Reviewed, UniProtKB/Swiss-Prot Q9NYU2 (UGGG1_HUMAN)

Names and origin

Protein names

Recommended name:
    UDP-glucose:glycoprotein glucosyltransferase 1
    EC=2.4.1.-
Alternative name(s):
    UDP-glucose ceramide glucosyltransferase-like 1
    UDP--Glc:glycoprotein glucosyltransferase
    HUGT1

Gene names

Name:	UGCGL1
Synonyms:	GT, UGGT, UGT1, UGTR

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1531 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.
Cofactor	Calcium or manganese.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Monomer as well as in a tight complex with SEP15 By similarity.
Subcellular location	Endoplasmic reticulum lumen. Endoplasmic reticulum-Golgi intermediate compartment.
Tissue specificity	Higher levels in pancreas, skeletal muscle, kidney, and brain. Low levels in lung and heart.
Induction	By tunicamycin and A23187. Induced 3-4 fold 10 hours after treatment.
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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	'de novo' posttranslational protein folding Ref.1 Traceable author statement. Source: UniProtKB protein amino acid glycosylation Inferred from electronic annotation. Source: InterPro
Cellular component	ER-Golgi intermediate compartment Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum Ref.1 Inferred from direct assay. Source: UniProtKB endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	UDP-glucose:glycoprotein glucosyltransferase activity Ref.1 Inferred from direct assay. Source: UniProtKB unfolded protein binding Ref.1 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CD40	P25942	1	EBI-1056389,EBI-525714
CHST12	Q9NRB3	1	EBI-1056389,EBI-1042837
HLA-A	P30450	1	EBI-1056389,EBI-1042870
HLA-A	P30457	1	EBI-1056389,EBI-1049899
SUSD2	Q9UGT4	1	EBI-1056389,EBI-1054721
TNFRSF14	Q92956	1	EBI-1056389,EBI-1056653
WISP1	O95388	1	EBI-1056389,EBI-1050638

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	By similarity
	Chain	19 – 1531	1513	UDP-glucose:glycoprotein glucosyltransferase 1		PRO_0000012271
Regions
	Region	1220 – 1531	312	Glucosyltransferase By similarity
	Motif	1528 – 1531	4	Prevents secretion from ER Potential
Amino acid modifications
	Modified residue	714	1	Phosphoserine
	Modified residue	717	1	Phosphotyrosine
	Modified residue	724	1	Phosphoserine
	Glycosylation	512	1	N-linked (GlcNAc...) Potential
	Glycosylation	1204	1	N-linked (GlcNAc...) Potential
Experimental info
	Mutagenesis	1428 – 1433	6	Missing: Inactive
	Mutagenesis	1428	1	D → A: Inactive
	Mutagenesis	1429	1	Q → A: 4% active
	Mutagenesis	1430	1	D → A: Inactive
	Mutagenesis	1431	1	L → A: 2% active
	Mutagenesis	1432	1	P → A: 41% active
	Mutagenesis	1433	1	N → A: 7% active
	Sequence conflict	1463	1	A → T in AAH41098. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9NYU2-1 [UniParc]. Last modified June 21, 2005. Version 2. Checksum: C3EDD499D6043569	FASTA	1,531	174,977
	10 20 30 40 50 60 MGVLVVLTVL WLFSSVKADS KAITTSLTTK WFSTPLLLEA SEFLAEDSQE KFWNFVEASQ 70 80 90 100 110 120 NIGSSDHDGT DYSYYHAILE AAFQFLSPLQ QNLFKFCLSL RSYSATIQAF QQIAADEPPP 130 140 150 160 170 180 EGCNSFFSVH GKKTCESDTL EALLLTASER PKPLLFKGDH RYPSSNPESP VVIFYSEIGS 190 200 210 220 230 240 EEFSNFHRQL ISKSNAGKIN YVFRHYIFNP RKEPVYLSGY GVELAIKSTE YKAKDDTQVK 250 260 270 280 290 300 GTEVNTTVIG ENDPIDEVQG FLFGKLRDLH PDLEGQLKEL RKHLVESTNE MAPLKVWQLQ 310 320 330 340 350 360 DLSFQTAARI LASPVELALV VMKDLSQNFP TKARAITKTA VSSELRTEVE ENQKYFKGTL 370 380 390 400 410 420 GLQPGDSALF INGLHMDLDT QDIFSLFDVL RNEARVMEGL HRLGIEGLSL HNVLKLNIQP 430 440 450 460 470 480 SEADYAVDIR SPAISWVNNL EVDSRYNSWP SSLQELLRPT FPGVIRQIRK NLHNMVFIVD 490 500 510 520 530 540 PAHETTAELM NTAEMFLSNH IPLRIGFIFV VNDSEDVDGM QDAGVAVLRA YNYVAQEVDD 550 560 570 580 590 600 YHAFQTLTHI YNKVRTGEKV KVEHVVSVLE KKYPYVEVNS ILGIDSAYDR NRKEARGYYE 610 620 630 640 650 660 QTGVGPLPVV LFNGMPFERE QLDPDELETI TMHKILETTT FFQRAVYLGE LPHDQDVVEY 670 680 690 700 710 720 IMNQPNVVPR INSRILTAER DYLDLTASNN FFVDDYARFT ILDSQGKTAA VANSMNYLTK 730 740 750 760 770 780 KGMSSKEIYD DSFIRPVTFW IVGDFDSPSG RQLLYDAIKH QKSSNNVRIS MINNPAKEIS 790 800 810 820 830 840 YENTQISRAI WAALQTQTSN AAKNFITKMA KEGAAEALAA GADIAEFSVG GMDFSLFKEV 850 860 870 880 890 900 FESSKMDFIL SHAVYCRDVL KLKKGQRAVI SNGRIIGPLE DSELFNQDDF HLLENIILKT 910 920 930 940 950 960 SGQKIKSHIQ QLRVEEDVAS DLVMKVDALL SAQPKGDPRI EYQFFEDRHS AIKLRPKEGE 970 980 990 1000 1010 1020 TYFDVVAVVD PVTREAQRLA PLLLVLAQLI NMNLRVFMNC QSKLSDMPLK SFYRYVLEPE 1030 1040 1050 1060 1070 1080 ISFTSDNSFA KGPIAKFLDM PQSPLFTLNL NTPESWMVES VRTPYDLDNI YLEEVDSVVA 1090 1100 1110 1120 1130 1140 AEYELEYLLL EGHCYDITTG QPPRGLQFTL GTSANPVIVD TIVMANLGYF QLKANPGAWI 1150 1160 1170 1180 1190 1200 LRLRKGRSED IYRIYSHDGT DSPPDADEVV IVLNNFKSKI IKVKVQKKAD MVNEDLLSDG 1210 1220 1230 1240 1250 1260 TSENESGFWD SFKWGFTGQK TEEVKQDKDD IINIFSVASG HLYERFLRIM MLSVLKNTKT 1270 1280 1290 1300 1310 1320 PVKFWFLKNY LSPTFKEFIP YMANEYNFQY ELVQYKWPRW LHQQTEKQRI IWGYKILFLD 1330 1340 1350 1360 1370 1380 VLFPLVVDKF LFVDADQIVR TDLKELRDFN LDGAPYGYTP FCDSRREMDG YRFWKSGYWA 1390 1400 1410 1420 1430 1440 SHLAGRKYHI SALYVVDLKK FRKIAAGDRL RGQYQGLSQD PNSLSNLDQD LPNNMIHQVP 1450 1460 1470 1480 1490 1500 IKSLPQEWLW CETWCDDASK KRAKTIDLCN NPMTKEPKLE AAVRIVPEWQ DYDQEIKQLQ 1510 1520 1530 IRFQKEKETG ALYKEKTKEP SREGPQKREE L

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: 10694380] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-1428; GLN-1429; ASP-1430; LEU-1431; PRO-1432 AND ASN-1433. 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. , 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: 15815621] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 686-1531. Tissue: Placenta.
[5]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714; TYR-717 AND SER-724, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF227905 mRNA. Translation: AAF66232.1. Different initiation. AC017079 Genomic DNA. Translation: AAY14735.1. AC108059 Genomic DNA. Translation: AAY14885.1. BC041098 mRNA. Translation: AAH41098.1. AK023671 mRNA. Translation: BAB14632.1. Different initiation.
RefSeq	NP_001020948.1. NP_064505.1.
UniGene	Hs.34180
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NYU2.
PTM databases
PhosphoSite	Q9NYU2.
Genome annotation databases
Ensembl	ENSG00000136731. Homo sapiens. [Contig view]
GeneID	56886.
KEGG	hsa:56886.
Organism-specific databases
H-InvDB	HIX0002447.
HGNC	HGNC:15663. UGCGL1.
HPA	HPA012761. HPA015127.
MIM	605897. gene.
PharmGKB	PA38014.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOVERGEN	Q9NYU2.
Gene expression databases
ArrayExpress	Q9NYU2.
CleanEx	HS_UGCGL1.
GermOnline	ENSG00000136731. Homo sapiens.
Family and domain databases
InterPro	IPR000886. ER_targeting_sequence. IPR009448. UDP-g_GGtrans. [Graphical view]
PANTHER	PTHR11226. UDP-g_GGtrans. 1 hit.
Pfam	PF06427. UDP-g_GGTase. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	62283.
SOURCE	Search...

Entry information

Entry name

UGGG1_HUMAN

Accession

Primary (citable) accession number: Q9NYU2
Secondary accession number(s): Q53QP2 , Q53SL3, Q8IW30, Q9H8I4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	June 21, 2005
Last modified:	November 25, 2008
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)