Search Results
Overview
| Uniprot ID | P35232 |
|---|---|
| Protein Name | Prohibitin 1 |
| Gene Name | PHB1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 128 | SITTEILKSVVARFD |
| 186 | FTEAVEAKQVAQQEA |
| 202 | RARFVVEKAEQQKKA |
| 208 | EKAEQQKKAAIISAE |
| 240 | DGLIELRKLEAAEDI |
| 4 | ****MAAKVFESIGK |
| 63 | FLIPWVQKPIIFDCR |
Function
Protein with pleiotropic attributes mediated in a cell-compartment- and tissue-specific manner, which include the plasma membrane-associated cell signaling functions, mitochondrial chaperone, and transcriptional co-regulator of transcription factors in the nucleus (PubMed:11302691, PubMed:20959514, PubMed:28017329, PubMed:31522117). Plays a role in adipose tissue and glucose homeostasis in a sex-specific manner (By similarity). Contributes to pulmonary vascular remodeling by accelerating proliferation of pulmonary arterial smooth muscle cells (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0009986 | cell surface |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005769 | early endosome |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005743 | mitochondrial inner membrane |
| Cellular Component | GO:0035632 | mitochondrial prohibitin complex |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005886 | plasma membrane |
| Molecular Function | GO:0001850 | complement component C3a binding |
| Molecular Function | GO:0001851 | complement component C3b binding |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0042826 | histone deacetylase binding |
| Molecular Function | GO:0046982 | protein heterodimerization activity |
| Molecular Function | GO:0031871 | proteinase activated receptor binding |
| Molecular Function | GO:0003714 | transcription corepressor activity |
| Biological Process | GO:0140374 | antiviral innate immune response |
| Biological Process | GO:0042113 | B cell activation |
| Biological Process | GO:0071354 | cellular response to interleukin-6 |
| Biological Process | GO:0071897 | DNA biosynthetic process |
| Biological Process | GO:0040029 | epigenetic regulation of gene expression |
| Biological Process | GO:0044830 | host-mediated perturbation of viral RNA genome replication |
| Biological Process | GO:0007005 | mitochondrion organization |
| Biological Process | GO:0060766 | negative regulation of androgen receptor signaling pathway |
| Biological Process | GO:0030308 | negative regulation of cell growth |
| Biological Process | GO:0008285 | negative regulation of cell population proliferation |
| Biological Process | GO:0045892 | negative regulation of DNA-templated transcription |
| Biological Process | GO:0070373 | negative regulation of ERK1 and ERK2 cascade |
| Biological Process | GO:2000323 | negative regulation of nuclear receptor-mediated glucocorticoid signaling pathway |
| Biological Process | GO:0042177 | negative regulation of protein catabolic process |
| Biological Process | GO:0010944 | negative regulation of transcription by competitive promoter binding |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
| Biological Process | GO:0001649 | osteoblast differentiation |
| Biological Process | GO:0045917 | positive regulation of complement activation |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:0070374 | positive regulation of ERK1 and ERK2 cascade |
| Biological Process | GO:0045745 | positive regulation of G protein-coupled receptor signaling pathway |
| Biological Process | GO:0010628 | positive regulation of gene expression |
| Biological Process | GO:0002639 | positive regulation of immunoglobulin production |
| Biological Process | GO:0032740 | positive regulation of interleukin-17 production |
| Biological Process | GO:0043525 | positive regulation of neuron apoptotic process |
| Biological Process | GO:1901224 | positive regulation of non-canonical NF-kappaB signal transduction |
| Biological Process | GO:0051897 | positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction |
| Biological Process | GO:0048661 | positive regulation of smooth muscle cell proliferation |
| Biological Process | GO:0050847 | progesterone receptor signaling pathway |
| Biological Process | GO:0050821 | protein stabilization |
| Biological Process | GO:0042981 | regulation of apoptotic process |
| Biological Process | GO:0006355 | regulation of DNA-templated transcription |
| Biological Process | GO:0039529 | RIG-I signaling pathway |
| Biological Process | GO:0007165 | signal transduction |
| Biological Process | GO:0046718 | symbiont entry into host cell |
| Biological Process | GO:0072538 | T-helper 17 type immune response |
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] 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.
[3] 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.
[4] 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.
[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.