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P38823

- DMA1_YEAST

UniProt

P38823 - DMA1_YEAST

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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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

Structurei

3D structure databases

ProteinModelPortaliP38823.
SMRiP38823. Positions 322-374.
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.
InParanoidiP38823.
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

        10         20         30         40         50
MSTNTVPSSP PNQTPPAASG IATSHDHTKF NNPIRLPISI SLTINDTPNN
60 70 80 90 100
NSNNNSVSNG LGILPSRTAT SLVVANNGSA NGNVGATAAA AATVETNTAP
110 120 130 140 150
AVNTTKSIRH FIYPPNQVNQ TEFSLDIHLP PNTSLPERID QSTLKRRMDK
160 170 180 190 200
HGLFSIRLTP FIDTSSTSVA NQGLFFDPII RTAGAGSQII IGRYTERVRE
210 220 230 240 250
AISKIPDQYH PVVFKSKVIS RTHGCFKVDD QGNWFLKDVK SSSGTFLNHQ
260 270 280 290 300
RLSSASTTSK DYLLHDGDII QLGMDFRGGT EEIYRCVKMK IELNKSWKLK
310 320 330 340 350
ANAFNKEALS RIKNLQKLTT GLEQEDCSIC LNKIKPCQAI FISPCAHSWH
360 370 380 390 400
FHCVRRLVIM NYPQFMCPNC RTNCDLETTL ESESESEFEN EDEDEPDIEM
410
DIDMEINNNL GVRLVD
Length:416
Mass (Da):46,098
Last modified:February 1, 1995 - v1
Checksum:i4344AB155C83CBF7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 322-374.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36548. 68 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.
InParanoidi P38823.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 120 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