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Q14376 (GALE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

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

Names and origin

Protein namesRecommended name:
UDP-glucose 4-epimerase

EC=5.1.3.2
Alternative name(s):
Galactowaldenase
UDP-galactose 4-epimerase
Gene names
Name:GALE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

NAD.

Pathway

Carbohydrate metabolism; galactose metabolism.

Subunit structure

Homodimer. Ref.9 Ref.15

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17

Sequence similarities

Belongs to the NAD(P)-dependent epimerase/dehydratase family.

Biophysicochemical properties

Kinetic parameters:

KM=69 µM for UDP-galactose (at 37 degrees Celsius and pH 8.8) Ref.13 Ref.15

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 348348UDP-glucose 4-epimerase
PRO_0000183189

Regions

Nucleotide binding4 – 3532NAD

Sites

Active site1571Proton acceptor
Binding site1321Substrate

Natural variations

Natural variant251A → V in EDG. Ref.16
VAR_037733
Natural variant341N → S in EDG; peripheral; nearly normal activity towards UDP-galactose. Ref.11 Ref.14 Ref.15
VAR_002539
Natural variant401R → C in EDG. Ref.16
Corresponds to variant rs144492228 [ dbSNP | Ensembl ].
VAR_037734
Natural variant691D → E in EDG. Ref.16
VAR_037735
Natural variant901G → E in EDG; 800-fold decrease in UDP-galactose epimerization activity. Ref.2 Ref.12 Ref.14 Ref.15
Corresponds to variant rs28940882 [ dbSNP | Ensembl ].
VAR_002540
Natural variant941V → 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. Ref.10 Ref.12 Ref.13 Ref.14 Ref.15
VAR_010058
Natural variant1031D → G in EDG; 7-fold decrease in UDP-galactose epimerization activity; very mild decrease in activity towards UDP-N-acetylgalactosamine. Ref.2 Ref.12 Ref.14 Ref.15
Corresponds to variant rs28940883 [ dbSNP | Ensembl ].
VAR_002541
Natural variant1651E → K in EDG. Ref.16
VAR_037736
Natural variant1691R → W in EDG. Ref.16
VAR_037737
Natural variant1801A → V. Ref.1 Ref.11
Corresponds to variant rs3204468 [ dbSNP | Ensembl ].
VAR_002542
Natural variant1831L → P in EDG; peripheral; 3-fold decrease in UDP-galactose epimerization activity. Ref.11 Ref.14 Ref.15
VAR_002543
Natural variant2391R → W in EDG. Ref.16
VAR_037738
Natural variant2571K → R in EDG; 7-fold decrease in UDP-galactose epimerization activity; does not affect affinity for UDP-galactose. Ref.2 Ref.14 Ref.15 Ref.17
Corresponds to variant rs28940884 [ dbSNP | Ensembl ].
VAR_002544
Natural variant3021G → D in EDG. Ref.16
VAR_037739
Natural variant3131L → M in EDG; 6-fold decrease in UDP-galactose epimerization activity; very mild decrease in activity towards UDP-N-acetylgalactosamine. Ref.2 Ref.12 Ref.14 Ref.15
Corresponds to variant rs3180383 [ dbSNP | Ensembl ].
VAR_002545
Natural variant3191G → E in EDG; nearly normal activity towards UDP-galactose; mild impairment under conditions of substrate limitation; may be a polymorphism. Ref.2 Ref.14 Ref.15 Ref.17
Corresponds to variant rs28940885 [ dbSNP | Ensembl ].
VAR_002546
Natural variant3351R → H in EDG; 2-fold decrease in UDP-galactose epimerization activity. Ref.14 Ref.15 Ref.16
VAR_037740

Experimental info

Mutagenesis1321S → A: Loss of activity. Ref.7
Mutagenesis1571Y → F: Loss of activity. Ref.7
Mutagenesis3071C → Y: No effect on activity towards UDP-galactose. Loss of activity towards UDP-N-acetylgalactosamine. Ref.7

Secondary structure

.............................................................. 348
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14376 [UniParc].

Last modified May 10, 2005. Version 2.
Checksum: 06FDBF9B1943DF49

FASTA34838,282
        10         20         30         40         50         60 
MAEKVLVTGG AGYIGSHTVL ELLEAGYLPV VIDNFHNAFR GGGSLPESLR RVQELTGRSV 

        70         80         90        100        110        120 
EFEEMDILDQ GALQRLFKKY SFMAVIHFAG LKAVGESVQK PLDYYRVNLT GTIQLLEIMK 

       130        140        150        160        170        180 
AHGVKNLVFS SSATVYGNPQ YLPLDEAHPT GGCTNPYGKS KFFIEEMIRD LCQADKTWNA 

       190        200        210        220        230        240 
VLLRYFNPTG AHASGCIGED PQGIPNNLMP YVSQVAIGRR EALNVFGNDY DTEDGTGVRD 

       250        260        270        280        290        300 
YIHVVDLAKG HIAALRKLKE QCGCRIYNLG TGTGYSVLQM VQAMEKASGK KIPYKVVARR 

       310        320        330        340 
EGDVAACYAN PSLAQEELGW TAALGLDRMC EDLWRWQKQN PSGFGTQA 

« Hide

References

« Hide 'large scale' references
[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]"Epimerase-deficiency galactosemia is not a binary condition."
Openo K.K., Schulz J.M., Vargas C.A., Orton C.S., Epstein M.P., Schnur R.E., Scaglia F., Berry G.T., Gottesman G.S., Ficicioglu C., Slonim A.E., Schroer R.J., Yu C., Rangel V.E., Keenan J., Lamance K., Fridovich-Keil J.L.
Am. J. Hum. Genet. 78:89-102(2006) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: 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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS242.1.
RefSeqNP_000394.2. NM_000403.3.
NP_001008217.1. NM_001008216.1.
NP_001121093.1. NM_001127621.1.
UniGeneHs.632380.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ14376.
SMRQ14376. Positions 1-346.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108855. 5 interactions.
IntActQ14376. 2 interactions.
MINTMINT-5001272.
STRING9606.ENSP00000313026.

Chemistry

BindingDBQ14376.
ChEMBLCHEMBL5843.

PTM databases

PhosphoSiteQ14376.

Polymorphism databases

DMDM68056598.

Proteomic databases

MaxQBQ14376.
PaxDbQ14376.
PRIDEQ14376.

Protocols and materials databases

DNASU2582.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374497; ENSP00000363621; ENSG00000117308.
GeneID2582.
KEGGhsa:2582.
UCSCuc001bhv.1. human.

Organism-specific databases

CTD2582.
GeneCardsGC01M024122.
GeneReviewsGALE.
HGNCHGNC:4116. GALE.
HPAHPA007340.
MIM230350. phenotype.
606953. gene.
neXtProtNX_Q14376.
Orphanet308473. Erythrocyte galactose epimerase deficiency.
308487. Generalized galactose epimerase deficiency.
PharmGKBPA28531.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1087.
HOGENOMHOG000168001.
HOVERGENHBG001396.
InParanoidQ14376.
KOK01784.
OMAFVAVIHF.
OrthoDBEOG77T14P.
PhylomeDBQ14376.
TreeFamTF105800.

Enzyme and pathway databases

BioCycMetaCyc:HS04117-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKQ14376.
UniPathwayUPA00214.

Gene expression databases

ArrayExpressQ14376.
BgeeQ14376.
CleanExHS_GALE.
GenevestigatorQ14376.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR025308. Epimerase_C.
IPR001509. Epimerase_deHydtase.
IPR005886. GalE.
IPR016040. NAD(P)-bd_dom.
IPR008089. Nuc_sugar_epim.
[Graphical view]
PANTHERPTHR10366:SF39. PTHR10366:SF39. 1 hit.
PfamPF01370. Epimerase. 1 hit.
PF13950. Epimerase_Csub. 1 hit.
[Graphical view]
PRINTSPR01713. NUCEPIMERASE.
TIGRFAMsTIGR01179. galE. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ14376.
GenomeRNAi2582.
NextBio10213.
PROQ14376.
SOURCESearch...

Entry information

Entry nameGALE_HUMAN
AccessionPrimary (citable) accession number: Q14376
Secondary accession number(s): Q38G75 expand/collapse secondary AC list , Q86W41, Q9BVE3, Q9UJB4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 10, 2005
Last modified: July 9, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM