PROSITE documentation PDOC51745PB1 domain profile
The PB1 (Phox and Bem1) domain, comprising about 80 amino acid residues, is conserved among animals, fungi, amoebas, and plants. It functions as a protein binding module through PB1-mediated heterodimerization or homo-oligomerization [1,2,3,4]. The PB1 domain is found in several signaling proteins including:
- Mammalian MEK5, a MAP kinase kinase implicated in epidermal growth factor- induced cell proliferation.
- Mammalian Sequestosome-1 (Sqstm1) or p62/ZIP, a protein linking the zeta isoform of protein kinase C to RIP and/or potassium channels.
- Mammalian neutrophil cytosol factor 4 (NCF-4) or p40(phox), a cytosolic factor of the superoxide-generating NADPH oxidase in phagocytes.
- Mammalian neutrophil cytosol factor 2 (NCF-2) or p67(phox), an oxidase activator.
- Yeast bud emergence protein 1 (Bem1), necessary for cell polarization during vegetative growth.
- Yeast cell division control protein 24 (CDC24), a guanine nucleotide exchange factor (GEF) for the small GTPase CDC42.
- Plant AUXIN RESPONSE FACTOR (ARF) transcription factor family, regulates gene expression in response to auxin.
- Plant AUXIN/INDOLE 3-ACETIC ACID (Aux/IAA) repressor proteins, repress ARF transcription factors via direct interaction under low auxin concentrations.
The PB1 domains adopt an ubiquitin-like β-grasp fold, containing two α helices and a mixed five-stranded β sheet (see <PDB:1WMH>). The β-sheet has a convex surface, and α1 fits into the cavity formed by the sheet. PB1 domains may display an acidic surface (type I), a basic surface (tape II), or both surfaces (type I/II) on opposite faces of the domain structure to allow for front-to-back orientation of multiple PB1 domains [1,2,3,4].
The profile we developed covers the entire PB1 domain.
Last update:January 2015 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Sumimoto H. Kamakura S. Ito T. |
| Title | Structure and function of the PB1 domain, a protein interaction module conserved in animals, fungi, amoebas, and plants. | |
| Source | Sci. STKE 2007:Re6-Re6(2007). | |
| PubMed ID | 17726178 | |
| DOI | 10.1126/stke.4012007re6 |
| 2 | Authors | Hirano Y. Yoshinaga S. Takeya R. Suzuki N.N. Horiuchi M. Kohjima M. Sumimoto H. Inagaki F. |
| Title | Structure of a cell polarity regulator, a complex between atypical PKC and Par6 PB1 domains. | |
| Source | J. Biol. Chem. 280:9653-9661(2005). | |
| PubMed ID | 15590654 | |
| DOI | 10.1074/jbc.M409823200 |
| 3 | Authors | Terasawa H. Noda Y. Ito T. Hatanaka H. Ichikawa S. Ogura K. Sumimoto H. Inagaki F. |
| Title | Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif. | |
| Source | EMBO J. 20:3947-3956(2001). | |
| PubMed ID | 11483498 | |
| DOI | 10.1093/emboj/20.15.3947 |
| 4 | Authors | Korasick D.A. Westfall C.S. Lee S.G. Nanao M.H. Dumas R. Hagen G. Guilfoyle T.J. Jez J.M. Strader L.C. |
| Title | Molecular basis for AUXIN RESPONSE FACTOR protein interaction and the control of auxin response repression. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 111:5427-5432(2014). | |
| PubMed ID | 24706860 | |
| DOI | 10.1073/pnas.1400074111 |
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