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Q9NYU2 (UGGG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-glucose:glycoprotein glucosyltransferase 1

Short name=UGT1
Short name=hUGT1
EC=2.4.1.-
Alternative name(s):
UDP--Glc:glycoprotein glucosyltransferase
UDP-glucose ceramide glucosyltransferase-like 1
Gene names
Name:UGGT1
Synonyms:GT, UGCGL1, UGGT, UGT1, UGTR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1555 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. Ref.1

Cofactor

Calcium or manganese. Ref.1

Pathway

Protein modification; protein glycosylation.

Subunit structure

Monomer as well as in a tight complex with SEP15 By similarity. Interacts with METTL23. Ref.7 UniProtKB Q9JLA3

Subcellular location

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

Tissue specificity

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

Induction

By tunicamycin and A23187. Induced 3-4 fold 10 hours after treatment. Ref.1

Domain

The N-terminal non-catalytic domain is assumed to mediate recognition of proteins with partial folding defects By similarity.

Sequence similarities

Belongs to the glycosyltransferase 8 family. Ref.1

Sequence caution

The sequence AAY14885.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAB14632.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NYU2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9NYU2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4242 By similarity
Chain43 – 15551513UDP-glucose:glycoprotein glucosyltransferase 1
PRO_0000012271

Regions

Region1244 – 1555312Glucosyltransferase By similarity
Motif1552 – 15554Prevents secretion from ER Potential

Amino acid modifications

Modified residue12771Phosphoserine Ref.6
Glycosylation5361N-linked (GlcNAc...) Potential
Glycosylation12281N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 2424Missing in isoform 2.
VSP_036508

Experimental info

Mutagenesis1452 – 14576Missing: Inactive. Ref.1
Mutagenesis14521D → A: Inactive. Ref.1
Mutagenesis14531Q → A: 4% active. Ref.1
Mutagenesis14541D → A: Inactive. Ref.1
Mutagenesis14551L → A: 2% active. Ref.1
Mutagenesis14561P → A: 41% active. Ref.1
Mutagenesis14571N → A: 7% active. Ref.1
Sequence conflict14871A → T in BAB14632. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 3, 2009. Version 3.
Checksum: 0A5274A4A65152D3

FASTA1,555177,190
        10         20         30         40         50         60 
MGCKGDASGA CAAGALPVTG VCYKMGVLVV LTVLWLFSSV KADSKAITTS LTTKWFSTPL 

        70         80         90        100        110        120 
LLEASEFLAE DSQEKFWNFV EASQNIGSSD HDGTDYSYYH AILEAAFQFL SPLQQNLFKF 

       130        140        150        160        170        180 
CLSLRSYSAT IQAFQQIAAD EPPPEGCNSF FSVHGKKTCE SDTLEALLLT ASERPKPLLF 

       190        200        210        220        230        240 
KGDHRYPSSN PESPVVIFYS EIGSEEFSNF HRQLISKSNA GKINYVFRHY IFNPRKEPVY 

       250        260        270        280        290        300 
LSGYGVELAI KSTEYKAKDD TQVKGTEVNT TVIGENDPID EVQGFLFGKL RDLHPDLEGQ 

       310        320        330        340        350        360 
LKELRKHLVE STNEMAPLKV WQLQDLSFQT AARILASPVE LALVVMKDLS QNFPTKARAI 

       370        380        390        400        410        420 
TKTAVSSELR TEVEENQKYF KGTLGLQPGD SALFINGLHM DLDTQDIFSL FDVLRNEARV 

       430        440        450        460        470        480 
MEGLHRLGIE GLSLHNVLKL NIQPSEADYA VDIRSPAISW VNNLEVDSRY NSWPSSLQEL 

       490        500        510        520        530        540 
LRPTFPGVIR QIRKNLHNMV FIVDPAHETT AELMNTAEMF LSNHIPLRIG FIFVVNDSED 

       550        560        570        580        590        600 
VDGMQDAGVA VLRAYNYVAQ EVDDYHAFQT LTHIYNKVRT GEKVKVEHVV SVLEKKYPYV 

       610        620        630        640        650        660 
EVNSILGIDS AYDRNRKEAR GYYEQTGVGP LPVVLFNGMP FEREQLDPDE LETITMHKIL 

       670        680        690        700        710        720 
ETTTFFQRAV YLGELPHDQD VVEYIMNQPN VVPRINSRIL TAERDYLDLT ASNNFFVDDY 

       730        740        750        760        770        780 
ARFTILDSQG KTAAVANSMN YLTKKGMSSK EIYDDSFIRP VTFWIVGDFD SPSGRQLLYD 

       790        800        810        820        830        840 
AIKHQKSSNN VRISMINNPA KEISYENTQI SRAIWAALQT QTSNAAKNFI TKMAKEGAAE 

       850        860        870        880        890        900 
ALAAGADIAE FSVGGMDFSL FKEVFESSKM DFILSHAVYC RDVLKLKKGQ RAVISNGRII 

       910        920        930        940        950        960 
GPLEDSELFN QDDFHLLENI ILKTSGQKIK SHIQQLRVEE DVASDLVMKV DALLSAQPKG 

       970        980        990       1000       1010       1020 
DPRIEYQFFE DRHSAIKLRP KEGETYFDVV AVVDPVTREA QRLAPLLLVL AQLINMNLRV 

      1030       1040       1050       1060       1070       1080 
FMNCQSKLSD MPLKSFYRYV LEPEISFTSD NSFAKGPIAK FLDMPQSPLF TLNLNTPESW 

      1090       1100       1110       1120       1130       1140 
MVESVRTPYD LDNIYLEEVD SVVAAEYELE YLLLEGHCYD ITTGQPPRGL QFTLGTSANP 

      1150       1160       1170       1180       1190       1200 
VIVDTIVMAN LGYFQLKANP GAWILRLRKG RSEDIYRIYS HDGTDSPPDA DEVVIVLNNF 

      1210       1220       1230       1240       1250       1260 
KSKIIKVKVQ KKADMVNEDL LSDGTSENES GFWDSFKWGF TGQKTEEVKQ DKDDIINIFS 

      1270       1280       1290       1300       1310       1320 
VASGHLYERF LRIMMLSVLK NTKTPVKFWF LKNYLSPTFK EFIPYMANEY NFQYELVQYK 

      1330       1340       1350       1360       1370       1380 
WPRWLHQQTE KQRIIWGYKI LFLDVLFPLV VDKFLFVDAD QIVRTDLKEL RDFNLDGAPY 

      1390       1400       1410       1420       1430       1440 
GYTPFCDSRR EMDGYRFWKS GYWASHLAGR KYHISALYVV DLKKFRKIAA GDRLRGQYQG 

      1450       1460       1470       1480       1490       1500 
LSQDPNSLSN LDQDLPNNMI HQVPIKSLPQ EWLWCETWCD DASKKRAKTI DLCNNPMTKE 

      1510       1520       1530       1540       1550 
PKLEAAVRIV PEWQDYDQEI KQLQIRFQKE KETGALYKEK TKEPSREGPQ KREEL 

« Hide

Isoform 2 [UniParc].

Checksum: C3EDD499D6043569
Show »

FASTA1,531174,977

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] (ISOFORM 1), FUNCTION, COFACTOR, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-1452; GLN-1453; ASP-1454; LEU-1455; PRO-1456 AND ASN-1457.
Tissue: Fetal liver.
[2]"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. expand/collapse author list , 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].
[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] (ISOFORM 2).
Tissue: Eye.
[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] OF 710-1555 (ISOFORMS 1/2).
Tissue: Placenta.
[5]"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].
[6]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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
AF227905 mRNA. Translation: AAF66232.1.
AC017079 Genomic DNA. Translation: AAY14735.1.
AC108059 Genomic DNA. Translation: AAY14885.1. Sequence problems.
BC041098 mRNA. Translation: AAH41098.1.
AK023671 mRNA. Translation: BAB14632.1. Different initiation.
CCDSCCDS2154.1. [Q9NYU2-1]
RefSeqNP_064505.1. NM_020120.3. [Q9NYU2-1]
UniGeneHs.743306.

3D structure databases

ProteinModelPortalQ9NYU2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121217. 28 interactions.
IntActQ9NYU2. 2 interactions.
STRING9606.ENSP00000259253.

Protein family/group databases

CAZyGT24. Glycosyltransferase Family 24.

PTM databases

PhosphoSiteQ9NYU2.

Polymorphism databases

DMDM224471872.

Proteomic databases

MaxQBQ9NYU2.
PaxDbQ9NYU2.
PRIDEQ9NYU2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259253; ENSP00000259253; ENSG00000136731. [Q9NYU2-1]
ENST00000375990; ENSP00000365158; ENSG00000136731. [Q9NYU2-2]
GeneID56886.
KEGGhsa:56886.
UCSCuc002tpr.3. human. [Q9NYU2-1]

Organism-specific databases

CTD56886.
GeneCardsGC02P128848.
H-InvDBHIX0002447.
HGNCHGNC:15663. UGGT1.
HPAHPA012761.
HPA015127.
MIM605897. gene.
neXtProtNX_Q9NYU2.
PharmGKBPA38014.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320899.
HOGENOMHOG000184622.
HOVERGENHBG079469.
InParanoidQ9NYU2.
KOK11718.
OMARDYLDLT.
OrthoDBEOG75J0M7.
PhylomeDBQ9NYU2.
TreeFamTF300320.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9NYU2.
BgeeQ9NYU2.
CleanExHS_UGCGL1.
GenevestigatorQ9NYU2.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR029044. Nucleotide-diphossugar_trans.
IPR009448. UDP-g_GGtrans.
[Graphical view]
PANTHERPTHR11226. PTHR11226. 1 hit.
PfamPF06427. UDP-g_GGTase. 1 hit.
[Graphical view]
SUPFAMSSF53448. SSF53448. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUGGT1. human.
GenomeRNAi56886.
NextBio62283.
PROQ9NYU2.
SOURCESearch...

Entry information

Entry nameUGGG1_HUMAN
AccessionPrimary (citable) accession number: Q9NYU2
Secondary accession number(s): Q53QP2 expand/collapse secondary AC list , Q53SL3, Q8IW30, Q9H8I4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: March 3, 2009
Last modified: July 9, 2014
This is version 112 of the entry and version 3 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 chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM