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Q9NYU2

- UGGG1_HUMAN

UniProt

Q9NYU2 - UGGG1_HUMAN

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Protein

UDP-glucose:glycoprotein glucosyltransferase 1

Gene

UGGT1

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.1 Publication

Cofactori

Calcium or manganese.1 Publication

Pathwayi

GO - Molecular functioni

  1. UDP-glucose:glycoprotein glucosyltransferase activity Source: UniProtKB
  2. unfolded protein binding Source: UniProtKB

GO - Biological processi

  1. 'de novo' posttranslational protein folding Source: UniProtKB
  2. cellular protein metabolic process Source: Reactome
  3. post-translational protein modification Source: Reactome
  4. protein folding Source: Reactome
  5. protein N-linked glycosylation via asparagine 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 1 (EC:2.4.1.-)
Short name:
UGT1
Short name:
hUGT1
Alternative name(s):
UDP--Glc:glycoprotein glucosyltransferase
UDP-glucose ceramide glucosyltransferase-like 1
Gene namesi
Name:UGGT1
Synonyms:GT, UGCGL1, UGGT, UGT11 Publication, UGTRBy similarity
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:15663. UGGT1.

Subcellular locationi

Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation. Endoplasmic reticulum-Golgi intermediate compartment 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  3. endoplasmic reticulum lumen Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1452 – 14576Missing: Inactive.
Mutagenesisi1452 – 14521D → A: Inactive. 1 Publication
Mutagenesisi1453 – 14531Q → A: 4% active. 1 Publication
Mutagenesisi1454 – 14541D → A: Inactive. 1 Publication
Mutagenesisi1455 – 14551L → A: 2% active. 1 Publication
Mutagenesisi1456 – 14561P → A: 41% active. 1 Publication
Mutagenesisi1457 – 14571N → A: 7% active. 1 Publication

Organism-specific databases

PharmGKBiPA38014.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4242By similarityAdd
BLAST
Chaini43 – 15551513UDP-glucose:glycoprotein glucosyltransferase 1PRO_0000012271Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi536 – 5361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1228 – 12281N-linked (GlcNAc...)Sequence Analysis
Modified residuei1277 – 12771Phosphoserine1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9NYU2.
PaxDbiQ9NYU2.
PRIDEiQ9NYU2.

PTM databases

PhosphoSiteiQ9NYU2.

Expressioni

Tissue specificityi

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

Inductioni

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

Gene expression databases

BgeeiQ9NYU2.
CleanExiHS_UGCGL1.
ExpressionAtlasiQ9NYU2. baseline and differential.
GenevestigatoriQ9NYU2.

Organism-specific databases

HPAiHPA012761.
HPA015127.

Interactioni

Subunit structurei

Monomer as well as in a tight complex with SEP15 By similarity. Interacts with METTL23.By similarity1 Publication

Protein-protein interaction databases

BioGridi121217. 30 interactions.
IntActiQ9NYU2. 2 interactions.
STRINGi9606.ENSP00000259253.

Structurei

3D structure databases

ProteinModelPortaliQ9NYU2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1244 – 1555312GlucosyltransferaseBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1552 – 15554Prevents secretion from ERPROSITE-ProRule annotation

Domaini

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

Sequence similaritiesi

Belongs to the glycosyltransferase 8 family.1 Publication

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG320899.
GeneTreeiENSGT00390000004600.
HOGENOMiHOG000184622.
HOVERGENiHBG079469.
InParanoidiQ9NYU2.
KOiK11718.
OMAiRDYLDLT.
OrthoDBiEOG75J0M7.
PhylomeDBiQ9NYU2.
TreeFamiTF300320.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR029044. Nucleotide-diphossugar_trans.
IPR009448. UDP-g_GGtrans.
[Graphical view]
PANTHERiPTHR11226. PTHR11226. 1 hit.
PfamiPF06427. UDP-g_GGTase. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NYU2-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGCKGDASGA CAAGALPVTG VCYKMGVLVV LTVLWLFSSV KADSKAITTS
60 70 80 90 100
LTTKWFSTPL LLEASEFLAE DSQEKFWNFV EASQNIGSSD HDGTDYSYYH
110 120 130 140 150
AILEAAFQFL SPLQQNLFKF CLSLRSYSAT IQAFQQIAAD EPPPEGCNSF
160 170 180 190 200
FSVHGKKTCE SDTLEALLLT ASERPKPLLF KGDHRYPSSN PESPVVIFYS
210 220 230 240 250
EIGSEEFSNF HRQLISKSNA GKINYVFRHY IFNPRKEPVY LSGYGVELAI
260 270 280 290 300
KSTEYKAKDD TQVKGTEVNT TVIGENDPID EVQGFLFGKL RDLHPDLEGQ
310 320 330 340 350
LKELRKHLVE STNEMAPLKV WQLQDLSFQT AARILASPVE LALVVMKDLS
360 370 380 390 400
QNFPTKARAI TKTAVSSELR TEVEENQKYF KGTLGLQPGD SALFINGLHM
410 420 430 440 450
DLDTQDIFSL FDVLRNEARV MEGLHRLGIE GLSLHNVLKL NIQPSEADYA
460 470 480 490 500
VDIRSPAISW VNNLEVDSRY NSWPSSLQEL LRPTFPGVIR QIRKNLHNMV
510 520 530 540 550
FIVDPAHETT AELMNTAEMF LSNHIPLRIG FIFVVNDSED VDGMQDAGVA
560 570 580 590 600
VLRAYNYVAQ EVDDYHAFQT LTHIYNKVRT GEKVKVEHVV SVLEKKYPYV
610 620 630 640 650
EVNSILGIDS AYDRNRKEAR GYYEQTGVGP LPVVLFNGMP FEREQLDPDE
660 670 680 690 700
LETITMHKIL ETTTFFQRAV YLGELPHDQD VVEYIMNQPN VVPRINSRIL
710 720 730 740 750
TAERDYLDLT ASNNFFVDDY ARFTILDSQG KTAAVANSMN YLTKKGMSSK
760 770 780 790 800
EIYDDSFIRP VTFWIVGDFD SPSGRQLLYD AIKHQKSSNN VRISMINNPA
810 820 830 840 850
KEISYENTQI SRAIWAALQT QTSNAAKNFI TKMAKEGAAE ALAAGADIAE
860 870 880 890 900
FSVGGMDFSL FKEVFESSKM DFILSHAVYC RDVLKLKKGQ RAVISNGRII
910 920 930 940 950
GPLEDSELFN QDDFHLLENI ILKTSGQKIK SHIQQLRVEE DVASDLVMKV
960 970 980 990 1000
DALLSAQPKG DPRIEYQFFE DRHSAIKLRP KEGETYFDVV AVVDPVTREA
1010 1020 1030 1040 1050
QRLAPLLLVL AQLINMNLRV FMNCQSKLSD MPLKSFYRYV LEPEISFTSD
1060 1070 1080 1090 1100
NSFAKGPIAK FLDMPQSPLF TLNLNTPESW MVESVRTPYD LDNIYLEEVD
1110 1120 1130 1140 1150
SVVAAEYELE YLLLEGHCYD ITTGQPPRGL QFTLGTSANP VIVDTIVMAN
1160 1170 1180 1190 1200
LGYFQLKANP GAWILRLRKG RSEDIYRIYS HDGTDSPPDA DEVVIVLNNF
1210 1220 1230 1240 1250
KSKIIKVKVQ KKADMVNEDL LSDGTSENES GFWDSFKWGF TGQKTEEVKQ
1260 1270 1280 1290 1300
DKDDIINIFS VASGHLYERF LRIMMLSVLK NTKTPVKFWF LKNYLSPTFK
1310 1320 1330 1340 1350
EFIPYMANEY NFQYELVQYK WPRWLHQQTE KQRIIWGYKI LFLDVLFPLV
1360 1370 1380 1390 1400
VDKFLFVDAD QIVRTDLKEL RDFNLDGAPY GYTPFCDSRR EMDGYRFWKS
1410 1420 1430 1440 1450
GYWASHLAGR KYHISALYVV DLKKFRKIAA GDRLRGQYQG LSQDPNSLSN
1460 1470 1480 1490 1500
LDQDLPNNMI HQVPIKSLPQ EWLWCETWCD DASKKRAKTI DLCNNPMTKE
1510 1520 1530 1540 1550
PKLEAAVRIV PEWQDYDQEI KQLQIRFQKE KETGALYKEK TKEPSREGPQ

KREEL
Length:1,555
Mass (Da):177,190
Last modified:March 3, 2009 - v3
Checksum:i0A5274A4A65152D3
GO
Isoform 2 (identifier: Q9NYU2-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,531
Mass (Da):174,977
Checksum:iC3EDD499D6043569
GO

Sequence cautioni

The sequence BAB14632.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAY14885.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1487 – 14871A → T in BAB14632. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2424Missing in isoform 2. 1 PublicationVSP_036508Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS2154.1. [Q9NYU2-1]
RefSeqiNP_064505.1. NM_020120.3. [Q9NYU2-1]
UniGeneiHs.743306.

Genome annotation databases

EnsembliENST00000259253; ENSP00000259253; ENSG00000136731. [Q9NYU2-1]
GeneIDi56886.
KEGGihsa:56886.
UCSCiuc002tpr.3. human. [Q9NYU2-1]

Polymorphism databases

DMDMi224471872.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS2154.1. [Q9NYU2-1 ]
RefSeqi NP_064505.1. NM_020120.3. [Q9NYU2-1 ]
UniGenei Hs.743306.

3D structure databases

ProteinModelPortali Q9NYU2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121217. 30 interactions.
IntActi Q9NYU2. 2 interactions.
STRINGi 9606.ENSP00000259253.

Protein family/group databases

CAZyi GT24. Glycosyltransferase Family 24.

PTM databases

PhosphoSitei Q9NYU2.

Polymorphism databases

DMDMi 224471872.

Proteomic databases

MaxQBi Q9NYU2.
PaxDbi Q9NYU2.
PRIDEi Q9NYU2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000259253 ; ENSP00000259253 ; ENSG00000136731 . [Q9NYU2-1 ]
GeneIDi 56886.
KEGGi hsa:56886.
UCSCi uc002tpr.3. human. [Q9NYU2-1 ]

Organism-specific databases

CTDi 56886.
GeneCardsi GC02P128848.
H-InvDB HIX0002447.
HGNCi HGNC:15663. UGGT1.
HPAi HPA012761.
HPA015127.
MIMi 605897. gene.
neXtProti NX_Q9NYU2.
PharmGKBi PA38014.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG320899.
GeneTreei ENSGT00390000004600.
HOGENOMi HOG000184622.
HOVERGENi HBG079469.
InParanoidi Q9NYU2.
KOi K11718.
OMAi RDYLDLT.
OrthoDBi EOG75J0M7.
PhylomeDBi Q9NYU2.
TreeFami TF300320.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi UGGT1. human.
GenomeRNAii 56886.
NextBioi 62283.
PROi Q9NYU2.
SOURCEi Search...

Gene expression databases

Bgeei Q9NYU2.
CleanExi HS_UGCGL1.
ExpressionAtlasi Q9NYU2. baseline and differential.
Genevestigatori Q9NYU2.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR029044. Nucleotide-diphossugar_trans.
IPR009448. UDP-g_GGtrans.
[Graphical view ]
PANTHERi PTHR11226. PTHR11226. 1 hit.
Pfami 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] (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 liverImported.
  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] [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: EyeImported.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 710-1555 (ISOFORMS 1/2).
    Tissue: PlacentaImported.
  5. 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.

Entry informationi

Entry nameiUGGG1_HUMAN
AccessioniPrimary (citable) accession number: Q9NYU2
Secondary accession number(s): Q53QP2
, Q53SL3, Q8IW30, Q9H8I4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: March 3, 2009
Last modified: October 29, 2014
This is version 115 of the entry and version 3 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3