Ubiquitin C

1C3T, 1CMX, 1D3Z, 1F9J, 1FXT, 1G6J, 1GJZ, 1NBF, 1OGW, 1Q5W, 1S1Q, 1SIF, 1TBE, 1UBI, 1UBQ, 1UD7, 1XD3, 1XQQ, 1YX5, 1YX6, 1ZGU, 2AYO, 2BGF, 2DEN, 2FUH, 2G45, 2GBJ, 2GBK, 2GBM, 2GBN, 2GBR, 2GMI, 2HTH, 2IBI, 2J7Q, 2JF5, 2JRI, 2JY6, 2JZZ, 2K25, 2K6D, 2K8B, 2K8C, 2KDF, 2KJH, 2KLG, 2KN5, 2KX0, 2L3Z, 2LD9, 2LVO, 2LVP, 2LVQ, 2LZ6, 2MBO, 2MBQ, 2MCN, 2MI8, 2MJ5, 2MOR, 2MRE, 2MWS, 2N2K, 2NR2, 2O6V, 2OJR, 2PE9, 2PEA, 2RR9, 2RU6, 2W9N, 2WDT, 2XEW, 2Z59, 2ZCB, 2ZVN, 2ZVO, 3A33, 3ALB, 3AUL, 3B08, 3B0A, 3BY4, 3C0R, 3DVG, 3DVN, 3EEC, 3EFU, 3EHV, 3H7P, 3H7S, 3HM3, 3IFW, 3IHP, 3JSV, 3JVZ, 3JW0, 3K9O, 3K9P, 3KVF, 3KW5, 3LDZ, 3MHS, 3MTN, 3N30, 3N32, 3N3K, 3NS8, 3O65, 3OFI, 3OJ4, 3ONS, 3PRM, 3PT2, 3PTF, 3Q3F, 3RUL, 3TMP, 3U30, 3UGB, 3V6C, 3V6E, 3VFK, 3VUW, 3VUX, 3VUY, 3WXE, 3WXF, 3ZNI, 3ZNZ, 4AUQ, 4BOS, 4BOZ, 4BVU, 4DDG, 4DDI, 4DHJ, 4DHZ, 4FJV, 4HK2, 4HXD, 4I6L, 4I6N, 4IG7, 4IUM, 4JQW, 4K1R, 4K7S, 4K7U, 4K7W, 4KSK, 4KSL, 4LCD, 4LDT, 4MDK, 4MM3, 4MSM, 4MSQ, 4NQK, 4UN2, 4V3K, 4V3L, 5AIU, 4XOK, 5AF6, 5AF5, 5AF4, 4XOL, 5C7J, 5C7M, 5E6J, 4ZQS, 4AP4,%%s4AP4731622190ENSG00000150991ENSMUSG00000008348P0CG48P0CG50NM_021009NM_019639NP_066289NP_062613Polyubiquitin-C is a protein encoded by the UBC gene in humans. Polyubiquitin-C is one of the sources of ubiquitin, along with UBB, UBA52, and RPS27A.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 HYDROLASES1d3z: UBIQUITIN NMR STRUCTURE1f9j: STRUCTURE OF A NEW CRYSTAL FORM OF TETRAUBIQUITIN1fxt: STRUCTURE OF A CONJUGATING ENZYME-UBIQUITIN THIOLESTER COMPLEX1g6j: STRUCTURE OF RECOMBINANT HUMAN UBIQUITIN IN AOT REVERSE MICELLES1gjz: SOLUTION STRUCTURE OF A DIMERIC N-TERMINAL FRAGMENT OF HUMAN UBIQUITIN1nbf: Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde1ogw: SYNTHETIC UBIQUITIN WITH FLUORO-LEU AT 50 AND 671otr: Solution Structure of a CUE-Ubiquitin Complex1p3q: Mechanism of Ubiquitin Recognition by the CUE Domain of VPS91q0w: Solution structure of Vps27 amino-terminal UIM-ubiquitin complex1q5w: Ubiquitin Recognition by Npl4 Zinc-Fingers1s1q: TSG101(UEV) domain in complex with Ubiquitin1sif: Crystal structure of a multiple hydrophobic core mutant of ubiquitin1tbe: STRUCTURE OF TETRAUBIQUITIN SHOWS HOW MULTIUBIQUITIN CHAINS CAN BE FORMED1ubi: SYNTHETIC STRUCTURAL AND BIOLOGICAL STUDIES OF THE UBIQUITIN SYSTEM. PART 11ubq: STRUCTURE OF UBIQUITIN REFINED AT 1.8 ANGSTROMS RESOLUTION1ud7: SOLUTION STRUCTURE OF THE DESIGNED HYDROPHOBIC CORE MUTANT OF UBIQUITIN, 1D71uzx: A COMPLEX OF THE VPS23 UEV WITH UBIQUITIN1v80: Solution structures of ubiquitin at 30 bar and 3 kbar1v81: Solution structures of ubiquitin at 30 bar and 3 kbar1wr1: The complex structure of Dsk2p UBA with ubiquitin1wr6: Crystal structure of GGA3 GAT domain in complex with ubiquitin1wrd: Crystal structure of Tom1 GAT domain in complex with ubiquitin1xd3: Crystal structure of UCHL3-UbVME complex1xqq: Simultaneous determination of protein structure and dynamics1yd8: COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN1yiw: X-ray Crystal Structure of a Chemically Synthesized Ubiquitin1yj1: X-ray Crystal Structure of a Chemically Synthesized Ubiquitin1yx5: Solution Structure of S5a UIM-1/Ubiquitin Complex1yx6: Solution Structure of S5a UIM-2/Ubiquitin Complex1zgu: Solution structure of the human Mms2-Ubiquitin complex2ayo: Structure of USP14 bound to ubquitin aldehyde2bgf: NMR STRUCTURE OF LYS48-LINKED DI-UBIQUITIN USING CHEMICAL SHIFT PERTURBATION DATA TOGETHER WITH RDCS AND 15N-RELAXATION DATA2c7m: HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN2c7n: HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN2d3g: Double sided ubiquitin binding of Hrs-UIM2den: Solution Structure of the Ubiquitin-Associated Domain of Human BMSC-UbP and its Complex with Ubiquitin2dx5: The complex structure between the mouse EAP45-GLUE domain and ubiquitin2fcm: X-ray Crystal Structure of a Chemically Synthesized Ubiquitin with a Cubic Space Group2fcn: X-ray Crystal Structure of a Chemically Synthesized Ubiquitin with a Cubic Space Group2fcq: X-ray Crystal Structure of a Chemically Synthesized Ubiquitin with a Cubic Space Group2fcs: X-ray Crystal Structure of a Chemically Synthesized Ubiquitin with a Cubic Space Group2fid: Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin2fif: Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin2fuh: Solution Structure of the UbcH5c/Ub Non-covalent Complex2g3q: Solution Structure of Ede1 UBA-ubiquitin complex2g45: Co-crystal structure of znf ubp domain from the deubiquitinating enzyme isopeptidase T (isot) in complex with ubiquitin2gbj: Crystal Structure of the 9-10 8 Glycine Insertion Mutant of Ubiquitin.2gbk: Crystal Structure of the 9-10 MoaD Insertion Mutant of Ubiquitin2gbm: Crystal Structure of the 35-36 8 Glycine Insertion Mutant of Ubiquitin2gbn: Crystal Structure of the 35-36 8 Glycine Insertion Mutant of Ubiquitin2gbr: Crystal Structure of the 35-36 MoaD Insertion Mutant of Ubiquitin2gmi: Mms2/Ubc13~Ubiquitin2hd5: USP2 in complex with ubiquitin2hth: Structural basis for ubiquitin recognition by the human EAP45/ESCRT-II GLUE domain2ibi: Covalent Ubiquitin-USP2 Complex2j7q: CRYSTAL STRUCTURE OF THE UBIQUITIN-SPECIFIC PROTEASE ENCODED BY MURINE CYTOMEGALOVIRUS TEGUMENT PROTEIN M48 IN COMPLEX WITH A UBQUITIN-BASED SUICIDE SUBSTRATE2nr2: The MUMO (minimal under-restraining minimal over-restraining) method for the determination of native states ensembles of proteins2o6v: Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH2oob: crystal structure of the UBA domain from Cbl-b ubiquitin ligase in complex with ubiquitin Polyubiquitin-C is a protein encoded by the UBC gene in humans. Polyubiquitin-C is one of the sources of ubiquitin, along with UBB, UBA52, and RPS27A. UBC gene is one of the two stress-regulated polyubiquitin genes (UBB and UBC) in mammals. It plays a key role in maintaining cellular ubiquitin levels under stress conditions. Defects of UBC gene could lead to mid-gestation embryonic lethality. UBC gene is located at chromosome 12q24.3, consisting of 2 exons. The promoter of the UBC gene contains putative heat shock elements (HSEs), which mediates UBC induction upon stress. UBC gene differs from UBB gene in the number of Ub coding units they contain. Nine to ten Ub units were in the UBC gene. In polyubiquitin-C, the C-terminus of a given ubiquitin molecule is covalently conjugated to either the N-terminal residue or one of seven lysine residues of another ubiquitin molecule. Different linking of ubiquitin chains results in distinct conformations. There are 8 linkage types of polyubiquitin-C, and each type possesses the linkage-dependent dynamics and a linkage-specific conformation. The diversity of polyubiquitin-C means that ubiquitylation contributes to the regulation of many cellular events. Polyubiquitin-C doesn’t activate the heat-shock response, but it plays a key role in sustaining the response. UBC gene transcription is induced during stress and provides extra ubiquitin necessary to remove damaged/unfolded proteins. Polyubiquitin-C has important role in diverse biological processes, such as innate immunity, DNA repair and kinase activity. Unanchored polyubiquitin-C are also key signaling molecules that connect and coordinate the proteasome and autophagy to eliminate toxic protein aggregates. Loss of a single UBC allele has no apparent phenotype, while homozygous deletion of UBC gene leads to mid-gestation embryonic lethality due to a defect in fetal liver development, as well as a delay in cell-cycle progression and increased susceptibility to cellular stress. It is also reported that homozygous deletion of UBC gene in mouse embryonic fibroblasts will cause decreased cellular Ub level and reduced viability under oxidative stress. Polyubiquitin-C has been shown to interact with: