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Q8C878

- UBA3_MOUSE

UniProt

Q8C878 - UBA3_MOUSE

Protein

NEDD8-activating enzyme E1 catalytic subunit

Gene

Uba3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Down-regulates steroid receptor activity. Necessary for cell cycle progression.1 Publication

    Enzyme regulationi

    Binding of TP53BP2 to the regulatory subunit NAE1 decreases activity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei211 – 2111Determines specificity for NEDD8By similarity
    Active sitei237 – 2371Glycyl thioester intermediatePROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi100 – 12425ATPBy similarityAdd
    BLAST
    Nucleotide bindingi148 – 17124ATPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. NEDD8 activating enzyme activity Source: RefGenome
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. endomitotic cell cycle Source: MGI
    2. mitotic cell cycle Source: MGI
    3. protein neddylation Source: RefGenome
    4. regulation of cell cycle Source: MGI

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Cell cycle, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00885.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NEDD8-activating enzyme E1 catalytic subunit (EC:6.3.2.-)
    Alternative name(s):
    NEDD8-activating enzyme E1C
    Ubiquitin-activating enzyme E1C
    Ubiquitin-like modifier-activating enzyme 3
    Short name:
    Ubiquitin-activating enzyme 3
    Gene namesi
    Name:Uba3
    Synonyms:Ube1c
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1341217. Uba3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: RefGenome
    2. nucleus Source: RefGenome

    Pathology & Biotechi

    Involvement in diseasei

    Defects in Uba3 are a cause of embryonic lethality. Mouse embryos deficient in Uba3 die at the preimplantation stage.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 462461NEDD8-activating enzyme E1 catalytic subunitPRO_0000194942Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8C878.
    PaxDbiQ8C878.
    PRIDEiQ8C878.

    PTM databases

    PhosphoSiteiQ8C878.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8C878.
    BgeeiQ8C878.
    CleanExiMM_UBA3.
    GenevestigatoriQ8C878.

    Interactioni

    Subunit structurei

    Heterodimer of UBA3 and NAE1. Interacts with NEDD8, UBE2F and UBE2M. Binds ESR1 and ESR2 with bound steroid ligand By similarity. Interacts with TBATA.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi204409. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C878.
    SMRiQ8C878. Positions 33-462.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 7018Interaction with UBE2M N-terminusBy similarityAdd
    BLAST
    Regioni157 – 1615Interaction with UBE2M N-terminusBy similarity
    Regioni192 – 21726Interaction with UBE2M N-terminusBy similarityAdd
    BLAST
    Regioni227 – 2293Interaction with NEDD8By similarity
    Regioni242 – 2487Interaction with NAE1By similarity
    Regioni292 – 2954Interaction with NAE1By similarity
    Regioni331 – 3388Interaction with UBE2M N-terminusBy similarity
    Regioni352 – 3576Interaction with NEDD8By similarity
    Regioni368 – 46295Interaction with UBE2M core domainBy similarityAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0476.
    GeneTreeiENSGT00550000074831.
    HOGENOMiHOG000166793.
    HOVERGENiHBG082736.
    InParanoidiQ3TG68.
    KOiK10686.
    OMAiDHIQWIF.
    TreeFamiTF300499.

    Family and domain databases

    Gene3Di1.10.10.520. 1 hit.
    3.10.20.260. 1 hit.
    3.40.50.720. 2 hits.
    InterProiIPR014929. E2_binding.
    IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR023318. Ub_act_enz_dom_a.
    IPR000127. UBact_repeat.
    IPR019572. Ubiquitin-activating_enzyme.
    IPR018074. UBQ-activ_enz_E1_AS.
    [Graphical view]
    PfamiPF08825. E2_bind. 1 hit.
    PF00899. ThiF. 1 hit.
    PF10585. UBA_e1_thiolCys. 1 hit.
    PF02134. UBACT. 1 hit.
    [Graphical view]
    SUPFAMiSSF69572. SSF69572. 1 hit.
    PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 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: Q8C878-1) [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

    MADGEEPEKK RRRIEELLAE KMAVDGGCGD TGDWEGRWNH VKKFLERSGP    50
    FTHPDFEPST ESLQFLLDTC KVLVIGAGGL GCELLKNLAL SGFRQIHVID 100
    MDTIDVSNLN RQFLFRPKDV GRPKAEVAAE FLNDRVPNCN VVPHFNKIQD 150
    FNDTFYRQFH IIVCGLDSII ARRWINGMLI SLLNYEDGVL DPSSIVPLID 200
    GGTEGFKGNA RVILPGMTAC IECTLELYPP QVNFPMCTIA SMPRLPEHCI 250
    EYVRMLQWPK EQPFGDGVPL DGDDPEHIQW IFQKSIERAS QYNIRGVTYR 300
    LTQGVVKRII PAVASTNAVI AAVCATEVFK IATSAYIPLN NYLVFNDVDG 350
    LYTYTFEAER KENCPACSQL PQNIQFSPSA KLQEVLDYLT NSASLQMKSP 400
    AITATLEGKN RTLYLQSVTS IEERTRPNLS KTLKELGLVD GQELAVADVT 450
    TPQTVLFKLH FT 462
    Length:462
    Mass (Da):51,737
    Last modified:July 27, 2011 - v2
    Checksum:i4034CE39E6E9A14E
    GO
    Isoform 2 (identifier: Q8C878-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         396-462: Missing.

    Show »
    Length:395
    Mass (Da):44,326
    Checksum:i01E494E63C4166CB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471K → E in BAB29346. (PubMed:16141072)Curated
    Sequence conflicti334 – 3341S → G in BAB29346. (PubMed:16141072)Curated
    Sequence conflicti397 – 3971M → I in BAC33258. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei396 – 46267Missing in isoform 2. 1 PublicationVSP_010787Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK014433 mRNA. Translation: BAB29346.1.
    AK032514 mRNA. Translation: BAC27905.1.
    AK048148 mRNA. Translation: BAC33258.1.
    AK159381 mRNA. Translation: BAE35036.1.
    AK168859 mRNA. Translation: BAE40680.1.
    CH466523 Genomic DNA. Translation: EDK99352.1.
    BC002002 mRNA. Translation: AAH02002.1.
    AF077330 mRNA. Translation: AAC27323.1.
    AY029181 mRNA. Translation: AAK33015.1.
    CCDSiCCDS51860.1. [Q8C878-1]
    RefSeqiNP_001104576.1. NM_001111106.1.
    NP_035796.2. NM_011666.2. [Q8C878-1]
    XP_006505974.1. XM_006505911.1.
    XP_006505975.1. XM_006505912.1.
    XP_006505976.1. XM_006505913.1.
    UniGeneiMm.277626.

    Genome annotation databases

    EnsembliENSMUST00000089287; ENSMUSP00000086701; ENSMUSG00000030061. [Q8C878-1]
    GeneIDi22200.
    KEGGimmu:22200.
    UCSCiuc009dam.2. mouse. [Q8C878-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK014433 mRNA. Translation: BAB29346.1 .
    AK032514 mRNA. Translation: BAC27905.1 .
    AK048148 mRNA. Translation: BAC33258.1 .
    AK159381 mRNA. Translation: BAE35036.1 .
    AK168859 mRNA. Translation: BAE40680.1 .
    CH466523 Genomic DNA. Translation: EDK99352.1 .
    BC002002 mRNA. Translation: AAH02002.1 .
    AF077330 mRNA. Translation: AAC27323.1 .
    AY029181 mRNA. Translation: AAK33015.1 .
    CCDSi CCDS51860.1. [Q8C878-1 ]
    RefSeqi NP_001104576.1. NM_001111106.1.
    NP_035796.2. NM_011666.2. [Q8C878-1 ]
    XP_006505974.1. XM_006505911.1.
    XP_006505975.1. XM_006505912.1.
    XP_006505976.1. XM_006505913.1.
    UniGenei Mm.277626.

    3D structure databases

    ProteinModelPortali Q8C878.
    SMRi Q8C878. Positions 33-462.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204409. 2 interactions.

    PTM databases

    PhosphoSitei Q8C878.

    Proteomic databases

    MaxQBi Q8C878.
    PaxDbi Q8C878.
    PRIDEi Q8C878.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000089287 ; ENSMUSP00000086701 ; ENSMUSG00000030061 . [Q8C878-1 ]
    GeneIDi 22200.
    KEGGi mmu:22200.
    UCSCi uc009dam.2. mouse. [Q8C878-1 ]

    Organism-specific databases

    CTDi 9039.
    MGIi MGI:1341217. Uba3.

    Phylogenomic databases

    eggNOGi COG0476.
    GeneTreei ENSGT00550000074831.
    HOGENOMi HOG000166793.
    HOVERGENi HBG082736.
    InParanoidi Q3TG68.
    KOi K10686.
    OMAi DHIQWIF.
    TreeFami TF300499.

    Enzyme and pathway databases

    UniPathwayi UPA00885 .
    Reactomei REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    NextBioi 302185.
    PROi Q8C878.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8C878.
    Bgeei Q8C878.
    CleanExi MM_UBA3.
    Genevestigatori Q8C878.

    Family and domain databases

    Gene3Di 1.10.10.520. 1 hit.
    3.10.20.260. 1 hit.
    3.40.50.720. 2 hits.
    InterProi IPR014929. E2_binding.
    IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR023318. Ub_act_enz_dom_a.
    IPR000127. UBact_repeat.
    IPR019572. Ubiquitin-activating_enzyme.
    IPR018074. UBQ-activ_enz_E1_AS.
    [Graphical view ]
    Pfami PF08825. E2_bind. 1 hit.
    PF00899. ThiF. 1 hit.
    PF10585. UBA_e1_thiolCys. 1 hit.
    PF02134. UBACT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69572. SSF69572. 1 hit.
    PROSITEi PS00865. UBIQUITIN_ACTIVAT_2. 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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Embryonic head, Kidney and Placenta.
    2. 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].
    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] OF 3-462 (ISOFORM 1).
    4. "Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway."
      Gong L., Yeh E.T.H.
      J. Biol. Chem. 274:12036-12042(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-462 (ISOFORM 1).
      Tissue: Liver.
    5. "The NEDD8 system is essential for cell cycle progression and morphogenetic pathway in mice."
      Tateishi K., Omata M., Tanaka K., Chiba T.
      J. Cell Biol. 155:571-580(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-462 (ISOFORM 1), FUNCTION.
      Strain: C57BL/6.
    6. Cited for: INTERACTION WITH TBATA.

    Entry informationi

    Entry nameiUBA3_MOUSE
    AccessioniPrimary (citable) accession number: Q8C878
    Secondary accession number(s): O88598, Q3TG68, Q9D6B7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 105 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Arg-211 acts as a selectivity gate, preventing misactivation of ubiquitin by this NEDD8-specific E1 complex.By similarity

    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