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Q9Y223

- GLCNE_HUMAN

UniProt

Q9Y223 - GLCNE_HUMAN

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
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    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 Source: UniProtKB-KW
    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. lipopolysaccharide biosynthetic process Source: InterPro
    4. N-acetylglucosamine biosynthetic process Source: UniProtKB-UniPathway
    5. N-acetylneuraminate biosynthetic process Source: InterPro
    6. N-acetylneuraminate metabolic process Source: ProtInc
    7. UDP-N-acetylglucosamine metabolic process Source: InterPro

    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

    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

    ArrayExpressiQ9Y223.
    BgeeiQ9Y223.
    CleanExiHS_GNE.
    GenevestigatoriQ9Y223.

    Organism-specific databases

    HPAiHPA007045.
    HPA027258.

    Interactioni

    Subunit structurei

    Homodimer and homohexamer.2 Publications

    Protein-protein interaction databases

    BioGridi115337. 11 interactions.
    STRINGi9606.ENSP00000379839.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MEKNGNNRKL RVCVATCNRA DYSKLAPIMF GIKTEPEFFE LDVVVLGSHL    50
    IDDYGNTYRM IEQDDFDINT RLHTIVRGED EAAMVESVGL ALVKLPDVLN 100
    RLKPDIMIVH GDRFDALALA TSAALMNIRI LHIEGGEVSG TIDDSIRHAI 150
    TKLAHYHVCC TRSAEQHLIS MCEDHDRILL AGCPSYDKLL SAKNKDYMSI 200
    IRMWLGDDVK SKDYIVALQH PVTTDIKHSI KMFELTLDAL ISFNKRTLVL 250
    FPNIDAGSKE MVRVMRKKGI EHHPNFRAVK HVPFDQFIQL VAHAGCMIGN 300
    SSCGVREVGA FGTPVINLGT RQIGRETGEN VLHVRDADTQ DKILQALHLQ 350
    FGKQYPCSKI YGDGNAVPRI LKFLKSIDLQ EPLQKKFCFP PVKENISQDI 400
    DHILETLSAL AVDLGGTNLR VAIVSMKGEI VKKYTQFNPK TYEERINLIL 450
    QMCVEAAAEA VKLNCRILGV GISTGGRVNP REGIVLHSTK LIQEWNSVDL 500
    RTPLSDTLHL PVWVDNDGNC AALAERKFGQ GKGLENFVTL ITGTGIGGGI 550
    IHQHELIHGS SFCAAELGHL VVSLDGPDCS CGSHGCIEAY ASGMALQREA 600
    KKLHDEDLLL VEGMSVPKDE AVGALHLIQA AKLGNAKAQS ILRTAGTALG 650
    LGVVNILHTM NPSLVILSGV LASHYIHIVK DVIRQQALSS VQDVDVVVSD 700
    LVDPALLGAA SMVLDYTTRR IY 722
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 11 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.
    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

    ArrayExpressi Q9Y223.
    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

    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: October 1, 2014
    This is version 125 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