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Methods for Quantification of in vivo Changes in Protein Ubiquitination following Proteasome and Deubiquitinase Inhibition


ABSTRACT: Data from MassIVE, [[http://proteomics.ucsd.edu/ProteoSAFe/status.jsp?task=TRANCHE-MSV000077546 MSV000077546]]. Experiment: exp2_rep1_Proteome, file: K20110724_NU_Jurkat_rep1B_Proteome_SILAC_L-no_M-17uMPR619_H-5uMMG13217uM_SCXFxn24.mzml. Published as part of Mol Cell Proteomics. 2012 May;11(5):148-59 . From the Abstract: {{i}} ... The introduction of antibodies that specifically recognize peptides with lysine residues that harbor a di-glycine remnant (K-eplison-GG) following tryptic digestion has dramatically improved the ability to enrich and identify ubiquitination sites from cellular lysates. We used this enrichment technique to study the effects of proteasome inhibition by MG-132 and deubiquitinase inhibition by PR-619 on ubiquitination sites in human Jurkat cells by quantitative high performance mass spectrometry. ... {{/i}}

INSTRUMENT(S): Instrument

ORGANISM(S): Human, Human_adenovirus_54, Human_adenovirus_a, Human_adenovirus_b, Human_adenovirus_c, Human_adenovirus_d, Human_adenovirus_e, Human_adenovirus_f, Human_adenovirus_g, Human_astrovirus, Human_bocavirus, Human_bocavirus_2, Human_bocavirus_3, Human_bocavirus_4, Human_coronavirus_229e, Human_coronavirus_hku1, Human_coronavirus_nl63, Human_coronavirus_oc43, Human_cosavirus_a, Human_cosavirus_b, Human_cosavirus_d, Human_cosavirus_e, Human_enteric_coronavirus_4408, Human_enterovirus_100, Human_enterovirus_a, Human_enterovirus_b, Human_enterovirus_c, Human_enterovirus_d, Human_erythrovirus_v9, Human_herpesvirus_1, Human_herpesvirus_2, Human_herpesvirus_3, Human_herpesvirus_4_type_1, Human_herpesvirus_4_type_2, Human_herpesvirus_5, Human_herpesvirus_6a, Human_herpesvirus_6b, Human_herpesvirus_7, Human_herpesvirus_8_type_p, Human_immunodeficiency_virus_1, Human_immunodeficiency_virus_2, Human_metapneumovirus, Human_papillomavirus_fa75_ki88_03, Human_papillomavirus_rtrx7, Human_papillomavirus_type_10, Human_papillomavirus_type_100, Human_papillomavirus_type_101, Human_papillomavirus_type_103, Human_papillomavirus_type_104, Human_papillomavirus_type_105, Human_papillomavirus_type_108, Human_papillomavirus_type_109, Human_papillomavirus_type_112, Human_papillomavirus_type_113, Human_papillomavirus_type_16, Human_papillomavirus_type_24, Human_papillomavirus_type_26, Human_papillomavirus_type_32, Human_papillomavirus_type_34, Human_papillomavirus_type_4, Human_papillomavirus_type_41, Human_papillomavirus_type_48, Human_papillomavirus_type_49, Human_papillomavirus_type_5, Human_papillomavirus_type_50, Human_papillomavirus_type_53, Human_papillomavirus_type_60, Human_papillomavirus_type_63, Human_papillomavirus_type_6b, Human_papillomavirus_type_7, Human_papillomavirus_type_71, Human_papillomavirus_type_88, Human_papillomavirus_type_9, Human_papillomavirus_type_92, Human_papillomavirus_type_96, Human_papillomavirus_type_98, Human_papillomavirus_type_99, Human_papillomavirus___1, Human_papillomavirus___18, Human_papillomavirus___2, Human_papillomavirus___54, Human_papillomavirus___61, Human_papillomavirus___cand90, Human_parainfluenza_virus_1, Human_parainfluenza_virus_2, Human_parainfluenza_virus_3, Human_parechovirus, Human_parvovirus_4, Human_parvovirus_b19, Human_picobirnavirus, Human_respiratory_syncytial_virus, Human_rhinovirus_a, Human_rhinovirus_b, Human_rhinovirus_c, Human_tmev_like_cardiovirus, Human_t_lymphotropic_virus_1, Human_t_lymphotropic_virus_2, Human_t_lymphotropic_virus_4

DISEASE(S): Not Available

SUBMITTER: Udeshi ND, et al.  

PROVIDER: GPM11210018396 | GPMDB |

REPOSITORIES: GPMDB

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Publications

Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.

Udeshi Namrata D ND   Mani D R DR   Eisenhaure Thomas T   Mertins Philipp P   Jaffe Jacob D JD   Clauser Karl R KR   Hacohen Nir N   Carr Steven A SA  

Molecular & cellular proteomics : MCP 20120414 5


Ubiquitination plays a key role in protein degradation and signal transduction. Ubiquitin is a small protein modifier that is adducted to lysine residues by the combined function of E1, E2, and E3 enzymes and is removed by deubiquitinating enzymes. Characterization of ubiquitination sites is important for understanding the role of this modification in cellular processes and disease. However, until recently, large-scale characterization of endogenous ubiquitination sites has been hampered by the  ...[more]

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