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P38823

- DMA1_YEAST

UniProt

P38823 - DMA1_YEAST

Protein

E3 ubiquitin-protein ligase DMA1

Gene

DMA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase which functions in cell cycle retarding in conjonction with the UBC4 and UBC13/MMS2 complex, 2 E2 ubiquitin conjugationg enzymes. Involved in nutritional control of the cell cycle. Required for proper spindle positioning, likely regulating septin ring deposition at the bud neck.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri327 – 37145RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. ubiquitin-protein transferase activity Source: SGD
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular bud neck septin ring organization Source: SGD
    2. establishment of mitotic spindle orientation Source: SGD
    3. mitotic nuclear division Source: UniProtKB-KW
    4. mitotic spindle orientation checkpoint Source: SGD
    5. protein autoubiquitination Source: SGD
    6. protein localization to bud neck Source: SGD
    7. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: SGD
    8. septin ring assembly Source: SGD

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31157-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase DMA1 (EC:6.3.2.-)
    Alternative name(s):
    Checkpoint forkhead associated with RING domains-containing protein 1
    Defective in mitotic arrest protein 1
    Gene namesi
    Name:DMA1
    Synonyms:CHF1
    Ordered Locus Names:YHR115C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VIII

    Organism-specific databases

    CYGDiYHR115c.
    SGDiS000001157. DMA1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi192 – 1921G → E: Decreases the interaction with CDC123. 1 Publication
    Mutagenesisi220 – 2201S → A: Decreases the interaction with CDC123, when associated with L-223. 1 Publication
    Mutagenesisi223 – 2231H → L: Decreases the interaction with CDC123, when associated with A-220. 1 Publication
    Mutagenesisi345 – 3451C → S: Decreases the interaction with CDC123, when associated with A-350. 1 Publication
    Mutagenesisi350 – 3501H → A: Decreases the interaction with CDC123, when associated with S-345. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 416416E3 ubiquitin-protein ligase DMA1PRO_0000056338Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki150 – 150Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki204 – 204Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki217 – 217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki237 – 237Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki240 – 240Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki260 – 260Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki300 – 300Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki306 – 306Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki313 – 313Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki317 – 317Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

    Post-translational modificationi

    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 UBC4.1 Publication

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiP38823.
    PaxDbiP38823.

    Expressioni

    Gene expression databases

    GenevestigatoriP38823.

    Interactioni

    Subunit structurei

    Interacts with CDC123.1 Publication

    Protein-protein interaction databases

    BioGridi36548. 65 interactions.
    DIPiDIP-1884N.
    IntActiP38823. 21 interactions.
    MINTiMINT-388035.
    STRINGi4932.YHR115C.

    Structurei

    3D structure databases

    ProteinModelPortaliP38823.
    SMRiP38823. Positions 323-374.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini189 – 25264FHAPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the DMA1 family.Curated
    Contains 1 FHA domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri327 – 37145RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG1716.
    GeneTreeiENSGT00510000054808.
    HOGENOMiHOG000248264.
    OMAiNESIATQ.
    OrthoDBiEOG793BJX.

    Family and domain databases

    Gene3Di2.60.200.20. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR000253. FHA_dom.
    IPR008984. SMAD_FHA_domain.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF00498. FHA. 1 hit.
    [Graphical view]
    SMARTiSM00240. FHA. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF49879. SSF49879. 1 hit.
    PROSITEiPS50006. FHA_DOMAIN. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38823-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTNTVPSSP PNQTPPAASG IATSHDHTKF NNPIRLPISI SLTINDTPNN    50
    NSNNNSVSNG LGILPSRTAT SLVVANNGSA NGNVGATAAA AATVETNTAP 100
    AVNTTKSIRH FIYPPNQVNQ TEFSLDIHLP PNTSLPERID QSTLKRRMDK 150
    HGLFSIRLTP FIDTSSTSVA NQGLFFDPII RTAGAGSQII IGRYTERVRE 200
    AISKIPDQYH PVVFKSKVIS RTHGCFKVDD QGNWFLKDVK SSSGTFLNHQ 250
    RLSSASTTSK DYLLHDGDII QLGMDFRGGT EEIYRCVKMK IELNKSWKLK 300
    ANAFNKEALS RIKNLQKLTT GLEQEDCSIC LNKIKPCQAI FISPCAHSWH 350
    FHCVRRLVIM NYPQFMCPNC RTNCDLETTL ESESESEFEN EDEDEPDIEM 400
    DIDMEINNNL GVRLVD 416
    Length:416
    Mass (Da):46,098
    Last modified:February 1, 1995 - v1
    Checksum:i4344AB155C83CBF7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BK005578 Genomic DNA. Translation: DAA05593.1.
    U00059 Genomic DNA. Translation: AAB68865.1.
    BK006934 Genomic DNA. Translation: DAA06809.1.
    PIRiS48957.
    RefSeqiNP_011983.1. NM_001179245.1.

    Genome annotation databases

    EnsemblFungiiYHR115C; YHR115C; YHR115C.
    GeneIDi856515.
    KEGGisce:YHR115C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BK005578 Genomic DNA. Translation: DAA05593.1 .
    U00059 Genomic DNA. Translation: AAB68865.1 .
    BK006934 Genomic DNA. Translation: DAA06809.1 .
    PIRi S48957.
    RefSeqi NP_011983.1. NM_001179245.1.

    3D structure databases

    ProteinModelPortali P38823.
    SMRi P38823. Positions 323-374.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36548. 65 interactions.
    DIPi DIP-1884N.
    IntActi P38823. 21 interactions.
    MINTi MINT-388035.
    STRINGi 4932.YHR115C.

    Proteomic databases

    MaxQBi P38823.
    PaxDbi P38823.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YHR115C ; YHR115C ; YHR115C .
    GeneIDi 856515.
    KEGGi sce:YHR115C.

    Organism-specific databases

    CYGDi YHR115c.
    SGDi S000001157. DMA1.

    Phylogenomic databases

    eggNOGi COG1716.
    GeneTreei ENSGT00510000054808.
    HOGENOMi HOG000248264.
    OMAi NESIATQ.
    OrthoDBi EOG793BJX.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31157-MONOMER.

    Miscellaneous databases

    NextBioi 982263.

    Gene expression databases

    Genevestigatori P38823.

    Family and domain databases

    Gene3Di 2.60.200.20. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR000253. FHA_dom.
    IPR008984. SMAD_FHA_domain.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF00498. FHA. 1 hit.
    [Graphical view ]
    SMARTi SM00240. FHA. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49879. SSF49879. 1 hit.
    PROSITEi PS50006. FHA_DOMAIN. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cdc123 and checkpoint forkhead associated with RING proteins control the cell cycle by controlling eIF2gamma abundance."
      Bieganowski P., Shilinski K., Tsichlis P.N., Brenner C.
      J. Biol. Chem. 279:44656-44666(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH CDC123, MUTAGENESIS OF GLY-192; SER-220; HIS-223; CYS-345 AND HIS-350.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "Functional characterization of Dma1 and Dma2, the budding yeast homologues of Schizosaccharomyces pombe Dma1 and human Chfr."
      Fraschini R., Bilotta D., Lucchini G., Piatti S.
      Mol. Biol. Cell 15:3796-3810(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Yeast Chfr homologs retard cell cycle at G1 and G2/M via Ubc4 and Ubc13/Mms2-dependent ubiquitination."
      Loring G.L., Christensen K.C., Gerber S.A., Brenner C.
      Cell Cycle 7:96-105(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, UBIQUITINATION AT LYS-150; LYS-204; LYS-217; LYS-237; LYS-240; LYS-260; LYS-300; LYS-306; LYS-313 AND LYS-317.

    Entry informationi

    Entry nameiDMA1_YEAST
    AccessioniPrimary (citable) accession number: P38823
    Secondary accession number(s): D3DL65, Q66GT1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2790 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome VIII
      Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

    External Data

    Dasty 3