Q9VX91 · UBR1_DROME

Function

function

E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein ubiquitination.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentubiquitin ligase complex
Molecular Functionubiquitin protein ligase activity
Molecular Functionubiquitin-protein transferase activity
Molecular Functionzinc ion binding
Biological Processprotein ubiquitination
Biological Processubiquitin-dependent protein catabolic process via the N-end rule pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase UBR1
  • EC number
  • Alternative names
    • N-recognin
    • RING-type E3 ubiquitin transferase UBR1
    • Ubiquitin-protein ligase E3-alpha

Gene names

    • Name
      Ubr1
    • ORF names
      CG9086

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    Q9VX91
  • Secondary accessions
    • B5RIU9
    • Q8SX71

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000561391-1824E3 ubiquitin-protein ligase UBR1

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for zinc finger, region, compositional bias.

TypeIDPosition(s)Description
Zinc finger107-178UBR-type
Region1006-1043Disordered
Compositional bias1013-1028Polar residues
Region1073-1093Disordered
Zinc finger1126-1220RING-type; atypical

Domain

The RING-H2 zinc finger is an atypical RING finger with a His ligand in place of the fourth Cys of the classical motif.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,824
  • Mass (Da)
    208,361
  • Last updated
    2002-10-01 v2
  • Checksum
    79992C11175E82A0
MDRYDMEDVVVAPPAECSSPLKEWRLKRQAGTLDRSDIIEFLKRESPKYFDYQTSATVKDTNVITLKCMFKESLAKEEIIDVVVEFMLGDNPSSALEKLRLEGNTATVCGKVFKNGEPTYSCRECGVDPTCVLCVNCFKRSAHRFHKYKMSTSGGGGCCDCGDDEAWKKDQYCELHLANRKNPLESKILTDAVLERVEICFGAILAFCVSYLEIEPNASLQCLDGNVEGGQVDGAQYCTVLYNDESHTFDQVIQTLTKIAKCRAKDAMEIVAAIDREGRAVVKCDTFEECNKLKVSIENQMILPTSLVSTARNNQSLRTSVLHIGAVACQQFALQLLGWFQEFLVRHYLFRKTFSELVQRKQETFCIRHILEYDVKLWKTARTCWHRLLISGMLMEYDNKMILAQEFSRRYATIVEDFISDDHDHAFSIVSLSVQLFTVPSIAHHLIAHEGIFDKLLHTFYHVAIEKFIRNKTLHFSKNIASLTFFKRANYILYDLRYLLSLKPDVLSNDLRNGFLEGCRALMRVLNVMQGMESMTRQTGQHMDYEPEWECAFNLHIKLATTISQVIDWASGDVKLLRKLYKMTMRALVSNSFIVGGEKVMQPKKVADHVANCLVYDISVQPVSIHLPLSRFFAGIYLHLGAHDLTYDGLQTETEALSIKLTPREIIEPVLCTQAMIAQVGAGLWRRNGYTLLHQLYFYRNVRCRVEMLDRDIACLQIGASLMESNEFLIHVLNRFNTIPWLQENYWSLLSGNEMNDDIIREASIFDEFLELLIVIIGERWMPGVSMVTEEDRLRKEIIQLLCIKPYSHSELSRALPDGNSGNSDNVFEEVINTVAVFKKPVGADSKGVYELKEHLLKEFNMYFYHYTKEDKSKAEELQRERRKAKKQLVCCPPPMLPKLTPAFTPMANILQCPVFLNICSLIMERALNAYSRSFTESHLQKVLHLLGYAIQEELSEHYPFLSFYERSQEYGILEKLEELARCPRLEAHYDFVLWTIERFKQLQAKQAPSDGRAGPSCSQQGTGGKLSLSAEEQAREERENRARLAAERRAHIMAQMQKAQKSFISSNAEMFADTENETRKESASTGPMDWEDIPPEEEQGAVALESKVACLGPDRKFYHGTDDTFKCILCFENCAISRGGRQLVSSAFVQTSRVIFTTPNLRNSQSALHISCCGHVMHYSCWLEYFTNEEFKELRRPHRNRAALAQAANVEFQCPYCRTLSNAIIPVTETLPAFSAPPSPNESYLPLDSFVEIMSTLAIELGNVKDHELTTLPSVSNILRLSGVVGGLAQFERSVQLIKNPPRLHADYIEGIEFLKKALLNTMKIQQSHLKDHPAIESIEMVPILWDSCSYTLQALEIYLYAVEKPLKAELSMRHQSCARNLVRACSRSSALEWETDLPLLPPMRSQAEFSSRLLDTIFNQNDTSVLEWDCFRVLVPFQFGVLNLMVPEKGYKTIIPSGSMFDFYIMQTMFLAQLTKAVLCFDVEKEKAKRAEKAPNSELTQLDYIEQLPSRIRDNMIDFYRRYNIPARVLQKTKQKQLVEEESEENQGHGQTVVIPCESHHLALLLEYVQRQMSSFLRCSCLFYRFLTDVDFPDTFPTDQPDRFDLMCQYLGLDPMLGVYFDMETVYATMMHSFASHPHIDREVEQRCQPDARRSLQVEPCLRPLPRLKVLCDDFSDLINSVSDIFCPNNEREEMKTPTMCLICGLILCGQSYCCQPELGKVSVGACTHHAHACGAEVGIFLRIRDCQVVYLGRGKGCFVPPPYLDEYGETDMGLRRGNPLRLSQAAYRKIYLQWLGHGLHGEIARLNDNANVAAAAQWHHM

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
M9NFA7M9NFA7_DROMEUbr11824

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias1013-1028Polar residues
Sequence conflict1661in Ref. 3; AAM11168

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE014298
EMBL· GenBank· DDBJ
AAF48687.2
EMBL· GenBank· DDBJ
Genomic DNA
AY094815
EMBL· GenBank· DDBJ
AAM11168.1
EMBL· GenBank· DDBJ
mRNA
BT044223
EMBL· GenBank· DDBJ
ACH92288.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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