Search Results
Overview
| Uniprot ID | Q15907 |
|---|---|
| Protein Name | Ras-related protein Rab-11B |
| Gene Name | RAB11B |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 179 | IYRIVSQKQIADRAA |
| 24 | IGDSGVGKSNLLSRF |
| 61 | QVDGKTIKAQIWDTA |
Function
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:14627637, PubMed:19029296, PubMed:19244346, PubMed:20717956, PubMed:21248079, PubMed:22129970, PubMed:26032412). RAB11B plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis (PubMed:14627637, PubMed:19029296, PubMed:19244346, PubMed:20717956, PubMed:21248079, PubMed:22129970). Promotes Rabin8/RAB3IP preciliary vesicular trafficking to mother centriole by forming a ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, thereby regulating ciliogenesis initiation (PubMed:25673879). On the contrary, upon LPAR1 receptor signaling pathway activation, interaction with phosphorylated WDR44 prevents Rab11-RAB3IP-RAB11FIP3 complex formation and cilia growth (PubMed:31204173). Also interacts with RABL3 to promote ciliary vesicle formation (PubMed:36052645)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005794 | Golgi apparatus |
| Cellular Component | GO:0045335 | phagocytic vesicle |
| Cellular Component | GO:0030670 | phagocytic vesicle membrane |
| Cellular Component | GO:0055037 | recycling endosome |
| Cellular Component | GO:0055038 | recycling endosome membrane |
| Cellular Component | GO:0008021 | synaptic vesicle |
| Cellular Component | GO:0030672 | synaptic vesicle membrane |
| Molecular Function | GO:0045296 | cadherin binding |
| Molecular Function | GO:0003925 | G protein activity |
| Molecular Function | GO:0019003 | GDP binding |
| Molecular Function | GO:0005525 | GTP binding |
| Molecular Function | GO:0003924 | GTPase activity |
| Molecular Function | GO:0031489 | myosin V binding |
| Biological Process | GO:0150093 | amyloid-beta clearance by transcytosis |
| Biological Process | GO:0071468 | cellular response to acidic pH |
| Biological Process | GO:0045054 | constitutive secretory pathway |
| Biological Process | GO:0032456 | endocytic recycling |
| Biological Process | GO:0090150 | establishment of protein localization to membrane |
| Biological Process | GO:0035773 | insulin secretion involved in cellular response to glucose stimulus |
| Biological Process | GO:0032402 | melanosome transport |
| Biological Process | GO:0001881 | receptor recycling |
| Biological Process | GO:0045055 | regulated exocytosis |
| Biological Process | GO:1902017 | regulation of cilium assembly |
| Biological Process | GO:2001135 | regulation of endocytic recycling |
| Biological Process | GO:0044070 | regulation of monoatomic anion transport |
| Biological Process | GO:2000008 | regulation of protein localization to cell surface |
| Biological Process | GO:0033572 | transferrin transport |
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] 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.