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Q96C23

- GALM_HUMAN

UniProt

Q96C23 - GALM_HUMAN

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Protein
Aldose 1-epimerase
Gene
GALM, BLOCK25
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose By similarity.2 Publications

Catalytic activityi

Alpha-D-glucose = beta-D-glucose.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei176 – 1761Proton donor
Binding sitei243 – 2431Substrate
Active sitei307 – 3071Proton acceptor

GO - Molecular functioni

  1. aldose 1-epimerase activity Source: UniProtKB-EC
  2. carbohydrate binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. galactose metabolic process Source: UniProt
  2. glucose metabolic process Source: UniProt
  3. hexose metabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS07125-MONOMER.
SABIO-RKQ96C23.
SignaLinkiQ96C23.
UniPathwayiUPA00242.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldose 1-epimerase (EC:5.1.3.3)
Alternative name(s):
Galactose mutarotase
Gene namesi
Name:GALM
ORF Names:BLOCK25
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:24063. GALM.

Subcellular locationi

Cytoplasm Inferred

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi107 – 1071H → A: Reduces activity over 5-fold. 1 Publication
Mutagenesisi176 – 1761H → A: Loss of activity. 1 Publication
Mutagenesisi307 – 3071E → A: Loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA134980075.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 342341Aldose 1-epimerase
PRO_0000197433Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ96C23.
PaxDbiQ96C23.
PeptideAtlasiQ96C23.
PRIDEiQ96C23.

PTM databases

PhosphoSiteiQ96C23.

Expressioni

Gene expression databases

ArrayExpressiQ96C23.
BgeeiQ96C23.
CleanExiHS_GALM.
GenevestigatoriQ96C23.

Organism-specific databases

HPAiHPA035472.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

IntActiQ96C23. 1 interaction.
MINTiMINT-5001489.
STRINGi9606.ENSP00000272252.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1210
Turni13 – 164
Beta strandi17 – 259
Beta strandi30 – 345
Beta strandi39 – 468
Beta strandi52 – 543
Helixi62 – 665
Beta strandi81 – 833
Helixi84 – 863
Beta strandi87 – 904
Beta strandi93 – 964
Beta strandi104 – 1063
Beta strandi109 – 1113
Helixi113 – 1153
Beta strandi119 – 1235
Beta strandi126 – 1338
Helixi137 – 1393
Beta strandi144 – 15310
Beta strandi156 – 16712
Beta strandi193 – 1964
Beta strandi198 – 2014
Helixi230 – 2367
Beta strandi243 – 2486
Beta strandi251 – 2533
Beta strandi255 – 2617
Turni263 – 2653
Beta strandi267 – 28115
Beta strandi287 – 2915
Helixi293 – 2953
Beta strandi297 – 2993
Beta strandi304 – 3107
Helixi314 – 3163
Beta strandi331 – 34111

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SNZX-ray2.20A/B1-342[»]
1SO0X-ray2.30A/B/C/D1-342[»]
ProteinModelPortaliQ96C23.
SMRiQ96C23. Positions 1-342.

Miscellaneous databases

EvolutionaryTraceiQ96C23.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni81 – 822Substrate binding

Sequence similaritiesi

Belongs to the aldose epimerase family.

Phylogenomic databases

eggNOGiCOG2017.
HOGENOMiHOG000072798.
HOVERGENiHBG051697.
InParanoidiQ96C23.
KOiK01785.
OMAiKRFCARV.
OrthoDBiEOG7V7666.
PhylomeDBiQ96C23.
TreeFamiTF324207.

Family and domain databases

Gene3Di2.70.98.10. 1 hit.
InterProiIPR018052. Ald1_epimerase_CS.
IPR015443. Aldose_1-epimerase.
IPR008183. Aldose_1/G6P_1-epimerase.
IPR011013. Gal_mutarotase_SF_dom.
IPR014718. Glyco_hydro-type_carb-bd_sub.
[Graphical view]
PfamiPF01263. Aldose_epim. 1 hit.
[Graphical view]
PIRSFiPIRSF005096. GALM. 1 hit.
SUPFAMiSSF74650. SSF74650. 1 hit.
PROSITEiPS00545. ALDOSE_1_EPIMERASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q96C23-1 [UniParc]FASTAAdd to Basket

« Hide

MASVTRAVFG ELPSGGGTVE KFQLQSDLLR VDIISWGCTI TALEVKDRQG    50
RASDVVLGFA ELEGYLQKQP YFGAVIGRVA NRIAKGTFKV DGKEYHLAIN 100
KEPNSLHGGV RGFDKVLWTP RVLSNGVQFS RISPDGEEGY PGELKVWVTY 150
TLDGGELIVN YRAQASQATP VNLTNHSYFN LAGQASPNIN DHEVTIEADT 200
YLPVDETLIP TGEVAPVQGT AFDLRKPVEL GKHLQDFHLN GFDHNFCLKG 250
SKEKHFCARV HHAASGRVLE VYTTQPGVQF YTGNFLDGTL KGKNGAVYPK 300
HSGFCLETQN WPDAVNQPRF PPVLLRPGEE YDHTTWFKFS VA 342
Length:342
Mass (Da):37,766
Last modified:December 1, 2001 - v1
Checksum:i611A54AE7E85813E
GO

Sequence cautioni

The sequence AAL62475.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti190 – 1901N → Y.
Corresponds to variant rs6741892 [ dbSNP | Ensembl ].
VAR_024451

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY064382
, AY064381, AY064379, AY064380, AY064378 Genomic DNA. Translation: AAL62475.1. Sequence problems.
AY064385
, AY064378, AY064380, AY064379, AY064381, AY064384, AY064383 Genomic DNA. Translation: AAL62476.1.
EU794611 mRNA. Translation: ACJ13665.1.
AK291489 mRNA. Translation: BAF84178.1.
AC074366 Genomic DNA. Translation: AAX93101.1.
CH471053 Genomic DNA. Translation: EAX00367.1.
BC014916 mRNA. Translation: AAH14916.1.
BC019263 mRNA. Translation: AAH19263.1.
CCDSiCCDS1797.1.
RefSeqiNP_620156.1. NM_138801.2.
UniGeneiHs.435012.

Genome annotation databases

EnsembliENST00000272252; ENSP00000272252; ENSG00000143891.
GeneIDi130589.
KEGGihsa:130589.
UCSCiuc002rqy.3. human.

Polymorphism databases

DMDMi67463772.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY064382
, AY064381 , AY064379 , AY064380 , AY064378 Genomic DNA. Translation: AAL62475.1 . Sequence problems.
AY064385
, AY064378 , AY064380 , AY064379 , AY064381 , AY064384 , AY064383 Genomic DNA. Translation: AAL62476.1 .
EU794611 mRNA. Translation: ACJ13665.1 .
AK291489 mRNA. Translation: BAF84178.1 .
AC074366 Genomic DNA. Translation: AAX93101.1 .
CH471053 Genomic DNA. Translation: EAX00367.1 .
BC014916 mRNA. Translation: AAH14916.1 .
BC019263 mRNA. Translation: AAH19263.1 .
CCDSi CCDS1797.1.
RefSeqi NP_620156.1. NM_138801.2.
UniGenei Hs.435012.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SNZ X-ray 2.20 A/B 1-342 [» ]
1SO0 X-ray 2.30 A/B/C/D 1-342 [» ]
ProteinModelPortali Q96C23.
SMRi Q96C23. Positions 1-342.
ModBasei Search...

Protein-protein interaction databases

IntActi Q96C23. 1 interaction.
MINTi MINT-5001489.
STRINGi 9606.ENSP00000272252.

PTM databases

PhosphoSitei Q96C23.

Polymorphism databases

DMDMi 67463772.

Proteomic databases

MaxQBi Q96C23.
PaxDbi Q96C23.
PeptideAtlasi Q96C23.
PRIDEi Q96C23.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000272252 ; ENSP00000272252 ; ENSG00000143891 .
GeneIDi 130589.
KEGGi hsa:130589.
UCSCi uc002rqy.3. human.

Organism-specific databases

CTDi 130589.
GeneCardsi GC02P038867.
HGNCi HGNC:24063. GALM.
HPAi HPA035472.
MIMi 608883. gene.
neXtProti NX_Q96C23.
PharmGKBi PA134980075.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2017.
HOGENOMi HOG000072798.
HOVERGENi HBG051697.
InParanoidi Q96C23.
KOi K01785.
OMAi KRFCARV.
OrthoDBi EOG7V7666.
PhylomeDBi Q96C23.
TreeFami TF324207.

Enzyme and pathway databases

UniPathwayi UPA00242 .
BioCyci MetaCyc:HS07125-MONOMER.
SABIO-RK Q96C23.
SignaLinki Q96C23.

Miscellaneous databases

ChiTaRSi GALM. human.
EvolutionaryTracei Q96C23.
GeneWikii Galactose_mutarotase.
GenomeRNAii 130589.
NextBioi 82783.
PROi Q96C23.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96C23.
Bgeei Q96C23.
CleanExi HS_GALM.
Genevestigatori Q96C23.

Family and domain databases

Gene3Di 2.70.98.10. 1 hit.
InterProi IPR018052. Ald1_epimerase_CS.
IPR015443. Aldose_1-epimerase.
IPR008183. Aldose_1/G6P_1-epimerase.
IPR011013. Gal_mutarotase_SF_dom.
IPR014718. Glyco_hydro-type_carb-bd_sub.
[Graphical view ]
Pfami PF01263. Aldose_epim. 1 hit.
[Graphical view ]
PIRSFi PIRSF005096. GALM. 1 hit.
SUPFAMi SSF74650. SSF74650. 1 hit.
PROSITEi PS00545. ALDOSE_1_EPIMERASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Physical/genetic map of the 2p22-2p21 region on chromosome 2."
    Gorry M.C., Zhang Y., Marks J.J., Suppes B., Hart P.S., Cortelli J.R., Pallos D., Hart T.C.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Li J.Y., Wang H.Y., Liu F.J., Liu J.
    Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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: Ovary.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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: Brain and Skin.
  7. "Identification and characterisation of human aldose 1-epimerase."
    Timson D.J., Reece R.J.
    FEBS Lett. 543:21-24(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF HIS-107; HIS-176 AND GLU-307.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION.

Entry informationi

Entry nameiGALM_HUMAN
AccessioniPrimary (citable) accession number: Q96C23
Secondary accession number(s): Q53RY1, Q8NIA2, V9HWA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: December 1, 2001
Last modified: September 3, 2014
This is version 113 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, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

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