| Feature (domain/motif or function) | Description/role | Key partners/cargos | Evidence/source (with publication year + journal) | URL |
|---|---|---|---|---|
| PB1 domain | N-terminal PB1 mediates strong PB1-PB1 interaction with p62/SQSTM1; metazoan NBR1 PB1 is monomeric but recruits NBR1 to p62 bodies and can act as a chain terminator that limits p62 filament length while promoting cargo clustering. | p62/SQSTM1; MEKK3 | Rasmussen et al., 2022, *Journal of Cell Biology* (pqac-00000004, pqac-00000010) | https://doi.org/10.1083/jcb.202208092 |
| ZZ zinc-finger domain | Conserved ZZ-type zinc-finger is part of canonical human NBR1 architecture shared with selective autophagy receptors; included in domain schematics for metazoan NBR1. | Protein-interaction module; specific human partners not detailed in the extracted contexts | Rasmussen et al., 2022, *Journal of Cell Biology* (pqac-00000000, pqac-00000006, pqac-00000025) | https://doi.org/10.1083/jcb.202208092 |
| CC1 / coiled-coil regions | Coiled-coil region supports NBR1 self-interaction/oligomerization and contributes to receptor assembly during cargo capture. | NBR1 self-association; cooperative assembly with p62 | Cerda-Troncoso et al., 2021, *Frontiers in Oncology* (pqac-00000002, pqac-00000007) | https://doi.org/10.3389/fonc.2020.619727 |
| FW domain | Four-tryptophan (FW) domain is distinctive for NBR1 and participates in cargo/adaptor recognition; in human NBR1 it binds MAP1B and TAX1BP1 and helps recruit TAX1BP1 to p62 bodies. | TAX1BP1; MAP1B | Rasmussen et al., 2022, *Journal of Cell Biology* (pqac-00000003, pqac-00000004) | https://doi.org/10.1083/jcb.202208092 |
| LIR motifs (LIR1/LIR2) | Human NBR1 has two LC3-interacting regions; LIR1 is the dominant functional site in cells. LIRs tether cargo-bound NBR1 to ATG8-family proteins and also connect to FIP200/TAX1BP1 through overlapping determinants in recent work. | LC3/GABARAP/ATG8 proteins; FIP200; TAX1BP1 | Rasmussen et al., 2022, *Journal of Cell Biology*; North et al., 2025, *bioRxiv* (preprint reporting 2024 work) (pqac-00000000, pqac-00000001, pqac-00000015) | https://doi.org/10.1083/jcb.202208092 ; https://doi.org/10.1101/2024.05.09.593318 |
| AH + UBA region | A C-terminal amphipathic helix adjacent to the UBA helps membrane association; coincident AH-UBA binding targets NBR1 to ubiquitinated peroxisomes and contributes to membrane/peroxisome localization. | PIP-containing membranes; ubiquitinated peroxisomes | Rasmussen et al., 2022, *Journal of Cell Biology* (pqac-00000000, pqac-00000005, pqac-00000011) | https://doi.org/10.1083/jcb.202208092 |
| UBA domain | C-terminal ubiquitin-associated domain binds mono- and polyubiquitin with high affinity, enabling selective recognition of ubiquitinated cargo for autophagic delivery. | Ubiquitinated protein aggregates; bacteria; peroxisomal proteins; MHC-I-associated cargo | Rasmussen et al., 2022, *Journal of Cell Biology*; Cerda-Troncoso et al., 2021, *Frontiers in Oncology* (pqac-00000000, pqac-00000002, pqac-00000011) | https://doi.org/10.1083/jcb.202208092 ; https://doi.org/10.3389/fonc.2020.619727 |
| Archetypal selective autophagy receptor | NBR1 is an evolutionarily ancient, ubiquitin-dependent selective autophagy receptor that bridges ubiquitinated cargo to autophagosomes through ubiquitin binding plus ATG8-family binding. | Ubiquitinated cargos broadly | Rasmussen et al., 2022, *Journal of Cell Biology*; Vargas et al., 2023, *Nature Reviews Molecular Cell Biology* (pqac-00000008, pqac-00000023) | https://doi.org/10.1083/jcb.202208092 ; https://doi.org/10.1038/s41580-022-00542-2 |
| Aggrephagy / p62-body organization | NBR1 is recruited to p62 bodies, enhances p62 phase separation with ubiquitin, and promotes clustering of ubiquitinated aggregates; however, receptor requirements can be cell-type dependent, with redundancy in mouse ESCs/neurons. | p62 condensates; ubiquitinated aggregates | Rasmussen et al., 2022, *Journal of Cell Biology*; Trapannone et al., 2023, *Life Science Alliance* (pqac-00000004, pqac-00000010, pqac-00000028, pqac-00000029) | https://doi.org/10.1083/jcb.202208092 ; https://doi.org/10.26508/lsa.202301936 |
| Pexophagy | NBR1 mediates selective degradation of ubiquitinated peroxisomes; AH, UBA, LIR, and CC regions are required, and p62 can enhance but is not strictly required. | Ubiquitinated peroxisomes; p62 | Rasmussen et al., 2022, *Journal of Cell Biology* (pqac-00000005, pqac-00000011) | https://doi.org/10.1083/jcb.202208092 |
| Xenophagy / antiviral defense | NBR1 participates in xenophagy, including recruitment to intracellular pathogens and turnover during HSV-1 infection; HSV-1 infection significantly lowers NBR1 protein in H4 and HaCaT cells, consistent with active xenophagic receptor clearance. | HSV-1-associated cargo; ubiquitinated pathogens | Pino-Belmar et al., 2024, *Cells*; Rasmussen et al., 2022, *Journal of Cell Biology* (pqac-00000016, pqac-00000018, pqac-00000021, pqac-00000033) | https://doi.org/10.3390/cells13151256 ; https://doi.org/10.1083/jcb.202208092 |
| Focal-adhesion turnover / migration | NBR1 binds ubiquitylated focal-adhesion proteins and mediates their selective autophagic turnover, promoting focal-adhesion turnover and cell migration/metastatic outgrowth in some cancer models. | Ubiquitylated focal-adhesion components | Cerda-Troncoso et al., 2021, *Frontiers in Oncology*; Rasmussen et al., 2022, *Journal of Cell Biology* (pqac-00000007, pqac-00000012, pqac-00000005) | https://doi.org/10.3389/fonc.2020.619727 ; https://doi.org/10.1083/jcb.202208092 |
| Disease-linked selective cargo clearance | In human nucleus pulposus cells, NBR1 directs autophagic-lysosomal clearance of SRBD1; NBR1 knockdown caused a proteomic shift with 1,082 differentially expressed proteins and ~50.6-fold SRBD1 upregulation, linking NBR1 to suppression of senescence/SASP pathways. | SRBD1 | Song et al., 2024, *International Journal of Biological Sciences* (pqac-00000014, pqac-00000030, pqac-00000035) | https://doi.org/10.7150/ijbs.90186 |
| Immune evasion / MHC-I regulation | NBR1-mediated selective autophagy can reduce MHC class I abundance in pancreatic ductal adenocarcinoma cells, linking cargo selection to tumor immune evasion. | Ubiquitylated MHC-I | Rasmussen et al., 2022, *Journal of Cell Biology*; Cerda-Troncoso et al., 2021, *Frontiers in Oncology* (pqac-00000002, pqac-00000009) | https://doi.org/10.1083/jcb.202208092 ; https://doi.org/10.3389/fonc.2020.619727 |


*Table: This table summarizes the validated domain architecture of human NBR1 (UniProt Q14596) and its best-supported molecular interactions and selective-autophagy functions. It is useful as a compact functional annotation reference grounded only in the provided source contexts.*