Search Results
Overview
| Uniprot ID | P49790 |
|---|---|
| Protein Name | Nuclear pore complex protein Nup153 |
| Gene Name | NUP153 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1071 | TCKTSEAKKEEMPAT |
| 15 | VGGGGGGKIRTRRCH |
| 317 | RILQSLEKMSSPLAD |
| 326 | SSPLADAKRIPSIVS |
| 353 | DITDFQAKREKVDSQ |
| 403 | TNQRIDNKCSTGYEK |
| 613 | GSVLDILKSPGFASP |
| 702 | TGIETPNKSGKTTLS |
| 705 | ETPNKSGKTTLSASG |
| 718 | SGTGFGDKFKPVIGT |
| 720 | TGFGDKFKPVIGTWD |
| 849 | SLGLEKFKKPEGSWD |
| 886 | PGTKSGFKGFDTSSS |
Function
Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat-containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0043657 | host cell |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005635 | nuclear envelope |
| Cellular Component | GO:0042405 | nuclear inclusion body |
| Cellular Component | GO:0031965 | nuclear membrane |
| Cellular Component | GO:0034399 | nuclear periphery |
| Cellular Component | GO:0005643 | nuclear pore |
| Cellular Component | GO:0044615 | nuclear pore nuclear basket |
| Cellular Component | GO:0005654 | nucleoplasm |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0140693 | molecular condensate scaffold activity |
| Molecular Function | GO:0008139 | nuclear localization sequence binding |
| Molecular Function | GO:0043495 | protein-membrane adaptor activity |
| Molecular Function | GO:0017056 | structural constituent of nuclear pore |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:1990000 | amyloid fibril formation |
| Biological Process | GO:0051028 | mRNA transport |
| Biological Process | GO:0046832 | negative regulation of RNA export from nucleus |
| Biological Process | GO:0051292 | nuclear pore complex assembly |
| Biological Process | GO:0006913 | nucleocytoplasmic transport |
| Biological Process | GO:0006606 | protein import into nucleus |
| Biological Process | GO:0006405 | RNA export from nucleus |
| Biological Process | GO:0046718 | symbiont entry into host cell |
| Biological Process | GO:0075732 | viral penetration into host nucleus |
Reference
[1] 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.
[2] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.
[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.