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Q9D8C3

- ALG13_MOUSE

UniProt

Q9D8C3 - ALG13_MOUSE

Protein

Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13

Gene

Alg13

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (15 Jun 2010)
      Previous versions | rss
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    Functioni

    Isoform 1: Possible multifunctional enzyme with both glycosyltransferase and deubiquitinase activities.
    Isoform 2: May be involved in protein N-glycosylation, second step of the dolichol-linked oligosaccharide pathway (By. similarity).

    Catalytic activityi

    UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-diphosphodolichol = UDP + N,N'-diacetylchitobiosyl-diphosphodolichol.
    Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei233 – 2331For deubiquitinase activityBy similarity
    Active sitei236 – 2361Nucleophile; for deubiquitinase activityBy similarity
    Active sitei339 – 3391For deubiquitinase activityBy similarity

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. cysteine-type peptidase activity Source: UniProtKB-KW
    3. N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. lipid glycosylation Source: InterPro

    Keywords - Molecular functioni

    Glycosyltransferase, Hydrolase, Protease, Thiol protease, Transferase

    Keywords - Biological processi

    Ubl conjugation pathway

    Protein family/group databases

    CAZyiGT1. Glycosyltransferase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13 (EC:2.4.1.141, EC:3.4.19.12)
    Alternative name(s):
    Asparagine-linked glycosylation 13 homolog
    Glycosyltransferase 28 domain-containing protein 1
    UDP-N-acetylglucosamine transferase subunit ALG13 homolog
    Gene namesi
    Name:Alg13
    Synonyms:Glt28d1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1914824. Alg13.

    Subcellular locationi

    Endoplasmic reticulum By similarity
    Note: Could be recruited to the cytosolic face of the endoplasmic reticulum membrane through its interaction with ALG14.By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11661166Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13PRO_0000254574Add
    BLAST

    Proteomic databases

    MaxQBiQ9D8C3.
    PaxDbiQ9D8C3.
    PRIDEiQ9D8C3.

    PTM databases

    PhosphoSiteiQ9D8C3.

    Expressioni

    Gene expression databases

    BgeeiQ9D8C3.
    GenevestigatoriQ9D8C3.

    Interactioni

    Subunit structurei

    Isoform 2 may interact with ALG14.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000042810.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D8C3.
    SMRiQ9D8C3. Positions 2-176, 215-343.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini225 – 346122OTUPROSITE-ProRule annotationAdd
    BLAST
    Domaini486 – 54661TudorPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 125125Glycosyltransferase activityBy similarityAdd
    BLAST
    Regioni126 – 394269Deubiquitinase activityBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi875 – 1033159Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyltransferase 28 family.Curated
    Contains 1 OTU domain.PROSITE-ProRule annotation
    Contains 1 Tudor domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5017.
    GeneTreeiENSGT00510000047493.
    HOGENOMiHOG000192807.
    HOVERGENiHBG056051.
    InParanoidiA3KGC8.
    KOiK07432.
    OMAiNERLMDN.
    OrthoDBiEOG7NPFVV.
    PhylomeDBiQ9D8C3.
    TreeFamiTF313788.

    Family and domain databases

    InterProiIPR007235. Glyco_trans_28_C.
    IPR003323. OTU.
    IPR002999. Tudor.
    [Graphical view]
    PfamiPF04101. Glyco_tran_28_C. 1 hit.
    PF02338. OTU. 1 hit.
    [Graphical view]
    PROSITEiPS50802. OTU. 1 hit.
    PS50304. TUDOR. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9D8C3-1) [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

    MKRAFVTVGT TSFDELVARV VANDCVQILE SLGYNHLVLQ VGRGTVVPKP     50
    FRTESFTLDV YRYKDSLKED LQQADLVISH AGAGSCLESL EKGKPLVVVV 100
    NEKLMNNHQF ELAKQLHKEG HLFYCTCRVL SCPAPVSLLL VLLGSAKILQ 150
    QLPSATLSCF GYLPTQAPVL VATAYSYLHS VFSSFPPLST FLIIPCTMQK 200
    GWKKYCGQKS LNEASMDEYL GSLGLFRKVV AKDASCLFRA ISEQLFHSQI 250
    HHLQIRRACV SYMKENQQAF ESYVEGSFEK YLERLGDPKE SAGQLELKAL 300
    SLIYNRDFII YRYPGKPPTQ VTDNGFEDKI ILCYSNNGHY DSVYSKEFQS 350
    TAGICQAILY ELLYKDVFVV DEETLKTAVD LFRSGSRRNK HHALTASVEG 400
    SSDQKSSTED RTEEAAACSS AASTPEGNKQ GTERQKVPES PSKMLFPYKV 450
    LKALDPEIYR NVEFDAWLDS RKELQKSECV EYGGRYYFLG DKCQVCMESG 500
    GKYYNAHIQE IDNDKSSVVV FIEEFAERHS IPLAHVRPVN QVALLPSWNA 550
    IPIRNGRGYP TITGGYFPEI VMTDMNMKQR KKMFKKFRGK EIYMTMAYSR 600
    GDPLVPSRIQ HSMHYGHDPL LYYSQTAGHI LSSQHFYPQH SSQRQGRGYG 650
    MPRDSSHLIS KQNLPNPKVG FCSGSGRKCC QSYDNVSYRS RSFRRSHRQM 700
    HCMNKGCQYG FAPENGVEET VTFYALEEGN ETAYSTLPNN GGPTTMVPAT 750
    SGYCVARQGY NSCKPPLNSG DSNDHCDNGG YHGDYLYSSE QGYETSSVYT 800
    TTVSTANLSL QDSGPSSVPQ DTVTSYNYPQ KVLENSAAIA VSWASHVPVP 850
    VIPNCAGDNE ALRTSDISSQ NAIQPGFVPP PAQGSPAYLE PSAAGAAGAA 900
    AAAAAAAAPV ATPVAAPLPL PPPLPPPPPA TLEAGDASGF PLPPPPPPPP 950
    PPPPPYSYDP SGSDLPQDTK VLQYYFNLGL QCYHHNYWHP MVYMPHVQQQ 1000
    LQPQPQPQPQ PQPQPQPQPQ PQPQQPQQQQ PPPQQQQQQQ EQVHGESYPD 1050
    CTEQPLVDQS APQVYSDVVR EDGTQADVST NDTFPIADAV PLPHGAVYYP 1100
    VMTDPYGSPL LGFDSYVPVA SDYSSIAMWH PVNAACGASA QIHGAMNPGP 1150
    IGYMLLPNSP HYTPQN 1166
    Length:1,166
    Mass (Da):128,664
    Last modified:June 15, 2010 - v2
    Checksum:i5F045ACF188BBE8A
    GO
    Isoform 2 (identifier: Q9D8C3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         128-165: RVLSCPAPVS...TLSCFGYLPT → STLPGLLQSM...FLDKVVGLQK
         166-1166: Missing.

    Show »
    Length:165
    Mass (Da):18,346
    Checksum:i947DFE404D54FA8C
    GO

    Sequence cautioni

    The sequence CAM45938.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAM45939.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 2 (identifier: Q9D8C3-2)
    Sequence conflicti149 – 1491Q → H in BAB29554. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei128 – 16538RVLSC…GYLPT → STLPGLLQSMDLSTLKCYPP GQPEKFSAFLDKVVGLQK in isoform 2. 2 PublicationsVSP_039304Add
    BLAST
    Alternative sequencei166 – 11661001Missing in isoform 2. 2 PublicationsVSP_039305Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK008162 mRNA. Translation: BAB25504.1.
    AK014790 mRNA. Translation: BAB29554.1.
    AK086546 mRNA. Translation: BAC39689.1.
    AK089102 mRNA. Translation: BAC40750.1.
    AL713978 Genomic DNA. Translation: CAM45936.1.
    AL713978 Genomic DNA. Translation: CAM45938.1. Sequence problems.
    AL713978 Genomic DNA. Translation: CAM45939.1. Sequence problems.
    CH466610 Genomic DNA. Translation: EDL14725.1.
    BC053004 mRNA. No translation available.
    BC137692 mRNA. Translation: AAI37693.1.
    CCDSiCCDS30456.1. [Q9D8C3-2]
    RefSeqiNP_080523.2. NM_026247.3. [Q9D8C3-2]
    UniGeneiMm.249084.
    Mm.484110.

    Genome annotation databases

    EnsembliENSMUST00000070801; ENSMUSP00000068403; ENSMUSG00000041718. [Q9D8C3-2]
    GeneIDi67574.
    KEGGimmu:67574.
    UCSCiuc009ums.2. mouse. [Q9D8C3-2]
    uc009umu.2. mouse. [Q9D8C3-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK008162 mRNA. Translation: BAB25504.1 .
    AK014790 mRNA. Translation: BAB29554.1 .
    AK086546 mRNA. Translation: BAC39689.1 .
    AK089102 mRNA. Translation: BAC40750.1 .
    AL713978 Genomic DNA. Translation: CAM45936.1 .
    AL713978 Genomic DNA. Translation: CAM45938.1 . Sequence problems.
    AL713978 Genomic DNA. Translation: CAM45939.1 . Sequence problems.
    CH466610 Genomic DNA. Translation: EDL14725.1 .
    BC053004 mRNA. No translation available.
    BC137692 mRNA. Translation: AAI37693.1 .
    CCDSi CCDS30456.1. [Q9D8C3-2 ]
    RefSeqi NP_080523.2. NM_026247.3. [Q9D8C3-2 ]
    UniGenei Mm.249084.
    Mm.484110.

    3D structure databases

    ProteinModelPortali Q9D8C3.
    SMRi Q9D8C3. Positions 2-176, 215-343.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000042810.

    Protein family/group databases

    CAZyi GT1. Glycosyltransferase Family 1.

    PTM databases

    PhosphoSitei Q9D8C3.

    Proteomic databases

    MaxQBi Q9D8C3.
    PaxDbi Q9D8C3.
    PRIDEi Q9D8C3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000070801 ; ENSMUSP00000068403 ; ENSMUSG00000041718 . [Q9D8C3-2 ]
    GeneIDi 67574.
    KEGGi mmu:67574.
    UCSCi uc009ums.2. mouse. [Q9D8C3-2 ]
    uc009umu.2. mouse. [Q9D8C3-1 ]

    Organism-specific databases

    CTDi 79868.
    MGIi MGI:1914824. Alg13.

    Phylogenomic databases

    eggNOGi COG5017.
    GeneTreei ENSGT00510000047493.
    HOGENOMi HOG000192807.
    HOVERGENi HBG056051.
    InParanoidi A3KGC8.
    KOi K07432.
    OMAi NERLMDN.
    OrthoDBi EOG7NPFVV.
    PhylomeDBi Q9D8C3.
    TreeFami TF313788.

    Miscellaneous databases

    NextBioi 324945.
    PROi Q9D8C3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9D8C3.
    Genevestigatori Q9D8C3.

    Family and domain databases

    InterProi IPR007235. Glyco_trans_28_C.
    IPR003323. OTU.
    IPR002999. Tudor.
    [Graphical view ]
    Pfami PF04101. Glyco_tran_28_C. 1 hit.
    PF02338. OTU. 1 hit.
    [Graphical view ]
    PROSITEi PS50802. OTU. 1 hit.
    PS50304. TUDOR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: C57BL/6J and NOD.
      Tissue: Head, Small intestine and Thymus.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6.
      Tissue: Fetal brain.

    Entry informationi

    Entry nameiALG13_MOUSE
    AccessioniPrimary (citable) accession number: Q9D8C3
    Secondary accession number(s): A3KGC8
    , A3KGD0, A3KGD1, Q8BUA4, Q9D5Z6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: June 15, 2010
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3