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P38823 (DMA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DMA1
Synonyms:CHF1
Ordered Locus Names:YHR115C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6 Ref.7

Subunit structure

Interacts with CDC123. Ref.1

Subcellular location

Cytoplasm Ref.4.

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.

Miscellaneous

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

Sequence similarities

Belongs to the DMA1 family.

Contains 1 FHA domain.

Contains 1 RING-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416E3 ubiquitin-protein ligase DMA1
PRO_0000056338

Regions

Domain189 – 25264FHA
Zinc finger327 – 37145RING-type

Amino acid modifications

Cross-link150Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Cross-link204Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Cross-link217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Cross-link237Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Cross-link240Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Cross-link260Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Cross-link300Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Cross-link306Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Cross-link313Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Cross-link317Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7

Experimental info

Mutagenesis1921G → E: Decreases the interaction with CDC123. Ref.1
Mutagenesis2201S → A: Decreases the interaction with CDC123, when associated with L-223. Ref.1
Mutagenesis2231H → L: Decreases the interaction with CDC123, when associated with A-220. Ref.1
Mutagenesis3451C → S: Decreases the interaction with CDC123, when associated with A-350. Ref.1
Mutagenesis3501H → A: Decreases the interaction with CDC123, when associated with S-345. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P38823 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 4344AB155C83CBF7

FASTA41646,098
        10         20         30         40         50         60 
MSTNTVPSSP PNQTPPAASG IATSHDHTKF NNPIRLPISI SLTINDTPNN NSNNNSVSNG 

        70         80         90        100        110        120 
LGILPSRTAT SLVVANNGSA NGNVGATAAA AATVETNTAP AVNTTKSIRH FIYPPNQVNQ 

       130        140        150        160        170        180 
TEFSLDIHLP PNTSLPERID QSTLKRRMDK HGLFSIRLTP FIDTSSTSVA NQGLFFDPII 

       190        200        210        220        230        240 
RTAGAGSQII IGRYTERVRE AISKIPDQYH PVVFKSKVIS RTHGCFKVDD QGNWFLKDVK 

       250        260        270        280        290        300 
SSSGTFLNHQ RLSSASTTSK DYLLHDGDII QLGMDFRGGT EEIYRCVKMK IELNKSWKLK 

       310        320        330        340        350        360 
ANAFNKEALS RIKNLQKLTT GLEQEDCSIC LNKIKPCQAI FISPCAHSWH FHCVRRLVIM 

       370        380        390        400        410 
NYPQFMCPNC RTNCDLETTL ESESESEFEN EDEDEPDIEM DIDMEINNNL GVRLVD 

« Hide

References

« Hide 'large scale' references
[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]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BK005578 Genomic DNA. Translation: DAA05593.1.
U00059 Genomic DNA. Translation: AAB68865.1.
BK006934 Genomic DNA. Translation: DAA06809.1.
PIRS48957.
RefSeqNP_011983.1. NM_001179245.1.

3D structure databases

ProteinModelPortalP38823.
SMRP38823. Positions 323-374.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36548. 64 interactions.
DIPDIP-1884N.
IntActP38823. 21 interactions.
MINTMINT-388035.
STRING4932.YHR115C.

Proteomic databases

MaxQBP38823.
PaxDbP38823.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR115C; YHR115C; YHR115C.
GeneID856515.
KEGGsce:YHR115C.

Organism-specific databases

CYGDYHR115c.
SGDS000001157. DMA1.

Phylogenomic databases

eggNOGCOG1716.
GeneTreeENSGT00510000054808.
HOGENOMHOG000248264.
OMANESIATQ.
OrthoDBEOG793BJX.

Enzyme and pathway databases

BioCycYEAST:G3O-31157-MONOMER.

Gene expression databases

GenevestigatorP38823.

Family and domain databases

Gene3D2.60.200.20. 1 hit.
3.30.40.10. 1 hit.
InterProIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF00498. FHA. 1 hit.
[Graphical view]
SMARTSM00240. FHA. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
PROSITEPS50006. FHA_DOMAIN. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982263.

Entry information

Entry nameDMA1_YEAST
AccessionPrimary (citable) accession number: P38823
Secondary accession number(s): D3DL65, Q66GT1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families