P38823 · DMA1_YEAST

Function

function

E3 ubiquitin-protein ligase which functions in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, 2 E2 ubiquitin conjugating enzymes (PubMed:18202552).
Involved in nutritional control of the cell cycle (PubMed:15319434).
Targets the G1 cyclin PCL1 for destruction (PubMed:23264631).
Required for proper spindle positioning, likely regulating septin ring deposition at the bud neck (PubMed:15146058).

Miscellaneous

Present with 2790 molecules/cell in log phase SD medium.

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)

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 Componentcell division site
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentubiquitin ligase complex
Molecular Functionmetal ion binding
Molecular Functionubiquitin protein ligase activity
Molecular Functionubiquitin-protein transferase activity
Biological Processcellular bud neck septin ring organization
Biological Processestablishment of mitotic spindle orientation
Biological Processmitotic spindle orientation checkpoint signaling
Biological Processprotein autoubiquitination
Biological Processprotein localization to bud neck
Biological Processprotein ubiquitination
Biological Processregulation of formin-nucleated actin cable assembly
Biological Processseptin ring assembly
Biological Processubiquitin-dependent protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase DMA1
  • EC number
  • Alternative names
    • Checkpoint forkhead associated with RING domains-containing protein 1
    • Defective in mitotic arrest protein 1
    • RING-type E3 ubiquitin transferase DMA1

Gene names

    • Name
      DMA1
    • Synonyms
      CHF1
    • Ordered locus names
      YHR115C

Organism names

Accessions

  • Primary accession
    P38823
  • Secondary accessions
    • D3DL65
    • Q66GT1

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis192Decreases the interaction with CDC123.
Mutagenesis220Decreases the interaction with CDC123, when associated with L-223.
Mutagenesis223Decreases the interaction with CDC123, when associated with A-220.
Mutagenesis345Decreases the interaction with CDC123, when associated with A-350.
Mutagenesis350Decreases the interaction with CDC123, when associated with S-345.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 6 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, cross-link.

Type
IDPosition(s)Description
ChainPRO_00000563381-416E3 ubiquitin-protein ligase DMA1
Cross-link150Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link204Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link237Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link240Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link260Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link300Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link306Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link313Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link317Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Post-translational modification

UBC4-dependent autoubiquitination occurs at Lys-150, Lys-204, Lys-217, Lys-237, Lys-240, Lys-260, Lys-300, Lys-306, Lys-313 and Lys-317. UBC4-dependent autoubiquitination is responsible for DMA2 turnover. UBC13/MMS2-dependent autoubiquitination occurs at Lys-237 and Lys-306. Lys-204 and Lys-306 are also ubiquitinated in trans by DMA2 E3 ligase in association with UBC4.

Keywords

Proteomic databases

PTM databases

Expression

Induction

Protein levels are regulated by nutrient status, being high under good nutrient conditions.

Interaction

Subunit

Interacts with CDC123 (PubMed:15319434).
Interacts with PCL1 (PubMed:23264631).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY P38823CDC123 Q057913EBI-24686, EBI-34676

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

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

Type
IDPosition(s)Description
Region1-30Disordered
Compositional bias15-30Polar residues
Domain189-252FHA
Zinc finger327-371RING-type

Sequence similarities

Belongs to the DMA1 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    416
  • Mass (Da)
    46,098
  • Last updated
    1995-02-01 v1
  • Checksum
    4344AB155C83CBF7
MSTNTVPSSPPNQTPPAASGIATSHDHTKFNNPIRLPISISLTINDTPNNNSNNNSVSNGLGILPSRTATSLVVANNGSANGNVGATAAAAATVETNTAPAVNTTKSIRHFIYPPNQVNQTEFSLDIHLPPNTSLPERIDQSTLKRRMDKHGLFSIRLTPFIDTSSTSVANQGLFFDPIIRTAGAGSQIIIGRYTERVREAISKIPDQYHPVVFKSKVISRTHGCFKVDDQGNWFLKDVKSSSGTFLNHQRLSSASTTSKDYLLHDGDIIQLGMDFRGGTEEIYRCVKMKIELNKSWKLKANAFNKEALSRIKNLQKLTTGLEQEDCSICLNKIKPCQAIFISPCAHSWHFHCVRRLVIMNYPQFMCPNCRTNCDLETTLESESESEFENEDEDEPDIEMDIDMEINNNLGVRLVD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias15-30Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BK005578
EMBL· GenBank· DDBJ
DAA05593.1
EMBL· GenBank· DDBJ
Genomic DNA
U00059
EMBL· GenBank· DDBJ
AAB68865.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006934
EMBL· GenBank· DDBJ
DAA06809.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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