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P41226

- UBA7_HUMAN

UniProt

P41226 - UBA7_HUMAN

Protein

Ubiquitin-like modifier-activating enzyme 7

Gene

UBA7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    Activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Catalyzes the ISGylation of influenza A virus NS1 protein.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei599 – 5991Glycyl thioester intermediatePROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi442 – 47130ATPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ISG15 activating enzyme activity Source: HGNC
    3. ubiquitin activating enzyme activity Source: RefGenome
    4. ubiquitin-protein transferase activity Source: RefGenome

    GO - Biological processi

    1. cellular protein modification process Source: HGNC
    2. cytokine-mediated signaling pathway Source: Reactome
    3. innate immune response Source: Reactome
    4. ISG15-protein conjugation Source: HGNC
    5. modification-dependent protein catabolic process Source: RefGenome
    6. negative regulation of type I interferon production Source: Reactome
    7. 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_115831. ISG15 antiviral mechanism.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-like modifier-activating enzyme 7
    Short name:
    Ubiquitin-activating enzyme 7
    Alternative name(s):
    D8
    Ubiquitin-activating enzyme E1 homolog
    Gene namesi
    Name:UBA7
    Synonyms:UBE1L, UBE2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:12471. UBA7.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162407761.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10121012Ubiquitin-like modifier-activating enzyme 7PRO_0000194937Add
    BLAST

    Post-translational modificationi

    ISGylated.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiP41226.
    PaxDbiP41226.
    PRIDEiP41226.

    PTM databases

    PhosphoSiteiP41226.

    Expressioni

    Tissue specificityi

    Expressed in a variety of normal and tumor cell types, but is reduced in lung cancer cell lines.

    Gene expression databases

    BgeeiP41226.
    CleanExiHS_UBA7.
    GenevestigatoriP41226.

    Organism-specific databases

    HPAiCAB015444.

    Interactioni

    Subunit structurei

    Monomer By similarity. Binds and is involved in the conjugation of G1P2/ISG15.By similarity

    Protein-protein interaction databases

    BioGridi113166. 5 interactions.
    DIPiDIP-60526N.
    IntActiP41226. 1 interaction.
    MINTiMINT-1454413.
    STRINGi9606.ENSP00000333266.

    Structurei

    3D structure databases

    ProteinModelPortaliP41226.
    SMRiP41226. Positions 10-1006.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati23 – 1591371-1Add
    BLAST
    Repeati423 – 5751531-2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni23 – 5755532 approximate repeatsAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ubiquitin-activating E1 family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0476.
    HOGENOMiHOG000167329.
    HOVERGENiHBG054199.
    InParanoidiP41226.
    KOiK10698.
    OMAiLGHWQLC.
    OrthoDBiEOG74R1PV.
    PhylomeDBiP41226.
    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.
    PROSITEiPS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P41226-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDALDASKLL DEELYSRQLY VLGSPAMQRI QGARVLVSGL QGLGAEVAKN     50
    LVLMGVGSLT LHDPHPTCWS DLAAQFLLSE QDLERSRAEA SQELLAQLNR 100
    AVQVVVHTGD ITEDLLLDFQ VVVLTAAKLE EQLKVGTLCH KHGVCFLAAD 150
    TRGLVGQLFC DFGEDFTVQD PTEAEPLTAA IQHISQGSPG ILTLRKGANT 200
    HYFRDGDLVT FSGIEGMVEL NDCDPRSIHV REDGSLEIGD TTTFSRYLRG 250
    GAITEVKRPK TVRHKSLDTA LLQPHVVAQS SQEVHHAHCL HQAFCALHKF 300
    QHLHGRPPQP WDPVDAETVV GLARDLEPLK RTEEEPLEEP LDEALVRTVA 350
    LSSAGVLSPM VAMLGAVAAQ EVLKAISRKF MPLDQWLYFD ALDCLPEDGE 400
    LLPSPEDCAL RGSRYDGQIA VFGAGFQEKL RRQHYLLVGA GAIGCELLKV 450
    FALVGLGAGN SGGLTVVDMD HIERSNLSRQ FLFRSQDVGR PKAEVAAAAA 500
    RGLNPDLQVI PLTYPLDPTT EHIYGDNFFS RVDGVAAALD SFQARRYVAA 550
    RCTHYLKPLL EAGTSGTWGS ATVFMPHVTE AYRAPASAAA SEDAPYPVCT 600
    VRYFPSTAEH TLQWARHEFE ELFRLSAETI NHHQQAHTSL ADMDEPQTLT 650
    LLKPVLGVLR VRPQNWQDCV AWALGHWKLC FHYGIKQLLR HFPPNKVLED 700
    GTPFWSGPKQ CPQPLEFDTN QDTHLLYVLA AANLYAQMHG LPGSQDWTAL 750
    RELLKLLPQP DPQQMAPIFA SNLELASASA EFGPEQQKEL NKALEVWSVG 800
    PPLKPLMFEK DDDSNFHVDF VVAAASLRCQ NYGIPPVNRA QSKRIVGQII 850
    PAIATTTAAV AGLLGLELYK VVSGPRPRSA FRHSYLHLAE NYLIRYMPFA 900
    PAIQTFHHLK WTSWDRLKVP AGQPERTLES LLAHLQEQHG LRVRILLHGS 950
    ALLYAAGWSP EKQAQHLPLR VTELVQQLTG QAPAPGQRVL VLELSCEGDD 1000
    EDTAFPPLHY EL 1012
    Length:1,012
    Mass (Da):111,694
    Last modified:November 25, 2008 - v2
    Checksum:iA01E1106D81778EB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti355 – 37824GVLSP…KAISR → RCLEPMVACWVSSCPGSAEG NLQ in AAA75388. (PubMed:8327486)CuratedAdd
    BLAST
    Sequence conflicti355 – 37824GVLSP…KAISR → RCLEPMVACWVSSCPGSAEG NLQ in AAG49557. (PubMed:7734949)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti712 – 7121P → S.
    Corresponds to variant rs11928913 [ dbSNP | Ensembl ].
    VAR_052434
    Natural varianti817 – 8171H → R.
    Corresponds to variant rs2230149 [ dbSNP | Ensembl ].
    VAR_047793

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13852 mRNA. Translation: AAA75388.1.
    AF294032 Genomic DNA. Translation: AAG49557.1.
    BT007026 mRNA. Translation: AAP35672.1.
    CH471055 Genomic DNA. Translation: EAW65023.1.
    BC006378 mRNA. Translation: AAH06378.1.
    CCDSiCCDS2805.1.
    RefSeqiNP_003326.2. NM_003335.2.
    UniGeneiHs.16695.

    Genome annotation databases

    EnsembliENST00000333486; ENSP00000333266; ENSG00000182179.
    GeneIDi7318.
    KEGGihsa:7318.
    UCSCiuc003cxr.3. human.

    Polymorphism databases

    DMDMi215273977.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13852 mRNA. Translation: AAA75388.1 .
    AF294032 Genomic DNA. Translation: AAG49557.1 .
    BT007026 mRNA. Translation: AAP35672.1 .
    CH471055 Genomic DNA. Translation: EAW65023.1 .
    BC006378 mRNA. Translation: AAH06378.1 .
    CCDSi CCDS2805.1.
    RefSeqi NP_003326.2. NM_003335.2.
    UniGenei Hs.16695.

    3D structure databases

    ProteinModelPortali P41226.
    SMRi P41226. Positions 10-1006.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113166. 5 interactions.
    DIPi DIP-60526N.
    IntActi P41226. 1 interaction.
    MINTi MINT-1454413.
    STRINGi 9606.ENSP00000333266.

    Chemistry

    ChEMBLi CHEMBL2321623.

    PTM databases

    PhosphoSitei P41226.

    Polymorphism databases

    DMDMi 215273977.

    Proteomic databases

    MaxQBi P41226.
    PaxDbi P41226.
    PRIDEi P41226.

    Protocols and materials databases

    DNASUi 7318.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000333486 ; ENSP00000333266 ; ENSG00000182179 .
    GeneIDi 7318.
    KEGGi hsa:7318.
    UCSCi uc003cxr.3. human.

    Organism-specific databases

    CTDi 7318.
    GeneCardsi GC03M049844.
    HGNCi HGNC:12471. UBA7.
    HPAi CAB015444.
    MIMi 191325. gene.
    neXtProti NX_P41226.
    PharmGKBi PA162407761.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0476.
    HOGENOMi HOG000167329.
    HOVERGENi HBG054199.
    InParanoidi P41226.
    KOi K10698.
    OMAi LGHWQLC.
    OrthoDBi EOG74R1PV.
    PhylomeDBi P41226.
    TreeFami TF300586.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    GeneWikii UBE1L.
    GenomeRNAii 7318.
    NextBioi 28610.
    PROi P41226.
    SOURCEi Search...

    Gene expression databases

    Bgeei P41226.
    CleanExi HS_UBA7.
    Genevestigatori P41226.

    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 PS00865. UBIQUITIN_ACTIVAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A gene in the chromosomal region 3p21 with greatly reduced expression in lung cancer is similar to the gene for ubiquitin-activating enzyme."
      Kok K., Hofstra R., Pilz A., van den Berg A., Terpstra P., Buys C.H.C.M., Carritt B.
      Proc. Natl. Acad. Sci. U.S.A. 90:6071-6075(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: B-cell.
    2. "The genomic structure of the human UBE1L gene."
      Kok K., Van den Berg A., Veldhuis P.M., Franke M., Terpstra P., Buys C.H.C.M.
      Gene Expr. 4:163-175(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Eye.
    6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-17.
      Tissue: Platelet.
    7. "Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein."
      Yuan W., Krug R.M.
      EMBO J. 20:362-371(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 973-987, INTERACTION WITH G1P2, PATHWAY.
    8. "Identification of interferon-stimulated gene 15 as an antiviral molecule during Sindbis virus infection in vivo."
      Lenschow D.J., Giannakopoulos N.V., Gunn L.J., Johnston C., O'Guin A.K., Schmidt R.E., Levine B., Virgin H.W. IV
      J. Virol. 79:13974-13983(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "ISG15 conjugation system targets the viral NS1 protein in influenza A virus-infected cells."
      Zhao C., Hsiang T.Y., Kuo R.L., Krug R.M.
      Proc. Natl. Acad. Sci. U.S.A. 107:2253-2258(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Covalent protein modification with ISG15 via a conserved cysteine in the hinge region."
      Bade V.N., Nickels J., Keusekotten K., Praefcke G.J.
      PLoS ONE 7:E38294-E38294(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISGYLATION.

    Entry informationi

    Entry nameiUBA7_HUMAN
    AccessioniPrimary (citable) accession number: P41226
    Secondary accession number(s): Q9BRB2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 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

    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.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3