|SMART accession number:||SM00213|
|Description:||Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression|
|Interpro abstract (IPR000626):|
Ubiquitinylation is an ATP-dependent process that involves the action of at least three enzymes: a ubiquitin-activating enzyme (E1, IPR000011), a ubiquitin-conjugating enzyme (E2, IPR000608), and a ubiquitin ligase (E3, IPR000569, IPR003613), which work sequentially in a cascade. There are many different E3 ligases, which are responsible for the type of ubiquitin chain formed, the specificity of the target protein, and the regulation of the ubiquitinylation process [(PUBMED:12646216)]. Ubiquitinylation is an important regulatory tool that controls the concentration of key signalling proteins, such as those involved in cell cycle control, as well as removing misfolded, damaged or mutant proteins that could be harmful to the cell. Several ubiquitin-like molecules have been discovered, such as Ufm1 (IPR005375), SUMO1 (IPR003653), NEDD8, Rad23 (IPR004806), Elongin B and Parkin (IPR003977), the latter being involved in Parkinson's disease [(PUBMED:15564047)].
Ubiquitin is a protein of 76 amino acid residues, found in all eukaryotic cells and whose sequence is extremely well conserved from protozoan to vertebrates. Ubiquitin acts through its post-translational attachment (ubiquitinylation) to other proteins, where these modifications alter the function, location or trafficking of the protein, or targets it for destruction by the 26S proteasome [(PUBMED:15454246)]. The terminal glycine in the C-terminal 4-residue tail of ubiquitin can form an isopeptide bond with a lysine residue in the target protein, or with a lysine in another ubiquitin molecule to form a ubiquitin chain that attaches itself to a target protein. Ubiquitin has seven lysine residues, any one of which can be used to link ubiquitin molecules together, resulting in different structures that alter the target protein in different ways. It appears that Lys(11)-, Lys(29) and Lys(48)-linked poly-ubiquitin chains target the protein to the proteasome for degradation, while mono-ubiquitinylated and Lys(6)- or Lys(63)-linked poly-ubiquitin chains signal reversible modifications in protein activity, location or trafficking [(PUBMED:14998368)]. For example, Lys(63)-linked poly-ubiquitinylation is known to be involved in DNA damage tolerance, inflammatory response, protein trafficking and signal transduction through kinase activation [(PUBMED:15556404)]. In addition, the length of the ubiquitin chain alters the fate of the target protein. Regulatory proteins such as transcription factors and histones are frequent targets of ubquitinylation [(PUBMED:15525528)].
|GO function:||protein binding (GO:0005515)|
Click on the following links for more information.
- Evolution (species in which this domain is found)
Click on to expand nodes. To display all proteins with a UBQ domain in a specific node, click on it.
This tree shows only several representative species. The complete taxonomic breakdown of all proteins with UBQ domain is also avaliable.
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Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes
- Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Bedford MT, Leder P
- The FF domain: a novel motif that often accompanies WW domains.
- Trends Biochem Sci. 1999; 24: 264-5
- Hofmann K, Bucher P
- The PCI domain: a common theme in three multiprotein complexes.
- Trends Biochem Sci. 1998; 23: 204-5
- Haas AL
- Introduction: evolving roles for ubiquitin in cellular regulation.
- FASEB J. 1997; 11: 1053-4
- Haas AL, Siepmann TJ
- Pathways of ubiquitin conjugation.
- FASEB J. 1997; 11: 1257-68
- Display abstract
The covalent attachment of the polypeptide ubiquitin to proteins marks them for degradation by the ubiquitin/26S proteasome-dependent degradation pathway. This pathway functions in regulating many fundamental processes required for cell viability. Phylogenetic analysis of ubiquitin sequences reveals greater variability among lower eukaryotes and defines essential residues, many of which are conserved among the three ubiquitin-like proteins known to undergo parallel ligation pathways. The hierarchical design of the ubiquitin conjugation mechanism provides great flexibility for the divergent evolution of new functions mediated by this posttranslational modification. Within this hierarchy, a single ubiquitin-activating enzyme provides charged intermediates to multiple targeting pathways defined by cognate ubiquitin carrier protein (E2)/ligase (E3) pairs. Sequence analysis of E2 isozymes shows that the E2 superfamily is composed of distinct function-specific families. The apparent lack of E2/E3 specificity suggested in the literature results from the presence of multiple isozymes within many E2 families and erroneous family assignments based on incomplete data sets. Other apparent inconsistencies are explained by interfamily sequence relationships among some E2 isoforms.
- Hershko A
- Roles of ubiquitin-mediated proteolysis in cell cycle control.
- Curr Opin Cell Biol. 1997; 9: 788-99
- Display abstract
Selective degradation of cyclins, inhibitors of cyclin-dependent kinases and anaphase inhibitors is responsible for several major cell cycle transitions. The degradation of these cell cycle regulators is controlled by the action of ubiquitin-protein-ligase complexes, which target the regulators for degradation by the 26S proteasome. Recent results indicate that two types of multisubunit ubiquitin ligase complexes, which are connected to the protein kinase regulatory network of the cell cycle in different ways, are responsible for the specific and programmed degradation of many cell cycle regulators.
- Saitoh H, Pu RT, Dasso M
- SUMO-1: wrestling with a new ubiquitin-related modifier.
- Trends Biochem Sci. 1997; 22: 374-6
- Hochstrasser M
- Ubiquitin-dependent protein degradation.
- Annu Rev Genet. 1996; 30: 405-39
- Display abstract
A growing number of cellular regulatory mechanisms are being linked to protein modification by the polypeptide ubiquitin. These include key transitions in the cell cycle, class I antigen processing, signal transduction pathways, and receptor-mediated endocytosis. In most, but not all, of these examples, ubiquitination of a protein leads to its degradation by the 26S proteasome. Following attachment of ubiquitin to a substrate and binding of the ubiquitinated protein to the proteasome, the bound substrate must be unfolded (and eventually deubiquitinated) and translocated through a narrow set of channels that leads to the proteasome interior, where the polypeptide is cleaved into short peptides. Protein ubiquitination and deubiquitination are both mediated by large enzyme families, and the proteasome itself comprises a family of related but functionally distinct particles. This diversity underlies both the high substrate specificity of the ubiquitin system and the variety of regulatory mechanisms that it serves.
- Hofmann K, Bucher P
- The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway.
- Trends Biochem Sci. 1996; 21: 172-3
- Isaksson A, Musti AM, Bohmann D
- Ubiquitin in signal transduction and cell transformation.
- Biochim Biophys Acta. 1996; 1288: 219-219
- Display abstract
Since the discovery of ubiquitin-dependent protein degradation almost two decades ago, great strides have been made towards a detailed understanding of the biochemistry of this process (reviewed in [1-3]). It was, however, only in recent years that the physiological role of the ubiquitin system in signal transduction and the regulation of several cell functions started to be appreciated and experimentally addressed. As with other principal mechanisms of signal transduction, such as phosphorylation or GTP hydrolysis, much of the information regarding the role of the ubiquitin system as a component of cell regulation and signaling cascades, was gained in studies of transformation and the control of cell growth. It seems, however, that ubiquitin-dependent proteolysis, and possibly other processes that are controlled by protein ubiquitination, play a role in many aspects of cellular function from the control of differentiation to intracellular trafficking [1,3,4]. Here we will review some of the results that implicate ubiquitin-dependent proteolysis in the control of cell growth and that indicate how perturbations of ubiquitin-dependent degradation of oncogene and tumor suppressor gene products may contribute to cell transformation and oncogenesis.
- Watkins JF, Sung P, Prakash L, Prakash S
- The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function.
- Mol Cell Biol. 1993; 13: 7757-65
- Display abstract
In eukaryotes, the posttranslational conjugation of ubiquitin to various cellular proteins marks them for degradation. Interestingly, several proteins have been reported to contain ubiquitin-like (ub-like) domains that are in fact specified by the DNA coding sequences of the proteins. The biological role of the ub-like domain in these proteins is not known; however, it has been proposed that this domain functions as a degradation signal rendering the proteins unstable. Here, we report that the product of the Saccharomyces cerevisiae RAD23 gene, which is involved in excision repair of UV-damaged DNA, bears a ub-like domain at its amino terminus. This finding has presented an opportunity to define the functional significance of this domain. We show that deletion of the ub-like domain impairs the DNA repair function of RAD23 and that this domain can be functionally substituted by the authentic ubiquitin sequence. Surprisingly, RAD23 is highly stable, and the studies reported herein indicate that its ub-like domain does not mediate protein degradation. Thus, in RAD23 at least, the ub-like domain affects protein function in a nonproteolytic manner.
- Ozkaynak E, Finley D, Solomon MJ, Varshavsky A
- The yeast ubiquitin genes: a family of natural gene fusions.
- EMBO J. 1987; 6: 1429-39
- Display abstract
Ubiquitin is a 76-residue protein highly conserved among eukaryotes. Conjugation of ubiquitin to intracellular proteins mediates their selective degradation in vivo. We describe a family of four ubiquitin-coding loci in the yeast Saccharomyces cerevisiae. UB11, UB12 and UB13 encode hybrid proteins in which ubiquitin is fused to unrelated ('tail') amino acid sequences. The ubiquitin coding elements of UB11 and UB12 are interrupted at identical positions by non-homologous introns. UB11 and UB12 encode identical 52-residue tails, whereas UB13 encodes a different 76-residue tail. The tail amino acid sequences are highly conserved between yeast and mammals. Each tail contains a putative metal-binding, nucleic acid-binding domain of the form Cys-X2-4-Cys-X2-15-Cys-X2-4-Cys, suggesting that these proteins may function by binding to DNA. The fourth gene, UB14, encodes a polyubiquitin precursor protein containing five ubiquitin repeats in a head-to-tail, spacerless arrangement. All four ubiquitin genes are expressed in exponentially growing cells, while in stationary-phase cells the expression of UB11 and UB12 is repressed. The UB14 gene, which is strongly inducible by starvation, high temperatures and other stresses, contains in its upstream region strong homologies to the consensus 'heat shock box' nucleotide sequence. Elsewhere we show that the essential function of the UB14 gene is to provide ubiquitin to cells under stress.
- Metabolism (metabolic pathways involving proteins which contain this domain)
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% proteins involved KEGG pathway ID Description 45.36 map03010 Ribosome 13.40 map05020 Parkinson's disease 13.40 map04120 Ubiquitin mediated proteolysis 11.34 map03320 PPAR signaling pathway 6.19 map05211 Renal cell carcinoma 5.15 map00380 Tryptophan metabolism 2.06 map01040 Biosynthesis of unsaturated fatty acids 1.03 map03022 Basal transcription factors 1.03 map00632 Benzoate degradation via CoA ligation 1.03 map00903 Limonene and pinene degradation
This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with UBQ domain which could be assigned to a KEGG orthologous group, and not all proteins containing UBQ domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.
- Structure (3D structures containing this domain)
3D Structures of UBQ domains in PDB
PDB code Main view Title 1a5r Structure determination of the small ubiquitin-related modifier sumo-1, nmr, 10 structures 1aar Structure of a diubiquitin conjugate and a model for interaction with ubiquitin conjugating enzyme (e2) 1bt0 Structure of ubiquitin-like protein, rub1 1c3t Rotamer strain as a determinant of protein structural specificity 1cmx Structural basis for the specificity of ubiquitin c- terminal hydrolases 1d3z Ubiquitin nmr structure 1euv X-ray structure of the c-terminal ulp1 protease domain in complex with smt3, the yeast ortholog of sumo. 1f9j Structure of a new crystal form of tetraubiquitin 1fxt Structure of a conjugating enzyme-ubiquitin thiolester complex 1g6j Structure of recombinant human ubiquitin in aot reverse micelles 1gjz Solution structure of a dimeric n-terminal fragment of human ubiquitin 1iyf Solution structure of ubiquitin-like domain of human parkin 1j8c Solution structure of the ubiquitin-like domain of hplic-2 1l2n Smt3 solution structure 1lm8 Structure of a hif-1a-pvhl-elonginb-elonginc complex 1lqb Crystal structure of a hydroxylated hif-1 alpha peptide bound to the pvhl/elongin-c/elongin-b complex 1m94 Solution structure of the yeast ubiquitin-like modifier protein hub1 1mg8 Nmr structure of ubiquitin-like domain in murine parkin 1nbf Crystal structure of a ubp-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde 1ndd Structure of nedd8 1ogw Synthetic ubiquitin with fluoro-leu at 50 and 67 1oqy Structure of the dna repair protein hhr23a 1otr Solution structure of a cue-ubiquitin complex 1p1a Nmr structure of ubiquitin-like domain of hhr23b 1p3q Mechanism of ubiquitin recognition by the cue domain of vps9 1p98 High-resolution nmr structure of the ubl-domain of hhr23a 1p9d High-resolution structure of the complex of hhr23a ubiquitin-like domain and the c-terminal ubiquitin- interacting motif of proteasome subunit s5a 1q0w Solution structure of vps27 amino-terminal uim-ubiquitin complex 1q5w Ubiquitin recognition by npl4 zinc-fingers 1qze Hhr23a protein structure based on residual dipolar coupling data 1r4m Appbp1-uba3-nedd8, an e1-ubiquitin-like protein complex 1r4n Appbp1-uba3-nedd8, an e1-ubiquitin-like protein complex with atp 1s1q Tsg101(uev) domain in complex with ubiquitin 1sif Crystal structure of a multiple hydrophobic core mutant of ubiquitin 1tbe Structure of tetraubiquitin shows how multiubiquitin chains can be formed 1tgz Structure of human senp2 in complex with sumo-1 1ttn Solution structure of the ubiquitin-like domain of human dc- ubp from dendritic cells 1u4a Solution structure of human sumo-3 c47s 1ubi Synthetic structural and biological studies of the ubiquitin system. part 1 1ubq Structure of ubiquitin refined at 1.8 angstroms resolution 1ud7 Solution structure of the designed hydrophobic core mutant of ubiquitin, 1d7 1uel Solution structure of ubiquitin-like domain of hhr23b complexed with ubiquitin-interacting motif of proteasome subunit s5a 1uzx A complex of the vps23 uev with ubiquitin 1v5o Solution structure of the ubiquitin-like domain from mouse hypothetical 1700011n24rik protein 1v5t Solution structure of the ubiquitin-like domain from mouse hypothetical 8430435i17rik protein 1v80 Solution structures of ubiquitin at 30 bar and 3 kbar 1v81 Solution structures of ubiquitin at 30 bar and 3 kbar 1v86 Solution structure of the ubiquitin domain from mouse d7wsu128e protein 1vcb The vhl-elonginc-elonginb structure 1we6 Solution structure of ubiquitin-like domain in splicing factor aal91182 1we7 Solution structure of ubiquitin-like domain in sf3a120 1wgd Solution structure of the ubl-domain of herp 1wgg Solution structure of the n-terminal ubiquitin-like domain of mouse ubiquitin specific protease 14 (usp14) 1wh3 Solution structure of c-terminal ubiquitin like domain of human 2'-5'-oligoadenylate synthetase-like protain (p59 oasl) 1wia Solution structure of mouse hypothetical ubiquitin-like protein bab25500 1wm2 Crystal structure of human sumo-2 protein 1wm3 Crystal structure of human sumo-2 protein 1wr1 The complex sturcture of dsk2p uba with ubiquitin 1wr6 Crystal structure of gga3 gat domain in complex with ubiquitin 1wrd Crystal structure of tom1 gat domain in complex with ubiquitin 1wx7 Solution structure of the n-terminal ubiquitin-like domain in the human ubiquilin 3 (ubqln3) 1wx8 Solution structure of the n-terminal ubiquitin-like domain in the 4931431f19rik protein 1wx9 Solution structure of the n-terminal ubiquitin-like domain in the human bat3 protein 1wxv Solution structure of the ubiquitin domain of bcl-2 binding athanogene-1 1wy8 Solution structure of the n-terminal ubiquitin-like domain in human np95/icbp90-like ring finger protein (nirf) 1wyw Crystal structure of sumo1-conjugated thymine dna glycosylase 1wz0 Solution structure of human sumo-2 (smt3b), a ubiquitin- like protein 1x1m Solution structure of the n-terminal ubiquitin-like domain in mouse ubiquitin-like protein sb132 1xd3 Crystal structure of uchl3-ubvme complex 1xqq Simultaneous determination of protein structure and dynamics 1xt9 Crystal structure of den1 in complex with nedd8 1y8r Sumo e1 activating enzyme sae1-sae2-sumo1-mg-atp complex 1yd8 Complex of human gga3 gat domain and ubiquitin 1yiw X-ray crystal structure of a chemically synthesized ubiquitin 1yj1 X-ray crystal structure of a chemically synthesized [d- gln35]ubiquitin 1yqb Human ubiquilin 3 1yx5 Solution structure of s5a uim-1/ubiquitin complex 1yx6 Solution structure of s5a uim-2/ubiquitin complex 1z2m Crystal structure of isg15, the interferon-induced ubiquitin cross reactive protein 1z5s Crystal structure of a complex between ubc9, sumo-1, rangap1 and nup358/ranbp2 1zgu Solution structure of the human mms2-ubiquitin complex 1zkh Solution structure of a human ubiquitin-like domain in sf3a1 1zw7 Elimination of the c-cap in ubiquitin structure, dynamics and thermodynamic consequences 2asq Solution structure of sumo-1 in complex with a sumo-binding motif (sbm) 2awt Solution structure of human small ubiquitin-like modifier protein isoform 2 (sumo-2) 2ayo Structure of usp14 bound to ubquitin aldehyde 2bf8 Crystal structure of sumo modified ubiquitin conjugating enzyme e2-25k 2bgf Nmr structure of lys48-linked di-ubiquitin using chemical shift perturbation data together with rdcs and 15n- relaxation data 2bkr Nedd8 nedp1 complex 2bwe The crystal structure of the complex between the uba and ubl domains of dsk2 2bwf Crystal sturcture of the ubl domain of dsk2 from s. cerevisiae 2c7m Human rabex-5 residues 1-74 in complex with ubiquitin 2c7n Human rabex-5 residues 1-74 in complex with ubiquitin 2c9w Crystal structure of socs-2 in complex with elongin-b and elongin-c at 1.9a resolution 2ckh Senp1-sumo2 complex 2d07 Crystal structure of sumo-3-modified thymine-dna glycosylase 2d3g Double sided ubiquitin binding of hrs-uim 2den Solution structure of the ubiquitin-associated domain of human bmsc-ubp and its complex with ubiquitin 2dx5 The complex structure between the mouse eap45-glue domain and ubiquitin 2dzi 2dzi/solution structure of the n-terminal ubiquitin-like domain in human ubiquitin-like protein 4a (gdx) 2eke Structure of a sumo-binding-motif mimic bound to smt3p- ubc9p: conservation of a noncovalent ubiquitin-like protein-e2 complex as a platform for selective interactions within a sumo pathway 2faz Ubiquitin-like domain of human nuclear zinc finger protein np95 2fcm X-ray crystal structure of a chemically synthesized [d- gln35]ubiquitin with a cubic space group 2fcn X-ray crystal structure of a chemically synthesized [d- val35]ubiquitin with a cubic space group 2fcq X-ray crystal structure of a chemically synthesized ubiquitin with a cubic space group 2fcs X-ray crystal structure of a chemically synthesized [l- gln35]ubiquitin with a cubic space group 2fid Crystal structure of a bovine rabex-5 fragment complexed with ubiquitin 2fif Crystal structure of a bovine rabex-5 fragment complexed with ubiquitin 2fnj Crystal structure of a b30.2/spry domain-containing protein gustavus in complex with elongin b and elongin c 2fuh Solution structure of the ubch5c/ub non-covalent complex 2g3q Solution structure of ede1 uba-ubiquitin complex 2g45 Co-crystal structure of znf ubp domain from the deubiquitinating enzyme isopeptidase t (isot) in complex with ubiquitin 2g4d Crystal structure of human senp1 mutant (c603s) in complex with sumo-1 2gbj Crystal structure of the 9-10 8 glycine insertion mutant of ubiquitin. 2gbk Crystal structure of the 9-10 moad insertion mutant of ubiquitin 2gbm Crystal structure of the 35-36 8 glycine insertion mutant of ubiquitin 2gbn Crystal structure of the 35-36 8 glycine insertion mutant of ubiquitin 2gbr Crystal structure of the 35-36 moad insertion mutant of ubiquitin 2gmi Mms2/ubc13~ubiquitin 2hd5 Usp2 in complex with ubiquitin 2hj8 Solution nmr structure of the c-terminal domain of the interferon alpha-inducible isg15 protein from homo sapiens. northeast structural genomics target hr2873b 2hth Structural basis for ubiquitin recognition by the human eap45/escrt-ii glue domain 2ibi Covalent ubiquitin-usp2 complex 2io0 Crystal structure of human senp2 in complex with presumo-2 2io1 Crystal structure of human senp2 in complex with presumo-3 2io2 Crystal structure of human senp2 in complex with rangap1- sumo-1 2io3 Crystal structure of human senp2 in complex with rangap1- sumo-2 2iy0 Senp1 (mutant) sumo1 rangap 2iy1 Senp1 (mutant) full length sumo1 2iyd Senp1 covalent complex with sumo-2 2izv Crystal structure of socs-4 in complex with elongin-b and elongin-c at 2.55a resolution 2j7q Crystal structure of the ubiquitin-specific protease encoded by murine cytomegalovirus tegument protein m48 in complex with a ubquitin-based suicide substrate 2jf5 Crystal structure of lys63-linked di-ubiquitin 2jri Solution structure of the josephin domain of ataxin-3 in complex with ubiquitin molecule. 2jt4 Solution structure of the sla1 sh3-3-ubiquitin complex 2jvc Nmr solution structure of ubiquitin like protein 2jwz Mutations in the hydrophobic core of ubiquitin differentially affect its recognition by receptor proteins 2jy6 Solution structure of the complex of ubiquitin and ubiquilin 1 uba domain 2jz3 Socs box elonginbc ternary complex 2jzz Solid-state nmr structure of microcrystalline ubiquitin 2k1f Sumo-3 from drosophila melanogaster (dsmt3) 2k25 Automated nmr structure of the ubb by fapsy 2k39 Recognition dynamics up to microseconds revealed from rdc derived ubiquitin ensemble in solution 2k6d Cin85 sh3-c domain in complex with ubiquitin 2k8b Solution structure of plaa family ubiquitin binding domain (pfuc) cis isomer in complex with ubiquitin 2k8c Solution structure of plaa family ubiquitin binding domain (pfuc) trans isomer in complex with ubiquitin 2k8h Solution structure of sumo from trypanosoma brucei 2kan Solution nmr structure of ubiquitin-like domain of arabidopsis thaliana protein at2g32350. northeast structural genomics consortium target ar3433a 2kd0 Nmr solution structure of o64736 protein from arabidopsis thaliana. northeast structural genomics consortium mega target ar3445a 2kde Nmr structure of major s5a (196-306):k48 linked diubiquitin species 2kdf Nmr structure of minor s5a (196-306):k48 linked diubiquitin species 2kk8 Nmr solution structure of a putative uncharacterized protein obtained from arabidopsis thaliana: northeast structural genomics consortium target ar3449a 2klc Nmr solution structure of human ubiquitin-like domain of ubiquilin 1, northeast structural genomics consortium (nesg) target ht5a 2klg Pere nmr structure of ubiquitin 2kn5 A correspondence between solution-state dynamics of an individual protein and the sequence and conformational diversity of its family 2ko3 Nedd8 solution structure 2nr2 The mumo (minimal under-restraining minimal over- restraining) method for the determination of native states ensembles of proteins 2nvu Structure of appbp1-uba3~nedd8-nedd8-mgatp-ubc12(c111a), a trapped ubiquitin-like protein activation complex 2o6v Crystal structure and solution nmr studies of lys48-linked tetraubiquitin at neutral ph 2ojr Structure of ubiquitin solved by sad using the lanthanide- binding tag 2oob Crystal structure of the uba domain from cbl-b ubiquitin ligase in complex with ubiquitin 2pe6 Non-covalent complex between human sumo-1 and human ubc9 2pe9 Nmr based structure of the open conformation of lys48- linked di-ubiquitin using experimental global rotational diffusion tensor from nmr relaxation measurements 2pea Nmr based structure of the closed conformation of lys48- linked di-ubiquitin using experimental global rotational diffusion tensor from nmr relaxation measurements 2qho Crystal structure of the uba domain from edd ubiquitin ligase in complex with ubiquitin 2rpq Solution structure of a sumo-interacting motif of mbd1- containing chromatin-associated factor 1 bound to sumo-3 2uyz Non-covalent complex between ubc9 and sumo1 2vrr Structure of sumo modified ubc9 2w9n Crystal structure of linear di-ubiquitin 2wwz Tab2 nzf domain in complex with lys63-linked di-ubiquitin, p212121 2wx0 Tab2 nzf domain in complex with lys63-linked di-ubiquitin, p21 2wx1 Tab2 nzf domain in complex with lys63-linked tri-ubiquitin, p212121 2z59 Complex structures of mouse rpn13 (22-130aa) and ubiquitin 2zcb Crystal structure of ubiquitin p37a/p38a 2zcc Ubiquitin crystallized under high pressure 2zeq Crystal structure of ubiquitin-like domain of murine parkin 2znv Crystal structure of human amsh-lp dub domain in complex with lys63-linked ubiquitin dimer 2zvn Nemo cozi domain incomplex with diubiquitin in p212121 space group 2zvo Nemo cozi domain in complex with diubiquitin in c2 space group 3a1q Crystal structure of the mouse rap80 uims in complex with lys63-linked di-ubiquitin 3a33 Ubiquitin related protein 3by4 Structure of ovarian tumor (otu) domain in complex with ubiquitin 3c0r Structure of ovarian tumor (otu) domain in complex with ubiquitin 3cmm Crystal structure of the uba1-ubiquitin complex 3dbh Structural dissection of a gating mechanism preventing misactivation of ubiquitin by nedd8's e1 (appbp1- uba3arg190ala-nedd8ala72arg) 3dbl Structural dissection of a gating mechanism preventing misactivation of ubiquitin by nedd8's e1 (appbp1- uba3arg190wt-nedd8ala72gln) 3dbr Structural dissection of a gating mechanism preventing misactivation of ubiquitin by nedd8's e1 (appbp1- uba3arg190gln-nedd8ala72arg) 3dcg Crystal structure of the hiv vif bc-box in complex with human elonginb and elonginc 3dqv Structural insights into nedd8 activation of cullin-ring ligases: conformational control of conjugation 3dvg Crystal structure of k63-specific fab apu.3a8 bound to k63- linked di-ubiquitin 3dvn Crystal structure of k63-specific fab apu2.16 bound to k63- linked di-ubiquitin 3eec X-ray structure of human ubiquitin cd(ii) adduct 3efu X-ray structure of human ubiquitin-hg(ii) adduct 3ehv X-ray structure of human ubiquitin zn(ii) adduct 3h1u Structure of ubiquitin in complex with cd ions 3h7p Crystal structure of k63-linked di-ubiquitin 3h7s Crystal structures of k63-linked di- and tri-ubiquitin reveal a highly extended chain architecture 3hm3 The structure and conformation of lys-63 linked tetra- ubiquitin 3i3t Crystal structure of covalent ubiquitin-usp21 complex 3ix6 Crystal structure of thymidylate synthase thya from brucella melitensis 3jsv Crystal structure of mouse nemo cozi in complex with lys63- linked di-ubiquitin
- Links (links to other resources describing this domain)
BLOCKS UBIQUITIN_1 PFAM ubiquitin INTERPRO IPR000626 PROSITE UBQ_DOMAIN