Search Results
Overview
| Uniprot ID | Q15431 |
|---|---|
| Protein Name | Synaptonemal complex protein 1 |
| Gene Name | SYCP1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 170 | EEGIQENKDLIKENN |
| 738 | ELGLYKSKEQEQSSL |
Function
Major component of the transverse filaments of synaptonemal complexes, formed between homologous chromosomes during meiotic prophase. Required for normal assembly of the central element of the synaptonemal complexes. Required for normal centromere pairing during meiosis. Required for normal meiotic chromosome synapsis during oocyte and spermatocyte development and for normal male and female fertility
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0030849 | autosome |
| Cellular Component | GO:0000801 | central element |
| Cellular Component | GO:0005694 | chromosome |
| Cellular Component | GO:0000775 | chromosome, centromeric region |
| Cellular Component | GO:0000794 | condensed nuclear chromosome |
| Cellular Component | GO:0001673 | male germ cell nucleus |
| Cellular Component | GO:0000795 | synaptonemal complex |
| Cellular Component | GO:0000802 | transverse filament |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0003690 | double-stranded DNA binding |
| Biological Process | GO:0051301 | cell division |
| Biological Process | GO:0051026 | chiasma assembly |
| Biological Process | GO:0007129 | homologous chromosome pairing at meiosis |
| Biological Process | GO:0035825 | homologous recombination |
| Biological Process | GO:0051878 | lateral element assembly |
| Biological Process | GO:0000711 | meiotic DNA repair synthesis |
| Biological Process | GO:0051289 | protein homotetramerization |
| Biological Process | GO:0007131 | reciprocal meiotic recombination |
| Biological Process | GO:0007283 | spermatogenesis |
| Biological Process | GO:0007130 | synaptonemal complex assembly |
Reference
[1] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[2] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.