Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9NYU1 (UGGG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-glucose:glycoprotein glucosyltransferase 2

Short name=UGT2
Short name=hUGT2
EC=2.4.1.-
Alternative name(s):
UDP--Glc:glycoprotein glucosyltransferase 2
UDP-glucose ceramide glucosyltransferase-like 1
Gene names
Name:UGGT2
Synonyms:UGCGL2, UGT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1516 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation By similarity.

Cofactor

Calcium or manganese.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Interacts with METTL23. Ref.8

Subcellular location

Endoplasmic reticulum lumen. Endoplasmic reticulum-Golgi intermediate compartment Ref.5.

Tissue specificity

Higher levels in kidney, pancreas, heart, and skeletal muscle. Ref.1

Sequence similarities

Belongs to the glycosyltransferase 8 family.

Caution

Has no enzymatic activity towards unfolded RNase B or thyroglobulin (Ref.1).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 15161489UDP-glucose:glycoprotein glucosyltransferase 2
PRO_0000012274

Regions

Region1220 – 1516297Glucosyltransferase
Motif1513 – 15164Prevents secretion from ER Potential

Amino acid modifications

Modified residue12891Phosphotyrosine Ref.6
Glycosylation2561N-linked (GlcNAc...) Potential
Glycosylation2861N-linked (GlcNAc...) Potential
Glycosylation9201N-linked (GlcNAc...) Potential
Glycosylation9501N-linked (GlcNAc...) Potential

Natural variations

Natural variant3231A → T. Ref.1
Corresponds to variant rs12863903 [ dbSNP | Ensembl ].
VAR_030006
Natural variant3281S → A. Ref.1 Ref.3
Corresponds to variant rs816142 [ dbSNP | Ensembl ].
VAR_030007
Natural variant8211A → T. Ref.1
Corresponds to variant rs33949518 [ dbSNP | Ensembl ].
VAR_055849
Natural variant8651K → R.
Corresponds to variant rs35060832 [ dbSNP | Ensembl ].
VAR_061196
Natural variant9241F → I.
Corresponds to variant rs35780499 [ dbSNP | Ensembl ].
VAR_055850
Natural variant9941M → L. Ref.1 Ref.3
Corresponds to variant rs12876018 [ dbSNP | Ensembl ].
VAR_030008
Natural variant12741F → L.
Corresponds to variant rs9525072 [ dbSNP | Ensembl ].
VAR_055851
Natural variant12851Y → F.
Corresponds to variant rs35123499 [ dbSNP | Ensembl ].
VAR_061197

Sequences

Sequence LengthMass (Da)Tools
Q9NYU1 [UniParc].

Last modified November 2, 2010. Version 4.
Checksum: BD216896ECA54E4F

FASTA1,516174,735
        10         20         30         40         50         60 
MAPAKATNVV RLLLGSTALW LSQLGSGTVA ASKSVTAHLA AKWPETPLLL EASEFMAEES 

        70         80         90        100        110        120 
NEKFWQFLET VQELAIYKQT ESDYSYYNLI LKKAGQFLDN LHINLLKFAF SIRAYSPAIQ 

       130        140        150        160        170        180 
MFQQIAADEP PPDGCNAFVV IHKKHTCKIN EIKKLLKKAA SRTRPYLFKG DHKFPTNKEN 

       190        200        210        220        230        240 
LPVVILYAEM GTRTFSAFHK VLSEKAQNEE ILYVLRHYIQ KPSSRKMYLS GYGVELAIKS 

       250        260        270        280        290        300 
TEYKALDDTQ VKTVTNTTVE DETETNEVQG FLFGKLKEIY SDLRDNLTAF QKYLIESNKQ 

       310        320        330        340        350        360 
MMPLKVWELQ DLSFQAASQI MSAPVYDSIK LMKDISQNFP IKARSLTRIA VNQHMREEIK 

       370        380        390        400        410        420 
ENQKDLQVRF KIQPGDARLF INGLRVDMDV YDAFSILDML KLEGKMMNGL RNLGINGEDM 

       430        440        450        460        470        480 
SKFLKLNSHI WEYTYVLDIR HSSIMWINDL ENDDLYITWP TSCQKLLKPV FPGSVPSIRR 

       490        500        510        520        530        540 
NFHNLVLFID PAQEYTLDFI KLADVFYSHE VPLRIGFVFI LNTDDEVDGA NDAGVALWRA 

       550        560        570        580        590        600 
FNYIAEEFDI SEAFISIVHM YQKVKKDQNI LTVDNVKSVL QNTFPHANIW DILGIHSKYD 

       610        620        630        640        650        660 
EERKAGASFY KMTGLGPLPQ ALYNGEPFKH EEMNIKELKM AVLQRMMDAS VYLQREVFLG 

       670        680        690        700        710        720 
TLNDRTNAID FLMDRNNVVP RINTLILRTN QQYLNLISTS VTADVEDFST FFFLDSQDKS 

       730        740        750        760        770        780 
AVIAKNMYYL TQDDESIISA VTLWIIADFD KPSGRKLLFN ALKHMKTSVH SRLGIIYNPT 

       790        800        810        820        830        840 
SKINEENTAI SRGILAAFLT QKNMFLRSFL GQLAKEEIAT AIYSGDKIKT FLIEGMDKNA 

       850        860        870        880        890        900 
FEKKYNTVGV NIFRTHQLFC QDVLKLRPGE MGIVSNGRFL GPLDEDFYAE DFYLLEKITF 

       910        920        930        940        950        960 
SNLGEKIKGI VENMGINANN MSDFIMKVDA LMSSVPKRAS RYDVTFLREN HSVIKTNPQE 

       970        980        990       1000       1010       1020 
NDMFFNVIAI VDPLTREAQK MAQLLVVLGK IINMKIKLFM NCRGRLSEAP LESFYRFVLE 

      1030       1040       1050       1060       1070       1080 
PELMSGANDV SSLGPVAKFL DIPESPLLIL NMITPEGWLV ETVHSNCDLD NIHLKDTEKT 

      1090       1100       1110       1120       1130       1140 
VTAEYELEYL LLEGQCFDKV TEQPPRGLQF TLGTKNKPAV VDTIVMAHHG YFQLKANPGA 

      1150       1160       1170       1180       1190       1200 
WILRLHQGKS EDIYQIVGHE GTDSQADLED IIVVLNSFKS KILKVKVKKE TDKIKEDILT 

      1210       1220       1230       1240       1250       1260 
DEDEKTKGLW DSIKSFTVSL HKENKKEKDV LNIFSVASGH LYERFLRIMM LSVLRNTKTP 

      1270       1280       1290       1300       1310       1320 
VKFWLLKNYL SPTFKEVIPH MAKEYGFRYE LVQYRWPRWL RQQTERQRII WGYKILFLDV 

      1330       1340       1350       1360       1370       1380 
LFPLAVDKII FVDADQIVRH DLKELRDFDL DGAPYGYTPF CDSRREMDGY RFWKTGYWAS 

      1390       1400       1410       1420       1430       1440 
HLLRRKYHIS ALYVVDLKKF RRIGAGDRLR SQYQALSQDP NSLSNLDQDL PNNMIYQVAI 

      1450       1460       1470       1480       1490       1500 
KSLPQDWLWC ETWCDDESKQ RAKTIDLCNN PKTKESKLKA AARIVPEWVE YDAEIRQLLD 

      1510 
HLENKKQDTI LTHDEL 

« Hide

References

« Hide 'large scale' references
[1]"Two homologues encoding human UDP-glucose:glycoprotein glucosyltransferase differ in mRNA expression and enzymatic activity."
Arnold S.M., Fessler L.I., Fessler J.H., Kaufman R.J.
Biochemistry 39:2149-2163(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS THR-323; ALA-328; THR-821 AND LEU-994.
Tissue: Fetal liver.
[2]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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], VARIANTS ALA-328 AND LEU-994.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 151-1516.
Tissue: Testis.
[5]"The noncatalytic portion of human UDP-glucose: glycoprotein glucosyltransferase I confers UDP-glucose binding and transferase function to the catalytic domain."
Arnold S.M., Kaufman R.J.
J. Biol. Chem. 278:43320-43328(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[7]"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].
[8]"A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
PLoS Genet. 9:E1003210-E1003210(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH METTL23.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF227906 mRNA. Translation: AAF66233.2.
AL136104 expand/collapse EMBL AC list , AL158192, AL162500, AL607038 Genomic DNA. Translation: CAH72447.1.
AL158192 expand/collapse EMBL AC list , AL136104, AL162500, AL607038 Genomic DNA. Translation: CAI13708.1.
AL607038 expand/collapse EMBL AC list , AL136104, AL158192, AL162500 Genomic DNA. Translation: CAI39962.1.
AL162500 expand/collapse EMBL AC list , AL136104, AL158192, AL607038 Genomic DNA. Translation: CAI40146.1.
BC125233 mRNA. Translation: AAI25234.1.
AL133051 mRNA. Translation: CAB61378.1.
CCDSCCDS9480.1.
PIRT42654.
RefSeqNP_064506.3. NM_020121.3.
UniGeneHs.193226.
Hs.656444.

3D structure databases

ProteinModelPortalQ9NYU1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120875. 7 interactions.
IntActQ9NYU1. 2 interactions.
STRING9606.ENSP00000365938.

Protein family/group databases

CAZyGT24. Glycosyltransferase Family 24.

PTM databases

PhosphoSiteQ9NYU1.

Polymorphism databases

DMDM311033544.

Proteomic databases

MaxQBQ9NYU1.
PaxDbQ9NYU1.
PRIDEQ9NYU1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376747; ENSP00000365938; ENSG00000102595.
GeneID55757.
KEGGhsa:55757.
UCSCuc001vmt.3. human.

Organism-specific databases

CTD55757.
GeneCardsGC13M096453.
H-InvDBHIX0011410.
HGNCHGNC:15664. UGGT2.
HPAHPA047955.
MIM605898. gene.
neXtProtNX_Q9NYU1.
PharmGKBPA38015.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320899.
HOGENOMHOG000184622.
HOVERGENHBG079469.
InParanoidQ9NYU1.
KOK11718.
OMAVEYDAEI.
OrthoDBEOG75J0M7.
PhylomeDBQ9NYU1.
TreeFamTF300320.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9NYU1.
BgeeQ9NYU1.
CleanExHS_UGCGL2.
GenevestigatorQ9NYU1.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
IPR009448. UDP-g_GGtrans.
[Graphical view]
PANTHERPTHR11226. PTHR11226. 1 hit.
PfamPF01501. Glyco_transf_8. 1 hit.
PF06427. UDP-g_GGTase. 1 hit.
[Graphical view]
SUPFAMSSF53448. SSF53448. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi55757.
NextBio60767.
PROQ9NYU1.
SOURCESearch...

Entry information

Entry nameUGGG2_HUMAN
AccessionPrimary (citable) accession number: Q9NYU1
Secondary accession number(s): Q08AD0, Q5JQR8, Q9UFC4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: November 2, 2010
Last modified: July 9, 2014
This is version 117 of the entry and version 4 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

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 13

Human chromosome 13: entries, gene names and cross-references to MIM