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Q9NYU2

- UGGG1_HUMAN

UniProt

Q9NYU2 - UGGG1_HUMAN

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
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 3 (03 Mar 2009)
      Previous versions | rss
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    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

    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

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1452 – 14576Missing: Inactive. 1 Publication
    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

    ArrayExpressiQ9NYU2.
    BgeeiQ9NYU2.
    CleanExiHS_UGCGL1.
    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. 29 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.
    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

    MGCKGDASGA CAAGALPVTG VCYKMGVLVV LTVLWLFSSV KADSKAITTS     50
    LTTKWFSTPL LLEASEFLAE DSQEKFWNFV EASQNIGSSD HDGTDYSYYH 100
    AILEAAFQFL SPLQQNLFKF CLSLRSYSAT IQAFQQIAAD EPPPEGCNSF 150
    FSVHGKKTCE SDTLEALLLT ASERPKPLLF KGDHRYPSSN PESPVVIFYS 200
    EIGSEEFSNF HRQLISKSNA GKINYVFRHY IFNPRKEPVY LSGYGVELAI 250
    KSTEYKAKDD TQVKGTEVNT TVIGENDPID EVQGFLFGKL RDLHPDLEGQ 300
    LKELRKHLVE STNEMAPLKV WQLQDLSFQT AARILASPVE LALVVMKDLS 350
    QNFPTKARAI TKTAVSSELR TEVEENQKYF KGTLGLQPGD SALFINGLHM 400
    DLDTQDIFSL FDVLRNEARV MEGLHRLGIE GLSLHNVLKL NIQPSEADYA 450
    VDIRSPAISW VNNLEVDSRY NSWPSSLQEL LRPTFPGVIR QIRKNLHNMV 500
    FIVDPAHETT AELMNTAEMF LSNHIPLRIG FIFVVNDSED VDGMQDAGVA 550
    VLRAYNYVAQ EVDDYHAFQT LTHIYNKVRT GEKVKVEHVV SVLEKKYPYV 600
    EVNSILGIDS AYDRNRKEAR GYYEQTGVGP LPVVLFNGMP FEREQLDPDE 650
    LETITMHKIL ETTTFFQRAV YLGELPHDQD VVEYIMNQPN VVPRINSRIL 700
    TAERDYLDLT ASNNFFVDDY ARFTILDSQG KTAAVANSMN YLTKKGMSSK 750
    EIYDDSFIRP VTFWIVGDFD SPSGRQLLYD AIKHQKSSNN VRISMINNPA 800
    KEISYENTQI SRAIWAALQT QTSNAAKNFI TKMAKEGAAE ALAAGADIAE 850
    FSVGGMDFSL FKEVFESSKM DFILSHAVYC RDVLKLKKGQ RAVISNGRII 900
    GPLEDSELFN QDDFHLLENI ILKTSGQKIK SHIQQLRVEE DVASDLVMKV 950
    DALLSAQPKG DPRIEYQFFE DRHSAIKLRP KEGETYFDVV AVVDPVTREA 1000
    QRLAPLLLVL AQLINMNLRV FMNCQSKLSD MPLKSFYRYV LEPEISFTSD 1050
    NSFAKGPIAK FLDMPQSPLF TLNLNTPESW MVESVRTPYD LDNIYLEEVD 1100
    SVVAAEYELE YLLLEGHCYD ITTGQPPRGL QFTLGTSANP VIVDTIVMAN 1150
    LGYFQLKANP GAWILRLRKG RSEDIYRIYS HDGTDSPPDA DEVVIVLNNF 1200
    KSKIIKVKVQ KKADMVNEDL LSDGTSENES GFWDSFKWGF TGQKTEEVKQ 1250
    DKDDIINIFS VASGHLYERF LRIMMLSVLK NTKTPVKFWF LKNYLSPTFK 1300
    EFIPYMANEY NFQYELVQYK WPRWLHQQTE KQRIIWGYKI LFLDVLFPLV 1350
    VDKFLFVDAD QIVRTDLKEL RDFNLDGAPY GYTPFCDSRR EMDGYRFWKS 1400
    GYWASHLAGR KYHISALYVV DLKKFRKIAA GDRLRGQYQG LSQDPNSLSN 1450
    LDQDLPNNMI HQVPIKSLPQ EWLWCETWCD DASKKRAKTI DLCNNPMTKE 1500
    PKLEAAVRIV PEWQDYDQEI KQLQIRFQKE KETGALYKEK TKEPSREGPQ 1550
    KREEL 1555
    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. 29 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.
    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

    ArrayExpressi Q9NYU2.
    Bgeei Q9NYU2.
    CleanExi HS_UGCGL1.
    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

    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 1, 2014
    This is version 114 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