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Q9QZU9

- UB2L6_MOUSE

UniProt

Q9QZU9 - UB2L6_MOUSE

Protein

Ubiquitin/ISG15-conjugating enzyme E2 L6

Gene

Ube2l6

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
  1. Functioni

    Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3 By similarity.By similarity

    Catalytic activityi

    ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei86 – 861Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ISG15 ligase activity Source: MGI
    3. protein binding Source: MGI
    4. small conjugating protein ligase activity Source: MGI

    GO - Biological processi

    1. ISG15-protein conjugation Source: MGI
    2. modification-dependent protein catabolic process Source: MGI
    3. protein ubiquitination Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198533. ISG15 antiviral mechanism.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin/ISG15-conjugating enzyme E2 L6 (EC:6.3.2.19)
    Alternative name(s):
    UbcM8
    Ubiquitin carrier protein L6
    Ubiquitin-protein ligase L6
    Gene namesi
    Name:Ube2l6
    Synonyms:Ubce8
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1914500. Ube2l6.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 153153Ubiquitin/ISG15-conjugating enzyme E2 L6PRO_0000082479Add
    BLAST

    Post-translational modificationi

    ISGylated.By similarity

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PaxDbiQ9QZU9.
    PRIDEiQ9QZU9.

    PTM databases

    PhosphoSiteiQ9QZU9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9QZU9.
    BgeeiQ9QZU9.
    CleanExiMM_UBE2L6.
    GenevestigatoriQ9QZU9.

    Interactioni

    Subunit structurei

    Interacts with RNF19A, RNF19B and RNF144B. Interacts with FLT3 (tyrosine phosphorylated) By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000107264.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9QZU9.
    SMRiQ9QZU9. Positions 3-152.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5078.
    GeneTreeiENSGT00740000115416.
    HOGENOMiHOG000233455.
    HOVERGENiHBG063308.
    KOiK04553.
    OMAiPEKPPYN.
    OrthoDBiEOG7GXPD8.
    TreeFamiTF313043.

    Family and domain databases

    Gene3Di3.10.110.10. 1 hit.
    InterProiIPR000608. UBQ-conjugat_E2.
    IPR023313. UBQ-conjugating_AS.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view]
    PfamiPF00179. UQ_con. 1 hit.
    [Graphical view]
    SUPFAMiSSF54495. SSF54495. 1 hit.
    PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
    PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9QZU9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMASKRVAKE LESLSKELPP YLRQLSSDDA NVLVWHMLLL PDQLPYGLKA    50
    FQVRIDFPRE YPFKPPTLRF TTKIYHPNVR EDGLVCLPLI SNENWKPYTK 100
    PYQVLEALNV LVSKPNLEEP VRLELADLLT QNPEMFRKKA EEFTLKFGVD 150
    RPS 153
    Length:153
    Mass (Da):17,841
    Last modified:May 26, 2009 - v3
    Checksum:i71EEFF050CDE57F1
    GO

    Sequence cautioni

    The sequence AAD55978.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 291D → Y in AAD55978. 1 PublicationCurated
    Sequence conflicti63 – 631F → L in AAH08238. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF159230 mRNA. Translation: AAD55978.1. Different initiation.
    AK010942 mRNA. Translation: BAB27282.1.
    AK013452 mRNA. Translation: BAB28861.1.
    AK152010 mRNA. Translation: BAE30873.1.
    AK152113 mRNA. Translation: BAE30957.1.
    AK168695 mRNA. Translation: BAE40539.1.
    AK171629 mRNA. Translation: BAE42574.1.
    CH466519 Genomic DNA. Translation: EDL27303.1.
    BC008238 mRNA. Translation: AAH08238.1.
    CCDSiCCDS16194.2.
    RefSeqiNP_064333.2. NM_019949.2.
    UniGeneiMm.38261.

    Genome annotation databases

    EnsembliENSMUST00000102642; ENSMUSP00000099702; ENSMUSG00000027078.
    GeneIDi56791.
    KEGGimmu:56791.
    UCSCiuc012byn.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF159230 mRNA. Translation: AAD55978.1 . Different initiation.
    AK010942 mRNA. Translation: BAB27282.1 .
    AK013452 mRNA. Translation: BAB28861.1 .
    AK152010 mRNA. Translation: BAE30873.1 .
    AK152113 mRNA. Translation: BAE30957.1 .
    AK168695 mRNA. Translation: BAE40539.1 .
    AK171629 mRNA. Translation: BAE42574.1 .
    CH466519 Genomic DNA. Translation: EDL27303.1 .
    BC008238 mRNA. Translation: AAH08238.1 .
    CCDSi CCDS16194.2.
    RefSeqi NP_064333.2. NM_019949.2.
    UniGenei Mm.38261.

    3D structure databases

    ProteinModelPortali Q9QZU9.
    SMRi Q9QZU9. Positions 3-152.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000107264.

    PTM databases

    PhosphoSitei Q9QZU9.

    Proteomic databases

    PaxDbi Q9QZU9.
    PRIDEi Q9QZU9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000102642 ; ENSMUSP00000099702 ; ENSMUSG00000027078 .
    GeneIDi 56791.
    KEGGi mmu:56791.
    UCSCi uc012byn.1. mouse.

    Organism-specific databases

    CTDi 9246.
    MGIi MGI:1914500. Ube2l6.

    Phylogenomic databases

    eggNOGi COG5078.
    GeneTreei ENSGT00740000115416.
    HOGENOMi HOG000233455.
    HOVERGENi HBG063308.
    KOi K04553.
    OMAi PEKPPYN.
    OrthoDBi EOG7GXPD8.
    TreeFami TF313043.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_198533. ISG15 antiviral mechanism.

    Miscellaneous databases

    ChiTaRSi UBE2L6. mouse.
    NextBioi 313332.
    PROi Q9QZU9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9QZU9.
    Bgeei Q9QZU9.
    CleanExi MM_UBE2L6.
    Genevestigatori Q9QZU9.

    Family and domain databases

    Gene3Di 3.10.110.10. 1 hit.
    InterProi IPR000608. UBQ-conjugat_E2.
    IPR023313. UBQ-conjugating_AS.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view ]
    Pfami PF00179. UQ_con. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54495. SSF54495. 1 hit.
    PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
    PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Progression from mammary hyperplasia to adenocarcinoma in MMTV-FGF8b transgenic mice is associated with altered expression of CD63, IGFBP7/mac25, alpha-synuclein, and UbcM8."
      Cook G., Lawshe A., MacArthur C.A.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
      Strain: C57BL/6J and NOD.
      Tissue: Bone marrow, Embryo and Embryonic liver.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-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].

    Entry informationi

    Entry nameiUB2L6_MOUSE
    AccessioniPrimary (citable) accession number: Q9QZU9
    Secondary accession number(s): Q3U8R0, Q922F1, Q9CQN0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: May 26, 2009
    Last modified: October 1, 2014
    This is version 113 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3