Ubiquitin C

PDB rendering based on 1aar.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes

1C3T, 1CMX, 1D3Z, 1F9J, 1FXT, 1G6J, 1GJZ, 1NBF, 1OGW, 1Q5W, 1S1Q, 1SIF, 1TBE, 1UBI, 1UBQ, 1UD7, 1XD3, 1XQQ, 1YX5, 1YX6, 1ZGU, 1ZO6, 2AYO, 2BGF, 2DEN, 2FUH, 2G45, 2GBJ, 2GBK, 2GBM, 2GBN, 2GBR, 2GMI, 2HTH, 2IBI, 2J7Q, 2JF5, 2JRI, 2JY6, 2JZZ, 2K25, 2K6D, 2K8B, 2K8C, 2KDF, 2KHW, 2KJH, 2KLG, 2KN5, 2KX0, 2L3Z, 2LD9, 2LVO, 2LVP, 2LVQ, 2LZ6, 2MBO, 2MBQ, 2MCN, 2MI8, 2MJ5, 2NR2, 2O6V, 2OJR, 2PE9, 2PEA, 2RR9, 2RU6, 2W9N, 2WDT, 2XEW, 2Y5B, 2Z59, 2ZCB, 2ZVN, 2ZVO, 3A33, 3ALB, 3AUL, 3B08, 3B0A, 3BY4, 3C0R, 3DVG, 3DVN, 3EEC, 3EFU, 3EHV, 3H7P, 3H7S, 3HM3, 3I3T, 3IFW, 3IHP, 3JSV, 3JVZ, 3JW0, 3K9O, 3K9P, 3KVF, 3KW5, 3LDZ, 3MHS, 3MTN, 3N30, 3N32, 3N3K, 3NS8, 3O65, 3OFI, 3OJ3, 3OJ4, 3ONS, 3PRM, 3PT2, 3PTF, 3Q3F, 3RUL, 3TMP, 3U30, 3UGB, 3V6C, 3V6E, 3VFK, 3VUW, 3VUX, 3VUY, 3ZLZ, 3ZNH, 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, 4NQK

Identifiers

Symbols

UBC ; HMG20

External IDs

OMIM: 191340 MGI: 98889 HomoloGene: 128418 GeneCards: UBC Gene

Gene ontology
Molecular function	• protease binding • protein binding • poly(A) RNA binding
Cellular component	• nucleoplasm • cytosol • plasma membrane • endosome membrane • endocytic vesicle membrane
Biological process	• G1/S transition of mitotic cell cycle • G2/M transition of mitotic cell cycle • negative regulation of transcription from RNA polymerase II promoter • activation of MAPK activity • protein polyubiquitination • mitotic cell cycle • toll-like receptor signaling pathway • antigen processing and presentation of peptide antigen via MHC class I • antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent • MyD88-dependent toll-like receptor signaling pathway • MyD88-independent toll-like receptor signaling pathway • carbohydrate metabolic process • glycogen biosynthetic process • glucose metabolic process • DNA repair • transcription, DNA-templated • transcription initiation from RNA polymerase II promoter • apoptotic process • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest • epidermal growth factor receptor signaling pathway • transforming growth factor beta receptor signaling pathway • Notch signaling pathway • Notch receptor processing • I-kappaB kinase/NF-kappaB signaling • JNK cascade • fibroblast growth factor receptor signaling pathway • gene expression • viral process • RNA metabolic process • mRNA metabolic process • endosomal transport • viral life cycle • virion assembly • viral protein processing • cytokine-mediated signaling pathway • negative regulation of transforming growth factor beta receptor signaling pathway • anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process • regulation of type I interferon production • negative regulation of type I interferon production • positive regulation of type I interferon production • toll-like receptor 2 signaling pathway • toll-like receptor 3 signaling pathway • toll-like receptor 4 signaling pathway • toll-like receptor 5 signaling pathway • toll-like receptor 9 signaling pathway • toll-like receptor 10 signaling pathway • ion transmembrane transport • TRIF-dependent toll-like receptor signaling pathway • nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway • Fc-epsilon receptor signaling pathway • toll-like receptor TLR1:TLR2 signaling pathway • toll-like receptor TLR6:TLR2 signaling pathway • negative regulation of epidermal growth factor receptor signaling pathway • antigen processing and presentation of exogenous peptide antigen via MHC class I • regulation of apoptotic process • positive regulation of apoptotic process • negative regulation of apoptotic process • positive regulation of I-kappaB kinase/NF-kappaB signaling • small molecule metabolic process • innate immune response • positive regulation of transcription from RNA polymerase II promoter • neurotrophin TRK receptor signaling pathway • T cell receptor signaling pathway • positive regulation of NF-kappaB transcription factor activity • stress-activated MAPK cascade • negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle • positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle • regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle • transmembrane transport • membrane organization • regulation of transcription from RNA polymerase II promoter in response to hypoxia • nucleotide-binding oligomerization domain containing signaling pathway • cellular response to hypoxia • intracellular transport of virus • apoptotic signaling pathway
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 12:
125.4 – 125.4 Mb

Chr 5:
125.39 – 125.39 Mb

PubMed search

Polyubiquitin-C is a protein encoded by the UBC gene in humans.^[1]^[2]^[3] It is one of the sources of ubiquitin, along with UBB, UBA52, and RPS27A.^[4]

Interactions

Ubiquitin C has been shown to interact with:

BIRC2,^[5]^[6]^[7]
Basigin,^[8]
C21orf59,^[9]
Cdk1,^[10]
E2F1,^[11]
Epidermal growth factor receptor,^[12]^[13]^[14]
HDAC3,^[10]
HIF1A,^[15]^[16]^[17]
IRAK1,^[18]^[19]^[20]^[21]
Kappa Opioid receptor,^[22]
MARK4,^[23]
Mdm2,^[24]^[25]^[26]
Mothers against decapentaplegic homolog 3,^[27]^[28]
NDUFA3,^[29]
NFE2L2,^[30]^[31]
NOTCH1,^[32]
NUAK1,^[23]
P53,^[12]^[24]^[25]^[26]^[33]^[34]^[35]^[36]
P70-S6 Kinase 1,^[37]
PCNA^[38]^[39]^[40]
Parkin (ligase),^[41]^[42]
RIPK1,^[18]^[43]^[44]^[5]^[45]
S100A10,^[46]
SCNN1A,^[47]^[48]
SCNN1G,^[47]^[48]
SFPQ,^[49]
SMURF2,^[50]^[51]
Sp1 transcription factor,^[52]
TRAF6,^[18]^[53]^[54]^[19]^[43] and
Thyroid hormone receptor alpha.^[10]

References

↑ Board PG, Coggan M, Baker RT, Vuust J, Webb GC (May 1992). "Localization of the human UBC polyubiquitin gene to chromosome band 12q24.3". Genomics 12 (4): 639–42. doi:10.1016/0888-7543(92)90287-3. PMID 1315303.
↑ Marinovic AC, Zheng B, Mitch WE, Price SR (May 2002). "Ubiquitin (UbC) expression in muscle cells is increased by glucocorticoids through a mechanism involving Sp1 and MEK1". J Biol Chem 277 (19): 16673–81. doi:10.1074/jbc.M200501200. PMID 11872750.
↑ "Entrez Gene: UBC ubiquitin C".
↑ Kimura Y, Tanaka K (2010). "Regulatory mechanisms involved in the control of ubiquitin homeostasis". J. Biochem. 147 (6): 793–8. doi:10.1093/jb/mvq044. PMID 20418328.
↑ 5.0 5.1 Bertrand MJ, Milutinovic S, Dickson KM, Ho WC, Boudreault A, Durkin J et al. "cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination". Mol. Cell 30 (6): 689–700. doi:10.1016/j.molcel.2008.05.014. PMID 18570872.
↑ Didelot C, Lanneau D, Brunet M, Bouchot A, Cartier J, Jacquel A et al. "Interaction of heat-shock protein 90 beta isoform (HSP90 beta) with cellular inhibitor of apoptosis 1 (c-IAP1) is required for cell differentiation". Cell Death Differ. 15 (5): 859–66. doi:10.1038/cdd.2008.5. PMID 18239673.
↑ Sekine K, Takubo K, Kikuchi R, Nishimoto M, Kitagawa M, Abe F et al. "Small molecules destabilize cIAP1 by activating auto-ubiquitylation". J. Biol. Chem. 283 (14): 8961–8. doi:10.1074/jbc.M709525200. PMID 18230607.
↑ Wang WJ, Li QQ, Xu JD, Cao XX, Li HX, Tang F et al. "Interaction between CD147 and P-glycoprotein and their regulation by ubiquitination in breast cancer cells". Chemotherapy 54 (4): 291–301. doi:10.1159/000151225. PMID 18689982.
↑ Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A et al. (2011). "Systematic and quantitative assessment of the ubiquitin-modified proteome". Mol. Cell 44 (2): 325–40. doi:10.1016/j.molcel.2011.08.025. PMC 3200427. PMID 21906983.
↑ 10.0 10.1 10.2 Tan F, Lu L, Cai Y, Wang J, Xie Y, Wang L et al. "Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells". Proteomics 8 (14): 2885–96. doi:10.1002/pmic.200700887. PMID 18655026.
↑ Zhou F, Zhang L, Wang A, Song B, Gong K, Zhang L et al. "The association of GSK3 beta with E2F1 facilitates nerve growth factor-induced neural cell differentiation". J. Biol. Chem. 283 (21): 14506–15. doi:10.1074/jbc.M706136200. PMID 18367454.
↑ 12.0 12.1 Sehat B, Andersson S, Girnita L, Larsson O. "Identification of c-Cbl as a new ligase for insulin-like growth factor-I receptor with distinct roles from Mdm2 in receptor ubiquitination and endocytosis". Cancer Res. 68 (14): 5669–77. doi:10.1158/0008-5472.CAN-07-6364. PMID 18632619.
↑ Pennock S, Wang Z. "A tale of two Cbls: interplay of c-Cbl and Cbl-b in epidermal growth factor receptor downregulation". Mol. Cell. Biol. 28 (9): 3020–37. doi:10.1128/MCB.01809-07. PMC 2293090. PMID 18316398.
↑ Umebayashi K, Stenmark H, Yoshimori T. "Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation". Mol. Biol. Cell 19 (8): 3454–62. doi:10.1091/mbc.E07-10-0988. PMC 2488299. PMID 18508924.
↑ André H, Pereira TS. "Identification of an alternative mechanism of degradation of the hypoxia-inducible factor-1alpha". J. Biol. Chem. 283 (43): 29375–84. doi:10.1074/jbc.M805919200. PMC 2662024. PMID 18694926. Vancouver style error (help)
↑ Park YK, Ahn DR, Oh M, Lee T, Yang EG, Son M et al. "Nitric oxide donor, (+/-)-S-nitroso-N-acetylpenicillamine, stabilizes transactive hypoxia-inducible factor-1alpha by inhibiting von Hippel-Lindau recruitment and asparagine hydroxylation". Mol. Pharmacol. 74 (1): 236–45. doi:10.1124/mol.108.045278. PMID 18426857.
↑ Kim BY, Kim H, Cho EJ, Youn HD. "Nur77 upregulates HIF-alpha by inhibiting pVHL-mediated degradation". Exp. Mol. Med. 40 (1): 71–83. doi:10.3858/emm.2008.40.1.71. PMC 2679322. PMID 18305400.
↑ 18.0 18.1 18.2 Newton K, Matsumoto ML, Wertz IE, Kirkpatrick DS, Lill JR, Tan J et al. "Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies". Cell 134 (4): 668–78. doi:10.1016/j.cell.2008.07.039. PMID 18724939.
↑ 19.0 19.1 Conze DB, Wu CJ, Thomas JA, Landstrom A, Ashwell JD. "Lys63-linked polyubiquitination of IRAK-1 is required for interleukin-1 receptor- and toll-like receptor-mediated NF-kappaB activation". Mol. Cell. Biol. 28 (10): 3538–47. doi:10.1128/MCB.02098-07. PMC 2423148. PMID 18347055.
↑ Xiao H, Qian W, Staschke K, Qian Y, Cui G, Deng L et al. "Pellino 3b negatively regulates interleukin-1-induced TAK1-dependent NF kappaB activation". J. Biol. Chem. 283 (21): 14654–64. doi:10.1074/jbc.M706931200. PMC 2386918. PMID 18326498.
↑ Windheim M, Stafford M, Peggie M, Cohen P. "Interleukin-1 (IL-1) induces the Lys63-linked polyubiquitination of IL-1 receptor-associated kinase 1 to facilitate NEMO binding and the activation of IkappaBalpha kinase". Mol. Cell. Biol. 28 (5): 1783–91. doi:10.1128/MCB.02380-06. PMC 2258775. PMID 18180283.
↑ Li JG, Haines DS, Liu-Chen LY. "Agonist-promoted Lys63-linked polyubiquitination of the human kappa-opioid receptor is involved in receptor down-regulation". Mol. Pharmacol. 73 (4): 1319–30. doi:10.1124/mol.107.042846. PMC 3489932. PMID 18212250.
↑ 23.0 23.1 Al-Hakim AK, Zagorska A, Chapman L, Deak M, Peggie M, Alessi DR. "Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains". Biochem. J. 411 (2): 249–60. doi:10.1042/BJ20080067. PMID 18363552.
↑ 24.0 24.1 Ivanchuk SM, Mondal S, Rutka JT. "p14ARF interacts with DAXX: effects on HDM2 and p53". Cell Cycle 7 (12): 1836–50. doi:10.4161/cc.7.12.6025. PMID 18583933.
↑ 25.0 25.1 Song MS, Song SJ, Kim SY, Oh HJ, Lim DS. "The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex". EMBO J. 27 (13): 1863–74. doi:10.1038/emboj.2008.115. PMC 2486425. PMID 18566590.
↑ 26.0 26.1 Yang W, Dicker DT, Chen J, El-Deiry WS. "CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing MDM2". Cell Cycle 7 (5): 670–82. doi:10.4161/cc.7.5.5701. PMID 18382127.
↑ Stolfi C, Fina D, Caruso R, Caprioli F, Fantini MC, Rizzo A et al. "Mesalazine negatively regulates CDC25A protein expression and promotes accumulation of colon cancer cells in S phase". Carcinogenesis 29 (6): 1258–66. doi:10.1093/carcin/bgn122. PMID 18495657.
↑ Guo X, Ramirez A, Waddell DS, Li Z, Liu X, Wang XF. "Axin and GSK3- control Smad3 protein stability and modulate TGF- signaling". Genes Dev. 22 (1): 106–20. doi:10.1101/gad.1590908. PMC 2151009. PMID 18172167.
↑ Wagner, S. A.; Beli, P; Weinert, B. T.; Nielsen, M. L.; Cox, J; Mann, M; Choudhary, C (2011). "A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles". Molecular & Cellular Proteomics 10 (10): M111.013284. doi:10.1074/mcp.M111.013284. PMC 3205876. PMID 21890473.
↑ Shibata T, Ohta T, Tong KI, Kokubu A, Odogawa R, Tsuta K et al. "Cancer related mutations in NRF2 impair its recognition by Keap1-Cul3 E3 ligase and promote malignancy". Proc. Natl. Acad. Sci. U.S.A. 105 (36): 13568–73. doi:10.1073/pnas.0806268105. PMC 2533230. PMID 18757741.
↑ Patel R, Maru G. "Polymeric black tea polyphenols induce phase II enzymes via Nrf2 in mouse liver and lungs". Free Radic. Biol. Med. 44 (11): 1897–911. doi:10.1016/j.freeradbiomed.2008.02.006. PMID 18358244.
↑ Chastagner P, Israël A, Brou C. Wölfl Stefan, ed. "AIP4/Itch regulates Notch receptor degradation in the absence of ligand". PLoS ONE 3 (7): e2735. doi:10.1371/journal.pone.0002735. PMC 2444042. PMID 18628966. Vancouver style error (help)
↑ Han JM, Park BJ, Park SG, Oh YS, Choi SJ, Lee SW et al. "AIMP2/p38, the scaffold for the multi-tRNA synthetase complex, responds to genotoxic stresses via p53". Proc. Natl. Acad. Sci. U.S.A. 105 (32): 11206–11. doi:10.1073/pnas.0800297105. PMC 2516205. PMID 18695251.
↑ Abe Y, Oda-Sato E, Tobiume K, Kawauchi K, Taya Y, Okamoto K et al. "Hedgehog signaling overrides p53-mediated tumor suppression by activating Mdm2". Proc. Natl. Acad. Sci. U.S.A. 105 (12): 4838–43. doi:10.1073/pnas.0712216105. PMC 2290789. PMID 18359851.
↑ Zhang Z, Zhang R. "Proteasome activator PA28 gamma regulates p53 by enhancing its MDM2-mediated degradation". EMBO J. 27 (6): 852–64. doi:10.1038/emboj.2008.25. PMC 2265109. PMID 18309296.
↑ Dohmesen C, Koeppel M, Dobbelstein M. "Specific inhibition of Mdm2-mediated neddylation by Tip60". Cell Cycle 7 (2): 222–31. doi:10.4161/cc.7.2.5185. PMID 18264029.
↑ Panasyuk G, Nemazanyy I, Filonenko V, Gout I. "Ribosomal protein S6 kinase 1 interacts with and is ubiquitinated by ubiquitin ligase ROC1". Biochem. Biophys. Res. Commun. 369 (2): 339–43. doi:10.1016/j.bbrc.2008.02.016. PMID 18279656.
↑ Motegi A, Liaw HJ, Lee KY, Roest HP, Maas A, Wu X et al. "Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks". Proc. Natl. Acad. Sci. U.S.A. 105 (34): 12411–6. doi:10.1073/pnas.0805685105. PMC 2518831. PMID 18719106.
↑ Unk I, Hajdú I, Fátyol K, Hurwitz J, Yoon JH, Prakash L et al. "Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination". Proc. Natl. Acad. Sci. U.S.A. 105 (10): 3768–73. doi:10.1073/pnas.0800563105. PMC 2268824. PMID 18316726. Vancouver style error (help)
↑ Brun J, Chiu R, Lockhart K, Xiao W, Wouters BG, Gray DA. "hMMS2 serves a redundant role in human PCNA polyubiquitination". BMC Mol. Biol. 9: 24. doi:10.1186/1471-2199-9-24. PMC 2263069. PMID 18284681.
↑ Yu F, Zhou J. "Parkin is ubiquitinated by Nrdp1 and abrogates Nrdp1-induced oxidative stress". Neurosci. Lett. 440 (1): 4–8. doi:10.1016/j.neulet.2008.05.052. PMID 18541373.
↑ Kawahara K, Hashimoto M, Bar-On P, Ho GJ, Crews L, Mizuno H et al. "alpha-Synuclein aggregates interfere with Parkin solubility and distribution: role in the pathogenesis of Parkinson disease". J. Biol. Chem. 283 (11): 6979–87. doi:10.1074/jbc.M710418200. PMID 18195004.
↑ 43.0 43.1 Ma Q, Zhou L, Shi H, Huo K. "NUMBL interacts with TAB2 and inhibits TNFalpha and IL-1beta-induced NF-kappaB activation". Cell. Signal. 20 (6): 1044–51. doi:10.1016/j.cellsig.2008.01.015. PMID 18299187.
↑ Varfolomeev E, Goncharov T, Fedorova AV, Dynek JN, Zobel K, Deshayes K et al. "c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFalpha)-induced NF-kappaB activation". J. Biol. Chem. 283 (36): 24295–9. doi:10.1074/jbc.C800128200. PMC 3259840. PMID 18621737.
↑ Liao W, Xiao Q, Tchikov V, Fujita K, Yang W, Wincovitch S et al. "CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation". Curr. Biol. 18 (9): 641–9. doi:10.1016/j.cub.2008.04.017. PMC 2587165. PMID 19138581.
↑ He KL, Deora AB, Xiong H, Ling Q, Weksler BB, Niesvizky R et al. "Endothelial cell annexin A2 regulates polyubiquitination and degradation of its binding partner S100A10/p11". J. Biol. Chem. 283 (28): 19192–200. doi:10.1074/jbc.M800100200. PMC 2443646. PMID 18434302.
↑ 47.0 47.1 Boulkroun S, Ruffieux-Daidié D, Vitagliano JJ, Poirot O, Charles RP, Lagnaz D et al. "Vasopressin-inducible ubiquitin-specific protease 10 increases ENaC cell surface expression by deubiquitylating and stabilizing sorting nexin 3". Am. J. Physiol. Renal Physiol. 295 (4): F889–900. doi:10.1152/ajprenal.00001.2008. PMID 18667480. Vancouver style error (help)
↑ 48.0 48.1 Raikwar NS, Thomas CP. "Nedd4-2 isoforms ubiquitinate individual epithelial sodium channel subunits and reduce surface expression and function of the epithelial sodium channel". Am. J. Physiol. Renal Physiol. 294 (5): F1157–65. doi:10.1152/ajprenal.00339.2007. PMC 2424110. PMID 18322022.
↑ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H et al. "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16179252.
↑ Carpentier I, Coornaert B, Beyaert R. "Smurf2 is a TRAF2 binding protein that triggers TNF-R2 ubiquitination and TNF-R2-induced JNK activation". Biochem. Biophys. Res. Commun. 374 (4): 752–7. doi:10.1016/j.bbrc.2008.07.103. PMID 18671942.
↑ Lee YS, Han JM, Son SH, Choi JW, Jeon EJ, Bae SC et al. "AIMP1/p43 downregulates TGF-beta signaling via stabilization of smurf2". Biochem. Biophys. Res. Commun. 371 (3): 395–400. doi:10.1016/j.bbrc.2008.04.099. PMID 18448069.
↑ Wang YT, Chuang JY, Shen MR, Yang WB, Chang WC, Hung JJ. "Sumoylation of specificity protein 1 augments its degradation by changing the localization and increasing the specificity protein 1 proteolytic process". J. Mol. Biol. 380 (5): 869–85. doi:10.1016/j.jmb.2008.05.043. PMID 18572193.
↑ Chen L, Dong W, Zou T, Ouyang L, He G, Liu Y et al. "Protein phosphatase 4 negatively regulates LPS cascade by inhibiting ubiquitination of TRAF6". FEBS Lett. 582 (19): 2843–9. doi:10.1016/j.febslet.2008.07.014. PMID 18634786.
↑ Lamothe B, Campos AD, Webster WK, Gopinathan A, Hur L, Darnay BG. "The RING domain and first zinc finger of TRAF6 coordinate signaling by interleukin-1, lipopolysaccharide, and RANKL". J. Biol. Chem. 283 (36): 24871–80. doi:10.1074/jbc.M802749200. PMC 2529010. PMID 18617513.

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PDB gallery

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

1d3z: UBIQUITIN NMR STRUCTURE

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

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

1otr: Solution Structure of a CUE-Ubiquitin Complex

1p3q: Mechanism of Ubiquitin Recognition by the CUE Domain of VPS9

1q0w: Solution structure of Vps27 amino-terminal UIM-ubiquitin complex

1q5w: Ubiquitin Recognition by Npl4 Zinc-Fingers

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

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

1uzx: A COMPLEX OF THE VPS23 UEV WITH UBIQUITIN

1v80: 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

1wr6: Crystal structure of GGA3 GAT domain in complex with ubiquitin

1wrd: Crystal structure of Tom1 GAT domain in complex with ubiquitin

1xd3: Crystal structure of UCHL3-UbVME complex

1xqq: Simultaneous determination of protein structure and dynamics

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

1yx5: Solution Structure of S5a UIM-1/Ubiquitin Complex

1yx6: Solution Structure of S5a UIM-2/Ubiquitin Complex

1zgu: Solution structure of the human Mms2-Ubiquitin complex

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

2c7m: 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

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

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

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

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

2hth: Structural basis for ubiquitin recognition by the human EAP45/ESCRT-II GLUE domain

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

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

2oob: crystal structure of the UBA domain from Cbl-b ubiquitin ligase in complex with ubiquitin

Ubiquitin C

Interactions

References

Further reading