ライフサイエンスコーパス: ubiquitin-like protein

1 ine motif (herein called Pup for prokaryotic ubiquitin-like protein).

2 15 is an interferon (IFN)-alpha/beta-induced ubiquitin-like protein.

3 old modifier 1 (UFM1), a recently identified ubiquitin-like protein.

4 fused at its N terminus to SUMO or any other ubiquitin-like protein.

5 -expressed developmentally downregulated), a ubiquitin-like protein.

6 y is concomitantly induced and modified by a ubiquitin-like protein.

7 l modification in the form of ubiquitin or a ubiquitin-like protein.

8 modification of the TOP1 by SUMO-1/Smt3p, a ubiquitin-like protein.

9 was found to be modified by conjugation to a ubiquitin-like protein.

10 ase machinery by conjugation of ubiquitin or ubiquitin-like proteins.

11 ilar to ubiquitin and were henceforth called ubiquitin-like proteins.

12 st steps in the conjugation of ubiquitin and ubiquitin-like proteins.

13 576) within the activating enzymes for other ubiquitin-like proteins.

14 that are predicted or shown to function with ubiquitin-like proteins.

15 d a positively-charged residue in many other ubiquitin-like proteins.

16 no acid region present in UBQLN3 and several ubiquitin-like proteins.

17 components, and Dsk2p and Rad23p, a pair of ubiquitin-like proteins.

18 olutionary relative of the progenitor of all ubiquitin-like proteins.

19 ved domains found in several recently cloned ubiquitin-like proteins.

20 and has facilitated the cloning of numerous ubiquitin-like proteins.

21 y all three members of the sentrin family of ubiquitin-like proteins.

22 fication of RanGAP1 by the sentrin member of ubiquitin-like proteins.

23 covalently modified by the sentrin family of ubiquitin-like proteins.

24 dification by the attachment of ubiquitin or ubiquitin-like proteins.

25 tein domains that interact with ubiquitin or ubiquitin-like proteins.

26 Ubiquitin-like protein 1 was up-regulated over 100 fold

27 Here we report that ubiquitin-like protein 4A (Ubl4A) plays a crucial role i

28 The ataxin-1 interacting ubiquitin-like protein (A1Up) contains an amino-terminal

29 Here, we have screened most known ubiquitin-like proteins after DNA damage and found that

30 ISG15 is an IFN-inducible ubiquitin-like protein and its expression and conjugatio

31 eins that are modified by the SUMO family of ubiquitin-like proteins and describes how mutation of co

32 of GPCR clustering reveals a new function of ubiquitin-like proteins and highlights a cellular requir

33 rse the modification of proteins by a single ubiquitin(-like) protein, and remodel polyubiquitin(-lik

34 Elongin B is a ubiquitin-like protein, and Elongin C is a Skp1-like pro

35 Expression of ISG15 (UCRP), a ubiquitin-like protein, and protein ISGylation are highl

36 f the ubiquitin system, including ubiquitin, ubiquitin-like proteins, and proteins that bind to ubiqu

37 Post-translational modifications by ubiquitin-like proteins are among the most important mec

38 Ubiquitin-like proteins are covalently conjugated to cel

39 However, the functions of these ubiquitin-like proteins are largely unknown.

40 In contrast, archaeal ubiquitin-like proteins are less conserved and not known

41 the autophagy scaffold protein Atg11 and the ubiquitin-like protein Atg8.

42 to the formation of the autophagosome is the ubiquitin-like protein autophagy-related (Atg)8 (microtu

43 ation requires ATP-coupled activation of the ubiquitin-like protein by members of a superfamily of ev

44 ling cascade, and utilize autophagy-specific ubiquitin-like protein cascades to tether proteins to au

45 ontains a domain that interacts with a mouse ubiquitin-like protein conjugating (E2) enzyme, mUBC9.

46 data provide a link between acetylation and ubiquitin-like protein conjugation and define a mechanis

47 erodimeric E1-activating enzyme in the Nedd8 ubiquitin-like protein conjugation pathway.

48 h conserved protein kinase, lipid kinase and ubiquitin-like protein conjugation subnetworks controlli

49 tes in the macroautophagy pathway includes a ubiquitin-like protein conjugation system and a protein

50 he localization of components of two related ubiquitin-like protein conjugation systems, Atg8 and Atg

51 Type I ubiquitin-like proteins constitute a family of protein m

52 cloned the gene and found it encodes a novel ubiquitin-like protein containing an NH2 terminus 36% id

53 ion, we have identified a fragment of UHRF1 (ubiquitin-like protein containing PHD and RING domains 1

54 loss of function of the epigenetic regulator ubiquitin-like protein containing PHD and RING finger do

55 NEDD8, a ubiquitin-like protein, covalently conjugates to cullin

56 ess via the interaction of DSK2 with ATG8, a ubiquitin-like protein directing autophagosome formation

57 The results imply that non-covalent ubiquitin-like protein-E2 complexes are conserved platfo

58 ication scheme can be applied to other small ubiquitin-like proteins, especially those with limited p

59 ISG15 is an IFN-inducible, ubiquitin-like protein expressed after bacterial or vira

60 tin were superior in inducing catalysis, and ubiquitin-like proteins failed to activate phospholipase

61 s the most recently identified member of the ubiquitin-like protein family.

62 a patient with HIVAN, it was found that the ubiquitin-like protein FAT10 is one of the most upregula

63 2, that activates both ubiquitin and another ubiquitin-like protein, FAT10.

64 FUBI belongs to the ubiquitin-like protein group that is capable of forming

65 Modification of CUL1 by the RUB1/NEDD8 ubiquitin-like protein has been proposed to free CUL1 fr

66 The NEDD8/Rub1 class of ubiquitin-like proteins has been implicated in progressi

67 NEDD8, a novel ubiquitin-like protein, has been shown to conjugate to p

68 Recently, a surprising number of ubiquitin-like proteins have been identified that also c

69 Ubiquitin-like proteins have been shown to be covalently

70 The fau gene encodes a ubiquitin-like protein (here called FUBI) fused to the r

71 We identified a ubiquitin-like protein, hPLIC1 (for human homolog 1 of p

72 trated that PML is co-localized with a novel ubiquitin-like protein in the nuclear bodies, which coul

73 Atg8 is a ubiquitin-like protein involved in autophagy in yeast th

74 Apg8 is a ubiquitin-like protein involved in autophagy in yeast.

75 The only other known yeast ubiquitin-like protein is encoded by the nucleotide exci

76 Modification by related ubiquitin-like proteins is turning out to have a diverse

77 eria, the C-terminal Gln of Pup (prokaryotic ubiquitin-like protein) is deamidated and isopeptide lin

78 N-stimulated gene 15 (ISG15), an IFN-induced ubiquitin-like protein, is known to have an immunomodula

79 Atg8, a lipid-conjugated ubiquitin-like protein, is required for the formation of

80 The ubiquitin-like protein ISG15 and its conjugation to prot

81 The expression of the ubiquitin-like protein ISG15 and protein modification by

82 Protein modification by the ubiquitin-like protein ISG15 is an interferon (IFN) effe

83 The interferon-inducible ubiquitin-like protein ISG15 is expressed in cells in re

84 Our study revealed that the IFN-induced ubiquitin-like protein ISG15 mimics the IFN effect and i

85 Induction of the 17-kDa ubiquitin-like protein ISG15/UCRP and its subsequent con

86 43 is a protease that specifically removes a ubiquitin-like protein, ISG15, from its targets.

87 -stimulated gene 15 (ISG15), which encodes a ubiquitin-like protein, ISG15.

88 many of which are conserved among the three ubiquitin-like proteins known to undergo parallel ligati

89 g synthesis and lipidation/activation of the ubiquitin-like protein LC3 and formation of autophagic d

90 Upon induction of autophagy, the ubiquitin-like protein LC3 is conjugated to phosphatidyl

91 Such domains are common in ubiquitin and ubiquitin-like protein ligases (E3s), but little was kno

92 tif and also reveal a novel mechanism for E3 ubiquitin-like protein ligases, with the Nup358/RanBP2 E

93 six members of the LC3 and GABARAP family of ubiquitin-like proteins (mATG8s).

94 of other ubiquitin ligases with ubiquitin or ubiquitin-like proteins may likewise have major function

95 Ubiquilin-1 (Ubqln1 or Ubqln), a ubiquitin-like protein, mediates degradation of misfolde

96 The Nedd8 ubiquitin-like protein modification pathway regulates ce

97 Moreover, the variety and function of ubiquitin-like protein modifications in the cell may be

98 on of the design strategy to other polymeric ubiquitin-like protein modifications.

99 , we have investigated the role of the small ubiquitin-like protein modifier (SUMO) in SC formation d

100 Previously we showed that the small ubiquitin-like protein modifier SUMO1 interacts with an

101 NEDD8 is a ubiquitin-like protein modifier that is conjugated to ta

102 FAT10 is a ubiquitin-like protein modifier that is induced in verte

103 Ubiquitin-like proteins modify target proteins, altering

104 Covalent modification of cullins by the ubiquitin-like protein NEDD8 (neddylation) regulates pro

105 modification of the cullin subunit with the ubiquitin-like protein Nedd8 (neddylation).

106 odification of their cullin subunit with the ubiquitin-like protein NEDD8 (NEural precursor cell expr

107 Covalent modification of cullins by the ubiquitin-like protein NEDD8 activates cullin ligases th

108 cell extracts depends on the presence of the ubiquitin-like protein Nedd8 and enzymes that catalyze N

109 ultiple cullins and promoted cleavage of the ubiquitin-like protein NEDD8 from Schizosaccharomyces po

110 COP9 signalosome (CSN) cleaves the ubiquitin-like protein Nedd8 from the Cul1 subunit of SC

111 nalosome (CSN) mediates deconjugation of the ubiquitin-like protein Nedd8 from the cullin subunits of

112 the enzymatic activity that deconjugates the ubiquitin-like protein Nedd8 from the SCF Cul1 component

113 The covalent attachment of the ubiquitin-like protein Nedd8 is required for cullin acti

114 In eukaryotes, the conjugation of the ubiquitin-like protein NEDD8 onto protein targets is an

115 creases in the relative concentration of the ubiquitin-like protein NEDD8 over ubiquitin lead to acti

116 Covalent attachment of the ubiquitin-like protein NEDD8 to a conserved C-terminal d

117 tes distinctive E3-dependent ligation of the ubiquitin-like protein Nedd8 to Cul1.

118 Conjugation of ubiquitin-like protein Nedd8 to cullins (neddylation) is

119 hat culminates in covalent attachment of the ubiquitin-like protein Nedd8 to cullins.

120 ical processes by covalently conjugating the ubiquitin-like protein NEDD8 to specific targets.

121 regulated by the covalent attachment of the ubiquitin-like protein Nedd8 to the cullin subunit.

122 NUB1 is a potent down-regulator of the ubiquitin-like protein NEDD8, because it targets NEDD8 t

123 hange in the subcellular localization of the ubiquitin-like protein NEDD8, which is activated by APP-

124 modification of the Cullin-1 subunit by the ubiquitin-like protein NEDD8.

125 modification of the cullin-1 subunit by the ubiquitin-like protein NEDD8.

126 modification of the cullin-1 subunit by the ubiquitin-like protein NEDD8.

127 (Cifs) into mammalian cells to deamidate the ubiquitin-like protein NEDD8.

128 bunit of the activating enzyme for the small ubiquitin-like protein NEDD8.

129 attention has been given to the role of the ubiquitin-like protein Nedd8.

130 s (CRLs) are regulated by modification of an ubiquitin-like protein, Nedd8 (also known as Rub1) on th

131 uitin ligase (CRL) complexes by removing the ubiquitin-like protein, NEDD8, from their cullin scaffol

132 l1 lysine residue, whose modification by the ubiquitin-like protein, Nedd8, is able to block Cand1-Cu

133 s distantly related to ubiquitin and another ubiquitin-like protein, NEDD8.

134 The recent discovery of three new ubiquitin-like proteins, NEDD8, Sentrin/SUMO, and Apg12,

135 UBL3 is a ubiquitin-like protein of unknown function with no conse

136 The SUMO ubiquitin-like proteins play regulatory roles in cell di

137 In a previous report the ubiquitin-like protein Plic-1 was shown to directly inte

138 ct interaction of GABA(A) receptors with the ubiquitin-like protein Plic-1.

139 ave identified an unprecedented role for the ubiquitin-like protein PLIC-2 as a negative regulator of

140 he innate immune response, its activity as a ubiquitin-like protein protease and its activity with re

141 tional modification in which the prokaryotic ubiquitin-like protein Pup is covalently attached to a l

142 The prokaryotic ubiquitin-like protein Pup targets substrates for degrad

143 tion, the covalent attachment of prokaryotic ubiquitin-like protein Pup to lysine side chains of the

144 proteins on lysine residues with prokaryotic ubiquitin-like protein Pup.

145 Prokaryotic ubiquitin-like protein (Pup) is a posttranslational modi

146 Prokaryotic ubiquitin-like protein (Pup) is covalently attached to t

147 Prokaryotic ubiquitin-like protein (Pup) is functionally analogous t

148 Protein degradation via prokaryotic ubiquitin-like protein (Pup) tagging is conserved in bac

149 post-translationally tagged with prokaryotic ubiquitin-like protein (Pup), an intrinsically disordere

150 tituting the recently discovered prokaryotic ubiquitin-like protein (Pup)--proteasome degradation sys

151 The prokaryotic ubiquitin-like protein (Pup)-based proteasomal system in

152 Deamidase of Pup (Dop), the prokaryotic ubiquitin-like protein (Pup)-deconjugating enzyme, is cr

153 nal regulatory mechanisms in the prokaryotic ubiquitin-like protein (Pup)-proteasome system (PPS), th

154 We have identified a prokaryotic ubiquitin-like protein, Pup (Rv2111c), which was specifi

155 The ubiquitin-like protein RELATED TO UBIQUITIN (RUB) is con

156 modification and possible regulation by the ubiquitin-like protein Related to Ubiquitin in vivo.

157 Post-translational modifications with ubiquitin-like proteins require three sequentially actin

158 al modification of the cullin subunit by the ubiquitin-like protein RUB/NEDD8 appears to regulate SCF

159 The ubiquitin-like protein RUB1 is conjugated to target prot

160 bx1 modules also activate conjugation of the ubiquitin-like protein Rub1 to Cdc53 and Cul2 by the ded

161 se transporter (ena1Delta), a putative NEDD8 ubiquitin-like protein (rub1Delta), and a phosphatidylin

162 Ubiquitin-like protein/sentrin-specific proteases (Ulp/S

163 unction of Smt3p, a Saccharomyces cerevisiae ubiquitin-like protein similar to the mammalian protein

164 e recognition sequence for attachment of the ubiquitin-like protein, small ubiquitin-like modifier-1

165 n factors are targets for conjugation to the ubiquitin-like protein Smt3 (also called SUMO).

166 gation and division (tonoplast aquaporin and ubiquitin-like protein SMT3), oxidative stress (glutathi

167 enzymes and readily reversed by a family of ubiquitin-like protein-specific proteases (Ulp) in yeast

168 cation of cellular proteins by ubiquitin and ubiquitin-like proteins, such as small ubiquitin-like mo

169 Modification by the ubiquitin-like protein SUMO affects hundreds of cellular

170 valent modification of proteins by the small ubiquitin-like protein SUMO has been implicated in the r

171 Modification of cellular proteins by the ubiquitin-like protein SUMO is essential for nuclear pro

172 Post-translational modification by the ubiquitin-like protein SUMO is often regulated by cellul

173 ination and results in the attachment of the ubiquitin-like protein Sumo onto target proteins.

174 Attachment of the ubiquitin-like protein SUMO to other proteins is an esse

175 The attachment of the ubiquitin-like protein SUMO to target proteins is involv

176 albicans septins are regulated by the small ubiquitin-like protein SUMO was examined in this study b

177 ARgamma, HMGA1, and the SUMO E2 ligase Ubc9 (ubiquitin-like protein SUMO-1 conjugating enzyme).

178 PML) becomes conjugated in vivo to the small ubiquitin-like protein SUMO-1, altering its behavior and

179 In fibroblasts, APA-1 was modified by the ubiquitin-like protein SUMO-1, which increased APA-1 hal

180 ocumented substrate for conjugation with the ubiquitin-like protein SUMO-1.

181 PODs is dependent on modification of PML by ubiquitin-like protein SUMO-1.

182 a 11.5 kDa protein similar to the mammalian ubiquitin-like protein SUMO-1.

183 ion marked by the covalent attachment of the ubiquitin-like protein SUMO-1/SMT3C has been implicated

184 NA-3C in a yeast two-hybrid screen, only the ubiquitin-like proteins SUMO-1 and SUMO-3/hSMT3B map to

185 Here, we show that modification by the small ubiquitin-like protein (SUMO) is required for sister chr

186 argets cellular proteins to be modified by a ubiquitin-like protein (SUMO).

187 ight serve as a modification site by a small ubiquitin-like protein (SUMO).

188 RanGAP1 is covalently modified by the small ubiquitin-like protein, SUMO-1, and we have recently pro

189 , Ubc9 catalyzed the covalent linkage of the ubiquitin-like protein, SUMO-1, to E1.

190 Vertebrate RanGAP1 is conjugated to a small ubiquitin-like protein, SUMO-1.

191 Here, we show that HIPK2 is regulated by a ubiquitin-like protein, SUMO-1.

192 oteins are known to be modified by the small ubiquitin-like protein, SUMO.

193 Paralleling other ubiquitin-like proteins, SUMO proteins are proteolytical

194 porin RanBP2 can act as an E3 enzyme for the ubiquitin-like protein SUMO1.

195 lso is stabilized by derivatization with the ubiquitin-like protein SUMO1.

196 eport the mechanical unfolding properties of ubiquitin-like proteins (SUMO1 and SUMO2) and their comp

197 degree of structural conservation across the ubiquitin-like protein superfamily suggests that the gen

198 SUMO is a member of a ubiquitin-like protein superfamily that is covalently at

199 RNAi of ubl-5, a gene encoding a ubiquitin-like protein, suppresses activation of the UPR

200 shes a framework for investigations of other ubiquitin-like protein systems.

201 proteins that direct the conjugation of two ubiquitin-like protein tags, ATG8 and ATG12, to phosphat

202 SUMO is a small ubiquitin-like protein that becomes covalently conjugate

203 Sentrin is a novel ubiquitin-like protein that can be conjugated to other p

204 SUMO-1 is a small ubiquitin-like protein that can be covalently conjugated

205 ISG15 is a ubiquitin-like protein that conjugates to numerous prote

206 NEDD8 is a ubiquitin-like protein that controls vital biological ev

207 NEDD8 is a ubiquitin-like protein that controls vital biological ev

208 NEDD8 is a ubiquitin-like protein that controls vital biological ev

209 Nedd8 is a ubiquitin-like protein that controls vital biological ev

210 Related to Ubiquitin (RUB)/Nedd8 is a ubiquitin-like protein that covalently attaches to culli

211 he small ubiquitin-like modifier (SUMO) is a ubiquitin-like protein that covalently modifies a large

212 ISG15 is a ubiquitin-like protein that functions in innate immunity

213 ISG15 is an IFN-alpha/beta-induced, ubiquitin-like protein that is conjugated to a wide arra

214 15 is an interferon (IFN)-alpha/beta-induced ubiquitin-like protein that is conjugated to cellular pr

215 ISG15 is an interferon (IFN)-induced ubiquitin-like protein that is conjugated to target prot

216 ISG15 is a ubiquitin-like protein that is induced by interferon and

217 O, or Smt3 in Saccharomyces cerevisiae, is a ubiquitin-like protein that is post-translationally atta

218 FAT10 is a ubiquitin-like protein that is upregulated in renal tubu

219 SUMO (also called Sentrin) is a ubiquitin-like protein that plays an important role in r

220 Sentrin is a novel ubiquitin-like protein that protects cells against both

221 f PIC1 shows 52% identity to a S. cerevisiae ubiquitin-like protein that was cloned as a suppressor o

222 quitin-like domain member 1 protein and NEK, ubiquitin-like proteins that promote proteosomal PC2 deg

223 lin-RING ubiquitin ligases (CRLs) requires a ubiquitin-like protein (that is, Nedd8) modification.

224 similar mechanism to activate their cognate ubiquitin-like proteins, the substrate-assisted inhibiti

225 ymes facilitate conjugation of ubiquitin and ubiquitin-like proteins through adenylation, thioester t

226 enzymes catalyze attachment of ubiquitin and ubiquitin-like proteins to lysine residues directly or t

227 m2 also promotes the conjugation of Nedd8, a ubiquitin-like protein, to p53, inhibiting its transcrip

228 ologous positions in structurally homologous ubiquitin-like proteins; to test sequence specificity, i

229 Ubiquitin-like proteins (ub-lps) are conjugated by a con

230 that mutations in UBQLN2, which encodes the ubiquitin-like protein ubiquilin 2, cause dominantly inh

231 lex containing the proteasome as well as the ubiquitin-like protein ubiquilin-1 (UBQLN1).

232 ing transcription factor DVE-1 and the small ubiquitin-like protein UBL-5, both of which are encoded

233 e C-terminal region of MccB is homologous to ubiquitin-like protein (UBL) activating enzyme (E1) aden

234 enzyme, Atg3, to mediate conjugation of the ubiquitin-like protein (UBL) Atg8 during autophagy.

235 se modifications an E1 enzyme activates each ubiquitin-like protein (Ubl) by adenylation of the Ubl C

236 In ubiquitin-like protein (UBL) cascades, a thioester-linke

237 activate a thioester-linked E2 approximately ubiquitin-like protein (UBL) intermediate and promote UB

238 Among these is ISG15, a ubiquitin-like protein (UBL) that can be covalently atta

239 E1 enzymes initiate ubiquitin-like protein (ubl) transfer cascades by cataly

240 of SUMO(KGG) conjugation alone, as no other ubiquitin-like protein (Ubl) yields this adduct upon Lys

241 ISG15 is an interferon-induced and antiviral ubiquitin-like protein (Ubl).

242 be modulated by ligation to ubiquitin or to ubiquitin-like proteins (Ubl proteins).

243 Ubiquitin-like proteins (Ubl's) are conjugated to target

244 modification of proteins with ubiquitin and ubiquitin-like proteins (Ubl) is vital to many cellular

245 E1 enzymes activate ubiquitin or ubiquitin-like proteins (Ubl) via an adenylate intermedi

246 that interacts with RAD52, RAD51, p53, and a ubiquitin-like protein UBL1.

247 It was previously reported that a ubiquitin-like protein, UBL1, associates with RAD51 in t

248 The autophagic ubiquitin-like protein (ublp) autophagy-related (ATG)12

249 enzymes play a central role in ubiquitin and ubiquitin-like protein (ublp) transfer cascades: the E2

250 Post-translational modification by ubiquitin-like proteins (Ublps) is an essential cellular

251 Ubiquitin-like proteins (UBLs) are conjugated by dynamic

252 Ubiquitin (Ub) and ubiquitin-like proteins (Ubls) are conjugated to their t

253 Ubiquitin and ubiquitin-like proteins (UBLs) are directed to targets b

254 Modification of proteins with ubiquitin or ubiquitin-like proteins (UBLs) by means of an E1-E2-E3 c

255 ability to form analogous adducts with other ubiquitin-like proteins (UBLs) catalyzed by their cognat

256 ational covalent attachment of ubiquitin and ubiquitin-like proteins (ubls) has emerged as a predomin

257 ional covalent modification by ubiquitin and ubiquitin-like proteins (UBLs) is a major eukaryotic mec

258 The ubiquitin-like proteins (UBLs) that are part of this fam

259 t Smt3 and its vertebrate homolog SUMO-1 are ubiquitin-like proteins (Ubls) that are reversibly ligat

260 Attachment of ubiquitin (Ub) and ubiquitin-like proteins (Ubls) to cellular proteins regu

261 n-activating enzyme, Uba1, and activates two ubiquitin-like proteins (UBLs), ubiquitin and FAT10.

262 modification is conjugation to ubiquitin and ubiquitin-like proteins (UBLs), which controls an enormo

263 t steps in conjugation of ubiquitin (Ub) and ubiquitin-like proteins (Ubls).

264 Hub1/Ubl5 is a member of the family of ubiquitin-like proteins (UBLs).

265 Ubiquitin and ubiquitin-like proteins use unique E1, E2, and E3 enzyme

266 lore the set of proteins modified by a small ubiquitin-like protein, we have developed a proteomic ap

267 tiple components of the immunoproteasome and ubiquitin-like proteins were strongly induced by both IF

268 Ubiquilin 1 (UBQLN1) is a ubiquitin-like protein, which has been shown to play a c

269 IFN-stimulatory gene factor 15 (ISG15) is a ubiquitin-like protein, which is conjugated to many cell

270 FAT10 is a TNF-alpha-inducible ubiquitin-like protein with a putative role in immune re

271 Here, we describe a role for ubiquilin-1, a ubiquitin-like protein with the capacity to interact wit

272 ISG15 is an interferon-stimulated, linear di-ubiquitin-like protein, with anti-viral activity.