Search Results
Overview
| Uniprot ID | P51572 |
|---|---|
| Protein Name | B-cell receptor-associated protein 31 |
| Gene Name | BCAP31 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 138 | ASNEAFKKQAESASE |
| 148 | ESASEAAKKYMEEND |
| 149 | SASEAAKKYMEENDQ |
| 158 | MEENDQLKKGAAVDG |
| 167 | GAAVDGGKLDVGNAE |
| 192 | KADLQKLKDELASTK |
| 199 | KDELASTKQKLEKAE |
| 204 | STKQKLEKAENQVLA |
| 72 | DAVREIRKYDDVTEK |
| 95 | AMEHFHMKLFRAQRN |
Function
Functions as a chaperone protein (PubMed:18287538, PubMed:9396746). Is one of the most abundant endoplasmic reticulum (ER) proteins (PubMed:18287538, PubMed:9396746). Plays a role in the export of secreted proteins in the ER, the recognition of abnormally folded protein and their targeting to the ER associated-degradation (ERAD) (PubMed:18287538, PubMed:9396746). Also serves as a cargo receptor for the export of transmembrane proteins (By similarity). Plays a role in the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) by stimulating the translocation of NDUFS4 and NDUFB11 from the cytosol to the mitochondria via interaction with TOMM40 (PubMed:31206022). In response to ER stress, delocalizes from the ER-mitochondria contact sites and binds BCL2 (PubMed:31206022). May be involved in CASP8-mediated apoptosis (PubMed:10958671)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0098553 | lumenal side of endoplasmic reticulum membrane |
| Cellular Component | GO:0030136 | clathrin-coated vesicle |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Cellular Component | GO:0033116 | endoplasmic reticulum-Golgi intermediate compartment membrane |
| Cellular Component | GO:0032580 | Golgi cisterna membrane |
| Cellular Component | GO:0000139 | Golgi membrane |
| Cellular Component | GO:0005811 | lipid droplet |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0044233 | mitochondria-associated endoplasmic reticulum membrane contact site |
| Cellular Component | GO:0097038 | perinuclear endoplasmic reticulum |
| Cellular Component | GO:0005886 | plasma membrane |
| Molecular Function | GO:0042288 | MHC class I protein binding |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Biological Process | GO:0006915 | apoptotic process |
| Biological Process | GO:0006888 | endoplasmic reticulum to Golgi vesicle-mediated transport |
| Biological Process | GO:0006886 | intracellular protein transport |
| Biological Process | GO:1904294 | positive regulation of ERAD pathway |
| Biological Process | GO:2001244 | positive regulation of intrinsic apoptotic signaling pathway |
| Biological Process | GO:1904154 | positive regulation of retrograde protein transport, ER to cytosol |
| Biological Process | GO:2000060 | positive regulation of ubiquitin-dependent protein catabolic process |
| Biological Process | GO:0070973 | protein localization to endoplasmic reticulum exit site |
| Biological Process | GO:0006626 | protein targeting to mitochondrion |
| Biological Process | GO:0034976 | response to endoplasmic reticulum stress |
| Biological Process | GO:0007283 | spermatogenesis |
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] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.
[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.