Property Summary

NCBI Gene PubMed Count 48
PubMed Score 34.10
PubTator Score 8.88

Knowledge Summary

Patent

No data available

TINX Plot

  Disease (2)

Disease Target Count P-value
acute quadriplegic myopathy 1157 6.9e-08
ovarian cancer 8491 1.4e-03
Disease Target Count Z-score Confidence
Obesity 616 3.5 1.7
Sigmoid colon cancer 3 3.075 1.5

Expression

  Differential Expression (2)

Disease log2 FC p
acute quadriplegic myopathy 1.117 6.9e-08
ovarian cancer 1.500 1.4e-03

Gene RIF (25)

PMID Text
22921402 the critical role of S5b/PSMD5 in negative regulation of proteasome by TNF-alpha/NFkappaB and provide insights into proteasome inhibition in human disease.
14614829 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
14564014 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
14557625 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
14550573 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
14528301 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
14528300 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
14527406 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
12970355 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
12920286 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
12914693 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
12859895 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
12840737 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
12830140 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
12809610 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
12808466 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
12808465 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
12750511 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
12719574 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
12419264 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
12167863 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
10893419 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
9846577 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
9811770 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication
9079628 HIV-1 Vif binds to the cellular cytidine deaminase APOBEC3G and targets it for degradation through an interaction with the proteasome, thereby inhibiting APOBEC3G mediated restriction of HIV-1 replication

AA Sequence

MAAQALALLREVARLEAPLEELRALHSVLQAVPLNELRQQAAELRLGPLFSLLNENHREKTTLCVSILER      1 - 70
LLQAMEPVHVARNLRVDLQRGLIHPDDSVKILTLSQIGRIVENSDAVTEILNNAELLKQIVYCIGGENLS     71 - 140
VAKAAIKSLSRISLTQAGLEALFESNLLDDLKSVMKTNDIVRYRVYELIIEISSVSPESLNYCTTSGLVT    141 - 210
QLLRELTGEDVLVRATCIEMVTSLAYTHHGRQYLAQEGVIDQISNIIVGADSDPFSSFYLPGFVKFFGNL    211 - 280
AVMDSPQQICERYPIFVEKVFEMIESQDPTMIGVAVDTVGILGSNVEGKQVLQKTGTRFERLLMRIGHQS    281 - 350
KNAPVELKIRCLDAISSLLYLPPEQQTDDLLRMTESWFSSLSRDPLELFRGISSQPFPELHCAALKVFTA    351 - 420
IANQPWAQKLMFNSPGFVEYVVDRSVEHDKASKDAKYELVKALANSKTIAEIFGNPNYLRLRTYLSEGPY    421 - 490
YVKPVSTTAVEGAE                                                            491 - 504
//

Text Mined References (54)

PMID Year Title
27107012 2016 Pooled-matrix protein interaction screens using Barcode Fusion Genetics.
26496610 2015 A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
25416956 2014 A proteome-scale map of the human interactome network.
24275569 2014 An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
22921402 2012 Role of S5b/PSMD5 in proteasome inhibition caused by TNF-?/NF?B in higher eukaryotes.
22901813 2012 Cancer vulnerabilities unveiled by genomic loss.
22814378 2012 N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
22223895 2012 Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-?-acetylation features.
21516116 2011 Next-generation sequencing to generate interactome datasets.
21269460 2011 Initial characterization of the human central proteome.
19490896 2009 Assembly pathway of the Mammalian proteasome base subcomplex is mediated by multiple specific chaperones.
19412159 2009 Chaperone-mediated pathway of proteasome regulatory particle assembly.
19217412 2009 Hsm3/S5b participates in the assembly pathway of the 19S regulatory particle of the proteasome.
18029348 2008 Toward a confocal subcellular atlas of the human proteome.
16341674 2005 Transcriptome analysis of human gastric cancer.
16189514 2005 Towards a proteome-scale map of the human protein-protein interaction network.
15489334 2004 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
15164053 2004 DNA sequence and analysis of human chromosome 9.
15029244 2004 Mammalian Cdh1/Fzr mediates its own degradation.
14702039 2004 Complete sequencing and characterization of 21,243 full-length human cDNAs.
14614829 2003 The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G.
14564014 2003 Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex.
14557625 2003 The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity.
14550573 2003 Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits.
14528301 2003 HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation.
14528300 2003 The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif.
14527406 2003 HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability.
12970355 2003 The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity.
12920286 2003 Virology. Weapons of mutational destruction.
12914693 2003 Death by deamination: a novel host restriction system for HIV-1.
12859895 2003 Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.
12840737 2003 Good to CU.
12830140 2003 DNA deamination: not just a trigger for antibody diversification but also a mechanism for defense against retroviruses.
12809610 2003 DNA deamination mediates innate immunity to retroviral infection.
12808466 2003 Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts.
12808465 2003 The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA.
12791267 2003 Prophase destruction of Emi1 by the SCF(betaTrCP/Slimb) ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase.
12750511 2003 Hypermutation of HIV-1 DNA in the absence of the Vif protein.
12719574 2003 Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions.
12665801 2003 Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.
12477932 2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.
12419264 2002 The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing.
12167863 2002 Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein.
11285280 2001 Anaphase-promoting complex/cyclosome-dependent proteolysis of human cyclin A starts at the beginning of mitosis and is not subject to the spindle assembly checkpoint.
10893419 2000 Degradation of HIV-1 integrase by the N-end rule pathway.
10625621 2000 Mapping subunit contacts in the regulatory complex of the 26 S proteasome. S2 and S5b form a tetramer with ATPase subunits S4 and S7.
9846577 1998 Evidence for a newly discovered cellular anti-HIV-1 phenotype.
9811770 1998 An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein.
9079628 1997 HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation.
8811196 1996 Structure and functions of the 20S and 26S proteasomes.
8125911 1994 A 26 S protease subunit that binds ubiquitin conjugates.
7584044 1994 Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1.
7559544 1995 Molecular cloning and expression of a 26 S protease subunit enriched in dileucine repeats.
1317798 1992 Demonstration that a human 26S proteolytic complex consists of a proteasome and multiple associated protein components and hydrolyzes ATP and ubiquitin-ligated proteins by closely linked mechanisms.