| Type | Description |
|---|---|
| Definition | Synaptonemal complex protein 4 |
| Date | Results | Publications |
|---|---|---|
| 2018-02-10 10:40:00 | The authors found that SYP-4 is phosphorylated dependent on Polo-like kinases PLK-1/2. They propose a model in which Polo-like kinases recognize crossover designation and phosphorylate SYP-4 thereby stabilizing the synaptonemal complex and making chromosomes less permissive for further double-strand break formation. | 28346135 |
| 2012-07-09 02:17:00 | SYP-3 interacts with SYP-4 which is required for synaptonemal complex assembly. | 19798442 |
| 2012-02-18 11:08:00 | Data show that while the C-terminal domain of SYP-3 localizes in close proximity to the chromosome axes, the N-terminal domains of both SYP-1 and SYP-4 (H27M09.3) and the C-terminal domain of SYP-2 are located in the middle of the synaptonemal complex. | 21840865 |
| Type | IDs |
|---|---|
| Gene |
UniProtKB-ID:
SYP4_CAEEL
UniprotKB:
Q9N5K3
UniParc:
UPI000007FDF1
EMBL:
BX284601
EnsemblGenome:
WBGene00019247
KO:
cel:CELE_H27M09.3
|
| Nucleutide sequences |
EMBL-CDS:
CCD72468.1
Gene_ORFName:
H27M09.3
EnsemblGenome_TRS:
H27M09.3.1
|
| Protein sequencees |
EnsemblGenome_PRO:
H27M09.3.1
RefSeq:
NP_491960.1
|
| Others |
UniRef100:
UniRef100_Q9N5K3
UniRef90:
UniRef90_Q9N5K3
UniRef50:
UniRef50_Q9N5K3
UniGene:
Cel.18549
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| Refseq |
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| Location | {{protein.contigId}} ( {{protein.positionStart}}..{{protein.positionEnd}} , {{protein.orientation}} ) | |||||||
| Conserved domain | Region: {{conservedDomain.region == '' || conservedDomain.region == null ? "-": conservedDomain.region}} GFID: {{conservedDomain.gfid == '' || conservedDomain.gfid == null ? "-": conservedDomain.gfid}} Family: {{conservedDomain.family == '' || conservedDomain.family == null ? "-": conservedDomain.family}} CDD: {{conservedDomain.cdd}} - |
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