D
IPR015940

Ubiquitin-associated domain

InterPro entry
Short nameUBA
domain relationships

Description

UBA domains are a commonly occurring sequence motif of approximately 45 amino acid residues that are found in diverse proteins involved in the ubiquitin/proteasome pathway, DNA excision-repair, and cell signalling via protein kinases
[2]
. The human homologue of yeast Rad23A is one example of a nucleotide excision-repair protein that contains both an internal and a C-terminal UBA domain. The solution structure of human Rad23A UBA(2) showed that the domain forms a compact three-helix bundle
[1]
. Comparison of the structures of UBA(1) and UBA(2) reveals that both form very similar folds and have a conserved large hydrophobic surface patch which may be a common protein-interacting surface present in diverse UBA domains. Evidence that ubiquitin binds to UBA domains leads to the prediction that the hydrophobic surface patch of UBA domains interacts with the hydrophobic surface on the five-stranded β-sheet of ubiquitin
[3]
.

This domain is similar in sequence to the N-terminal domain of translation elongation factor EF1B (or EF-Ts) from bacteria, mitochondria and chloroplasts
[4]
.

References

1.Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr. Dieckmann T, Withers-Ward ES, Jarosinski MA, Liu CF, Chen IS, Feigon J. Nat. Struct. Biol. 5, 1042-7, (1998). View articlePMID: 9846873

2.The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Hofmann K, Bucher P. Trends Biochem. Sci. 21, 172-3, (1996). View articlePMID: 8871400

3.Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions. Mueller TD, Feigon J. J. Mol. Biol. 319, 1243-55, (2002). View articlePMID: 12079361

4.The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution. Kawashima T, Berthet-Colominas C, Wulff M, Cusack S, Leberman R. Nature 379, 511-8, (1996). View articlePMID: 8596629

Further reading

5. The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a SOUBA domain. Agromayor M, Soler N, Caballe A, Kueck T, Freund SM, Allen MD, Bycroft M, Perisic O, Ye Y, McDonald B, Scheel H, Hofmann K, Neil SJ, Martin-Serrano J, Williams RL. Structure 20, 414-28, (2012). View articlePMID: 22405001

6. Biochemical and structural analysis of the interaction between the UBA(2) domain of the DNA repair protein HHR23A and HIV-1 Vpr. Withers-Ward ES, Mueller TD, Chen IS, Feigon J. Biochemistry 39, 14103-12, (2000). View articlePMID: 11087358

7. DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a. Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM. Proc. Natl. Acad. Sci. U.S.A. 100, 12694-9, (2003). View articlePMID: 14557549

8. Structure of the UBA domain of Dsk2p in complex with ubiquitin molecular determinants for ubiquitin recognition. Ohno A, Jee J, Fujiwara K, Tenno T, Goda N, Tochio H, Kobayashi H, Hiroaki H, Shirakawa M. Structure 13, 521-32, (2005). View articlePMID: 15837191

9. Structural basis of E2-25K/UBB+1 interaction leading to proteasome inhibition and neurotoxicity. Ko S, Kang GB, Song SM, Lee JG, Shin DY, Yun JH, Sheng Y, Cheong C, Jeon YH, Jung YK, Arrowsmith CH, Avvakumov GV, Dhe-Paganon S, Yoo YJ, Eom SH, Lee W. J. Biol. Chem. 285, 36070-80, (2010). View articlePMID: 20826778

Cross References

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