Overview
| Uniprot ID | Q04323 |
|---|
| Protein Name | UBX domain-containing protein 1 |
|---|
| Gene Name | UBXN1 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 154 |
AEERRREKAEELAAR |
| 178 |
DKAERAKKYGGSVGS |
Function
Ubiquitin-binding protein that plays a role in the modulation of innate immune response. Blocks both the RIG-I-like receptors (RLR) and NF-kappa-B pathways. Following viral infection, UBXN1 is induced and recruited to the RLR component MAVS. In turn, interferes with MAVS oligomerization, and disrupts the MAVS/TRAF3/TRAF6 signalosome. This function probably serves as a brake to prevent excessive RLR signaling (PubMed:23545497). Interferes with the TNFalpha-triggered NF-kappa-B pathway by interacting with cellular inhibitors of apoptosis proteins (cIAPs) and thereby inhibiting their recruitment to TNFR1 (PubMed:25681446). Also prevents the activation of NF-kappa-B by associating with CUL1 and thus inhibiting NF-kappa-B inhibitor alpha/NFKBIA degradation that remains bound to NF-kappa-B (PubMed:28152074). Interacts with the BRCA1-BARD1 heterodimer and regulates its activity. Specifically binds 'Lys-6'-linked polyubiquitin chains. Interaction with autoubiquitinated BRCA1 leads to the inhibition of the E3 ubiquitin-protein ligase activity of the BRCA1-BARD1 heterodimer (PubMed:20351172). Component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol
Protein Sequence
10
MAELTALESL
20
IEMGFPRGRA
30
EKALALTGNQ
40
GIEAAMDWLM
50
EHEDDPDVDE
60
PLETPLGHIL
70
GREPTSSEQG
80
GLEGSGSAAG
90
EGKPALSEEE
100
RQEQTKRMLE
110
LVAQKQRERE
120
EREEREALER
130
ERQRRRQGQE
140
LSAARQRLQE
150
DEMRRAAEER
160
RREKAEELAA
170
RQRVREKIER
180
DKAERAKKYG
190
GSVGSQPPPV
200
APEPGPVPSS
210
PSQEPPTKRE
220
YDQCRIQVRL
230
PDGTSLTQTF
240
RAREQLAAVR
250
LYVELHRGEE
260
LGGGQDPVQL
270
LSGFPRRAFS
280
EADMERPLQE
290
LGLVPSAVLI
VAKKCPS
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005783 |
endoplasmic reticulum |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0034098 |
VCP-NPL4-UFD1 AAA ATPase complex |
| Molecular Function |
GO:0051117 |
ATPase binding |
| Molecular Function |
GO:0036435 |
K48-linked polyubiquitin modification-dependent protein binding |
| Molecular Function |
GO:0071796 |
K6-linked polyubiquitin modification-dependent protein binding |
| Molecular Function |
GO:0031593 |
polyubiquitin modification-dependent protein binding |
| Molecular Function |
GO:1904855 |
proteasome regulatory particle binding |
| Molecular Function |
GO:0043130 |
ubiquitin binding |
| Molecular Function |
GO:0031625 |
ubiquitin protein ligase binding |
| Biological Process |
GO:1904293 |
negative regulation of ERAD pathway |
| Biological Process |
GO:0032435 |
negative regulation of proteasomal ubiquitin-dependent protein catabolic process |
| Biological Process |
GO:1903094 |
negative regulation of protein K48-linked deubiquitination |
| Biological Process |
GO:0031397 |
negative regulation of protein ubiquitination |
| Biological Process |
GO:0043161 |
proteasome-mediated ubiquitin-dependent protein catabolic process |
| Biological Process |
GO:0006511 |
ubiquitin-dependent protein catabolic process |
Reference
[1] 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.