Search Results
Overview
| Uniprot ID | P55072 |
|---|---|
| Protein Name | Transitional endoplasmic reticulum ATPase |
| Gene Name | VCP |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 109 | IQPCPDVKYGKRIHV |
| 148 | EAYRPIRKGDIFLVR |
| 164 | GMRAVEFKVVETDPS |
| 18 | DLSTAILKQKNRPNR |
| 211 | DDIGGCRKQLAQIKE |
| 231 | LRHPALFKAIGVKPP |
| 251 | YGPPGTGKTLIARAV |
| 277 | NGPEIMSKLAGESES |
| 312 | ELDAIAPKREKTHGE |
| 386 | EILQIHTKNMKLADD |
| 502 | YPVEHPDKFLKFGMT |
| 505 | EHPDKFLKFGMTPSK |
| 524 | YGPPGCGKTLLAKAI |
| 565 | NVREIFDKARQAAPC |
| 614 | EMDGMSTKKNVFIIG |
| 658 | KSRVAILKANLRKSP |
| 668 | LRKSPVAKDVDLEFL |
| 696 | EICQRACKLAIRESI |
| 754 | VSDNDIRKYEMFAQT |
Function
Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-protein ligase activity of RNF19A. Component of the VCP/p97-AMFR/gp78 complex that participates in the final step of the sterol-mediated ubiquitination and endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Mediates the endoplasmic reticulum-associated degradation of CHRNA3 in cortical neurons as part of the STUB1-VCP-UBXN2A complex (PubMed:26265139). Involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation (PubMed:26565908). Involved in clearance process by mediating G3BP1 extraction from stress granules (PubMed:29804830, PubMed:34739333). Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA damage sites (PubMed:22020440, PubMed:22120668). Recruited to stalled replication forks by SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage (PubMed:23042605, PubMed:23042607). Together with SPRTN metalloprotease, involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis (PubMed:32152270). Involved in interstrand cross-link repair in response to replication stress by mediating unloading of the ubiquitinated CMG helicase complex (By similarity). Mediates extraction of PARP1 trapped to chromatin: recognizes and binds ubiquitinated PARP1 and promotes its removal (PubMed:35013556). Required for cytoplasmic retrotranslocation of stressed/damaged mitochondrial outer-membrane proteins and their subsequent proteasomal degradation (PubMed:16186510, PubMed:21118995). Essential for the maturation of ubiquitin-containing autophagosomes and the clearance of ubiquitinated protein by autophagy (PubMed:20104022, PubMed:27753622, PubMed:38762759). Acts as a negative regulator of type I interferon production by interacting with RIGI: interaction takes place when RIGI is ubiquitinated via 'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit RNF125 and promote ubiquitination and degradation of RIGI (PubMed:26471729). May play a role in the ubiquitin-dependent sorting of membrane proteins to lysosomes where they undergo degradation (PubMed:21822278). May more particularly play a role in caveolins sorting in cells (PubMed:21822278, PubMed:23335559). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Molecular Function | GO:0036435 | K48-linked polyubiquitin modification-dependent protein binding |
| Cellular Component | GO:1904949 | ATPase complex |
| Cellular Component | GO:0035578 | azurophil granule lumen |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0010494 | cytoplasmic stress granule |
| Cellular Component | GO:0000153 | cytoplasmic ubiquitin ligase complex |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0036513 | Derlin-1 retrotranslocation complex |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:1904813 | ficolin-1-rich granule lumen |
| Cellular Component | GO:0098978 | glutamatergic synapse |
| Cellular Component | GO:0043231 | intracellular membrane-bounded organelle |
| Cellular Component | GO:0005811 | lipid droplet |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
| Cellular Component | GO:0000502 | proteasome complex |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:0034774 | secretory granule lumen |
| Cellular Component | GO:0035861 | site of double-strand break |
| Cellular Component | GO:0034098 | VCP-NPL4-UFD1 AAA ATPase complex |
| Cellular Component | GO:1990730 | VCP-NSFL1C complex |
| Molecular Function | GO:0043531 | ADP binding |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:1904288 | BAT3 complex binding |
| Molecular Function | GO:0035800 | deubiquitinase activator activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0008289 | lipid binding |
| Molecular Function | GO:0042288 | MHC class I protein binding |
| Molecular Function | GO:0031593 | polyubiquitin modification-dependent protein binding |
| Molecular Function | GO:0019904 | protein domain specific binding |
| Molecular Function | GO:0019903 | protein phosphatase binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Molecular Function | GO:0044389 | ubiquitin-like protein ligase binding |
| Molecular Function | GO:0140036 | ubiquitin-modified protein reader activity |
| Molecular Function | GO:1990381 | ubiquitin-specific protease binding |
| Biological Process | GO:0046034 | ATP metabolic process |
| Biological Process | GO:0097352 | autophagosome maturation |
| Biological Process | GO:0006914 | autophagy |
| Biological Process | GO:1903843 | cellular response to arsenite ion |
| Biological Process | GO:0034605 | cellular response to heat |
| Biological Process | GO:0071218 | cellular response to misfolded protein |
| Biological Process | GO:0140455 | cytoplasm protein quality control |
| Biological Process | GO:0006974 | DNA damage response |
| Biological Process | GO:0006281 | DNA repair |
| Biological Process | GO:0006302 | double-strand break repair |
| Biological Process | GO:0061857 | endoplasmic reticulum stress-induced pre-emptive quality control |
| Biological Process | GO:0006888 | endoplasmic reticulum to Golgi vesicle-mediated transport |
| Biological Process | GO:0030968 | endoplasmic reticulum unfolded protein response |
| Biological Process | GO:0032510 | endosome to lysosome transport via multivesicular body sorting pathway |
| Biological Process | GO:0036503 | ERAD pathway |
| Biological Process | GO:0045184 | establishment of protein localization |
| Biological Process | GO:0072389 | flavin adenine dinucleotide catabolic process |
| Biological Process | GO:0036297 | interstrand cross-link repair |
| Biological Process | GO:0016236 | macroautophagy |
| Biological Process | GO:0000423 | mitophagy |
| Biological Process | GO:0051228 | mitotic spindle disassembly |
| Biological Process | GO:0019674 | NAD+ metabolic process |
| Biological Process | GO:0035331 | negative regulation of hippo signaling |
| Biological Process | GO:0120186 | negative regulation of protein localization to chromatin |
| Biological Process | GO:0045879 | negative regulation of smoothened signaling pathway |
| Biological Process | GO:2001171 | positive regulation of ATP biosynthetic process |
| Biological Process | GO:0090263 | positive regulation of canonical Wnt signaling pathway |
| Biological Process | GO:0010918 | positive regulation of mitochondrial membrane potential |
| Biological Process | GO:1901224 | positive regulation of non-canonical NF-kappaB signal transduction |
| Biological Process | GO:1903862 | positive regulation of oxidative phosphorylation |
| Biological Process | GO:0032436 | positive regulation of proteasomal ubiquitin-dependent protein catabolic process |
| Biological Process | GO:0045732 | positive regulation of protein catabolic process |
| Biological Process | GO:1903006 | positive regulation of protein K63-linked deubiquitination |
| Biological Process | GO:0031334 | positive regulation of protein-containing complex assembly |
| Biological Process | GO:0010498 | proteasomal protein catabolic process |
| Biological Process | GO:0043161 | proteasome-mediated ubiquitin-dependent protein catabolic process |
| Biological Process | GO:0016567 | protein ubiquitination |
| Biological Process | GO:0043335 | protein unfolding |
| Biological Process | GO:0106300 | protein-DNA covalent cross-linking repair |
| Biological Process | GO:1903715 | regulation of aerobic respiration |
| Biological Process | GO:0042981 | regulation of apoptotic process |
| Biological Process | GO:1905634 | regulation of protein localization to chromatin |
| Biological Process | GO:0050807 | regulation of synapse organization |
| Biological Process | GO:0072344 | rescue of stalled cytosolic ribosome |
| Biological Process | GO:0030970 | retrograde protein transport, ER to cytosol |
| Biological Process | GO:1990116 | ribosome-associated ubiquitin-dependent protein catabolic process |
| Biological Process | GO:0035617 | stress granule disassembly |
| Biological Process | GO:0019985 | translesion synthesis |
| Biological Process | GO:0006511 | ubiquitin-dependent protein catabolic process |
| Biological Process | GO:0019079 | viral genome replication |
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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[4] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.
[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.