Ubikvitin C

С Википедије, слободне енциклопедије
Ubikvitin C
PDB prikaz baziran na 1aar​.
Dostupne strukture
1aar​, 1cmx​, 1d3z​, 1f9j​, 1fxt​, 1g6j​, 1gjz​, 1nbf​, 1ogw​, 1otr​, 1p3q​, 1q0w​, 1q5w​, 1s1q​, 1sif​, 1tbe​, 1ubi​, 1ubq​, 1ud7​, 1uzx​, 1v80​, 1v81​, 1wr1​, 1wr6​, 1wrd​, 1xd3​, 1xqq​, 1yd8​, 1yiw​, 1yj1​, 1yx5​, 1yx6​, 1zgu​, 2ayo​, 2bgf​, 2c7m​, 2c7n​, 2d3g​, 2den​, 2dx5​, 2fcm​, 2fcn​, 2fcq​, 2fcs​, 2fid​, 2fif​, 2fuh​, 2g3q​, 2g45​, 2gbj​, 2gbk​, 2gbm​, 2gbn​, 2gbr​, 2gmi​, 2hd5​, 2hth​, 2ibi​, 2j7q​, 2nr2​, 2o6v​, 2oob​
Identifikatori
Simboli UBC; HMG20
Vanjski ID OMIM: 191340 MGI: 98889 HomoloGene: 39626 GeneCards: UBC Gene
Pregled RNK izražavanja
podaci
Ortolozi
Vrsta Čovek Miš
Entrez 7316 22190
Ensembl ENSG00000150991 ENSMUSG00000008348
UniProt P0CG48 Q3TH47
RefSeq (mRNA) XM_001132949 XM_001001910
RefSeq (protein) XP_001132949 XP_001001910
Lokacija (UCSC) Chr 12:
123.96 - 123.97 Mb		 Chr 5:
125.68 - 125.68 Mb
PubMed pretraga [1] [2]

Ubikvitin je protein koji je kod čoveka kodiran UBC genom.[1][2][3]

Interakcije[уреди | уреди извор]

Za ubikvitin C je pokazano da interaguje sa SCNN1A,[4][5] SCNN1G,[4][5] Parkin (ligazom),[6][7] P70-S6 kinazom 1,[8] TRAF6,[9][10][11][12][13] HDAC3,[14] SFPQ,[15] S100A10,[16] SMAD3,[17][18] NOTCH1,[19] HIF1A,[20][21][22] receptorom epidermalnog faktora rasta,[23][24][25] E2F1,[26] Basigin,[27] IRAK1,[9][12][28][29] NFE2L2,[30][31] RIPK1,[9][13][32][33][34] Mdm2,[35][36][37] Kapa opioidnim receptorom,[38] NUAK1,[39] BIRC2,[33][40][41] tiroidnim hormonskim receptorom alfa,[14] Sp1 transkriptnim faktorom,[42] SMURF2,[43][44] MARK4,[39] Cdk1,[14] PCNA[45][46][47] i P53.[23][35][36][37][48][49][50][51]

Reference[уреди | уреди извор]

  1. ^ Board PG, Coggan M, Baker RT, Vuust J, Webb GC (1992). „Localization of the human UBC polyubiquitin gene to chromosome band 12q24.3”. Genomics. 12 (4): 639—42. PMID 1315303. doi:10.1016/0888-7543(92)90287-3. 
  2. ^ Marinovic AC, Zheng B, Mitch WE, Price SR (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. PMID 11872750. doi:10.1074/jbc.M200501200. 
  3. ^ „Entrez Gene: UBC ubiquitin C”. 
  4. ^ а б Boulkroun, Sheerazed; Ruffieux-Daidié Dorothée; et al. (2008). „Vasopressin-inducible ubiquitin-specific protease 10 increases ENaC cell surface expression by deubiquitylating and stabilizing sorting nexin 3”. Am. J. Physiol. Renal Physiol. United States. 295 (4): F889—900. ISSN 0363-6127. PMID 18632802. doi:10.1152/ajprenal.00001.2008. 
  5. ^ а б Raikwar, Nandita S.; Thomas Christie P (2008). „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. United States. 294 (5): F1157—65. ISSN 0363-6127. PMC 2424110 Слободан приступ. PMID 18322022. doi:10.1152/ajprenal.00339.2007. 
  6. ^ Yu, Furong; Jianhua, Zhou (2008). „Parkin is ubiquitinated by Nrdp1 and abrogates Nrdp1-induced oxidative stress”. Neurosci. Lett. Ireland. 440 (1): 4—8. ISSN 0304-3940. PMID 18541373. doi:10.1016/j.neulet.2008.05.052. 
  7. ^ Kawahara, Kohichi; Makoto, Hashimoto; et al. (2008). „alpha-Synuclein aggregates interfere with Parkin solubility and distribution: role in the pathogenesis of Parkinson disease”. J. Biol. Chem. United States. 283 (11): 6979—87. ISSN 0021-9258. PMID 18195004. doi:10.1074/jbc.M710418200. 
  8. ^ Panasyuk, Ganna; Ivan, Nemazanyy; et al. (2008). „Ribosomal protein S6 kinase 1 interacts with and is ubiquitinated by ubiquitin ligase ROC1”. Biochem. Biophys. Res. Commun. United States. 369 (2): 339—43. PMID 18279656. doi:10.1016/j.bbrc.2008.02.016. 
  9. ^ а б в Newton, Kim; Matsumoto Marissa L; et al. (2008). „Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies”. Cell. United States. 134 (4): 668—78. PMID 18724939. doi:10.1016/j.cell.2008.07.039. 
  10. ^ Chen, Lu; Wei, Dong; et al. (2008). „Protein phosphatase 4 negatively regulates LPS cascade by inhibiting ubiquitination of TRAF6”. FEBS Lett. Netherlands. 582 (19): 2843—9. ISSN 0014-5793. PMID 18634786. doi:10.1016/j.febslet.2008.07.014. 
  11. ^ Lamothe, Betty; Campos Alejandro D; et al. (2008). „The RING domain and first zinc finger of TRAF6 coordinate signaling by interleukin-1, lipopolysaccharide, and RANKL”. J. Biol. Chem. United States. 283 (36): 24871—80. ISSN 0021-9258. PMC 2529010 Слободан приступ. PMID 18617513. doi:10.1074/jbc.M802749200. 
  12. ^ а б Conze, Dietrich B.; Wu Chuan-Jin; et al. (2008). „Lys63-linked polyubiquitination of IRAK-1 is required for interleukin-1 receptor- and toll-like receptor-mediated NF-kappaB activation”. Mol. Cell. Biol. United States. 28 (10): 3538—47. PMC 2423148 Слободан приступ. PMID 18347055. doi:10.1128/MCB.02098-07. 
  13. ^ а б Ma, Qi; Li, Zhou; et al. (2008). „NUMBL interacts with TAB2 and inhibits TNFalpha and IL-1beta-induced NF-kappaB activation”. Cell. Signal. England. 20 (6): 1044—51. ISSN 0898-6568. PMID 18299187. doi:10.1016/j.cellsig.2008.01.015. 
  14. ^ а б в Tan, Fengwei; Lifang, Lu; et al. (2008). „Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells”. Proteomics. Germany. 8 (14): 2885—96. PMID 18655026. doi:10.1002/pmic.200700887. 
  15. ^ Stelzl, Ulrich; Uwe, Worm; et al. (2005). „A human protein-protein interaction network: a resource for annotating the proteome”. Cell. United States. 122 (6): 957—68. ISSN 0092-8674. PMID 16169070. doi:10.1016/j.cell.2005.08.029. 
  16. ^ He, Kai-Li; Deora Arunkumar B; et al. (2008). „Endothelial cell annexin A2 regulates polyubiquitination and degradation of its binding partner S100A10/p11”. J. Biol. Chem. United States. 283 (28): 19192—200. ISSN 0021-9258. PMC 2443646 Слободан приступ. PMID 18434302. doi:10.1074/jbc.M800100200. 
  17. ^ Stolfi, Carmine; Daniele, Fina; et al. (2008). „Mesalazine negatively regulates CDC25A protein expression and promotes accumulation of colon cancer cells in S phase”. Carcinogenesis. England. 29 (6): 1258—66. PMID 18495657. doi:10.1093/carcin/bgn122. 
  18. ^ Guo, Xing; Alejandro, Ramirez; et al. (2008). „Axin and GSK3- control Smad3 protein stability and modulate TGF- signaling”. Genes Dev. United States. 22 (1): 106—20. ISSN 0890-9369. PMC 2151009 Слободан приступ. PMID 18172167. doi:10.1101/gad.1590908. 
  19. ^ Chastagner, Patricia; Alain, Israël; Christel, Brou (2008). Wölfl, Stefan, ур. „AIP4/Itch regulates Notch receptor degradation in the absence of ligand”. PLoS ONE. United States. 3 (7): e2735. PMC 2444042 Слободан приступ. PMID 18628966. doi:10.1371/journal.pone.0002735. 
  20. ^ André, Helder; Pereira Teresa S (2008). „Identification of an alternative mechanism of degradation of the hypoxia-inducible factor-1alpha”. J. Biol. Chem. United States. 283 (43): 29375—84. ISSN 0021-9258. PMC 2662024 Слободан приступ. PMID 18694926. doi:10.1074/jbc.M805919200. 
  21. ^ Park, Young-Kwon; Ahn Dae-Ro; et al. (2008). „Nitric oxide donor, (+/-)-S-nitroso-N-acetylpenicillamine, stabilizes transactive hypoxia-inducible factor-1alpha by inhibiting von Hippel-Lindau recruitment and asparagine hydroxylation”. Mol. Pharmacol. United States. 74 (1): 236—45. PMID 18426857. doi:10.1124/mol.108.045278. 
  22. ^ Kim, Bu Yeon; Hyungsoo, Kim; et al. (2008). „Nur77 upregulates HIF-alpha by inhibiting pVHL-mediated degradation”. Exp. Mol. Med. Korea (South). 40 (1): 71—83. ISSN 1226-3613. PMC 2679322 Слободан приступ. PMID 18305400. doi:10.3858/emm.2008.40.1.71. 
  23. ^ а б Sehat, Bita; Sandra, Andersson; et al. (2008). „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. United States. 68 (14): 5669—77. PMID 18632619. doi:10.1158/0008-5472.CAN-07-6364. 
  24. ^ Pennock, Steven; Zhixiang, Wang (2008). „A tale of two Cbls: interplay of c-Cbl and Cbl-b in epidermal growth factor receptor downregulation”. Mol. Cell. Biol. United States. 28 (9): 3020—37. PMC 2293090 Слободан приступ. PMID 18316398. doi:10.1128/MCB.01809-07. 
  25. ^ Umebayashi, Kyohei; Harald, Stenmark; Tamotsu, Yoshimori (2008). „Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation”. Mol. Biol. Cell. United States. 19 (8): 3454—62. PMC 2488299 Слободан приступ. PMID 18508924. doi:10.1091/mbc.E07-10-0988. 
  26. ^ Zhou, Fangfang; Long, Zhang; et al. (2008). „The association of GSK3 beta with E2F1 facilitates nerve growth factor-induced neural cell differentiation”. J. Biol. Chem. United States. 283 (21): 14506—15. ISSN 0021-9258. PMID 18367454. doi:10.1074/jbc.M706136200. 
  27. ^ Wang, Wen-Juan; Li Qing-Quan; et al. (2008). „Interaction between CD147 and P-glycoprotein and their regulation by ubiquitination in breast cancer cells”. Chemotherapy. Switzerland. 54 (4): 291—301. PMID 18689982. doi:10.1159/000151225. 
  28. ^ Xiao, Hui; Wen, Qian; et al. (2008). „Pellino 3b negatively regulates interleukin-1-induced TAK1-dependent NF kappaB activation”. J. Biol. Chem. United States. 283 (21): 14654—64. ISSN 0021-9258. PMC 2386918 Слободан приступ. PMID 18326498. doi:10.1074/jbc.M706931200. 
  29. ^ Windheim, Mark; Margaret, Stafford; et al. (2008). „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. United States. 28 (5): 1783—91. PMC 2258775 Слободан приступ. PMID 18180283. doi:10.1128/MCB.02380-06. 
  30. ^ Shibata, Tatsuhiro; Tsutomu, Ohta; et al. (2008). „Cancer related mutations in NRF2 impair its recognition by Keap1-Cul3 E3 ligase and promote malignancy”. Proc. Natl. Acad. Sci. U.S.A. United States. 105 (36): 13568—73. PMC 2533230 Слободан приступ. PMID 18757741. doi:10.1073/pnas.0806268105. 
  31. ^ Patel, Rachana; Girish, Maru (2008). „Polymeric black tea polyphenols induce phase II enzymes via Nrf2 in mouse liver and lungs”. Free Radic. Biol. Med. United States. 44 (11): 1897—911. ISSN 0891-5849. PMID 18358244. doi:10.1016/j.freeradbiomed.2008.02.006. 
  32. ^ Varfolomeev, Eugene; Tatiana, Goncharov; et al. (2008). „c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFalpha)-induced NF-kappaB activation”. J. Biol. Chem. United States. 283 (36): 24295—9. ISSN 0021-9258. PMID 18621737. doi:10.1074/jbc.C800128200. 
  33. ^ а б Bertrand, Mathieu J M; Snezana, Milutinovic; et al. (2008). „cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination”. Mol. Cell. United States. 30 (6): 689—700. PMID 18570872. doi:10.1016/j.molcel.2008.05.014. 
  34. ^ Liao, Wentao; Qi, Xiao; et al. (2008). „CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation”. Curr. Biol. England. 18 (9): 641—9. ISSN 0960-9822. PMC 2587165 Слободан приступ. PMID 18450452. doi:10.1016/j.cub.2008.04.017. 
  35. ^ а б Ivanchuk, Stacey M.; Soma, Mondal; Rutka James T (2008). „p14ARF interacts with DAXX: effects on HDM2 and p53”. Cell Cycle. United States. 7 (12): 1836—50. PMID 18583933. doi:10.4161/cc.7.12.6025. 
  36. ^ а б Song, Min Sup; Song Su Jung; et al. (2008). „The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex”. EMBO J. England. 27 (13): 1863—74. PMC 2486425 Слободан приступ. PMID 18566590. doi:10.1038/emboj.2008.115. 
  37. ^ а б Yang, Wensheng; Dicker David T; et al. (2008). „CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing MDM2”. Cell Cycle. United States. 7 (5): 670—82. PMID 18382127. doi:10.4161/cc.7.5.5701. 
  38. ^ Li, Jian-Guo; Haines Dale S; Liu-Chen Lee-Yuan (2008). „Agonist-promoted Lys63-linked polyubiquitination of the human kappa-opioid receptor is involved in receptor down-regulation”. Mol. Pharmacol. United States. 73 (4): 1319—30. PMID 18212250. doi:10.1124/mol.107.042846. 
  39. ^ а б Al-Hakim, Abdallah K.; Anna, Zagorska; et al. (2008). „Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains”. Biochem. J. England. 411 (2): 249—60. PMID 18254724. doi:10.1042/BJ20080067. 
  40. ^ Didelot, C; D, Lanneau; et al. (2008). „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. England. 15 (5): 859—66. ISSN 1350-9047. PMID 18239673. doi:10.1038/cdd.2008.5. 
  41. ^ Sekine, Keiko; Kohei, Takubo; et al. (2008). „Small molecules destabilize cIAP1 by activating auto-ubiquitylation”. J. Biol. Chem. United States. 283 (14): 8961—8. ISSN 0021-9258. PMID 18230607. doi:10.1074/jbc.M709525200. 
  42. ^ Wang, Yi-Ting; Chuang Jian-Ying; et al. (2008). „Sumoylation of specificity protein 1 augments its degradation by changing the localization and increasing the specificity protein 1 proteolytic process”. J. Mol. Biol. England. 380 (5): 869—85. PMID 18572193. doi:10.1016/j.jmb.2008.05.043. 
  43. ^ Carpentier, Isabelle; Beatrice, Coornaert; Rudi, Beyaert (2008). „Smurf2 is a TRAF2 binding protein that triggers TNF-R2 ubiquitination and TNF-R2-induced JNK activation”. Biochem. Biophys. Res. Commun. United States. 374 (4): 752—7. PMID 18671942. doi:10.1016/j.bbrc.2008.07.103. 
  44. ^ Lee, Yeon Sook; Han Jung Min; et al. (2008). „AIMP1/p43 downregulates TGF-beta signaling via stabilization of smurf2”. Biochem. Biophys. Res. Commun. United States. 371 (3): 395—400. PMID 18448069. doi:10.1016/j.bbrc.2008.04.099. 
  45. ^ Motegi, Akira; Liaw Hung-Jiun; et al. (2008). „Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks”. Proc. Natl. Acad. Sci. U.S.A. United States. 105 (34): 12411—6. PMC 2518831 Слободан приступ. PMID 18719106. doi:10.1073/pnas.0805685105. 
  46. ^ Unk, Ildiko; Ildikó, Hajdú; et al. (2008). „Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination”. Proc. Natl. Acad. Sci. U.S.A. United States. 105 (10): 3768—73. PMC 2268824 Слободан приступ. PMID 18316726. doi:10.1073/pnas.0800563105. 
  47. ^ Brun, Jan; Roland, Chiu; et al. (2008). „hMMS2 serves a redundant role in human PCNA polyubiquitination”. BMC Mol. Biol. England. 9: 24. PMC 2263069 Слободан приступ. PMID 18284681. doi:10.1186/1471-2199-9-24. 
  48. ^ Han, Jung Min; Park Bum-Joon; et al. (2008). „AIMP2/p38, the scaffold for the multi-tRNA synthetase complex, responds to genotoxic stresses via p53”. Proc. Natl. Acad. Sci. U.S.A. United States. 105 (32): 11206—11. PMC 2516205 Слободан приступ. PMID 18695251. doi:10.1073/pnas.0800297105. 
  49. ^ Abe, Yoshinori; Oda-Sato Eri; et al. (2008). „Hedgehog signaling overrides p53-mediated tumor suppression by activating Mdm2”. Proc. Natl. Acad. Sci. U.S.A. United States. 105 (12): 4838—43. PMC 2290789 Слободан приступ. PMID 18359851. doi:10.1073/pnas.0712216105. 
  50. ^ Zhang, Zhuo; Ruiwen, Zhang (2008). „Proteasome activator PA28 gamma regulates p53 by enhancing its MDM2-mediated degradation”. EMBO J. England. 27 (6): 852—64. PMC 2265109 Слободан приступ. PMID 18309296. doi:10.1038/emboj.2008.25. 
  51. ^ Dohmesen, Christoph; Max, Koeppel; Matthias, Dobbelstein (2008). „Specific inhibition of Mdm2-mediated neddylation by Tip60”. Cell Cycle. United States. 7 (2): 222—31. PMID 18264029. doi:10.4161/cc.7.2.5185. 

Literatura[уреди | уреди извор]

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