Search Results
Overview
| Uniprot ID | Q13416 |
|---|---|
| Protein Name | Origin recognition complex subunit 2 |
| Gene Name | ORC2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 108 | KHSEKMAKLASELAK |
| 115 | KLASELAKTPQKSVS |
| 119 | ELAKTPQKSVSFSLK |
| 140 | INVPQSSKGHSASDK |
| 147 | KGHSASDKVQPKNND |
| 155 | VQPKNNDKSEFLSTA |
| 224 | VVSAPVGKETPSKRM |
| 266 | LQKLKRAKLDQQTLR |
| 278 | TLRNLLSKVSPSFSA |
| 47 | AQLLVNPKKIIKKPE |
| 48 | QLLVNPKKIIKKPEY |
| 51 | VNPKKIIKKPEYDLE |
| 93 | SATGGGNKVYSFQNR |
Function
Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K20me3 and H4K27me3. Stabilizes LRWD1, by protecting it from ubiquitin-mediated proteasomal degradation. Also stabilizes ORC3
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005813 | centrosome |
| Cellular Component | GO:0000781 | chromosome, telomeric region |
| Cellular Component | GO:0000792 | heterochromatin |
| Cellular Component | GO:0000939 | inner kinetochore |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005664 | nuclear origin of replication recognition complex |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0000808 | origin recognition complex |
| Molecular Function | GO:0003688 | DNA replication origin binding |
| Biological Process | GO:0006270 | DNA replication initiation |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[4] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[5] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[6] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.