{PDOC51322}
{PS51322; UEV}
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* UEV domain profile *
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The N-terminal  ubiquitin  E2 variant (UEV) domain is ~145 amino acid residues
in length  and  shows  significant sequence similarity to E2 ubiquitin ligases
(see <PDOC00163>) but is unable to catalyze ubiquitin transfer as it lacks the
active site  cysteine  that  forms  the  transient  thioester bond with the C-
terminus of ubiquitin (Ub). Nevertheless, at least some UEVs have retained the
ability to  bind  Ub,  and appear to act either as cofactors in ubiquitylation
reactions, or  as ubiquitin sensors. UEV domains also frequently contain other
protein recognition  motifs,  and may generally serve to couple protein and Ub
binding functions  to  facilitate  the  formation  of  multiprotein  complexes
[1,2,3,4].

The UEV  domain  consists  of  a twisted four-stranded antiparallel beta-sheet
having a  meander topology, with four alpha-helices packed against one face of
the sheet  (see <PDB:1KPP>). The UEV fold is generally similar to canonical E2
ligases in  the  hydrophobic  core  and  'active  site'  regions,  but differs
significantly at both its N- and C-termini [3,4].

Some proteins known to contain a UEV domain are listed below:

 - Yeast vacuolar protein sorting-associated protein 23 (Vps23).
 - Mammalian tumor susceptibility gene TSG101 protein, the homologue of Vps23.

The profile we developed covers the entire UEV domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: June 2010 / First entry.

[ 1] Koonin E.V., Abagyan R.A.
     "TSG101 may be the prototype of a class of dominant negative ubiquitin
     regulators."
     Nat. Genet. 16:330-331(1997).
     PubMed=9241264; DOI=10.1038/ng0897-330
[ 2] Ponting C.P., Cai Y.-D., Bork P.
     "The breast cancer gene product TSG101: a regulator of
     ubiquitination?"
     J. Mol. Med. 75:467-469(1997).
     PubMed=9253709
[ 3] Pornillos O., Alam S.L., Rich R.L., Myszka D.G., Davis D.R.,
     Sundquist W.I.
     "Structure and functional interactions of the Tsg101 UEV domain."
     EMBO J. 21:2397-2406(2002).
     PubMed=12006492; DOI=10.1093/emboj/21.10.2397
[ 4] Teo H., Veprintsev D.B., Williams R.L.
     "Structural insights into endosomal sorting complex required for
     transport (ESCRT-I) recognition of ubiquitinated proteins."
     J. Biol. Chem. 279:28689-28696(2004).
     PubMed=15044434; DOI=10.1074/jbc.M400023200

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