SMART: UBQ domain annotation

UBQ Ubiquitin homologues

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)
Family alignment:	View or

There are 5702 UBQ domains in 4266 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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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)

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

BLOCKS	UBIQUITIN_1
PFAM	ubiquitin
INTERPRO	IPR000626
PROSITE	UBQ_DOMAIN