Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q14376

- GALE_HUMAN

UniProt

Q14376 - GALE_HUMAN

Protein

UDP-glucose 4-epimerase

Gene

GALE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (10 May 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes two distinct but analogous reactions: the epimerization of UDP-glucose to UDP-galactose and the epimerization of UDP-N-acetylglucosamine to UDP-N-acetylgalactosamine.

    Catalytic activityi

    UDP-alpha-D-glucose = UDP-alpha-D-galactose.

    Cofactori

    NAD.

    Kineticsi

    1. KM=69 µM for UDP-galactose (at 37 degrees Celsius and pH 8.8)2 Publications

    Vmax=1.22 mmol/min/mg enzyme with UDP-galactose as substrate2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei132 – 1321Substrate1 Publication
    Active sitei157 – 1571Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi4 – 3532NAD1 PublicationAdd
    BLAST

    GO - Molecular functioni

    1. coenzyme binding Source: InterPro
    2. protein homodimerization activity Source: UniProtKB
    3. UDP-glucose 4-epimerase activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cellular metabolic process Source: InterPro
    3. galactose catabolic process Source: UniProtKB
    4. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Carbohydrate metabolism, Galactose metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04117-MONOMER.
    ReactomeiREACT_532. Galactose catabolism.
    SABIO-RKQ14376.
    UniPathwayiUPA00214.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-glucose 4-epimerase (EC:5.1.3.2)
    Alternative name(s):
    Galactowaldenase
    UDP-galactose 4-epimerase
    Gene namesi
    Name:GALE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4116. GALE.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Involvement in diseasei

    Epimerase-deficiency galactosemia (EDG) [MIM:230350]: Clinical features include early-onset cataracts, liver damage, deafness and mental retardation. There are two clinically distinct forms of EDG. (1) A benign, or 'peripheral' form with no detectable GALE activity in red blood cells and characterized by mild symptoms. Some patients may suffer no symptoms beyond raised levels of galactose-1-phosphate in the blood. (2) A much rarer 'generalized' form with undetectable levels of GALE activity in all tissues and resulting in severe features such as restricted growth and mental development.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251A → V in EDG. 1 Publication
    VAR_037733
    Natural varianti34 – 341N → S in EDG; peripheral; nearly normal activity towards UDP-galactose. 2 Publications
    VAR_002539
    Natural varianti40 – 401R → C in EDG. 1 Publication
    Corresponds to variant rs144492228 [ dbSNP | Ensembl ].
    VAR_037734
    Natural varianti69 – 691D → E in EDG. 1 Publication
    VAR_037735
    Natural varianti90 – 901G → E in EDG; 800-fold decrease in UDP-galactose epimerization activity. 2 Publications
    Corresponds to variant rs28940882 [ dbSNP | Ensembl ].
    VAR_002540
    Natural varianti94 – 941V → M in EDG; generalized; 30-fold decrease in UDP-galactose epimerization activity; 2-fold decrease in affinity for UDP-galactose; 24% of normal activity with respect to UDP-N-acetylgalactosamine. 2 Publications
    VAR_010058
    Natural varianti103 – 1031D → G in EDG; 7-fold decrease in UDP-galactose epimerization activity; very mild decrease in activity towards UDP-N-acetylgalactosamine. 2 Publications
    Corresponds to variant rs28940883 [ dbSNP | Ensembl ].
    VAR_002541
    Natural varianti165 – 1651E → K in EDG. 1 Publication
    VAR_037736
    Natural varianti169 – 1691R → W in EDG. 1 Publication
    VAR_037737
    Natural varianti183 – 1831L → P in EDG; peripheral; 3-fold decrease in UDP-galactose epimerization activity. 2 Publications
    VAR_002543
    Natural varianti239 – 2391R → W in EDG. 1 Publication
    VAR_037738
    Natural varianti257 – 2571K → R in EDG; 7-fold decrease in UDP-galactose epimerization activity; does not affect affinity for UDP-galactose. 2 Publications
    Corresponds to variant rs28940884 [ dbSNP | Ensembl ].
    VAR_002544
    Natural varianti302 – 3021G → D in EDG. 1 Publication
    VAR_037739
    Natural varianti313 – 3131L → M in EDG; 6-fold decrease in UDP-galactose epimerization activity; very mild decrease in activity towards UDP-N-acetylgalactosamine. 2 Publications
    Corresponds to variant rs3180383 [ dbSNP | Ensembl ].
    VAR_002545
    Natural varianti319 – 3191G → E in EDG; nearly normal activity towards UDP-galactose; mild impairment under conditions of substrate limitation; may be a polymorphism. 2 Publications
    Corresponds to variant rs28940885 [ dbSNP | Ensembl ].
    VAR_002546
    Natural varianti335 – 3351R → H in EDG; 2-fold decrease in UDP-galactose epimerization activity. 2 Publications
    VAR_037740

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi132 – 1321S → A: Loss of activity. 1 Publication
    Mutagenesisi157 – 1571Y → F: Loss of activity. 1 Publication
    Mutagenesisi307 – 3071C → Y: No effect on activity towards UDP-galactose. Loss of activity towards UDP-N-acetylgalactosamine. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi230350. phenotype.
    Orphaneti308473. Erythrocyte galactose epimerase deficiency.
    308487. Generalized galactose epimerase deficiency.
    PharmGKBiPA28531.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 348348UDP-glucose 4-epimerasePRO_0000183189Add
    BLAST

    Proteomic databases

    MaxQBiQ14376.
    PaxDbiQ14376.
    PRIDEiQ14376.

    PTM databases

    PhosphoSiteiQ14376.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14376.
    BgeeiQ14376.
    CleanExiHS_GALE.
    GenevestigatoriQ14376.

    Organism-specific databases

    HPAiHPA007340.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi108855. 5 interactions.
    IntActiQ14376. 2 interactions.
    MINTiMINT-5001272.
    STRINGi9606.ENSP00000313026.

    Structurei

    Secondary structure

    1
    348
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86
    Turni9 – 113
    Helixi13 – 2412
    Beta strandi29 – 335
    Beta strandi35 – 384
    Beta strandi42 – 465
    Helixi47 – 5610
    Beta strandi61 – 644
    Helixi70 – 7910
    Beta strandi82 – 876
    Helixi94 – 996
    Helixi101 – 12121
    Beta strandi126 – 1327
    Helixi133 – 1364
    Beta strandi140 – 1445
    Helixi156 – 17419
    Beta strandi179 – 1857
    Beta strandi187 – 1893
    Beta strandi195 – 1973
    Beta strandi202 – 2043
    Helixi208 – 2169
    Beta strandi219 – 2213
    Beta strandi223 – 2264
    Beta strandi230 – 2367
    Beta strandi241 – 2433
    Helixi244 – 25815
    Turni259 – 2613
    Beta strandi264 – 2696
    Helixi277 – 28812
    Beta strandi294 – 2974
    Beta strandi305 – 3073
    Helixi312 – 3165
    Helixi326 – 33914

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EK5X-ray1.80A1-348[»]
    1EK6X-ray1.50A/B1-348[»]
    1HZJX-ray1.50A/B1-348[»]
    1I3KX-ray1.50A/B1-348[»]
    1I3LX-ray1.50A/B1-348[»]
    1I3MX-ray1.50A/B1-348[»]
    1I3NX-ray1.50A/B1-348[»]
    ProteinModelPortaliQ14376.
    SMRiQ14376. Positions 1-346.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14376.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1087.
    HOGENOMiHOG000168001.
    HOVERGENiHBG001396.
    InParanoidiQ14376.
    KOiK01784.
    OMAiFVAVIHF.
    OrthoDBiEOG77T14P.
    PhylomeDBiQ14376.
    TreeFamiTF105800.

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    InterProiIPR025308. Epimerase_C.
    IPR001509. Epimerase_deHydtase.
    IPR005886. GalE.
    IPR016040. NAD(P)-bd_dom.
    IPR008089. Nuc_sugar_epim.
    [Graphical view]
    PANTHERiPTHR10366:SF39. PTHR10366:SF39. 1 hit.
    PfamiPF01370. Epimerase. 1 hit.
    PF13950. Epimerase_Csub. 1 hit.
    [Graphical view]
    PRINTSiPR01713. NUCEPIMERASE.
    TIGRFAMsiTIGR01179. galE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q14376-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEKVLVTGG AGYIGSHTVL ELLEAGYLPV VIDNFHNAFR GGGSLPESLR    50
    RVQELTGRSV EFEEMDILDQ GALQRLFKKY SFMAVIHFAG LKAVGESVQK 100
    PLDYYRVNLT GTIQLLEIMK AHGVKNLVFS SSATVYGNPQ YLPLDEAHPT 150
    GGCTNPYGKS KFFIEEMIRD LCQADKTWNA VLLRYFNPTG AHASGCIGED 200
    PQGIPNNLMP YVSQVAIGRR EALNVFGNDY DTEDGTGVRD YIHVVDLAKG 250
    HIAALRKLKE QCGCRIYNLG TGTGYSVLQM VQAMEKASGK KIPYKVVARR 300
    EGDVAACYAN PSLAQEELGW TAALGLDRMC EDLWRWQKQN PSGFGTQA 348
    Length:348
    Mass (Da):38,282
    Last modified:May 10, 2005 - v2
    Checksum:i06FDBF9B1943DF49
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251A → V in EDG. 1 Publication
    VAR_037733
    Natural varianti34 – 341N → S in EDG; peripheral; nearly normal activity towards UDP-galactose. 2 Publications
    VAR_002539
    Natural varianti40 – 401R → C in EDG. 1 Publication
    Corresponds to variant rs144492228 [ dbSNP | Ensembl ].
    VAR_037734
    Natural varianti69 – 691D → E in EDG. 1 Publication
    VAR_037735
    Natural varianti90 – 901G → E in EDG; 800-fold decrease in UDP-galactose epimerization activity. 2 Publications
    Corresponds to variant rs28940882 [ dbSNP | Ensembl ].
    VAR_002540
    Natural varianti94 – 941V → M in EDG; generalized; 30-fold decrease in UDP-galactose epimerization activity; 2-fold decrease in affinity for UDP-galactose; 24% of normal activity with respect to UDP-N-acetylgalactosamine. 2 Publications
    VAR_010058
    Natural varianti103 – 1031D → G in EDG; 7-fold decrease in UDP-galactose epimerization activity; very mild decrease in activity towards UDP-N-acetylgalactosamine. 2 Publications
    Corresponds to variant rs28940883 [ dbSNP | Ensembl ].
    VAR_002541
    Natural varianti165 – 1651E → K in EDG. 1 Publication
    VAR_037736
    Natural varianti169 – 1691R → W in EDG. 1 Publication
    VAR_037737
    Natural varianti180 – 1801A → V.2 Publications
    Corresponds to variant rs3204468 [ dbSNP | Ensembl ].
    VAR_002542
    Natural varianti183 – 1831L → P in EDG; peripheral; 3-fold decrease in UDP-galactose epimerization activity. 2 Publications
    VAR_002543
    Natural varianti239 – 2391R → W in EDG. 1 Publication
    VAR_037738
    Natural varianti257 – 2571K → R in EDG; 7-fold decrease in UDP-galactose epimerization activity; does not affect affinity for UDP-galactose. 2 Publications
    Corresponds to variant rs28940884 [ dbSNP | Ensembl ].
    VAR_002544
    Natural varianti302 – 3021G → D in EDG. 1 Publication
    VAR_037739
    Natural varianti313 – 3131L → M in EDG; 6-fold decrease in UDP-galactose epimerization activity; very mild decrease in activity towards UDP-N-acetylgalactosamine. 2 Publications
    Corresponds to variant rs3180383 [ dbSNP | Ensembl ].
    VAR_002545
    Natural varianti319 – 3191G → E in EDG; nearly normal activity towards UDP-galactose; mild impairment under conditions of substrate limitation; may be a polymorphism. 2 Publications
    Corresponds to variant rs28940885 [ dbSNP | Ensembl ].
    VAR_002546
    Natural varianti335 – 3351R → H in EDG; 2-fold decrease in UDP-galactose epimerization activity. 2 Publications
    VAR_037740

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L41668 mRNA. Translation: AAB86498.1.
    AF022382 Genomic DNA. Translation: AAC39645.1.
    DQ233667 Genomic DNA. Translation: ABB04109.1.
    DQ233668 mRNA. Translation: ABB04110.1.
    AK314397 mRNA. Translation: BAG37021.1.
    AL031295 Genomic DNA. Translation: CAB40159.1.
    BC001273 mRNA. Translation: AAH01273.1.
    BC050685 mRNA. Translation: AAH50685.2.
    CCDSiCCDS242.1.
    RefSeqiNP_000394.2. NM_000403.3.
    NP_001008217.1. NM_001008216.1.
    NP_001121093.1. NM_001127621.1.
    UniGeneiHs.632380.

    Genome annotation databases

    EnsembliENST00000374497; ENSP00000363621; ENSG00000117308.
    GeneIDi2582.
    KEGGihsa:2582.
    UCSCiuc001bhv.1. human.

    Polymorphism databases

    DMDMi68056598.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L41668 mRNA. Translation: AAB86498.1 .
    AF022382 Genomic DNA. Translation: AAC39645.1 .
    DQ233667 Genomic DNA. Translation: ABB04109.1 .
    DQ233668 mRNA. Translation: ABB04110.1 .
    AK314397 mRNA. Translation: BAG37021.1 .
    AL031295 Genomic DNA. Translation: CAB40159.1 .
    BC001273 mRNA. Translation: AAH01273.1 .
    BC050685 mRNA. Translation: AAH50685.2 .
    CCDSi CCDS242.1.
    RefSeqi NP_000394.2. NM_000403.3.
    NP_001008217.1. NM_001008216.1.
    NP_001121093.1. NM_001127621.1.
    UniGenei Hs.632380.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EK5 X-ray 1.80 A 1-348 [» ]
    1EK6 X-ray 1.50 A/B 1-348 [» ]
    1HZJ X-ray 1.50 A/B 1-348 [» ]
    1I3K X-ray 1.50 A/B 1-348 [» ]
    1I3L X-ray 1.50 A/B 1-348 [» ]
    1I3M X-ray 1.50 A/B 1-348 [» ]
    1I3N X-ray 1.50 A/B 1-348 [» ]
    ProteinModelPortali Q14376.
    SMRi Q14376. Positions 1-346.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108855. 5 interactions.
    IntActi Q14376. 2 interactions.
    MINTi MINT-5001272.
    STRINGi 9606.ENSP00000313026.

    Chemistry

    BindingDBi Q14376.
    ChEMBLi CHEMBL5843.

    PTM databases

    PhosphoSitei Q14376.

    Polymorphism databases

    DMDMi 68056598.

    Proteomic databases

    MaxQBi Q14376.
    PaxDbi Q14376.
    PRIDEi Q14376.

    Protocols and materials databases

    DNASUi 2582.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374497 ; ENSP00000363621 ; ENSG00000117308 .
    GeneIDi 2582.
    KEGGi hsa:2582.
    UCSCi uc001bhv.1. human.

    Organism-specific databases

    CTDi 2582.
    GeneCardsi GC01M024122.
    GeneReviewsi GALE.
    HGNCi HGNC:4116. GALE.
    HPAi HPA007340.
    MIMi 230350. phenotype.
    606953. gene.
    neXtProti NX_Q14376.
    Orphaneti 308473. Erythrocyte galactose epimerase deficiency.
    308487. Generalized galactose epimerase deficiency.
    PharmGKBi PA28531.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1087.
    HOGENOMi HOG000168001.
    HOVERGENi HBG001396.
    InParanoidi Q14376.
    KOi K01784.
    OMAi FVAVIHF.
    OrthoDBi EOG77T14P.
    PhylomeDBi Q14376.
    TreeFami TF105800.

    Enzyme and pathway databases

    UniPathwayi UPA00214 .
    BioCyci MetaCyc:HS04117-MONOMER.
    Reactomei REACT_532. Galactose catabolism.
    SABIO-RK Q14376.

    Miscellaneous databases

    EvolutionaryTracei Q14376.
    GenomeRNAii 2582.
    NextBioi 10213.
    PROi Q14376.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14376.
    Bgeei Q14376.
    CleanExi HS_GALE.
    Genevestigatori Q14376.

    Family and domain databases

    Gene3Di 3.40.50.720. 2 hits.
    InterProi IPR025308. Epimerase_C.
    IPR001509. Epimerase_deHydtase.
    IPR005886. GalE.
    IPR016040. NAD(P)-bd_dom.
    IPR008089. Nuc_sugar_epim.
    [Graphical view ]
    PANTHERi PTHR10366:SF39. PTHR10366:SF39. 1 hit.
    Pfami PF01370. Epimerase. 1 hit.
    PF13950. Epimerase_Csub. 1 hit.
    [Graphical view ]
    PRINTSi PR01713. NUCEPIMERASE.
    TIGRFAMsi TIGR01179. galE. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, characterization, and mapping of a full-length cDNA encoding human UDP-galactose 4'-epimerase."
      Daude N., Gallaher T.K., Zeschnigk M., Starzinski-Powitz A., Petry K.G., Haworth I.S., Reichardt J.K.V.
      Biochem. Mol. Med. 56:1-7(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-180.
    2. "Human UDP-galactose 4'epimerase (GALE) gene and identification of five missense mutations in patients with epimerase deficiency galactosemia."
      Maceratesi P., Daude N., Dallapiccola B., Novelli G., Allen R., Okano Y., Reichardt J.K.V.
      Mol. Genet. Metab. 63:26-30(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS EDG GLU-90; GLY-103; ARG-257; MET-313 AND GLU-319.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cervix and Skin.
    7. "Determinants of function and substrate specificity in human UDP-galactose 4'-epimerase."
      Schulz J.M., Watson A.L., Sanders R., Ross K.L., Thoden J.B., Holden H.M., Fridovich-Keil J.L.
      J. Biol. Chem. 279:32796-32803(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-132; TYR-157 AND CYS-307.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Crystallographic evidence for Tyr 157 functioning as the active site Proton acceptor in human UDP-galactose 4-epimerase."
      Thoden J.B., Wohlers T.M., Fridovich-Keil J.L., Holden H.M.
      Biochemistry 39:5691-5701(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE, SUBUNIT.
    10. "Molecular basis for severe epimerase deficiency galactosemia. X-ray structure of the human V94m-substituted UDP-galactose 4-epimerase."
      Thoden J.B., Wohlers T.M., Fridovich-Keil J.L., Holden H.M.
      J. Biol. Chem. 276:20617-20623(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF VARIANT EDG MET-94.
    11. "Characterization of two mutations associated with epimerase-deficiency galactosemia, by use of a yeast expression system for human UDP-galactose-4-epimerase."
      Quimby B.B., Alano A., Almashanu S., Desandro A.M., Cowan T.M., Fridovich-Keil J.L.
      Am. J. Hum. Genet. 61:590-598(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDG SER-34 AND PRO-183, VARIANT VAL-180.
    12. "Identification and characterization of a mutation, in the human UDP-galactose-4-epimerase gene, associated with generalized epimerase-deficiency galactosemia."
      Wohlers T.M., Christacos N.C., Harreman M.T., Fridovich-Keil J.L.
      Am. J. Hum. Genet. 64:462-470(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDG MET-94, CHARACTERIZATION OF VARIANTS EDG GLU-90; MET-94; GLY-103 AND MET-313.
    13. "Studies of the V94M-substituted human UDPgalactose-4-epimerase enzyme associated with generalized epimerase-deficiency galactosaemia."
      Wohlers T.M., Fridovich-Keil J.L.
      J. Inherit. Metab. Dis. 23:713-729(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANT MET-94.
    14. "A PCR-based method for detecting known mutations in the human UDP galactose-4'-epimerase gene associated with epimerase-deficiency galactosemia."
      Henderson J.M., Huguenin S.M., Cowan T.M., Fridovich-Keil J.L.
      Clin. Genet. 60:350-355(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDG SER-34; GLU-90; MET-94; GLY-103; PRO-183; ARG-257; MET-313; GLU-319 AND HIS-335.
    15. "Functional analysis of disease-causing mutations in human UDP-galactose 4-epimerase."
      Timson D.J.
      FEBS J. 272:6170-6177(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS EDG SER-34; GLU-90; MET-94; GLY-103; PRO-183; ARG-257; MET-313; GLU-319 AND HIS-335, SUBUNIT.
    16. "The molecular basis of UDP-galactose-4-epimerase (GALE) deficiency galactosemia in Korean patients."
      Park H.-D., Park K.U., Kim J.Q., Shin C.H., Yang S.W., Lee D.H., Song Y.-H., Song J.
      Genet. Med. 7:646-649(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDG VAL-25; CYS-40; GLU-69; LYS-165; TRP-169; TRP-239; ASP-302 AND HIS-335.
    17. "Functional characterization of the K257R and G319E-hGALE alleles found in patients with ostensibly peripheral epimerase deficiency galactosemia."
      Wasilenko J., Lucas M.E., Thoden J.B., Holden H.M., Fridovich-Keil J.L.
      Mol. Genet. Metab. 84:32-38(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS EDG ARG-257 AND GLU-319.

    Entry informationi

    Entry nameiGALE_HUMAN
    AccessioniPrimary (citable) accession number: Q14376
    Secondary accession number(s): Q38G75
    , Q86W41, Q9BVE3, Q9UJB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 10, 2005
    Last modified: October 1, 2014
    This is version 153 of the entry and version 2 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, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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