A0A095CDZ1 · A0A095CDZ1_SCHHA

Function

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.

Features

Showing features for binding site.

117102004006008001,0001,2001,4001,600
TypeIDPosition(s)Description
Binding site104ATP (UniProtKB | ChEBI)

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 ComponentHULC complex
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionprotein serine/threonine kinase activity
Molecular Functionubiquitin protein ligase activity
Biological Processchromatin organization
Biological Processprotein phosphorylation
Biological Processprotein ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    RING-type E3 ubiquitin transferase
  • EC number

Gene names

    • ORF names
      MS3_09438

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Spiralia > Lophotrochozoa > Platyhelminthes > Trematoda > Digenea > Strigeidida > Schistosomatoidea > Schistosomatidae > Schistosoma

Accessions

  • Primary accession
    A0A095CDZ1

Subcellular Location

PTM/Processing

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain, coiled coil.

Type
IDPosition(s)Description
Region1-28Disordered
Compositional bias14-28Basic and acidic residues
Domain75-397Protein kinase
Domain270-341AGC-kinase C-terminal
Region349-374Disordered
Coiled coil689-716
Region837-873Disordered
Coiled coil938-972
Coiled coil999-1033
Coiled coil1059-1100
Coiled coil1147-1188
Compositional bias1207-1233Polar residues
Region1207-1290Disordered
Compositional bias1256-1287Polar residues
Coiled coil1509-1543
Coiled coil1579-1634
Domain1657-1696RING-type

Sequence similarities

Belongs to the BRE1 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,710
  • Mass (Da)
    193,254
  • Last updated
    2014-11-26 v1
  • Checksum
    F5F1D38929722A3D
MTSTGVFHLDMPEAPSYDDSEENSHDYCSTHGGVEDEFLERGPLKPDELDENIKTVEICEETVNPGQPKVRPHDFQLLKVLGKGGYGKVFLARKNDTGQTYAMKVLKKASIVTNAKDTAHTKSERNILEMIKHPFLVQLHFAFQSPGKLYLVLEFLAGGELFMQLEKEGVFMEDQARAPEILLRQGHGRAVDWWSLGTLMYDMLSGSPPFTGDDRRQTIDLILRGDFIPVPYLSREAVSLISKLLVVDVSRRLGSGPSDSEAIKMHPFFRNTDWDRVLKKQVEPPFRPTLTSDTDVSLFDPKFTQENPVESPDEGLPISAMVSDVFEGFTYVDPQIHIDMARDPWVSTWQTSSRSRRRSGISSSSSPGFVGHTIMANPNTLMQGTDILHVGTPHPEQLQSTLVAHLPNTVQTSIPTQSQPFVFAEDFEDMDVASTNLTYSNNPLDSHSTVINTVNISTSNSVRPTYALPLGSHRLENSRVMETGICDPYSSRSGEHVNGVIPKPIDTRLVSPSSSAAAQVSALAAAALATSSRLVGSSVHIPSIASHNSPNRPFMNEHMMFDPQNIRLMNLGKSQPQTPLAAVEIAVYEDVSVRKWYSILFLTQTRSLYTECITIFCKFEKMKRSFSEDTNPDHDLLHGSTSQLDSTPPISKRLISAASEPISFIRISSLEELDKRALQLQNKKLWEALMERRAAIAELKERIEHLENRQTKDDALLCVVNRYWNQLDEDSLIILQRFDSDAEEEISTSTESFLKQLASWDKEEVPEKLQERVHFSKRIIARLLSAYEKQVLLISLCLNFHVSMVTHQFRLRQLLGNTTETASVSVGSEISDNILPIHSSSSAPYGTQNSNSEGNNQSTSSSQEPASTTCSRSGAVDLHEEITLLNKENLRLQSLCTNLHSKHRQSSLRLRELQDLAQTNSDASAEWQAKYEDLDYKLAEAMKQVTRLDHRLYEAQEKNKKMEVELSALKCSDSPGREDPSNIDGSITRNKYNDLACELEEYRELANNRINELERLQRHLEDKVSECASLNMQLRDIPEHIITESPQYLSLKTQFNILYNEAIQLRSQLEEARSTIQNNRHNHLKQIEEMEANEAAIQNQMRSEMLLIEGQYSQLRHKYETMELDFKQALTHNEQAGPISCEMRSLISTLQTQNKQLKAEVTRYRRKCEETVQEREMIRADLKCTEDELIRVRTALSEATAAVITACEKSDQSTPSTPQSSNLPQTSVTMPDVGSPTADPELKAKNSIPIKVEENVKYSSPSSSTARSGTVTTSASSHVNGSGPEKVLKTESTPDFRCNVSCSSPSNEIIRDLKEQLKRSQESQKEMSVLLNMYKVIPKDQRDKAALLQCEAKLRGSSITTNEDAATTEVNAERSLTSHGNIPLSPSKTCKTGLVSPEEKSSSISVSLPITSCGKSKISASDWQISELQMELYIVRRKSQSVEEQLKLHQQRLVAAKQQEDVLLKEMEITVQAFEDAQEQNVRLVKTLREKDDAHLKLMAERMKTAQLARLLKEDKQLLEEQIRLMQAKIEALNRAVLKQEEKERLLLTNLATLEKEASARQKSQEAYKRKALESQQVSEDLKVTVQKYQSQLKDAQTTVQEKASAFERVSFGHQRLQEELVTVRRKYERLRKIEQSHNADEFLLAEIQDYKEQLTCPTCKINRKDAILTKCFHVFCLNCLKVRYETRNRKCPKCNATFGANDYHRIYLT

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias14-28Basic and acidic residues
Compositional bias1207-1233Polar residues
Compositional bias1256-1287Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KL251651
EMBL· GenBank· DDBJ
KGB40943.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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