| Tag | Content |
|---|
| CPLM ID | CPLM-007023 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | E3 ubiquitin-protein ligase DMA1 |
Protein Synonyms/Alias | Checkpoint forkhead associated with RING domains-containing protein 1; Defective in mitotic arrest protein 1 |
Gene Name | DMA1 |
Gene Synonyms/Alias | CHF1; YHR115C |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 106 | APAVNTTKSIRHFIY | ubiquitination | [1] | | 306 | LKANAFNKEALSRIK | ubiquitination | [1] | | 317 | SRIKNLQKLTTGLEQ | ubiquitination | [1] |
|
Reference | [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J. Nat Methods. 2013 Jul;10(7):676-82. [ PMID: 23749301] |
Functional Description | 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. |
Sequence Annotation | DOMAIN 189 252 FHA.
ZN_FING 327 371 RING-type.
CROSSLNK 150 150 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 204 204 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 217 217 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 237 237 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 240 240 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 260 260 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 300 300 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 306 306 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 313 313 Glycyl lysine isopeptide (Lys-Gly)
CROSSLNK 317 317 Glycyl lysine isopeptide (Lys-Gly) |
Keyword | Cell cycle; Cell division; Complete proteome; Cytoplasm; Isopeptide bond; Ligase; Metal-binding; Mitosis; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 416 AA |
Protein Sequence | MSTNTVPSSP PNQTPPAASG IATSHDHTKF NNPIRLPISI SLTINDTPNN NSNNNSVSNG 60
LGILPSRTAT SLVVANNGSA NGNVGATAAA AATVETNTAP AVNTTKSIRH FIYPPNQVNQ 120
TEFSLDIHLP PNTSLPERID QSTLKRRMDK HGLFSIRLTP FIDTSSTSVA NQGLFFDPII 180
RTAGAGSQII IGRYTERVRE AISKIPDQYH PVVFKSKVIS RTHGCFKVDD QGNWFLKDVK 240
SSSGTFLNHQ RLSSASTTSK DYLLHDGDII QLGMDFRGGT EEIYRCVKMK IELNKSWKLK 300
ANAFNKEALS RIKNLQKLTT GLEQEDCSIC LNKIKPCQAI FISPCAHSWH FHCVRRLVIM 360
NYPQFMCPNC RTNCDLETTL ESESESEFEN EDEDEPDIEM DIDMEINNNL GVRLVD 416 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:SGD. GO:0004842; F:ubiquitin-protein ligase activity; IMP:SGD. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0032186; P:cellular bud neck septin ring organization; IGI:SGD. GO:0000132; P:establishment of mitotic spindle orientation; IGI:SGD. GO:0007067; P:mitosis; IEA:UniProtKB-KW. GO:0031578; P:mitotic spindle orientation checkpoint; IGI:SGD. GO:0051865; P:protein autoubiquitination; IDA:SGD. GO:0097271; P:protein localization to bud neck; IGI:SGD. GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IGI:SGD. GO:0000921; P:septin ring assembly; IGI:SGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |