Primary Information |
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| BoMiProt ID | Bomi319 |
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| Protein Name | Proteasome assembly chaperone 2 |
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| Organism | Bos taurus |
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| Uniprot ID | Q2NL24 |
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| Milk Fraction | Exosome |
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| Ref Sequence ID | NP_001039830.1 |
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| Aminoacid Length | 264 |
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| Molecular Weight | 29224 |
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| FASTA Sequence |
Download |
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| Gene Name | PSMG2 |
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| Gene ID | 533993 |
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| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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| Protein Function | regulates assembly of its catalytic 20S core particle |
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| Biochemical Properties | As found in human, proteasome-assembling chaperon
PAC4 has a hydrophobic surface that is surrounded by charged residues;
The hydrophobic surface is complementary to that of its binding partner, PAC3; The surface
also exhibits charge complementarity with the proteasomal a4–5 subunits; Hydrophobic patches are commonly found in the centers of b-sheet surfaces
that forms PAC3–PAC4 interface; PAC4 forms a heterodimeric
complex with PAC3 through its hydrophobic surface
surrounded by the charged residues; PAC3 interface is dimeric which can be a target of inhibitors
against chaperone dimerization |
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| Significance in milk | Higher expression indicate enhanced mammary protein catabolism in cows |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Bibliography | 1. Kurimoto, E. et al. (2017) ‘Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation’, Protein Science, 26(5), pp. 1080–1085. doi: 10.1002/pro.3153. |
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