMRi Q9Y223. Positions 9-376, 406-717.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115337. 13 interactions.
STRINGi 9606.ENSP00000379839.

PTM databases

PhosphoSitei Q9Y223.

Polymorphism databases

DMDMi 45476991.

Proteomic databases

MaxQBi Q9Y223.
PaxDbi Q9Y223.
PeptideAtlasi Q9Y223.
PRIDEi Q9Y223.

Protocols and materials databases

DNASUi 10020.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000377902 ; 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 . [Q9Y223-3 ]
GeneIDi 10020.
KEGGi hsa:10020.
UCSCi uc010mlg.3. human. [Q9Y223-4 ]
uc010mlh.3. human. [Q9Y223-1 ]
uc010mli.3. human. [Q9Y223-2 ]
uc011lpl.2. human. [Q9Y223-5 ]

Organism-specific databases

CTDi 10020.
GeneCardsi GC09M036204.
GeneReviewsi GNE.
HGNCi HGNC:23657. GNE.
HPAi HPA007045.
HPA027258.
MIMi 269921. phenotype.
600737. phenotype.
603824. gene.
605820. phenotype.
neXtProti NX_Q9Y223.
Orphaneti 602. Distal myopathy, Nonaka type.
3166. Sialuria.
PharmGKBi PA134987566.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0381.
GeneTreei ENSGT00390000017246.
HOGENOMi HOG000008254.
HOVERGENi HBG051733.
InParanoidi Q9Y223.
KOi K12409.
OMAi LIQEWSS.
OrthoDBi EOG73V6JN.
PhylomeDBi Q9Y223.
TreeFami TF332239.

Enzyme and pathway databases

UniPathwayi UPA00630 .
Reactomei REACT_200874. Sialic acid metabolism.

Miscellaneous databases

ChiTaRSi GNE. human.
EvolutionaryTracei Q9Y223.
GeneWikii GNE_(gene).
GenomeRNAii 10020.
NextBioi 35522674.
PROi Q9Y223.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y223.
CleanExi HS_GNE.
Genevestigatori Q9Y223.

Family and domain databases

InterProi IPR001312. Hexokinase.
IPR000600. ROK.
IPR020004. UDP-GlcNAc_Epase.
IPR003331. UDP_GlcNAc_Epimerase_2.
[Graphical view ]
Pfami PF02350. Epimerase_2. 1 hit.
PF00480. ROK. 1 hit.
[Graphical view ]
PRINTSi PR00475. HEXOKINASE.
TIGRFAMsi TIGR03568. NeuC_NnaA. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. 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. 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. 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. Cited for: VARIANTS IBM2 SER-27; SER-206; GLN-246; SER-519 AND THR-600.

Entry informationi

Entry nameiGLCNE_HUMAN
AccessioniPrimary (citable) accession number: Q9Y223
Secondary accession number(s): A6PZH2
, A6PZH3, A7UNU7, B2R6E1, B7Z372, B7Z428, D3DRP7, F5H499, H0YFA7, Q0VA94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: November 1, 1999
Last modified: November 26, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3