Ubiquitin A-52 residue ribosomal protein fusion product 1

Human protein
UBA52
Available structures
PDBHuman UniProt search: PDBe RCSB
List of PDB id codes

2LJ5, 2MBH, 2MJB, 2MUR, 2RSU, 4HJK, 4JIO, 4P4H, 4PIG, 4PIH, 4PIJ, 4RF0, 4RF1, 4S1Z, 4UG0, 4V6X, 5AJ0, 4UJD, 4D67, 4UJC, 3J7P, 3J7Q, 4XKL, 3J92, 4D5Y, 3J7O, 3J7R, 3PHD, 2KOX, 4UJE, 5A5B, 2N3V, 2N3U, 2N3W, 2NBD, 2NBE, 3VDZ, 5HPS, 3I3T, 5HPT, 5JBV, 5HPL, 5HPK, 5J8P

Identifiers
AliasesUBA52, CEP52, HUBCEP52, L40, RPL40, Ubiquitin A-52 residue ribosomal protein fusion product 1
External IDsOMIM: 191321; MGI: 3644625; HomoloGene: 68307; GeneCards: UBA52; OMA:UBA52 - orthologs
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for UBA52
Genomic location for UBA52
Band19p13.11Start18,571,730 bp[1]
End18,577,550 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • blood

  • right testis

  • left testis

  • granulocyte

  • sperm

  • stromal cell of endometrium

  • lymph node

  • left ovary

  • mononuclear cell

  • monocyte
    n/a
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • structural constituent of ribosome
  • protein binding
  • protein tag
  • ubiquitin protein ligase binding
Cellular component
  • cytoplasm
  • endocytic vesicle membrane
  • nucleus
  • ribosome
  • extracellular exosome
  • endosome membrane
  • lysosomal membrane
  • extracellular space
  • nucleoplasm
  • mitochondrial outer membrane
  • endoplasmic reticulum
  • cytosol
  • plasma membrane
  • endoplasmic reticulum quality control compartment
  • vesicle
  • endoplasmic reticulum membrane
  • host cell
  • cytosolic large ribosomal subunit
  • cytosolic small ribosomal subunit
  • synapse
Biological process
  • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest
  • negative regulation of epidermal growth factor receptor signaling pathway
  • interstrand cross-link repair
  • nucleotide-excision repair, DNA damage recognition
  • positive regulation of canonical Wnt signaling pathway
  • tumor necrosis factor-mediated signaling pathway
  • regulation of type I interferon production
  • TRIF-dependent toll-like receptor signaling pathway
  • Fc-epsilon receptor signaling pathway
  • endosomal transport
  • global genome nucleotide-excision repair
  • NIK/NF-kappaB signaling
  • G2/M transition of mitotic cell cycle
  • stress-activated MAPK cascade
  • transforming growth factor beta receptor signaling pathway
  • macroautophagy
  • negative regulation of canonical Wnt signaling pathway
  • nucleotide-excision repair, DNA gap filling
  • viral transcription
  • error-free translesion synthesis
  • regulation of tumor necrosis factor-mediated signaling pathway
  • stimulatory C-type lectin receptor signaling pathway
  • negative regulation of transforming growth factor beta receptor signaling pathway
  • SRP-dependent cotranslational protein targeting to membrane
  • JNK cascade
  • regulation of transcription from RNA polymerase II promoter in response to hypoxia
  • nucleotide-excision repair, DNA incision
  • I-kappaB kinase/NF-kappaB signaling
  • innate immune response
  • Notch signaling pathway
  • regulation of mRNA stability
  • protein polyubiquitination
  • negative regulation of apoptotic process
  • negative regulation of transcription by RNA polymerase II
  • virion assembly
  • positive regulation of NF-kappaB transcription factor activity
  • anaphase-promoting complex-dependent catabolic process
  • negative regulation of type I interferon production
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
  • nucleotide-binding oligomerization domain containing signaling pathway
  • intracellular transport of virus
  • viral life cycle
  • MyD88-dependent toll-like receptor signaling pathway
  • error-prone translesion synthesis
  • MAPK cascade
  • fibroblast growth factor receptor signaling pathway
  • ion transmembrane transport
  • glycogen biosynthetic process
  • positive regulation of apoptotic process
  • translational initiation
  • positive regulation of I-kappaB kinase/NF-kappaB signaling
  • translesion synthesis
  • transcription-coupled nucleotide-excision repair
  • T cell receptor signaling pathway
  • MyD88-independent toll-like receptor signaling pathway
  • positive regulation of transcription by RNA polymerase II
  • positive regulation of epidermal growth factor receptor signaling pathway
  • proteasome-mediated ubiquitin-dependent protein catabolic process
  • regulation of signal transduction by p53 class mediator
  • Wnt signaling pathway, planar cell polarity pathway
  • nucleotide-excision repair, DNA incision, 5'-to lesion
  • protein biosynthesis
  • nucleotide-excision repair, preincision complex assembly
  • rRNA processing
  • Wnt signaling pathway
  • ERBB2 signaling pathway
  • nucleotide-excision repair, DNA duplex unwinding
  • protein folding
  • negative regulation of G2/M transition of mitotic cell cycle
  • protein ubiquitination
  • protein deubiquitination
  • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process
  • entry of bacterium into host cell
  • transmembrane transport
  • regulation of necroptotic process
  • membrane organization
  • endoplasmic reticulum mannose trimming
  • cellular iron ion homeostasis
  • regulation of hematopoietic stem cell differentiation
  • protein targeting to peroxisome
  • cytokine-mediated signaling pathway
  • modification-dependent protein catabolic process
  • interleukin-1-mediated signaling pathway
  • response to insecticide
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7311

665964

Ensembl

ENSG00000221983

n/a

UniProt

P62987

n/a

RefSeq (mRNA)
NM_001033930
NM_003333
NM_001321017
NM_001321018
NM_001321019

NM_001321020
NM_001321021
NM_001321022

n/a

RefSeq (protein)
NP_001029102
NP_001307946
NP_001307947
NP_001307948
NP_001307949

NP_001307950
NP_001307951
NP_003324

n/a

Location (UCSC)Chr 19: 18.57 – 18.58 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

60S ribosomal protein L40 (RPL40) is a protein that in humans is encoded by the UBA52 gene.[4][5]

Function

Ubiquitin is a highly conserved nuclear and cytoplasmic protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome. It is also involved in the maintenance of chromatin structure, the regulation of gene expression, and the stress response. Ubiquitin is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin moiety fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the N-terminus and ribosomal protein L40 at the C-terminus, a C-terminal extension protein (CEP). Multiple processed pseudogenes derived from this gene are present in the genome.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000221983 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Webb GC, Baker RT, Coggan M, Board PG (Jun 1994). "Localization of the human UBA52 ubiquitin fusion gene to chromosome band 19p13.1-p12". Genomics. 19 (3): 567–9. doi:10.1006/geno.1994.1108. PMID 8188300.
  5. ^ a b "Entrez Gene: UBA52 ubiquitin A-52 residue ribosomal protein fusion product 1".

Further reading

  • Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochem. Cell Biol. 73 (11–12): 933–47. doi:10.1139/o95-101. PMID 8722009.
  • Murphey RK, Godenschwege TA (2002). "New roles for ubiquitin in the assembly and function of neuronal circuits". Neuron. 36 (1): 5–8. doi:10.1016/S0896-6273(02)00943-1. PMID 12367500. S2CID 15764136.
  • Baker RT, Board PG (1992). "The human ubiquitin/52-residue ribosomal protein fusion gene subfamily (UbA52) is composed primarily of processed pseudogenes". Genomics. 14 (2): 520–2. doi:10.1016/S0888-7543(05)80258-7. PMID 1330885.
  • Baker RT, Board PG (1991). "The human ubiquitin-52 amino acid fusion protein gene shares several structural features with mammalian ribosomal protein genes". Nucleic Acids Res. 19 (5): 1035–40. doi:10.1093/nar/19.5.1035. PMC 333777. PMID 1850507.
  • Monia BP, Ecker DJ, Jonnalagadda S, et al. (1989). "Gene synthesis, expression, and processing of human ubiquitin carboxyl extension proteins". J. Biol. Chem. 264 (7): 4093–103. doi:10.1016/S0021-9258(19)84967-0. PMID 2537304.
  • Lund PK, Moats-Staats BM, Simmons JG, et al. (1985). "Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor". J. Biol. Chem. 260 (12): 7609–13. doi:10.1016/S0021-9258(17)39652-7. PMID 2581967.
  • Salvesen G, Lloyd C, Farley D (1987). "cDNA encoding a human homolog of yeast ubiquitin 1". Nucleic Acids Res. 15 (13): 5485. doi:10.1093/nar/15.13.5485. PMC 305980. PMID 3037496.
  • Cross SH, Charlton JA, Nan X, Bird AP (1994). "Purification of CpG islands using a methylated DNA binding column". Nat. Genet. 6 (3): 236–44. doi:10.1038/ng0394-236. PMID 8012384. S2CID 12847618.
  • Cook WJ, Jeffrey LC, Kasperek E, Pickart CM (1994). "Structure of tetraubiquitin shows how multiubiquitin chains can be formed". J. Mol. Biol. 236 (2): 601–9. doi:10.1006/jmbi.1994.1169. PMID 8107144.
  • Vadlamudi RK, Joung I, Strominger JL, Shin J (1996). "p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins". J. Biol. Chem. 271 (34): 20235–7. doi:10.1074/jbc.271.34.20235. PMID 8702753.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Kenmochi N, Kawaguchi T, Rozen S, et al. (1998). "A map of 75 human ribosomal protein genes". Genome Res. 8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID 9582194.
  • Cruz C, Ventura F, Bartrons R, Rosa JL (2001). "HERC3 binding to and regulation by ubiquitin". FEBS Lett. 488 (1–2): 74–80. doi:10.1016/S0014-5793(00)02371-1. PMID 11163799. S2CID 20091003.
  • Lee TA, Tyers M (2002). "Ubiquitin junction, what's your function?". Genome Biol. 2 (10): REPORTS4025. doi:10.1186/gb-2001-2-10-reports4025. PMC 138970. PMID 11597332.
  • Yoshihama M, Uechi T, Asakawa S, et al. (2002). "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes". Genome Res. 12 (3): 379–90. doi:10.1101/gr.214202. PMC 155282. PMID 11875025.
  • Bishop N, Horman A, Woodman P (2002). "Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates". J. Cell Biol. 157 (1): 91–101. doi:10.1083/jcb.200112080. PMC 2173266. PMID 11916981.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • v
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  • 1aar: STRUCTURE OF A DIUBIQUITIN CONJUGATE AND A MODEL FOR INTERACTION WITH UBIQUITIN CONJUGATING ENZYME (E2)
    1aar: STRUCTURE OF A DIUBIQUITIN CONJUGATE AND A MODEL FOR INTERACTION WITH UBIQUITIN CONJUGATING ENZYME (E2)
  • 1cmx: STRUCTURAL BASIS FOR THE SPECIFICITY OF UBIQUITIN C-TERMINAL HYDROLASES
    1cmx: STRUCTURAL BASIS FOR THE SPECIFICITY OF UBIQUITIN C-TERMINAL HYDROLASES
  • 1d3z: UBIQUITIN NMR STRUCTURE
    1d3z: UBIQUITIN NMR STRUCTURE
  • 1f9j: STRUCTURE OF A NEW CRYSTAL FORM OF TETRAUBIQUITIN
    1f9j: STRUCTURE OF A NEW CRYSTAL FORM OF TETRAUBIQUITIN
  • 1fxt: STRUCTURE OF A CONJUGATING ENZYME-UBIQUITIN THIOLESTER COMPLEX
    1fxt: STRUCTURE OF A CONJUGATING ENZYME-UBIQUITIN THIOLESTER COMPLEX
  • 1g6j: STRUCTURE OF RECOMBINANT HUMAN UBIQUITIN IN AOT REVERSE MICELLES
    1g6j: STRUCTURE OF RECOMBINANT HUMAN UBIQUITIN IN AOT REVERSE MICELLES
  • 1gjz: SOLUTION STRUCTURE OF A DIMERIC N-TERMINAL FRAGMENT OF HUMAN UBIQUITIN
    1gjz: SOLUTION STRUCTURE OF A DIMERIC N-TERMINAL FRAGMENT OF HUMAN UBIQUITIN
  • 1nbf: Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    1nbf: Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
  • 1ogw: SYNTHETIC UBIQUITIN WITH FLUORO-LEU AT 50 AND 67
    1ogw: SYNTHETIC UBIQUITIN WITH FLUORO-LEU AT 50 AND 67
  • 1otr: Solution Structure of a CUE-Ubiquitin Complex
    1otr: Solution Structure of a CUE-Ubiquitin Complex
  • 1p3q: Mechanism of Ubiquitin Recognition by the CUE Domain of VPS9
    1p3q: Mechanism of Ubiquitin Recognition by the CUE Domain of VPS9
  • 1q0w: Solution structure of Vps27 amino-terminal UIM-ubiquitin complex
    1q0w: Solution structure of Vps27 amino-terminal UIM-ubiquitin complex
  • 1q5w: Ubiquitin Recognition by Npl4 Zinc-Fingers
    1q5w: Ubiquitin Recognition by Npl4 Zinc-Fingers
  • 1s1q: TSG101(UEV) domain in complex with Ubiquitin
    1s1q: TSG101(UEV) domain in complex with Ubiquitin
  • 1sif: Crystal structure of a multiple hydrophobic core mutant of ubiquitin
    1sif: Crystal structure of a multiple hydrophobic core mutant of ubiquitin
  • 1tbe: STRUCTURE OF TETRAUBIQUITIN SHOWS HOW MULTIUBIQUITIN CHAINS CAN BE FORMED
    1tbe: STRUCTURE OF TETRAUBIQUITIN SHOWS HOW MULTIUBIQUITIN CHAINS CAN BE FORMED
  • 1ubi: SYNTHETIC STRUCTURAL AND BIOLOGICAL STUDIES OF THE UBIQUITIN SYSTEM. PART 1
    1ubi: SYNTHETIC STRUCTURAL AND BIOLOGICAL STUDIES OF THE UBIQUITIN SYSTEM. PART 1
  • 1ubq: STRUCTURE OF UBIQUITIN REFINED AT 1.8 ANGSTROMS RESOLUTION
    1ubq: STRUCTURE OF UBIQUITIN REFINED AT 1.8 ANGSTROMS RESOLUTION
  • 1ud7: SOLUTION STRUCTURE OF THE DESIGNED HYDROPHOBIC CORE MUTANT OF UBIQUITIN, 1D7
    1ud7: SOLUTION STRUCTURE OF THE DESIGNED HYDROPHOBIC CORE MUTANT OF UBIQUITIN, 1D7
  • 1uzx: A COMPLEX OF THE VPS23 UEV WITH UBIQUITIN
    1uzx: A COMPLEX OF THE VPS23 UEV WITH UBIQUITIN
  • 1v80: Solution structures of ubiquitin at 30 bar and 3 kbar
    1v80: Solution structures of ubiquitin at 30 bar and 3 kbar
  • 1v81: Solution structures of ubiquitin at 30 bar and 3 kbar
    1v81: Solution structures of ubiquitin at 30 bar and 3 kbar
  • 1wr1: The complex structure of Dsk2p UBA with ubiquitin
    1wr1: The complex structure of Dsk2p UBA with ubiquitin
  • 1wr6: Crystal structure of GGA3 GAT domain in complex with ubiquitin
    1wr6: Crystal structure of GGA3 GAT domain in complex with ubiquitin
  • 1wrd: Crystal structure of Tom1 GAT domain in complex with ubiquitin
    1wrd: Crystal structure of Tom1 GAT domain in complex with ubiquitin
  • 1xd3: Crystal structure of UCHL3-UbVME complex
    1xd3: Crystal structure of UCHL3-UbVME complex
  • 1xqq: Simultaneous determination of protein structure and dynamics
    1xqq: Simultaneous determination of protein structure and dynamics
  • 1yd8: COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN
    1yd8: COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN
  • 1yiw: X-ray Crystal Structure of a Chemically Synthesized Ubiquitin
    1yiw: X-ray Crystal Structure of a Chemically Synthesized Ubiquitin
  • 1yj1: X-ray Crystal Structure of a Chemically Synthesized [D-Gln35]Ubiquitin
    1yj1: X-ray Crystal Structure of a Chemically Synthesized [D-Gln35]Ubiquitin
  • 1yx5: Solution Structure of S5a UIM-1/Ubiquitin Complex
    1yx5: Solution Structure of S5a UIM-1/Ubiquitin Complex
  • 1yx6: Solution Structure of S5a UIM-2/Ubiquitin Complex
    1yx6: Solution Structure of S5a UIM-2/Ubiquitin Complex
  • 1zgu: Solution structure of the human Mms2-Ubiquitin complex
    1zgu: Solution structure of the human Mms2-Ubiquitin complex
  • 2ayo: Structure of USP14 bound to ubquitin aldehyde
    2ayo: Structure of USP14 bound to ubquitin aldehyde
  • 2bgf: NMR STRUCTURE OF LYS48-LINKED DI-UBIQUITIN USING CHEMICAL SHIFT PERTURBATION DATA TOGETHER WITH RDCS AND 15N-RELAXATION DATA
    2bgf: NMR STRUCTURE OF LYS48-LINKED DI-UBIQUITIN USING CHEMICAL SHIFT PERTURBATION DATA TOGETHER WITH RDCS AND 15N-RELAXATION DATA
  • 2c7m: HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN
    2c7m: HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN
  • 2c7n: HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN
    2c7n: HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN
  • 2d3g: Double sided ubiquitin binding of Hrs-UIM
    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
    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
    2dx5: The complex structure between the mouse EAP45-GLUE domain and ubiquitin
  • 2fcm: X-ray Crystal Structure of a Chemically Synthesized [D-Gln35]Ubiquitin with a Cubic Space Group
    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
    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
    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
    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
    2fid: Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin
  • 2fif: Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin
    2fif: Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin
  • 2fuh: Solution Structure of the UbcH5c/Ub Non-covalent Complex
    2fuh: Solution Structure of the UbcH5c/Ub Non-covalent Complex
  • 2g3q: Solution Structure of Ede1 UBA-ubiquitin 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
    2g45: Co-crystal structure of znf ubp domain from the deubiquitinating enzyme isopeptidase T (isot) in complex with ubiquitin
  • 2gbj: Crystal Structure of the 9-10 8 Glycine Insertion Mutant of Ubiquitin.
    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
    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
    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
    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
    2gbr: Crystal Structure of the 35-36 MoaD Insertion Mutant of Ubiquitin
  • 2gmi: Mms2/Ubc13~Ubiquitin
    2gmi: Mms2/Ubc13~Ubiquitin
  • 2hd5: USP2 in complex with ubiquitin
    2hd5: USP2 in complex with ubiquitin
  • 2hth: Structural basis for ubiquitin recognition by the human EAP45/ESCRT-II GLUE domain
    2hth: Structural basis for ubiquitin recognition by the human EAP45/ESCRT-II GLUE domain
  • 2ibi: Covalent Ubiquitin-USP2 Complex
    2ibi: Covalent Ubiquitin-USP2 Complex
  • 2j7q: CRYSTAL STRUCTURE OF THE UBIQUITIN-SPECIFIC PROTEASE ENCODED BY MURINE CYTOMEGALOVIRUS TEGUMENT PROTEIN M48 IN COMPLEX WITH A UBQUITIN-BASED SUICIDE SUBSTRATE
    2j7q: CRYSTAL STRUCTURE OF THE UBIQUITIN-SPECIFIC PROTEASE ENCODED BY MURINE CYTOMEGALOVIRUS TEGUMENT PROTEIN M48 IN COMPLEX WITH A UBQUITIN-BASED SUICIDE SUBSTRATE
  • 2nr2: The MUMO (minimal under-restraining minimal over-restraining) method for the determination of native states ensembles of proteins
    2nr2: The MUMO (minimal under-restraining minimal over-restraining) method for the determination of native states ensembles of proteins
  • 2o6v: Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH
    2o6v: Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH
  • 2oob: crystal structure of the UBA domain from Cbl-b ubiquitin ligase in complex with ubiquitin
    2oob: crystal structure of the UBA domain from Cbl-b ubiquitin ligase in complex with ubiquitin


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