Ubiquitin C

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, 2NR2, 2O6V, 2OJR, 2PE9, 2PEA, 2RR9, 2W9N, 2WDT, 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, 3TMP, 3U30, 3UGB, 4DDG, 4DDI, 4DHJ, 4DHZ

Identifiers

Symbols

UBC; HMG20

External IDs

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

Gene Ontology
Molecular function	• protease binding • protein binding
Cellular component	• nucleoplasm • cytosol • endosome membrane • endocytic vesicle membrane
Biological process	• cell cycle checkpoint • G1 phase of mitotic cell cycle • G1/S transition of mitotic cell cycle • S phase of mitotic cell cycle • M phase of mitotic cell cycle • mitotic anaphase • 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 • DNA repair • transcription, DNA-dependent • transcription initiation from RNA polymerase II promoter • apoptotic process • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest • male meiosis I • female meiosis I • epidermal growth factor receptor signaling pathway • transforming growth factor beta receptor signaling pathway • Notch signaling pathway • Notch receptor processing • I-kappaB kinase/NF-kappaB cascade • JNK cascade • fibroblast growth factor receptor signaling pathway • female gonad development • gene expression • ubiquitin homeostasis • viral reproduction • cellular membrane organization • RNA metabolic process • mRNA metabolic process • endosomal transport • virion assembly • viral protein processing • cytokine-mediated signaling pathway • hypothalamus gonadotrophin-releasing hormone neuron development • viral reproductive process • negative regulation of transforming growth factor beta receptor signaling pathway • anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process • negative regulation of type I interferon production • positive regulation of type I interferon production • cellular response to stress • 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 • 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 • negative regulation of apoptotic process • positive regulation of I-kappaB kinase/NF-kappaB cascade • innate immune response • positive regulation of transcription from RNA polymerase II promoter • egress of virus within host cell • 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 • fat pad development • regulation of transcription from RNA polymerase II promoter in response to hypoxia • nucleotide-binding oligomerization domain containing signaling pathway • cellular response to hypoxia • seminiferous tubule development • energy homeostasis • 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

[1]

[2]

Ubiquitin is a protein that is encoded by the UBC gene in humans.^[1]^[2]^[3]

Interactions[edit]

Ubiquitin C has been shown to interact with:

C21orf59,^[4]
SCNN1A,^[5]^[6]
SCNN1G,^[5]^[6]
Parkin (ligase),^[7]^[8]
P70-S6 Kinase 1,^[9]
TRAF6,^[10]^[11]^[12]^[13]^[14]
HDAC3,^[15]
SFPQ,^[16]
S100A10,^[17]
NOTCH1,^[18]
HIF1A,^[19]^[20]^[21]
Epidermal growth factor receptor,^[22]^[23]^[24]
E2F1,^[25]
Basigin,^[26]
IRAK1,^[10]^[13]^[27]^[28]
NFE2L2,^[29]^[30]
RIPK1,^[10]^[14]^[31]^[32]^[33]
Mdm2,^[34]^[35]^[36]
Kappa Opioid receptor,^[37]
NUAK1,^[38]
BIRC2,^[32]^[39]^[40]
Thyroid hormone receptor alpha,^[15]
Sp1 transcription factor,^[41]
SMURF2,^[42]^[43]
MARK4,^[38]
Cdk1,^[15]
PCNA^[44]^[45]^[46]
P53.^[22]^[34]^[35]^[36]^[47]^[48]^[49]^[50]
Mothers against decapentaplegic homolog 3,^[51]^[52]

References[edit]

^ 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".
^ Kim, W.; Bennett, E. J.; Huttlin, E. L.; Guo, A.; Li, J.; Possemato, A.; Sowa, M. E.; Rad, R. et al. (2011). "Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome". Molecular Cell 44 (2): 325–340. doi:10.1016/j.molcel.2011.08.025. PMC 3200427. PMID 21906983. |displayauthors= suggested (help) edit
^ ^a ^b Boulkroun, Sheerazed; Ruffieux-Daidié Dorothée, Vitagliano Jean-Jacques, Poirot Olivier, Charles Roch-Philippe, Lagnaz Dagmara, Firsov Dmitri, Kellenberger Stephan, Staub Olivier (Oct. 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. doi:10.1152/ajprenal.00001.2008. ISSN 0363-6127. PMID 18632802. Unknown parameter |unused_data= ignored (help)
^ ^a ^b Raikwar, Nandita S; Thomas Christie P (May. 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. doi:10.1152/ajprenal.00339.2007. ISSN 0363-6127. PMC 2424110. PMID 18322022.
^ Yu, Furong; Zhou Jianhua (Jul. 2008). "Parkin is ubiquitinated by Nrdp1 and abrogates Nrdp1-induced oxidative stress". Neurosci. Lett. (Ireland) 440 (1): 4–8. doi:10.1016/j.neulet.2008.05.052. ISSN 0304-3940. PMID 18541373.
^ Kawahara, Kohichi; Hashimoto Makoto, Bar-On Pazit, Ho Gilbert J, Crews Leslie, Mizuno Hideya, Rockenstein Edward, Imam Syed Z, Masliah Eliezer (Mar. 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. doi:10.1074/jbc.M710418200. ISSN 0021-9258. PMID 18195004.
^ Panasyuk, Ganna; Nemazanyy Ivan, Filonenko Valeriy, Gout Ivan (May. 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. doi:10.1016/j.bbrc.2008.02.016. PMID 18279656.
^ ^a ^b ^c Newton, Kim; Matsumoto Marissa L, Wertz Ingrid E, Kirkpatrick Donald S, Lill Jennie R, Tan Jenille, Dugger Debra, Gordon Nathaniel, Sidhu Sachdev S, Fellouse Frederic A, Komuves Laszlo, French Dorothy M, Ferrando Ronald E, Lam Cynthia, Compaan Deanne, Yu Christine, Bosanac Ivan, Hymowitz Sarah G, Kelley Robert F, Dixit Vishva M (Aug. 2008). "Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies". Cell (United States) 134 (4): 668–78. doi:10.1016/j.cell.2008.07.039. PMID 18724939.
^ Chen, Lu; Dong Wei, Zou Tingting, Ouyang Lu, He Guoqing, Liu Yingle, Qi Yipeng (Aug. 2008). "Protein phosphatase 4 negatively regulates LPS cascade by inhibiting ubiquitination of TRAF6". FEBS Lett. (Netherlands) 582 (19): 2843–9. doi:10.1016/j.febslet.2008.07.014. ISSN 0014-5793. PMID 18634786.
^ Lamothe, Betty; Campos Alejandro D, Webster William K, Gopinathan Ambily, Hur Lana, Darnay Bryant G (Sep. 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. doi:10.1074/jbc.M802749200. ISSN 0021-9258. PMC 2529010. PMID 18617513.
^ ^a ^b Conze, Dietrich B; Wu Chuan-Jin, Thomas James A, Landstrom Allison, Ashwell Jonathan D (May. 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. doi:10.1128/MCB.02098-07. PMC 2423148. PMID 18347055.
^ ^a ^b Ma, Qi; Zhou Li, Shi Huili, Huo Keke (Jun. 2008). "NUMBL interacts with TAB2 and inhibits TNFalpha and IL-1beta-induced NF-kappaB activation". Cell. Signal. (England) 20 (6): 1044–51. doi:10.1016/j.cellsig.2008.01.015. ISSN 0898-6568. PMID 18299187.
^ ^a ^b ^c Tan, Fengwei; Lu Lifang, Cai Yun, Wang Jinglan, Xie Yunfei, Wang Lin, Gong Yanhua, Xu Bing-E, Wu Jun, Luo Ying, Qiang Boqin, Yuan Jiangang, Sun Xiaoqing, Peng Xiaozhong (Jul. 2008). "Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells". Proteomics (Germany) 8 (14): 2885–96. doi:10.1002/pmic.200700887. PMID 18655026.
^ Stelzl, Ulrich; Worm Uwe, Lalowski Maciej, Haenig Christian, Brembeck Felix H, Goehler Heike, Stroedicke Martin, Zenkner Martina, Schoenherr Anke, Koeppen Susanne, Timm Jan, Mintzlaff Sascha, Abraham Claudia, Bock Nicole, Kietzmann Silvia, Goedde Astrid, Toksöz Engin, Droege Anja, Krobitsch Sylvia, Korn Bernhard, Birchmeier Walter, Lehrach Hans, Wanker Erich E (Sep. 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell (United States) 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. ISSN 0092-8674. PMID 16169070. Unknown parameter |unused_data= ignored (help)
^ He, Kai-Li; Deora Arunkumar B, Xiong Huabao, Ling Qi, Weksler Babette B, Niesvizky Ruben, Hajjar Katherine A (Jul. 2008). "Endothelial cell annexin A2 regulates polyubiquitination and degradation of its binding partner S100A10/p11". J. Biol. Chem. (United States) 283 (28): 19192–200. doi:10.1074/jbc.M800100200. ISSN 0021-9258. PMC 2443646. PMID 18434302.
^ Chastagner, Patricia; Israël Alain, Brou Christel (2008). "AIP4/Itch regulates Notch receptor degradation in the absence of ligand". In Wölfl, Stefan. PLoS ONE (United States) 3 (7): e2735. doi:10.1371/journal.pone.0002735. PMC 2444042. PMID 18628966.
^ André, Helder; Pereira Teresa S (Oct. 2008). "Identification of an alternative mechanism of degradation of the hypoxia-inducible factor-1alpha". J. Biol. Chem. (United States) 283 (43): 29375–84. doi:10.1074/jbc.M805919200. ISSN 0021-9258. PMC 2662024. PMID 18694926.
^ Park, Young-Kwon; Ahn Dae-Ro, Oh Myoungsuk, Lee Taekyoung, Yang Eun Gyeong, Son Miwon, Park Hyunsung (Jul. 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. doi:10.1124/mol.108.045278. PMID 18426857.
^ Kim, Bu Yeon; Kim Hyungsoo, Cho Eun Jung, Youn Hong Duk (Feb. 2008). "Nur77 upregulates HIF-alpha by inhibiting pVHL-mediated degradation". Exp. Mol. Med. (Korea (South)) 40 (1): 71–83. doi:10.3858/emm.2008.40.1.71. ISSN 1226-3613. PMC 2679322. PMID 18305400.
^ ^a ^b Sehat, Bita; Andersson Sandra, Girnita Leonard, Larsson Olle (Jul. 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. doi:10.1158/0008-5472.CAN-07-6364. PMID 18632619.
^ Pennock, Steven; Wang Zhixiang (May. 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. doi:10.1128/MCB.01809-07. PMC 2293090. PMID 18316398.
^ Umebayashi, Kyohei; Stenmark Harald, Yoshimori Tamotsu (Aug. 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. doi:10.1091/mbc.E07-10-0988. PMC 2488299. PMID 18508924.
^ Zhou, Fangfang; Zhang Long, Wang Aijun, Song Bo, Gong Kai, Zhang Lihai, Hu Min, Zhang Xiufang, Zhao Nanming, Gong Yandao (May. 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. doi:10.1074/jbc.M706136200. ISSN 0021-9258. PMID 18367454.
^ Wang, Wen-Juan; Li Qing-Quan, Xu Jing-Da, Cao Xi-Xi, Li Hai-Xia, Tang Feng, Chen Qi, Yang Jin-Ming, Xu Zu-De, Liu Xiu-Ping (2008). "Interaction between CD147 and P-glycoprotein and their regulation by ubiquitination in breast cancer cells". Chemotherapy (Switzerland) 54 (4): 291–301. doi:10.1159/000151225. PMID 18689982.
^ Xiao, Hui; Qian Wen, Staschke Kirk, Qian Youcun, Cui Grace, Deng Li, Ehsani Mariam, Wang Xiliang, Qian Yue-Wei, Chen Zhijian J, Gilmour Raymond, Jiang Zhengfan, Li Xiaoxia (May. 2008). "Pellino 3b negatively regulates interleukin-1-induced TAK1-dependent NF kappaB activation". J. Biol. Chem. (United States) 283 (21): 14654–64. doi:10.1074/jbc.M706931200. ISSN 0021-9258. PMC 2386918. PMID 18326498.
^ Windheim, Mark; Stafford Margaret, Peggie Mark, Cohen Philip (Mar. 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. doi:10.1128/MCB.02380-06. PMC 2258775. PMID 18180283.
^ Shibata, Tatsuhiro; Ohta Tsutomu, Tong Kit I, Kokubu Akiko, Odogawa Reiko, Tsuta Koji, Asamura Hisao, Yamamoto Masayuki, Hirohashi Setsuo (Sep. 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. doi:10.1073/pnas.0806268105. PMC 2533230. PMID 18757741.
^ Patel, Rachana; Maru Girish (Jun. 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. doi:10.1016/j.freeradbiomed.2008.02.006. ISSN 0891-5849. PMID 18358244.
^ Varfolomeev, Eugene; Goncharov Tatiana, Fedorova Anna V, Dynek Jasmin N, Zobel Kerry, Deshayes Kurt, Fairbrother Wayne J, Vucic Domagoj (Sep. 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. doi:10.1074/jbc.C800128200. ISSN 0021-9258. PMID 18621737.
^ ^a ^b Bertrand, Mathieu J M; Milutinovic Snezana, Dickson Kathleen M, Ho Wai Chi, Boudreault Alain, Durkin Jon, Gillard John W, Jaquith James B, Morris Stephen J, Barker Philip A (Jun. 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. doi:10.1016/j.molcel.2008.05.014. PMID 18570872.
^ Liao, Wentao; Xiao Qi, Tchikov Vladimir, Fujita Ken-ichi, Yang Wensheng, Wincovitch Stephen, Garfield Susan, Conze Dietrich, El-Deiry Wafik S, Schütze Stefan, Srinivasula Srinivasa M (May. 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. doi:10.1016/j.cub.2008.04.017. ISSN 0960-9822. PMC 2587165. PMID 18450452. Unknown parameter |unused_data= ignored (help)
^ ^a ^b Ivanchuk, Stacey M; Mondal Soma, Rutka James T (Jun. 2008). "p14ARF interacts with DAXX: effects on HDM2 and p53". Cell Cycle (United States) 7 (12): 1836–50. doi:10.4161/cc.7.12.6025. PMID 18583933.
^ ^a ^b Song, Min Sup; Song Su Jung, Kim So Yeon, Oh Hyun Jung, Lim Dae-Sik (Jul. 2008). "The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex". EMBO J. (England) 27 (13): 1863–74. doi:10.1038/emboj.2008.115. PMC 2486425. PMID 18566590.
^ ^a ^b Yang, Wensheng; Dicker David T, Chen Jiandong, El-Deiry Wafik S (Mar. 2008). "CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing MDM2". Cell Cycle (United States) 7 (5): 670–82. doi:10.4161/cc.7.5.5701. PMID 18382127.
^ Li, Jian-Guo; Haines Dale S, Liu-Chen Lee-Yuan (Apr. 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. doi:10.1124/mol.107.042846. PMID 18212250.
^ ^a ^b Al-Hakim, Abdallah K; Zagorska Anna, Chapman Louise, Deak Maria, Peggie Mark, Alessi Dario R (Apr. 2008). "Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains". Biochem. J. (England) 411 (2): 249–60. doi:10.1042/BJ20080067. PMID 18254724. Unknown parameter |unused_data= ignored (help)
^ Didelot, C; Lanneau D, Brunet M, Bouchot A, Cartier J, Jacquel A, Ducoroy P, Cathelin S, Decologne N, Chiosis G, Dubrez-Daloz L, Solary E, Garrido C (May. 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. doi:10.1038/cdd.2008.5. ISSN 1350-9047. PMID 18239673.
^ Sekine, Keiko; Takubo Kohei, Kikuchi Ryo, Nishimoto Michie, Kitagawa Masayuki, Abe Fuminori, Nishikawa Kiyohiro, Tsuruo Takashi, Naito Mikihiko (Apr. 2008). "Small molecules destabilize cIAP1 by activating auto-ubiquitylation". J. Biol. Chem. (United States) 283 (14): 8961–8. doi:10.1074/jbc.M709525200. ISSN 0021-9258. PMID 18230607.
^ Wang, Yi-Ting; Chuang Jian-Ying, Shen Meng-Ru, Yang Wen-Bin, Chang Wen-Chang, Hung Jan-Jong (Jul. 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. doi:10.1016/j.jmb.2008.05.043. PMID 18572193.
^ Carpentier, Isabelle; Coornaert Beatrice, Beyaert Rudi (Oct. 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. doi:10.1016/j.bbrc.2008.07.103. PMID 18671942.
^ Lee, Yeon Sook; Han Jung Min, Son Sung Hwa, Choi Jin Woo, Jeon Eun Ju, Bae Suk-Chul, Park Young In, Kim Sunghoon (Jul. 2008). "AIMP1/p43 downregulates TGF-beta signaling via stabilization of smurf2". Biochem. Biophys. Res. Commun. (United States) 371 (3): 395–400. doi:10.1016/j.bbrc.2008.04.099. PMID 18448069.
^ Motegi, Akira; Liaw Hung-Jiun, Lee Kyoo-Young, Roest Henk P, Maas Alex, Wu Xiaoli, Moinova Helen, Markowitz Sanford D, Ding Hao, Hoeijmakers Jan H J, Myung Kyungjae (Aug. 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. doi:10.1073/pnas.0805685105. PMC 2518831. PMID 18719106.
^ Unk, Ildiko; Hajdú Ildikó, Fátyol Károly, Hurwitz Jerard, Yoon Jung-Hoon, Prakash Louise, Prakash Satya, Haracska Lajos (Mar. 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. doi:10.1073/pnas.0800563105. PMC 2268824. PMID 18316726.
^ Brun, Jan; Chiu Roland, Lockhart Katherine, Xiao Wei, Wouters Bradly G, Gray Douglas A (2008). "hMMS2 serves a redundant role in human PCNA polyubiquitination". BMC Mol. Biol. (England) 9: 24. doi:10.1186/1471-2199-9-24. PMC 2263069. PMID 18284681.
^ Han, Jung Min; Park Bum-Joon, Park Sang Gyu, Oh Young Sun, Choi So Jung, Lee Sang Won, Hwang Soon-Kyung, Chang Seung-Hee, Cho Myung-Haing, Kim Sunghoon (Aug. 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. doi:10.1073/pnas.0800297105. PMC 2516205. PMID 18695251.
^ Abe, Yoshinori; Oda-Sato Eri, Tobiume Kei, Kawauchi Keiko, Taya Yoichi, Okamoto Koji, Oren Moshe, Tanaka Nobuyuki (Mar. 2008). "Hedgehog signaling overrides p53-mediated tumor suppression by activating Mdm2". Proc. Natl. Acad. Sci. U.S.A. (United States) 105 (12): 4838–43. doi:10.1073/pnas.0712216105. PMC 2290789. PMID 18359851.
^ Zhang, Zhuo; Zhang Ruiwen (Mar. 2008). "Proteasome activator PA28 gamma regulates p53 by enhancing its MDM2-mediated degradation". EMBO J. (England) 27 (6): 852–64. doi:10.1038/emboj.2008.25. PMC 2265109. PMID 18309296.
^ Dohmesen, Christoph; Koeppel Max, Dobbelstein Matthias (Jan. 2008). "Specific inhibition of Mdm2-mediated neddylation by Tip60". Cell Cycle (United States) 7 (2): 222–31. doi:10.4161/cc.7.2.5185. PMID 18264029.
^ Stolfi, Carmine; Fina Daniele, Caruso Roberta, Caprioli Flavio, Fantini Massimo Claudio, Rizzo Angelamaria, Sarra Massimiliano, Pallone Francesco, Monteleone Giovanni (Jun. 2008). "Mesalazine negatively regulates CDC25A protein expression and promotes accumulation of colon cancer cells in S phase". Carcinogenesis (England) 29 (6): 1258–66. doi:10.1093/carcin/bgn122. PMID 18495657.
^ Guo, Xing; Ramirez Alejandro, Waddell David S, Li Zhizhong, Liu Xuedong, Wang Xiao-Fan (Jan. 2008). "Axin and GSK3- control Smad3 protein stability and modulate TGF- signaling". Genes Dev. (United States) 22 (1): 106–20. doi:10.1101/gad.1590908. ISSN 0890-9369. PMC 2151009. PMID 18172167.

Interactions[edit]

References[edit]

Further reading[edit]