Q9NYU1 (UGGG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1516 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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).

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UDP-glucosylation Inferred from sequence or structural similarity. Source: GOC cellular protein metabolic process Traceable author statement. Source: Reactome post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome protein folding Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum lumen Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum-Golgi intermediate compartment Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	UDP-glucose:glycoprotein glucosyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Potential
	Chain	28 – 1516	1489	UDP-glucose:glycoprotein glucosyltransferase 2		PRO_0000012274
Regions
	Region	1220 – 1516	297	Glucosyltransferase
	Motif	1513 – 1516	4	Prevents secretion from ER Potential
Amino acid modifications
	Modified residue	1289	1	Phosphotyrosine Ref.6
	Glycosylation	256	1	N-linked (GlcNAc...) Potential
	Glycosylation	286	1	N-linked (GlcNAc...) Potential
	Glycosylation	920	1	N-linked (GlcNAc...) Potential
	Glycosylation	950	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	323	1	A → T. Ref.1 Corresponds to variant rs12863903 [ dbSNP | Ensembl ].		VAR_030006
	Natural variant	328	1	S → A. Ref.1 Ref.3 Corresponds to variant rs816142 [ dbSNP | Ensembl ].		VAR_030007
	Natural variant	821	1	A → T. Ref.1 Corresponds to variant rs33949518 [ dbSNP | Ensembl ].		VAR_055849
	Natural variant	865	1	K → R. Corresponds to variant rs35060832 [ dbSNP | Ensembl ].		VAR_061196
	Natural variant	924	1	F → I. Corresponds to variant rs35780499 [ dbSNP | Ensembl ].		VAR_055850
	Natural variant	994	1	M → L. Ref.1 Ref.3 Corresponds to variant rs12876018 [ dbSNP | Ensembl ].		VAR_030008
	Natural variant	1274	1	F → L. Corresponds to variant rs9525072 [ dbSNP | Ensembl ].		VAR_055851
	Natural variant	1285	1	Y → F. Corresponds to variant rs35123499 [ dbSNP | Ensembl ].		VAR_061197

Sequences

	Sequence		Length	Mass (Da)
	Q9NYU1 [UniParc]. Last modified November 2, 2010. Version 4. Checksum: BD216896ECA54E4F	FASTA	1,516	174,735
	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

References

	« Hide 'large scale' referencesShow '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. , 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 , 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.
PIR	T42654.
RefSeq	NP_064506.3. NM_020121.3.
UniGene	Hs.193226. Hs.656444.
3D structure databases
ProteinModelPortal	Q9NYU1.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	120875. 7 interactions.
IntAct	Q9NYU1. 2 interactions.
STRING	9606.ENSP00000365938.
Protein family/group databases
CAZy	GT24. Glycosyltransferase Family 24.
PTM databases
PhosphoSite	Q9NYU1.
Polymorphism databases
DMDM	311033544.
Proteomic databases
PaxDb	Q9NYU1.
PRIDE	Q9NYU1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000376747; ENSP00000365938; ENSG00000102595.
GeneID	55757.
KEGG	hsa:55757.
UCSC	uc001vmt.3. human.
Organism-specific databases
CTD	55757.
GeneCards	GC13M096453.
H-InvDB	HIX0011410.
HGNC	HGNC:15664. UGGT2.
HPA	HPA047955.
MIM	605898. gene.
neXtProt	NX_Q9NYU1.
PharmGKB	PA38015.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG320899.
HOGENOM	HOG000184622.
HOVERGEN	HBG079469.
InParanoid	Q9NYU1.
KO	K11718.
OMA	TEMDGYR.
OrthoDB	EOG75J0M7.
PhylomeDB	Q9NYU1.
TreeFam	TF300320.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q9NYU1.
Bgee	Q9NYU1.
CleanEx	HS_UGCGL2.
Genevestigator	Q9NYU1.
Family and domain databases
InterPro	IPR002495. Glyco_trans_8. IPR009448. UDP-g_GGtrans. [Graphical view]
PANTHER	PTHR11226. PTHR11226. 1 hit.
Pfam	PF01501. Glyco_transf_8. 1 hit. PF06427. UDP-g_GGTase. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	55757.
NextBio	60767.
PRO	Q9NYU1.
SOURCE	Search...

Entry information

Entry name

UGGG2_HUMAN

Accession

Primary (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:	April 16, 2014
This is version 114 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.