DMA2/YNL116W Protein Information Help

Standard Name Dma2p 1
Systematic Name Ynl116wp
Alias Chf2p 2
ORF Classification Verified
Description Ubiquitin-protein ligase (E3); controls septin dynamics and spindle position checkpoint (SPOC) with ligase Dma1p by regulating recruitment of Elm1p to bud neck; regulates levels of eIF2 subunit Gcd11p, as well as abundance, localization, and ubiquitination of Cdk inhibitory kinase Swe1p; ortholog of human RNF8, similar to human Chfr; contains FHA and RING finger domains; DMA2 has a paralog, DMA1, that arose from the whole genome duplication (1, 2, 3, 4, 5, 6, 7)
Name Description Defective in Mitotic Arrest 1
Experimental Data
Molecules/cell 1750 8
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 522
Molecular Weight (Da) 57,584
Isoelectric Point (pI) 7.04

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Dma2p (InterPro)
Physical Interactions There are 27 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000013BB75 | P53924
MIPS: YNL116W
NCBI: 1183957 | 125863489 | 125863499 | 125863509 | 125863519 | 125863528 | 125863541 | 125863552 | 125863562 | 125863572 | 125863582 | 125863592 | 125863612 | 1302041 | 1730767 | 398364793 | NP_014283.3 | NM_001182954.3
GenBank/EMBL/DDBJ: ABN58541.1 | ABN58550.1 | ABN58559.1 | ABN58568.1 | ABN58576.1 | ABN58586.1 | ABN58595.1 | ABN58604.1 | ABN58613.1 | ABN58622.1 | ABN58631.1 | ABN58649.1 | CAA93391.1 | CAA95996.1 | DAA05594.1 | DAA10432.1 | EF125216 | EF125217 | EF125218 | EF125219 | EF125220 | EF125221 | EF125222 | EF125223 | EF125224 | EF125225 | EF125226 | EF125228 | Z69382 | Z71392
External Classifications EC: 6.3.2.- [Acid-Amino-Acid Ligases (Peptide Synthases)]
Amino Acid Sequence (or in FASTA format)
       1  MYTPIPANTP APTAPTSSMT SNSSSASNAN TTSSSGINPR NRASGTPSNE
      51  RARPASGISS FLNTFGIRQN SQTASSSAAP DQRLFGTTPS NSHMSVAMES
     101  IDTAPQQQEP RLHHPIQMPL SAQFHVHRNY QLPISISLTA PTTTDHQQSS
     151  AHNFEGNNVG NVQESLNQRQ PNGTNNTTTS IISMAPAATT RNIVGGADGS
     201  TIVNNSQEMY KNLRHLIYAA NQPNGTEILH LDLPATSAEE SNNMFNVDEV
     251  TLKQRKDKHG LFSIRLTPFI DSSSTTNQGL FFEPIIRKAG PGSQLVIGRY
     301  TERVRDAISK IPEQYHPVVF KSKVVSRTHG CFKVDSQGNW YIKDVKSSSG
     351  TFLNHQRLSP ASSLSKDTPL RDGDILQLGM DFRGGTEEIY RCVRMRIELN
     401  RSWKLKANSF NKEALQRLQN LQKLTTGIEE EDCSICLCKI KPCQAIFISP
     451  CAHSWHFRCV RRLVMLSYPQ FVCPNCRSSC DLEASFESSD EEDESDVESE
     501  GDQLVDQLSV LMETSKDVDS HP*                             

external links for Dma2p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily LoQate
Ashbya (AGD) BOND GPMdb (Mass Spec.) Organelle DB
Candida (CGD) CYC2008 (complexes) MIPS YPL+
YGOB Complexome Pfam domains YeastGFP
YOGY DIP YeastRC Structure Prediction (Seattle) YeastRC Public Image Repository

GeneMANIA


IMP


YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Dma2p
1) Fraschini R, et al.  (2004) Functional characterization of Dma1 and Dma2, the budding yeast homologues of Schizosaccharomyces pombe Dma1 and human Chfr. Mol Biol Cell 15(8):3796-810
2) Bieganowski P, et al.  (2004) Cdc123 and checkpoint forkhead associated with RING proteins control the cell cycle by controlling eIF2gamma abundance. J Biol Chem 279(43):44656-66
3) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
4) Tuttle RL, et al.  (2007) Defective in mitotic arrest 1/ring finger 8 is a checkpoint protein that antagonizes the human mitotic exit network. Mol Cancer Res 5(12):1304-11
5) Loring GL, et al.  (2008) Yeast Chfr homologs retard cell cycle at G1 and G2/M via Ubc4 and Ubc13/Mms2-dependent ubiquitination. Cell Cycle 7(1):96-105
6) Raspelli E, et al.  (2011) Budding yeast Dma1 and Dma2 participate in regulation of Swe1 levels and localization. Mol Biol Cell 22(13):2185-97
7) Merlini L, et al.  (2012) Budding yeast dma proteins control septin dynamics and the spindle position checkpoint by promoting the recruitment of the elm1 kinase to the bud neck. PLoS Genet 8(4):e1002670
8) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41