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Q9NYU1

- UGGG2_HUMAN

UniProt

Q9NYU1 - UGGG2_HUMAN

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Protein
UDP-glucose:glycoprotein glucosyltransferase 2
Gene
UGGT2, UGCGL2, UGT2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Cofactori

Calcium or manganese.

Pathwayi

GO - Molecular functioni

  1. UDP-glucose:glycoprotein glucosyltransferase activity Source: UniProtKB

GO - Biological processi

  1. UDP-glucosylation Source: GOC
  2. cellular protein metabolic process Source: Reactome
  3. post-translational protein modification Source: Reactome
  4. protein N-linked glycosylation via asparagine Source: Reactome
  5. protein folding Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_25091. ER Quality Control Compartment (ERQC).
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT24. Glycosyltransferase Family 24.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-glucose:glycoprotein glucosyltransferase 2 (EC:2.4.1.-)
Short name:
UGT2
Short name:
hUGT2
Alternative name(s):
UDP--Glc:glycoprotein glucosyltransferase 2
UDP-glucose ceramide glucosyltransferase-like 1
Gene namesi
Name:UGGT2
Synonyms:UGCGL2, UGT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:15664. UGGT2.

Subcellular locationi

Endoplasmic reticulum lumen. Endoplasmic reticulum-Golgi intermediate compartment 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB
  2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38015.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727 Reviewed prediction
Add
BLAST
Chaini28 – 15161489UDP-glucose:glycoprotein glucosyltransferase 2
PRO_0000012274Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi256 – 2561N-linked (GlcNAc...) Reviewed prediction
Glycosylationi286 – 2861N-linked (GlcNAc...) Reviewed prediction
Glycosylationi920 – 9201N-linked (GlcNAc...) Reviewed prediction
Glycosylationi950 – 9501N-linked (GlcNAc...) Reviewed prediction
Modified residuei1289 – 12891Phosphotyrosine1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9NYU1.
PaxDbiQ9NYU1.
PRIDEiQ9NYU1.

PTM databases

PhosphoSiteiQ9NYU1.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ9NYU1.
BgeeiQ9NYU1.
CleanExiHS_UGCGL2.
GenevestigatoriQ9NYU1.

Organism-specific databases

HPAiHPA047955.

Interactioni

Subunit structurei

Interacts with METTL23.1 Publication

Protein-protein interaction databases

BioGridi120875. 7 interactions.
IntActiQ9NYU1. 2 interactions.
STRINGi9606.ENSP00000365938.

Structurei

3D structure databases

ProteinModelPortaliQ9NYU1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1220 – 1516297Glucosyltransferase
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1513 – 15164Prevents secretion from ER Reviewed prediction

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG320899.
HOGENOMiHOG000184622.
HOVERGENiHBG079469.
InParanoidiQ9NYU1.
KOiK11718.
OMAiVEYDAEI.
OrthoDBiEOG75J0M7.
PhylomeDBiQ9NYU1.
TreeFamiTF300320.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
IPR009448. UDP-g_GGtrans.
[Graphical view]
PANTHERiPTHR11226. PTHR11226. 1 hit.
PfamiPF01501. Glyco_transf_8. 1 hit.
PF06427. UDP-g_GGTase. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9NYU1-1 [UniParc]FASTAAdd to Basket

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MAPAKATNVV RLLLGSTALW LSQLGSGTVA ASKSVTAHLA AKWPETPLLL     50
EASEFMAEES NEKFWQFLET VQELAIYKQT ESDYSYYNLI LKKAGQFLDN 100
LHINLLKFAF SIRAYSPAIQ MFQQIAADEP PPDGCNAFVV IHKKHTCKIN 150
EIKKLLKKAA SRTRPYLFKG DHKFPTNKEN LPVVILYAEM GTRTFSAFHK 200
VLSEKAQNEE ILYVLRHYIQ KPSSRKMYLS GYGVELAIKS TEYKALDDTQ 250
VKTVTNTTVE DETETNEVQG FLFGKLKEIY SDLRDNLTAF QKYLIESNKQ 300
MMPLKVWELQ DLSFQAASQI MSAPVYDSIK LMKDISQNFP IKARSLTRIA 350
VNQHMREEIK ENQKDLQVRF KIQPGDARLF INGLRVDMDV YDAFSILDML 400
KLEGKMMNGL RNLGINGEDM SKFLKLNSHI WEYTYVLDIR HSSIMWINDL 450
ENDDLYITWP TSCQKLLKPV FPGSVPSIRR NFHNLVLFID PAQEYTLDFI 500
KLADVFYSHE VPLRIGFVFI LNTDDEVDGA NDAGVALWRA FNYIAEEFDI 550
SEAFISIVHM YQKVKKDQNI LTVDNVKSVL QNTFPHANIW DILGIHSKYD 600
EERKAGASFY KMTGLGPLPQ ALYNGEPFKH EEMNIKELKM AVLQRMMDAS 650
VYLQREVFLG TLNDRTNAID FLMDRNNVVP RINTLILRTN QQYLNLISTS 700
VTADVEDFST FFFLDSQDKS AVIAKNMYYL TQDDESIISA VTLWIIADFD 750
KPSGRKLLFN ALKHMKTSVH SRLGIIYNPT SKINEENTAI SRGILAAFLT 800
QKNMFLRSFL GQLAKEEIAT AIYSGDKIKT FLIEGMDKNA FEKKYNTVGV 850
NIFRTHQLFC QDVLKLRPGE MGIVSNGRFL GPLDEDFYAE DFYLLEKITF 900
SNLGEKIKGI VENMGINANN MSDFIMKVDA LMSSVPKRAS RYDVTFLREN 950
HSVIKTNPQE NDMFFNVIAI VDPLTREAQK MAQLLVVLGK IINMKIKLFM 1000
NCRGRLSEAP LESFYRFVLE PELMSGANDV SSLGPVAKFL DIPESPLLIL 1050
NMITPEGWLV ETVHSNCDLD NIHLKDTEKT VTAEYELEYL LLEGQCFDKV 1100
TEQPPRGLQF TLGTKNKPAV VDTIVMAHHG YFQLKANPGA WILRLHQGKS 1150
EDIYQIVGHE GTDSQADLED IIVVLNSFKS KILKVKVKKE TDKIKEDILT 1200
DEDEKTKGLW DSIKSFTVSL HKENKKEKDV LNIFSVASGH LYERFLRIMM 1250
LSVLRNTKTP VKFWLLKNYL SPTFKEVIPH MAKEYGFRYE LVQYRWPRWL 1300
RQQTERQRII WGYKILFLDV LFPLAVDKII FVDADQIVRH DLKELRDFDL 1350
DGAPYGYTPF CDSRREMDGY RFWKTGYWAS HLLRRKYHIS ALYVVDLKKF 1400
RRIGAGDRLR SQYQALSQDP NSLSNLDQDL PNNMIYQVAI KSLPQDWLWC 1450
ETWCDDESKQ RAKTIDLCNN PKTKESKLKA AARIVPEWVE YDAEIRQLLD 1500
HLENKKQDTI LTHDEL 1516
Length:1,516
Mass (Da):174,735
Last modified:November 2, 2010 - v4
Checksum:iBD216896ECA54E4F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti323 – 3231A → T.1 Publication
Corresponds to variant rs12863903 [ dbSNP | Ensembl ].
VAR_030006
Natural varianti328 – 3281S → A.2 Publications
Corresponds to variant rs816142 [ dbSNP | Ensembl ].
VAR_030007
Natural varianti821 – 8211A → T.1 Publication
Corresponds to variant rs33949518 [ dbSNP | Ensembl ].
VAR_055849
Natural varianti865 – 8651K → R.
Corresponds to variant rs35060832 [ dbSNP | Ensembl ].
VAR_061196
Natural varianti924 – 9241F → I.
Corresponds to variant rs35780499 [ dbSNP | Ensembl ].
VAR_055850
Natural varianti994 – 9941M → L.2 Publications
Corresponds to variant rs12876018 [ dbSNP | Ensembl ].
VAR_030008
Natural varianti1274 – 12741F → L.
Corresponds to variant rs9525072 [ dbSNP | Ensembl ].
VAR_055851
Natural varianti1285 – 12851Y → F.
Corresponds to variant rs35123499 [ dbSNP | Ensembl ].
VAR_061197

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF227906 mRNA. Translation: AAF66233.2.
AL136104
, AL158192, AL162500, AL607038 Genomic DNA. Translation: CAH72447.1.
AL158192
, AL136104, AL162500, AL607038 Genomic DNA. Translation: CAI13708.1.
AL607038
, AL136104, AL158192, AL162500 Genomic DNA. Translation: CAI39962.1.
AL162500
, AL136104, AL158192, AL607038 Genomic DNA. Translation: CAI40146.1.
BC125233 mRNA. Translation: AAI25234.1.
AL133051 mRNA. Translation: CAB61378.1.
CCDSiCCDS9480.1.
PIRiT42654.
RefSeqiNP_064506.3. NM_020121.3.
UniGeneiHs.193226.
Hs.656444.

Genome annotation databases

EnsembliENST00000376747; ENSP00000365938; ENSG00000102595.
GeneIDi55757.
KEGGihsa:55757.
UCSCiuc001vmt.3. human.

Polymorphism databases

DMDMi311033544.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF227906 mRNA. Translation: AAF66233.2 .
AL136104
, AL158192 , AL162500 , AL607038 Genomic DNA. Translation: CAH72447.1 .
AL158192
, AL136104 , AL162500 , AL607038 Genomic DNA. Translation: CAI13708.1 .
AL607038
, AL136104 , AL158192 , AL162500 Genomic DNA. Translation: CAI39962.1 .
AL162500
, AL136104 , AL158192 , AL607038 Genomic DNA. Translation: CAI40146.1 .
BC125233 mRNA. Translation: AAI25234.1 .
AL133051 mRNA. Translation: CAB61378.1 .
CCDSi CCDS9480.1.
PIRi T42654.
RefSeqi NP_064506.3. NM_020121.3.
UniGenei Hs.193226.
Hs.656444.

3D structure databases

ProteinModelPortali Q9NYU1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120875. 7 interactions.
IntActi Q9NYU1. 2 interactions.
STRINGi 9606.ENSP00000365938.

Protein family/group databases

CAZyi GT24. Glycosyltransferase Family 24.

PTM databases

PhosphoSitei Q9NYU1.

Polymorphism databases

DMDMi 311033544.

Proteomic databases

MaxQBi Q9NYU1.
PaxDbi Q9NYU1.
PRIDEi Q9NYU1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000376747 ; ENSP00000365938 ; ENSG00000102595 .
GeneIDi 55757.
KEGGi hsa:55757.
UCSCi uc001vmt.3. human.

Organism-specific databases

CTDi 55757.
GeneCardsi GC13M096453.
H-InvDB HIX0011410.
HGNCi HGNC:15664. UGGT2.
HPAi HPA047955.
MIMi 605898. gene.
neXtProti NX_Q9NYU1.
PharmGKBi PA38015.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG320899.
HOGENOMi HOG000184622.
HOVERGENi HBG079469.
InParanoidi Q9NYU1.
KOi K11718.
OMAi VEYDAEI.
OrthoDBi EOG75J0M7.
PhylomeDBi Q9NYU1.
TreeFami TF300320.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_25091. ER Quality Control Compartment (ERQC).

Miscellaneous databases

GenomeRNAii 55757.
NextBioi 60767.
PROi Q9NYU1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NYU1.
Bgeei Q9NYU1.
CleanExi HS_UGCGL2.
Genevestigatori Q9NYU1.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR002495. Glyco_trans_8.
IPR029044. Nucleotide-diphossugar_trans.
IPR009448. UDP-g_GGtrans.
[Graphical view ]
PANTHERi PTHR11226. PTHR11226. 1 hit.
Pfami PF01501. Glyco_transf_8. 1 hit.
PF06427. UDP-g_GGTase. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiUGGG2_HUMAN
AccessioniPrimary (citable) accession number: Q9NYU1
Secondary accession number(s): Q08AD0, Q5JQR8, Q9UFC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: November 2, 2010
Last modified: September 3, 2014
This is version 118 of the entry and version 4 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

Caution

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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