Q75F74 · Q75F74_EREGS

Function

function

Ubiquitin ligase protein 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 Componentproteasome regulatory particle, base subcomplex
Cellular Componentubiquitin ligase complex
Cellular ComponentUBR1-RAD6 ubiquitin ligase complex
Molecular Functionproteasome regulatory particle binding
Molecular Functionubiquitin protein ligase activity
Molecular Functionzinc ion binding
Biological Processcytoplasm protein quality control by the ubiquitin-proteasome system
Biological ProcessERAD pathway
Biological Processmitochondria-associated ubiquitin-dependent protein catabolic process
Biological Processprotein monoubiquitination
Biological Processprotein polyubiquitination
Biological Processprotein ubiquitination
Biological Processregulation of dipeptide transport
Biological Processribosome-associated ubiquitin-dependent protein catabolic process
Biological Processstress-induced homeostatically regulated protein degradation pathway
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
  • EC number

Gene names

    • ORF names
      AGOS_AAL146W

Organism names

Accessions

  • Primary accession
    Q75F74

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, zinc finger, region, compositional bias.

TypeIDPosition(s)Description
Domain111-184UBR-type
Zinc finger111-184UBR-type
Region1800-1824Disordered
Compositional bias1807-1824Acidic residues
Compositional bias1869-1886Polar residues
Region1869-1900Disordered

Sequence similarities

Belongs to the UBR1 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,900
  • Mass (Da)
    218,309
  • Last updated
    2004-07-05 v1
  • Checksum
    15FDA5904A68D783
MIREGAGEVQRHLRHTLESLHDHEYFKSPRGPQERSEMDKVLRSFVFRYLYYVLSDNGRLLPHLFAGAPKDKFPTSVEDAMQVDSPSLSKADIFYAIDEITGAKSHRHTGRNCGRAFQPGEPLYRCQECAYDDTCVLCISCFNPDDHVNHHVSTHICNELHDGICDCGDAEAWNVPLHCKAEEDDSDGDEEDSVFENDYNMELFEAVLEELFDHFIEVFNQNIEPLPTIQKDLTMKLREIIQDGKTQEKFELLSALAYRNQYMEAQKPSSGPASFETEQDLDKKLDGYVVLIYNDEYHNFSQATSALRQGGPDNKHTDQLTARIDGEGRAMLKCSRDLSAVIGGFFSVQTNGLSATLTPWSEYIHQEACKYMIHWVKNCLSIPNPSFQKVFREAMGKVLCSEYIRASETTDMTPVIDKYFIPDRRNTGCHIYADLSVLGKGNVIPLGHHKVLLQESLNEIALNLNNYEELKYRRYSNSRLQQILFFDNRYWKKLRKDIRRAVIPTLASSVKYKPTFSQQVVEIFNHMTRSVAFMDREPQLSALADCVVQLFTCPTTVRTIFENENFPDIMWSVIDIFTEFSKVDDGILLWQRVQKSNPSKSYSYSFKHGLYAVETLLSKVENANLILRPPEFISIVTLCKLFNGAWRIKRKEGEHVLREDQHFILYLEYTTSIYNIIRAMNRVLDSSRAALSEDTLLQAIGLLNTFLGHRTLPYKLVQEAHDVIAFKVSKQKVAFMNPVHTLFSCLIEKVPLAKAFEAVSSTKDFLTIADFSLRAAVLCSQIDVGFWVRNGMSVLHQSAYYRTNPEINSYSRDIHLNQLAFLKENDDLPRVIYNLLDRWELLGWFTGAEQYETTVYEERITNIIQQFIAFVYHILSERHFFRYFGSSAERETHTMKNIIIYSLLMKPLPYSELLKSVPDYLSEKLSVFDECLHEVSEYVEPKGLEDSGVFSLKKEMYKKIDPLRLLNMKNDFEHSATIVKTHLAEGSNAVGQVVLQPQLISPKHLDELAAHLGDFTRTQVFAKLIYKLLQACIDREDGTYLYELLHLLHGIFKDDELLRGKSSIPEAYISKPICNLLLLIDTKANVFSENAIRKADFLLEHMIRKRHNDIFESLAAYFGQDYVEQYKAKKLNQGINFEETEKDRKKRLARLRQQKIMAKFSKQQAKFVRSNPNVITDDLFDAEVRTGSDGLVCSLCQDEESLDAFVIPAYHESSPIFFYGDYTPQNFAKPWNGFVNDDDNLTFYDDLKLYSLQEARKGSTTTFVSCNHIIHYECFRRYIQKKRFSNNLFICPLCQTFSNCVLPIPHWSLRLPKSPVTVDQLLSQPSEENLINLFIDDQTPNSTAAMNMLKEVCKKNGNYDKSYGSVSQEFVTSILTCHWANTISMIEIASRIEKNTHQTLLQGKEQKFKTLRGVLSAIGWFYKCMGTPRQKFVPYVFHGEDDGPANQVFQYIVHKSLFSGAPVSETISHALAIWIRTLATQFLISSNKTGYEITYHQAVSLGPVYEAPPEFTTACSSLDQIIAIEDTTLKTKMVDLTYTMLMKTLLPTLRRCMIMLYVFSGLLSAESCLRIDGLDLSADLPFEDLPSYFQKLVTLLCKTGFVSIFNRSTIETMDHQYLRNIPMEYAGTVKLVDLAKYLNTYVTNTKQLKLRDEATSMQSRNIKNRLDFKICLTCGVRVYSRSDGTEIMKHMAKNCFKAYSLFLIPHDSEVRLVLQHPHSHISIPAPYLNSHGESGKNAIQRGDLTTLNIHRYEHLNYLWLNNEIPGYISRIMGDEFRVSIISSGVVFNFDRNVLRRQMRANVGNEESSEEEDLMDDDEMSPDDDPDFRWEVTPEEFFRDGILRLGGAPGQGGDIRDFFQFITNLRTDDRNDNIPTFQFTNGALGRNQNDDDDQDGDEILP

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1807-1824Acidic residues
Compositional bias1869-1886Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE016814
EMBL· GenBank· DDBJ
AAS50220.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp