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Q5U300

- UBA1_RAT

UniProt

Q5U300 - UBA1_RAT

Protein

Ubiquitin-like modifier-activating enzyme 1

Gene

Uba1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (07 Dec 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Essential for the formation of radiation-induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei632 – 6321Glycyl thioester intermediateBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi478 – 50730ATPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ubiquitin activating enzyme activity Source: RefGenome
    3. ubiquitin-protein transferase activity Source: RefGenome

    GO - Biological processi

    1. modification-dependent protein catabolic process Source: RefGenome
    2. protein ubiquitination Source: RefGenome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-like modifier-activating enzyme 1By similarity
    Alternative name(s):
    Ubiquitin-activating enzyme E1By similarity
    Gene namesi
    Name:Uba1Imported
    Synonyms:Ube1By similarity
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome X

    Organism-specific databases

    RGDi1359327. Uba1.

    Subcellular locationi

    Cytoplasm By similarity. Mitochondrion By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: RefGenome
    3. mitochondrion Source: UniProtKB
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 10581057Ubiquitin-like modifier-activating enzyme 1PRO_0000365096Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei4 – 41PhosphoserineBy similarity
    Modified residuei13 – 131PhosphoserineBy similarity
    Modified residuei46 – 461PhosphoserineBy similarity
    Modified residuei55 – 551PhosphotyrosineBy similarity
    Modified residuei528 – 5281N6-succinyllysineBy similarity
    Modified residuei671 – 6711N6-acetyllysineBy similarity
    Modified residuei800 – 8001PhosphothreonineBy similarity
    Modified residuei810 – 8101PhosphoserineBy similarity
    Modified residuei816 – 8161PhosphoserineBy similarity
    Modified residuei820 – 8201PhosphoserineBy similarity
    Modified residuei835 – 8351PhosphoserineBy similarity
    Modified residuei980 – 9801N6-acetyllysineBy similarity

    Post-translational modificationi

    ISGylated.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ5U300.
    PRIDEiQ5U300.

    PTM databases

    PhosphoSiteiQ5U300.

    Expressioni

    Gene expression databases

    GenevestigatoriQ5U300.

    Interactioni

    Subunit structurei

    Monomer. Interacts with GAN (via BTB domain) By similarity.By similarity

    Protein-protein interaction databases

    BioGridi260716. 3 interactions.
    STRINGi10116.ENSRNOP00000033950.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5U300.
    SMRiQ5U300. Positions 48-1057.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati63 – 1991371-1Sequence AnalysisAdd
    BLAST
    Repeati459 – 6111531-2Sequence AnalysisAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni63 – 6115492 approximate repeatsSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ubiquitin-activating E1 family.Sequence Analysis

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0476.
    GeneTreeiENSGT00390000016689.
    HOGENOMiHOG000167329.
    HOVERGENiHBG054199.
    InParanoidiQ5U300.
    KOiK03178.
    OMAiPFFAFSE.
    OrthoDBiEOG74R1PV.
    PhylomeDBiQ5U300.
    TreeFamiTF300586.

    Family and domain databases

    Gene3Di1.10.3240.10. 1 hit.
    3.40.50.720. 4 hits.
    InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR018965. Ub-activating_enz_e1_C.
    IPR023280. Ub-like_act_enz_cat_cys_dom.
    IPR000127. UBact_repeat.
    IPR019572. Ubiquitin-activating_enzyme.
    IPR018075. UBQ-activ_enz_E1.
    IPR018074. UBQ-activ_enz_E1_AS.
    IPR000011. UBQ/SUMO-activ_enz_E1-like.
    [Graphical view]
    PfamiPF00899. ThiF. 2 hits.
    PF09358. UBA_e1_C. 1 hit.
    PF10585. UBA_e1_thiolCys. 1 hit.
    PF02134. UBACT. 2 hits.
    [Graphical view]
    PRINTSiPR01849. UBIQUITINACT.
    SMARTiSM00985. UBA_e1_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF69572. SSF69572. 2 hits.
    TIGRFAMsiTIGR01408. Ube1. 1 hit.
    PROSITEiPS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
    PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q5U300-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSPLSKKR RVSGPDPKPG SNCSSAQSVL SEVSSVPTNG MAKNGSEADI     50
    DESLYSRQLY VLGHEAMKML QTSSVLVSGL RGLGVEIAKN IILGGVKAVT 100
    LHDQGTTQWA DLSSQFYLRE EDIGKNRAEV SQPRLAELNS YVPVTAYTGP 150
    LVEDFLSGFQ VVVLTNSPLE EQLRVGEFCH SRGIKLVVAD TRGLFGQLFC 200
    DFGEEMVLTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH GFETGDFVSF 250
    SEVQGMVQLN GCQPIEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK 300
    ISFKSLPASL AEPDFVMTDF AKYSRPAQLH IGFQALHQFC AQHNRPPRPR 350
    NEEDATELVT LAQAVNARSP PAVQQDNVDE DLIRKLAYVA AGDLAPINAF 400
    IGGLAAQEVM KACSGKFMPI MQWLYFDALE CLPEDKEALT EDKCLPRQNR 450
    YDGQVAVFGS DLQEKLGKQK YFLVGAGAIG CELLKNFAMI GLGCGEGGEV 500
    VVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN PYIQVTSHQN 550
    RVGPDTERIY DDDFFQNLDG VANALDNVDA RMYMDRRCVY YRKPLLESGT 600
    LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD 650
    EFEGLFKQPA ENVNQYLTDS KFVERTLRLA GTQPLEVLEA VQRSLVLQRP 700
    QTWGDCVTWA CHHWHTQYCN NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH 750
    PLTFDVNNTL HLDYVMAAAN LFAQTYGLTG SQDRAAVASL LQSVQVPEFT 800
    PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP GFKMYPIDFE 850
    KDDDSNFHMD FIVAASNLRA ENYDISPADR HKSKLIAGKI IPAIATTTAA 900
    VVGLVCLELY KVVQGHQQLD SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ 950
    EWTLWDRFEV QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF 1000
    FMPAAKLKER LDQPMTEIVS RVSKRKLGRH VRALVLELCC NDESGEDVEV 1050
    PYVRYTIR 1058
    Length:1,058
    Mass (Da):117,788
    Last modified:December 7, 2004 - v1
    Checksum:iFAC21190A3014F79
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH474009 Genomic DNA. Translation: EDL97701.1.
    CH474009 Genomic DNA. Translation: EDL97702.1.
    BC085791 mRNA. Translation: AAH85791.1.
    RefSeqiNP_001014102.1. NM_001014080.1.
    XP_006256674.1. XM_006256612.1.
    UniGeneiRn.11800.

    Genome annotation databases

    EnsembliENSRNOT00000031115; ENSRNOP00000033950; ENSRNOG00000019164.
    GeneIDi314432.
    KEGGirno:314432.
    UCSCiRGD:1359327. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH474009 Genomic DNA. Translation: EDL97701.1 .
    CH474009 Genomic DNA. Translation: EDL97702.1 .
    BC085791 mRNA. Translation: AAH85791.1 .
    RefSeqi NP_001014102.1. NM_001014080.1.
    XP_006256674.1. XM_006256612.1.
    UniGenei Rn.11800.

    3D structure databases

    ProteinModelPortali Q5U300.
    SMRi Q5U300. Positions 48-1057.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 260716. 3 interactions.
    STRINGi 10116.ENSRNOP00000033950.

    PTM databases

    PhosphoSitei Q5U300.

    Proteomic databases

    PaxDbi Q5U300.
    PRIDEi Q5U300.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000031115 ; ENSRNOP00000033950 ; ENSRNOG00000019164 .
    GeneIDi 314432.
    KEGGi rno:314432.
    UCSCi RGD:1359327. rat.

    Organism-specific databases

    CTDi 7317.
    RGDi 1359327. Uba1.

    Phylogenomic databases

    eggNOGi COG0476.
    GeneTreei ENSGT00390000016689.
    HOGENOMi HOG000167329.
    HOVERGENi HBG054199.
    InParanoidi Q5U300.
    KOi K03178.
    OMAi PFFAFSE.
    OrthoDBi EOG74R1PV.
    PhylomeDBi Q5U300.
    TreeFami TF300586.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    NextBioi 667673.
    PROi Q5U300.

    Gene expression databases

    Genevestigatori Q5U300.

    Family and domain databases

    Gene3Di 1.10.3240.10. 1 hit.
    3.40.50.720. 4 hits.
    InterProi IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    IPR018965. Ub-activating_enz_e1_C.
    IPR023280. Ub-like_act_enz_cat_cys_dom.
    IPR000127. UBact_repeat.
    IPR019572. Ubiquitin-activating_enzyme.
    IPR018075. UBQ-activ_enz_E1.
    IPR018074. UBQ-activ_enz_E1_AS.
    IPR000011. UBQ/SUMO-activ_enz_E1-like.
    [Graphical view ]
    Pfami PF00899. ThiF. 2 hits.
    PF09358. UBA_e1_C. 1 hit.
    PF10585. UBA_e1_thiolCys. 1 hit.
    PF02134. UBACT. 2 hits.
    [Graphical view ]
    PRINTSi PR01849. UBIQUITINACT.
    SMARTi SM00985. UBA_e1_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69572. SSF69572. 2 hits.
    TIGRFAMsi TIGR01408. Ube1. 1 hit.
    PROSITEi PS00536. UBIQUITIN_ACTIVAT_1. 1 hit.
    PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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].
    2. "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].
      Strain: Brown Norway1 Publication.
      Tissue: KidneyImported.
    3. Maurya D.K., Bhargava P.
      Submitted (JAN-2009) to UniProtKB
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiUBA1_RAT
    AccessioniPrimary (citable) accession number: Q5U300
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 3, 2009
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are two active sites within the E1 molecule, allowing it to accommodate two ubiquitin moieties at a time, with a new ubiquitin forming an adenylate intermediate as the previous one is transferred to the thiol site.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3