Ubiquitin Ligase Table
The Ubiquitin Ligase Table provides a list of E3 ubiquitin ligases, along with their substrates (when known), and corresponding references. This table was generated using PhosphoSitePlus®, Cell Signaling Technology’s protein modification resource.
Ubiquitin Ligase Table
|AMFR||KAI1||AMFR is also known as gp78. AMFR is an integral ER membrane protein and functions in ER-associated degradation (ERAD). AMFR has been found to promote tumor metastasis through ubiquitination of the metastasis supressor, KAI1.||(1)|
|APC/Cdc20||Cyclin B||The anaphase promoting complex/cyclosome (APC/C) is a multiprotein complex with E3 ligase activity that regulates cell cycle progression through degradation of cyclins and other mitotic proteins. APC is found in a complex with CDC20, CDC27, SPATC1, and TUBG1.||(2)|
|APC/Cdh1||Cdc20, Cyclin B, Cyclin A, Aurora A, Securin, Skp2, Claspin||The anaphase promoting complex/cyclosome (APC/C) is a multiprotein complex with E3 ligase activity that regulates cell cycle progression through degradation of cyclins and other mitotic proteins. The APC/C-Cdh1 dimeric complex is activated during anaphase and telophase, and remains active until onset of the next S phase.||(3, 4, 5, 6, 7)|
|C6orf157||Cyclin B||C6orf157 is also known as H10BH. C6orf157 is an E3 ubiquitin ligase that has been shown to ubiquitinate cyclin B.||(8)|
|Cbl||Cbl-b and c-Cbl are members of the Cbl family of adaptor proteins that are highly expressed in hematopoietic cells. Cbl proteins possess E3 ubiquitin ligase activity that downregulates numerous signaling proteins and RTKs in several pathways such as EGFR, T cell and B cell receptors, and integrin receptors. Cbl proteins play an important role in T cell receptor signaling pathways.||(9, 10)|
|CBLL1||CDH1||CBLL1 is also known as Hakai. CBLL1 is an E3 ubiquitin ligase that ubiquitinates the phosphorylated form of E-Cadherin, causing its degradation and loss of cell-cell adhesions.||(11)|
|CHFR||PLK1, Aurora A||CHFR is an E3 ubiquitin ligase that functions as a mitotic stress checkpoint protein that delays entry into mitosis in response to stress. CHFR has been shown to ubiquitinate and degrade the kinases PLK1 and Aurora A.||(12, 13)|
|CHIP||HSP70/90, iNOS, Runx1, LRRK2||CHIP is an E3 ubiquitin ligase that acts as a co-chaperone protein and interacts with several heat shock proteins, including HSP70 and HSP90, as well as the non-heat shock proteins iNOS, Runx1 and LRRK2.||(14, 15, 16, 17)|
|DTL (Cdt2)||p21||DTL is an E3 ubiquitin ligase that complexes with Cullin4 and DDB1, and promotes p21 degradation after UV damage.||(18)|
|E6-AP||p53, Dlg||E6-AP is also known as UBE3A. E6-AP is a HECT domain E3 ubiquitin ligase that interacts with Hepatitis C virus (HCV) core protein and targets it for degradation. The HCV core protein is central to packaging viral DNA and other cellular processes. E6-AP also interacts with the E6 protein of the human papillomavirus types 16 and 18, and targets the p53 tumor-suppressor protein for degradation.||(19)|
|HACE1||HACE1 is an E3 ubiquitin ligase and tumor suppressor. Aberrant methylation of HACE1 is frequently found in Wilms’ tumors and colorectal cancer.||(20)|
|HECTD1||HECTD1 is an ubiquitin E3 ligase required for neural tube closure and normal development of the mesenchyme.||(21)|
|HECTD2||HECTD2 is a probable E3 ubiquitin ligase and may act as a succeptibility gene for neurodegeneration and prion disease.||(22)|
|HECTD3||HECTD3 is a probable E3 ubiquitin ligase and may play a role in cytoskeletal regulation, actin remodeling, and vesicle trafficking.||(23)|
|HECW1||DVL1, mutant SOD1, p53||HECW1 is also known as NEDL1. HECW1 interacts with p53 and the Wnt signaling protein DVL1, and may play a role in p53-mediated cell death in neurons.||(24, 25)|
|HECW2||p73||HECW2 is also known as NEDL2. HECW2 ubiquitinates p73, which is a p53 family member. Ubiquitination of p73 increases protein stability.||(26)|
|HERC2||RNF8||HERC2 belongs to a family of E3 ubiquitin ligases involved in membrane trafficking events. HERC2 plays a role in the DNA damage response through interaction with RNF8.||(27)|
|HERC3||HERC3 belongs to a family of E3 ubiquitin ligases involved in membrane trafficking events. HERC3 interacts with hPLIC-1 and hPLIC-2 and localizes to the late endosomes and lysosomes.||(28)|
|HERC4||HERC4 belongs to a family of E3 ubiquitin ligases involved in membrane trafficking events. HERC4 is highly expressed in testis and may play a role in spermatogenesis.||(29)|
|HERC5||HERC5 belongs to a family of E3 ubiquitin ligases involved in membrane trafficking events. HERC5 is induced by interferon and other pro-inflammatory cytokines and plays a role in interferon-induced ISG15 conjugation during the innate immune response.||(30, 31)|
|HUWE1||N-Myc, C-Myc, p53, Mcl-1, TopBP1||HUWE1 is also known as Mule. HUWE1 is a HECT domain E3 ubiquitin ligase that regulates degradation of Mcl-1 and therefore regulates DNA damage-induced apoptosis. HUWE1 also controls neuronal differentiation by destabilizing N-Myc, and regulates p53-dependent and independent tumor suppression via ARF.||(32)|
|HYD||CHK2||HYD is also known as EDD or UBR5. HYD is a regulator of the DNA damage response and is overexpressed in many forms of cancer.||(33)|
|ITCH||MKK4, RIP2, Foxp3||ITCH plays a role in T cell receptor activation and signaling through ubiquitination of multiple proteins including MKK4, RIP2 and Foxp3. Loss of ITCH function leads to an abberrant immune response and T helper cell differentiation.||(34, 35, 36)|
|LNX1||NUMB||LNX1 is an E3 ubiquitin ligase that plays a role in cell fate determination during embryogenesis through regulation of NUMB, the negative regulator of Notch signaling.||(37)|
|mahogunin||Mahogunin is an E3 ubiquitin ligase involved in melanocortin signaling. Loss of mahogunin function leads to neurodegeneration and loss of pigmentation, and may be the mechanism of action in prion disease.||(38, 39)|
|MARCH-I||HLA-DRβ||MARCH1 is an E3 ubiquitin ligase found on antigen presenting cells (APCs). MARCH1 ubiquitinates MHC class II proteins and downregulates their cell surface expression.||(40)|
|MARCH-II||MARCH-II is a member of the MARCH family of E3 ubiquitin ligases. It associates with syntaxin6 in the endosomes and helps to regulate vesicle trafficking.||(41)|
|MARCH-III||MARCH-III is a member of the MARCH family of E3 ubiquitin ligases. MARCH-III associates with syntaxin6 in the endosomes and helps to regulate vesicle trafficking.||(42)|
|MARCH-IV||MHC class I||MARCH-IV is a member of the MARCH family of E3 ubiquitin ligases. MARCH-IV ubiquitinates MHC class I proteins and downregulates their cell surface expression.||(43)|
|MARCH-VI||MARCH-VI is also known as TEB4 and is a member of the MARCH family of E3 ubiquitin ligases. It localizes to the endoplasmic reticulum and participates in ER-associated protein degradation.||(44)|
|MARCH-VII||gp190||MARCH-VII is also known as axotrophin. MARCH-VII was originally identified as a neural stem cell gene, but has since been shown to play a role in LIF signaling in T lymphocytes through degradation of the LIF-receptor subunit, gp190.||(45)|
|MARCH-VIII||B7-2, MHC class II||MARCH-VIII is also known as c-MIR. MARCH-VIII causes the ubiquitination/degradation of B7-2, which is a co-stimulatory molecule for antigen presentation. MARCH-VIII has also been shown to ubiquitinate MHC class II proteins.||(46)|
|MARCH-X||MARCH-X is also known as RNF190. MARCH-X is a member of the MARCH family of E3 ubiquitin ligases. The putative role of MARCH-X is not currently known.|
|MDM2||p53||MDM2, an E3 ubiquitin ligase for p53, plays a central role in regulation of the stability of p53. Akt-mediated phosphorylation of MDM2 at Ser166 and Ser186 increases its interaction with p300, allowing MDM2-mediated ubiquitination and degradation of p53.||(47)|
|MEKK1||c-Jun, Erk||MEKK1 is a well known protein kinase of the STE11 family. MEKK1 phosphorylates and activates MKK4/7, which in turn activates JNK1/2/3. MEKK1 contains a RING finger domain and exhibits E3 ubiquitin ligase activity toward c-Jun and Erk.||(48, 49)|
|MIB1||Delta, Jagged||Mindbomb homolog 1 (MIB1) is an E3 ligase that facilitates the ubiquitination and subsequent endocytosis of the Notch ligands, Delta and Jagged.||(50)|
|MIB2||Delta, Jagged||Mind Bomb 2 (MIB2) is an E3 ligase that positively regulates Notch Signaling. MIB2 has been shown to play a role in myotube differentiation and muscle stability. MIB2 ubiquitinates NMDAR subunits to help regulate synaptic plasticity in neurons.||(51, 52, 53)|
|MycBP2||Fbxo45, TSC2||MycBP2 is an E3 ubiquitin ligase also known as PAM. MycBP2 associates with Fbxo45 to play a role in neuronal development. MycBP2 also regulates the mTOR pathway through ubiquitination of TSC2.||(54, 55)|
|NEDD4||NEDD4 is an E3 ubiquitin ligase highly expressed in the early mouse embryonic central nervous system. NEDD4 downregulates both neuronal voltage-gated Na+ channels (NaVs) and epithelial Na+ channels (ENaCs) in response to increased intracellular Na+ concentrations.||(56, 57)|
|NEDD4L||Smad2||NEDD4L is an E3 ubiquitin ligase highly expressed in the early mouse embryonic central nervous system. NEDD4L has been shown to negatively regulate TGF-β signaling by targeting Smad2 for degradation.||(58)|
|Parkin||Parkin is an E3 ubiquitin ligase that has been shown to be a key regulator of the autophagy pathway. Mutations in Parkin can lead to Parkinson’s Disease.||(59)|
|PELI1||TRIP, IRAK||PELI1 is an E3 ubiquitin ligase that plays a role in Toll-like Receptor (TLR3 and TLR4) signaling to NF-κB via the TRIP adaptor protein. PELI1 has also been shown to ubiquitinate IRAK.||(60, 61)|
|Pirh2||TP53||Pirh2 is also known as RCHY1. Pirh2 is a RING domain E3 ubiquitin ligase. Pirh2 binds p53 and promotes proteosomal degradation of p53 independent of MDM2. Pirh2 gene expression is controlled by p53, making this interaction part of an autoinhibitory feedback loop.||(62, 63)|
|PJA1||ELF||PJA1 is also known as PRAJA. PJA1 plays a role in downregulating TGF-β signaling in gastric cancer via ubiquitination of the SMAD4 adaptor protein ELF.||(64)|
|PJA2||PJA2 is an E3 ubiquitin ligase found in neuronal synapses. The exact role and substrates of PJA2 are unclear.||(65)|
|RFFL||p53||RFFL is also known as CARP2 and is an E3 ubiquitin ligase that inhibits endosome recycling. RFFL also degrades p53 through stabilization of MDM2.||(66, 67)|
|RFWD2||MTA1, p53, FoxO1||RFWD2 is also known as COP1. RFWD2 is an E3 ubiquitin ligase that ubiquitinates several proteins involved in the DNA damage response and apoptosis including MTA1, p53, and FoxO1.||(68, 69, 70)|
|Rictor||SGK1||Rictor interacts with Cullin1-Rbx1 to form an E3 ubiquitin ligase complex, and promotes ubiquitination and degradation of SGK1.|
|RNF5||JAMP, paxillin||RNF5 is also known as RMA5. RNF5 plays a role in ER-associated degradation of misfolded proteins and ER stress response through ubiquitination of JAMP. RNF5 also plays a role in cell motility and has been shown to ubiquitinate paxillin.||(71, 72)|
|RNF8||H2A,H2AX||RNF8 is a RING domain E3 ubiquitin ligase that plays a role in the repair of damaged chromosomes. RNF8 ubiquitinates Histone H2A and H2A.X at double-strand breaks (DSBs) which recruits 53BP1 and BRCA1 repair proteins.||(73)|
|RNF19||SOD1||RNF19 is also known as Dorfin. Accumulation and aggregation of mutant SOD1 leads to ALS disease. RNF19 ubiquitinates mutant SOD1 protein, causing a decrease in neurotoxicity.||(74)|
|RNF20||Histone H2B||RNF20 is also known as BRE1. RNF20 is an E3 ubiquitin ligase that monoubiquitinates Histone H2B. H2B ubiquitination is associated with areas of active transcription.||(75)|
|RNF34||Caspase-8, -10||RNF34 is also known as RFI. RNF34 inhibits death receptor mediated apoptosis through ubiquitination/degradation of caspase-8 and -10.||(76)|
|RNF40||Histone H2B||RNF40 is also known as BRE1-B. RNF40 forms a protein complex with RNF20 resulting in the ubiquitination of Histone H2B. H2B ubiquitination is associated with areas of active transcription.||(77)|
|RNF125||RNF125 is also known as TRAC-1. RNF125 has been shown to positively regulate T cell activation.||(78)|
|RNF128||RNF128 is also known as GRAIL. RNF128 promotes T cell anergy and may play a role in actin cytoskeletal organization in T cell/APC interactions.||(79)|
|RNF138||TCF/LEF||RNF138 is also known as NARF. RNF138 is associated with Nemo-like Kinase (NLK) and suppresses Wnt/β-Catenin signaling through ubiquitination/degradation of TCF/LEF.||(80)|
|RNF168||H2A, H2A.X||RNF168 is an E3 ubiquitin ligase that helps protect genome integrity by working together with RNF8 to ubiquitinate Histone H2A and H2A.X at DNA double-strand breaks (DSB).||(81)|
|SCF/β-TrCP||IκBα, Wee1, Cdc25A, β-Catenin||SCF/β-TrCP is an E3 ubiquitin ligase complex composed of SCF (SKP1-CUL1-F-box protein) and the substrate recognition component, β-TrCP (also known as BTRC). SCF/β-TrCP mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction, and transcription. SCF/β-TrCP also regulates the stability of β-catenin and participates in Wnt signaling.||(82, 83, 84, 85)|
|SCF/FBW7||Cyclin E, c-Myc, c-Jun||SCF/FBW7 is an E3 ubiquitin ligase complex composed of SCF (SKP1-CUL1-F-box protein) and the substrate recognition component, FBW7. SCF/FBW7 mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction, and transcription. Target proteins for SCF/FBW7 include the phosphorylated forms of c-Myc, Cyclin E, Notch intracellular domain (NICD), and c-Jun. Defects in FBXW7 may be a cause of breast cancer.||(86, 87, 88)|
|SCF/Skp2||p27, p21, Fox01||SCF/Skp2 is an E3 ubiquitin ligase complex composed of SCF (SKP1-CUL1-F-box protein) and the substrate recognition component, Skp2. SCF/Skp2 mediates the ubiquitination of proteins involved in cell cycle progression (specifically the G1/S transition), signal transduction and transcription. Target proteins for SCF/Skp2 include the phosphorylated forms of p27Kip1, p21Waf1/Cip1, and FoxO1.||(89, 90)|
|SHPRH||PCNA||SHPRH is an E3 ubiquitin ligase that plays a role in DNA replication through ubiquitination of PCNA. PCNA ubiquitination prevents genomic instability from stalled replication forks after DNA damage.||(91)|
|SIAH1||β-catenin, Bim, TRB3||SIAH1 is an E3 ubiquitin ligase that plays a role in inhibition of Wnt signaling through ubiquitination of β-catenin. SIAH1 has also been shown to promote apoptosis through upregulation of Bim, and to ubiquitinate the signaling adaptor protein TRB3.||(92, 93, 94)|
|SIAH2||HIPK2, PHD1/3||SIAH2 is an E3 ubiquitin ligase that plays a role in hypoxia through ubiquitination and degradation of HIPK2. SIAH2 also ubiquitinates PHD1/3, which regulates levels of HIF-1α in response to hypoxia.||(95, 96)|
|SMURF1||Smads||SMURF1 is an E3 ubiquitin ligase that interacts with BMP pathway Smad effectors, leading to Smad protein ubiquitination and degradation. Smurf1 negatively regulates osteoblast differentiation and bone formation in vivo.||(97, 98)|
|SMURF2||Smads, Mad2||SMURF2 is an E3 ubiquitin ligase that interacts with Smads from both the BMP and TGF-β pathways. SMURF2 also regulates the mitotic spindle checkpoint through ubiquitination of Mad2.||(99, 100)|
|TOPORS||p53, NKX3.1||TOPORS is an E3 ubiquitin ligase and a SUMO ligase. TOPORS ubiquitinates and sumoylates p53, which regulates p53 stability. TOPORS has also been shown to ubiquitinate the tumor supressor NKX3.1.||(101, 102)|
|TRAF6||NEMO, Akt1||TRAF6 is an E3 ubiquitin ligase that functions as an adaptor protein in IL-1R, CD40, and TLR signaling. TRAF6 promotes NF-κB signaling through K63 polyubiquitination of IKK, resulting in IKK activation. TRAF6 has also been shown to ubiquitinate Akt1, causing its translocation to the cell membrane.||(103, 104)|
|TRAF7||TRAF7 is an E3 ubiquitin ligase and SUMO ligase that functions as an adaptor protein in TNF Receptor and TLR signaling. TRAF7 has been shown to be capable of self-ubiquitination and plays a role in apoptosis via MEKK3-mediated activation of NF-κB.||(105)|
|TRIM63||Troponin I, MyBP-C, MyLC1/2||TRIM63 is also known as Murf-1. TRIM63 is a muscle-specific E3 ubiquitin ligase whose expression is upregulated during muscle atrophy. TRIM63 has been shown to ubiquitinate several important muscle proteins including troponin I, MyBP-C, and MyLC1/2.||(106)|
|UBE3B||UBE3B is an E3 ubiquitin ligase identified through sequence analysis. The specific substrates and cellular function of UBE3B is currently unknown.||(107)|
|UBE3C||UBE3C is an E3 ubiquitin ligase also known as KIAA10. UBE3C is highly expressed in muscle and may interact with the transcriptional regulator TIP120B.||(108)|
|UBR1||UBR1 is an E3 ubiquitin ligase responsible for proteasomal degradation of misfolded cytoplasmic proteins. UBR1 has also been shown to be a ubiquitin ligase of the N-end rule proteolytic pathway, which regulates degradation of short-lived proteins.||(109, 110)|
|UBR2||Histone H2A||UBR2 is an E3 ubiquitin ligase that has been shown to ubiquitinate histone H2A, resulting in transcriptional silencing. UBR2 is also part of the N-end rule proteolytic pathway.||(111, 112)|
|UHRF2||PCNP||UHRF2 is also known as NIRF. UHRF2 is a nuclear protein that may regulate cell cycle progression through association with Chk2. UHRF2 also ubiquitinates PCNP and has been shown to play a role in degradation of nuclear aggregates containing polyglutamine repeats.||(113, 114, 115)|
|VHL||HIF-1α||VHL is the substrate recognition component of the ECV (Elongin B/C, Cullen-2, VHL) E3 ubiquitin ligase complex responsible for degradation of the transcription factor HIF-1α. Ubiquitination and degradation of HIF-1α takes place only during periods of normoxia, but not during hypoxia, thereby playing a central role in the regulation of gene expression by oxygen.||(116)|
|WWP1||ErbB4||WWP1 is an E3 ubiquitin ligase commonly found to be overexpressed in breast cancer. WWP1 has been shown to ubiquitinate and degrade ErbB4. Interestingly, the WWP1 homolog in C. elegans was found to increase life expectancy in response to dietary restriction.||(117, 118)|
|WWP2||Oct-4||WWP2 is an E3 ubiquitin ligase that has been shown to ubiquitinate/degrade the stem cell pluripotency factor Oct-4. WWP2 also ubiquitinates the transcription factor EGR2 to inhibit activation-induced T cell death.||(119, 120)|
|ZNRF1||ZNRF1 is an E3 ubiquitin ligase highly expressed in neuronal cells. ZNRF1 is found in synaptic vesicle membranes and may regulate neuronal transmissions and plasticity.||(121)|
We would like to thank Prof. Wenyi Wei, Beth Israel Deaconess Medical Center, Harvard Medical School, for contributing to this table.
- Tsai YC, Mendoza A, Mariano JM, Zhou M, Kostova Z, Chen B, Veenstra T, Hewitt SM, Helman LJ, Khanna C, Weissman AM (2007) The ubiquitin ligase gp78 promotes sarcoma metastasis by targeting KAI1 for degradation. Nat. Med. 13(12), 1504–9.
- Ban KH, Torres JZ, Miller JJ, Mikhailov A, Nachury MV, Tung JJ, Rieder CL, Jackson PK (2007) The END network couples spindle pole assembly to inhibition of the anaphase-promoting complex/cyclosome in early mitosis. Dev. Cell 13(1), 29–42.
- Lukas C, Sørensen CS, Kramer E, Santoni-Rugiu E, Lindeneg C, Peters JM, Bartek J, Lukas J (1999) Accumulation of cyclin B1 requires E2F and cyclin-A-dependent rearrangement of the anaphase-promoting complex. Nature 401(6755), 815–8.
- Hagting A, Den Elzen N, Vodermaier HC, Waizenegger IC, Peters JM, Pines J (2002) Human securin proteolysis is controlled by the spindle checkpoint and reveals when the APC/C switches from activation by Cdc20 to Cdh1. J. Cell Biol. 157(7), 1125–37.
- Pfleger CM, Lee E, Kirschner MW (2001) Substrate recognition by the Cdc20 and Cdh1 components of the anaphase-promoting complex. Genes Dev. 15(18), 2396–407.
- Wei W, Ayad NG, Wan Y, Zhang GJ, Kirschner MW, Kaelin WG (2004) Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex. Nature 428(6979), 194–8.
- Gao D, Inuzuka H, Korenjak M, Tseng A, Wu T, Wan L, Kirschner M, Dyson N, Wei W (2009) Cdh1 regulates cell cycle through modulating the claspin/Chk1 and the Rb/E2F1 pathways. Mol. Biol. Cell 20(14), 3305–16.
- Kobirumaki F, Miyauchi Y, Fukami K, Tanaka H (2005) A novel UbcH10-binding protein facilitates the ubiquitinylation of cyclin B in vitro. J. Biochem. 137(2), 133–9.
- Huang F, Gu H (2008) Negative regulation of lymphocyte development and function by the Cbl family of proteins. Immunol. Rev. 224, 229–38.
- Thien CB, Langdon WY (1998) c-Cbl: a regulator of T cell receptor-mediated signalling. Immunol. Cell Biol. 76(5), 473–82.
- Fujita Y, Krause G, Scheffner M, Zechner D, Leddy HE, Behrens J, Sommer T, Birchmeier W (2002) Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex. Nat. Cell Biol. 4(3), 222–31.
- Bothos J, Summers MK, Venere M, Scolnick DM, Halazonetis TD (2003) The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form Lys63-linked polyubiquitin chains. Oncogene 22(46), 7101–7.
- Kwon YE, Kim YS, Oh YM, Seol JH (2009) Nuclear localization of Chfr is crucial for its checkpoint function. Mol. Cells 27(3), 359–63.
- Kundrat L, Regan L (2010) Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP. J. Mol. Biol. 395(3), 587–94.
- Chen L, Kong X, Fu J, Xu Y, Fang S, Hua P, Luo L, Yin Z (2009) CHIP facilitates ubiquitination of inducible nitric oxide synthase and promotes its proteasomal degradation. Cell. Immunol. 258(1), 38–43.
- Shang Y, Zhao X, Xu X, Xin H, Li X, Zhai Y, He D, Jia B, Chen W, Chang Z (2009) CHIP functions an E3 ubiquitin ligase of Runx1. Biochem. Biophys. Res. Commun. 386(1), 242–6.
- Ding X, Goldberg MS (2009) Regulation of LRRK2 stability by the E3 ubiquitin ligase CHIP. PLoS ONE 4(6), e5949.
- Abbas T, Sivaprasad U, Terai K, Amador V, Pagano M, Dutta A (2008) PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex. Genes Dev. 22(18), 2496–506.
- Shirakura M, Murakami K, Ichimura T, Suzuki R, Shimoji T, Fukuda K, Abe K, Sato S, Fukasawa M, Yamakawa Y, Nishijima M, Moriishi K, Matsuura Y, Wakita T, Suzuki T, Howley PM, Miyamura T, Shoji I (2007) E6AP ubiquitin ligase mediates ubiquitylation and degradation of hepatitis C virus core protein. J. Virol. 81(3), 1174–85.
- Zhang L, Anglesio MS, O'Sullivan M, Zhang F, Yang G, Sarao R, Mai PN, Cronin S, Hara H, Melnyk N, Li L, Wada T, Liu PP, Farrar J, Arceci RJ, Sorensen PH, Penninger JM (2007) The E3 ligase HACE1 is a critical chromosome 6q21 tumor suppressor involved in multiple cancers. Nat. Med. 13(9), 1060–9.
- Zohn IE, Anderson KV, Niswander L (2007) The Hectd1 ubiquitin ligase is required for development of the head mesenchyme and neural tube closure. Dev. Biol. 306(1), 208–21.
- Lloyd SE, Maytham EG, Pota H, Grizenkova J, Molou E, Uphill J, Hummerich H, Whitfield J, Alpers MP, Mead S, Collinge J (2009) HECTD2 is associated with susceptibility to mouse and human prion disease. PLoS Genet. 5(2), e1000383.
- Yu J, Lan J, Zhu Y, Li X, Lai X, Xue Y, Jin C, Huang H (2008) The E3 ubiquitin ligase HECTD3 regulates ubiquitination and degradation of Tara. Biochem. Biophys. Res. Commun. 367(4), 805–12.
- Miyazaki K, Fujita T, Ozaki T, Kato C, Kurose Y, Sakamoto M, Kato S, Goto T, Itoyama Y, Aoki M, Nakagawara A (2004) NEDL1, a novel ubiquitin-protein isopeptide ligase for dishevelled-1, targets mutant superoxide dismutase-1. J. Biol. Chem. 279(12), 11327–35.
- Li Y, Ozaki T, Kikuchi H, Yamamoto H, Ohira M, Nakagawara A (2008) A novel HECT-type E3 ubiquitin protein ligase NEDL1 enhances the p53-mediated apoptotic cell death in its catalytic activity-independent manner. Oncogene 27(26), 3700–9.
- Miyazaki K, Ozaki T, Kato C, Hanamoto T, Fujita T, Irino S, Watanabe K, Nakagawa T, Nakagawara A (2003) A novel HECT-type E3 ubiquitin ligase, NEDL2, stabilizes p73 and enhances its transcriptional activity. Biochem. Biophys. Res. Commun. 308(1), 106–13.
- Bekker-Jensen S, Rendtlew Danielsen J, Fugger K, Gromova I, Nerstedt A, Lukas C, Bartek J, Lukas J, Mailand N (2010) HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Nat. Cell Biol. 12(1), 80–6; sup pp 1.
- Hochrainer K, Kroismayr R, Baranyi U, Binder BR, Lipp J (2008) Highly homologous HERC proteins localize to endosomes and exhibit specific interactions with hPLIC and Nm23B. Cell. Mol. Life Sci. 65(13), 2105–17.
- Rodriguez CI, Stewart CL (2007) Disruption of the ubiquitin ligase HERC4 causes defects in spermatozoon maturation and impaired fertility. Dev. Biol. 312(2), 501–8.
- Dastur A, Beaudenon S, Kelley M, Krug RM, Huibregtse JM (2006) Herc5, an interferon-induced HECT E3 enzyme, is required for conjugation of ISG15 in human cells. J. Biol. Chem. 281(7), 4334–8.
- Wong JJ, Pung YF, Sze NS, Chin KC (2006) HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets. Proc. Natl. Acad. Sci. U.S.A. 103(28), 10735–40.
- Zhong Q, Gao W, Du F, Wang X (2005) Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis. Cell 121(7), 1085–95.
- Munoz MA, Saunders DN, Henderson MJ, Clancy JL, Russell AJ, Lehrbach G, Musgrove EA, Watts CK, Sutherland RL (2007) The E3 ubiquitin ligase EDD regulates S-phase and G(2)/M DNA damage checkpoints. Cell Cycle 6(24), 3070–7.
- Ahn YH, Kurie JM (2009) MKK4/SEK1 is negatively regulated through a feedback loop involving the E3 ubiquitin ligase itch. J. Biol. Chem. 284(43), 29399–404.
- Tao M, Scacheri PC, Marinis JM, Harhaj EW, Matesic LE, Abbott DW (2009) ITCH K63-ubiquitinates the NOD2 binding protein, RIP2, to influence inflammatory signaling pathways. Curr. Biol. 19(15), 1255–63.
- Su J, Liu YC (2010) Foxp3 positive regulatory T cells: a functional regulation by the E3 ubiquitin ligase Itch. Semin Immunopathol 32(2), 149–56.
- Nie J, McGill MA, Dermer M, Dho SE, Wolting CD, McGlade CJ (2002) LNX functions as a RING type E3 ubiquitin ligase that targets the cell fate determinant Numb for ubiquitin-dependent degradation. EMBO J. 21(1-2), 93–102.
- Pérez-Oliva AB, Olivares C, Jiménez-Cervantes C, García-Borrón JC (2009) Mahogunin ring finger-1 (MGRN1) E3 ubiquitin ligase inhibits signaling from melanocortin receptor by competition with Galphas. J. Biol. Chem. 284(46), 31714–25.
- Chakrabarti O, Hegde RS (2009) Functional depletion of mahogunin by cytosolically exposed prion protein contributes to neurodegeneration. Cell 137(6), 1136–47.
- Jabbour M, Campbell EM, Fares H, Lybarger L (2009) Discrete domains of MARCH1 mediate its localization, functional interactions, and posttranscriptional control of expression. J. Immunol. 183(10), 6500–12.
- Nakamura N, Fukuda H, Kato A, Hirose S (2005) MARCH-II is a syntaxin-6-binding protein involved in endosomal trafficking. Mol. Biol. Cell 16(4), 1696–710.
- Fukuda H, Nakamura N, Hirose S (2006) MARCH-III Is a novel component of endosomes with properties similar to those of MARCH-II. J. Biochem. 139(1), 137–45.
- Bartee E, Mansouri M, Hovey Nerenberg BT, Gouveia K, Früh K (2004) Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins. J. Virol. 78(3), 1109–20.
- Kreft SG, Wang L, Hochstrasser M (2006) Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI). J. Biol. Chem. 281(8), 4646–53.
- Szigyarto CA, Sibbons P, Williams G, Uhlen M, Metcalfe SM (2010) The E3 ligase axotrophin/MARCH-7: protein expression profiling of human tissues reveals links to adult stem cells. J. Histochem. Cytochem. 58(4), 301–8.
- Ohmura-Hoshino M, Matsuki Y, Aoki M, Goto E, Mito M, Uematsu M, Kakiuchi T, Hotta H, Ishido S (2006) Inhibition of MHC class II expression and immune responses by c-MIR. J. Immunol. 177(1), 341–54.
- Haupt Y, Maya R, Kazaz A, Oren M (1997) Mdm2 promotes the rapid degradation of p53. Nature 387(6630), 296–9.
- Lu Z, Xu S, Joazeiro C, Cobb MH, Hunter T (2002) The PHD domain of MEKK1 acts as an E3 ubiquitin ligase and mediates ubiquitination and degradation of ERK1/2. Mol. Cell 9(5), 945–56.
- Xia Y, Wang J, Xu S, Johnson GL, Hunter T, Lu Z (2007) MEKK1 mediates the ubiquitination and degradation of c-Jun in response to osmotic stress. Mol. Cell. Biol. 27(2), 510–7.
- Koo BK, Lim HS, Song R, Yoon MJ, Yoon KJ, Moon JS, Kim YW, Kwon MC, Yoo KW, Kong MP, Lee J, Chitnis AB, Kim CH, Kong YY (2005) Mind bomb 1 is essential for generating functional Notch ligands to activate Notch. Development 132(15), 3459–70.
- Koo BK, Yoon KJ, Yoo KW, Lim HS, Song R, So JH, Kim CH, Kong YY (2005) Mind bomb-2 is an E3 ligase for Notch ligand. J. Biol. Chem. 280(23), 22335–42.
- Carrasco-Rando M, Ruiz-Gómez M (2008) Mind bomb 2, a founder myoblast-specific protein, regulates myoblast fusion and muscle stability. Development 135(5), 849–57.
- Jurd R, Thornton C, Wang J, Luong K, Phamluong K, Kharazia V, Gibb SL, Ron D (2008) Mind bomb-2 is an E3 ligase that ubiquitinates the N-methyl-D-aspartate receptor NR2B subunit in a phosphorylation-dependent manner. J. Biol. Chem. 283(1), 301–10.
- Saiga T, Fukuda T, Matsumoto M, Tada H, Okano HJ, Okano H, Nakayama KI (2009) Fbxo45 forms a novel ubiquitin ligase complex and is required for neuronal development. Mol. Cell. Biol. 29(13), 3529–43.
- Han S, Witt RM, Santos TM, Polizzano C, Sabatini BL, Ramesh V (2008) Pam (Protein associated with Myc) functions as an E3 ubiquitin ligase and regulates TSC/mTOR signaling. Cell. Signal. 20(6), 1084–91.
- Dinudom A, Harvey KF, Komwatana P, Young JA, Kumar S, Cook DI (1998) Nedd4 mediates control of an epithelial Na+ channel in salivary duct cells by cytosolic Na+. Proc. Natl. Acad. Sci. U.S.A. 95(12), 7169–73.
- Goulet CC, Volk KA, Adams CM, Prince LS, Stokes JB, Snyder PM (1998) Inhibition of the epithelial Na+ channel by interaction of Nedd4 with a PY motif deleted in Liddle's syndrome. J. Biol. Chem. 273(45), 30012–7.
- Gao S, Alarcón C, Sapkota G, Rahman S, Chen PY, Goerner N, Macias MJ, Erdjument-Bromage H, Tempst P, Massagué J (2009) Ubiquitin ligase Nedd4L targets activated Smad2/3 to limit TGF-beta signaling. Mol. Cell 36(3), 457–68.
- Chin LS, Olzmann JA, Li L (2010) Parkin-mediated ubiquitin signalling in aggresome formation and autophagy. Biochem. Soc. Trans. 38(Pt 1), 144–9.
- Chang M, Jin W, Sun SC (2009) Peli1 facilitates TRIF-dependent Toll-like receptor signaling and proinflammatory cytokine production. Nat. Immunol. 10(10), 1089–95.
- Butler MP, Hanly JA, Moynagh PN (2007) Kinase-active interleukin-1 receptor-associated kinases promote polyubiquitination and degradation of the Pellino family: direct evidence for PELLINO proteins being ubiquitin-protein isopeptide ligases. J. Biol. Chem. 282(41), 29729–37.
- Leng RP, Lin Y, Ma W, Wu H, Lemmers B, Chung S, Parant JM, Lozano G, Hakem R, Benchimol S (2003) Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation. Cell 112(6), 779–91.
- Corcoran CA, Montalbano J, Sun H, He Q, Huang Y, Sheikh MS (2009) Identification and characterization of two novel isoforms of Pirh2 ubiquitin ligase that negatively regulate p53 independent of RING finger domains. J. Biol. Chem. 284(33), 21955–70.
- Mishra L, Katuri V, Evans S (2005) The role of PRAJA and ELF in TGF-beta signaling and gastric cancer. Cancer Biol. Ther. 4(7), 694–9.
- Yu P, Chen Y, Tagle DA, Cai T (2002) PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X chromosome gene abundantly expressed in brain. Genomics 79(6), 869–74.
- Coumailleau F, Das V, Alcover A, Raposo G, Vandormael-Pournin S, Le Bras S, Baldacci P, Dautry-Varsat A, Babinet C, Cohen-Tannoudji M (2004) Over-expression of Rififylin, a new RING finger and FYVE-like domain-containing protein, inhibits recycling from the endocytic recycling compartment. Mol. Biol. Cell 15(10), 4444–56.
- Yang W, Dicker DT, Chen J, El-Deiry WS (2008) CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing MDM2. Cell Cycle 7(5), 670–82.
- Li DQ, Ohshiro K, Reddy SD, Pakala SB, Lee MH, Zhang Y, Rayala SK, Kumar R (2009) E3 ubiquitin ligase COP1 regulates the stability and functions of MTA1. Proc. Natl. Acad. Sci. U.S.A. 106(41), 17493–8.
- Dornan D, Shimizu H, Mah A, Dudhela T, Eby M, O'rourke K, Seshagiri S, Dixit VM (2006) ATM engages autodegradation of the E3 ubiquitin ligase COP1 after DNA damage. Science 313(5790), 1122–6.
- Kato S, Ding J, Pisck E, Jhala US, Du K (2008) COP1 functions as a FoxO1 ubiquitin E3 ligase to regulate FoxO1-mediated gene expression. J. Biol. Chem. 283(51), 35464–73.
- Tcherpakov M, Delaunay A, Toth J, Kadoya T, Petroski MD, Ronai ZA (2009) Regulation of endoplasmic reticulum-associated degradation by RNF5-dependent ubiquitination of JNK-associated membrane protein (JAMP). J. Biol. Chem. 284(18), 12099–109.
- Didier C, Broday L, Bhoumik A, Israeli S, Takahashi S, Nakayama K, Thomas SM, Turner CE, Henderson S, Sabe H, Ronai Z (2003) RNF5, a RING finger protein that regulates cell motility by targeting paxillin ubiquitination and altered localization. Mol. Cell. Biol. 23(15), 5331–45.
- Mailand N, Bekker-Jensen S, Faustrup H, Melander F, Bartek J, Lukas C, Lukas J (2007) RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. Cell 131(5), 887–900.
- Sone J, Niwa J, Kawai K, Ishigaki S, Yamada S, Adachi H, Katsuno M, Tanaka F, Doyu M, Sobue G (2010) Dorfin ameliorates phenotypes in a transgenic mouse model of amyotrophic lateral sclerosis. J. Neurosci. Res. 88(1), 123–35.
- Shema E, Tirosh I, Aylon Y, Huang J, Ye C, Moskovits N, Raver-Shapira N, Minsky N, Pirngruber J, Tarcic G, Hublarova P, Moyal L, Gana-Weisz M, Shiloh Y, Yarden Y, Johnsen SA, Vojtesek B, Berger SL, Oren M (2008) The histone H2B-specific ubiquitin ligase RNF20/hBRE1 acts as a putative tumor suppressor through selective regulation of gene expression. Genes Dev. 22(19), 2664–76.
- Sasaki S, Watanabe T, Kobunai T, Konishi T, Nagase H, Sugimoto Y, Oka T, Nagawa H (2006) hRFI overexpressed in HCT116 cells modulates Bcl-2 family proteins when treated with 5-fluorouracil. Oncol. Rep. 15(5), 1293–8.
- Zhu B, Zheng Y, Pham AD, Mandal SS, Erdjument-Bromage H, Tempst P, Reinberg D (2005) Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation. Mol. Cell 20(4), 601–11.
- Giannini AL, Gao Y, Bijlmakers MJ (2008) T-cell regulator RNF125/TRAC-1 belongs to a novel family of ubiquitin ligases with zinc fingers and a ubiquitin-binding domain. Biochem. J. 410(1), 101–11.
- Schartner JM, Simonson WT, Wernimont SA, Nettenstrom LM, Huttenlocher A, Seroogy CM (2009) Gene related to anergy in lymphocytes (GRAIL) expression in CD4+ T cells impairs actin cytoskeletal organization during T cell/antigen-presenting cell interactions. J. Biol. Chem. 284(50), 34674–81.
- Yamada M, Ohnishi J, Ohkawara B, Iemura S, Satoh K, Hyodo-Miura J, Kawachi K, Natsume T, Shibuya H (2006) NARF, an nemo-like kinase (NLK)-associated ring finger protein regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF). J. Biol. Chem. 281(30), 20749–60.
- Doil C, Mailand N, Bekker-Jensen S, Menard P, Larsen DH, Pepperkok R, Ellenberg J, Panier S, Durocher D, Bartek J, Lukas J, Lukas C (2009) RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins. Cell 136(3), 435–46.
- Tan P, Fuchs SY, Chen A, Wu K, Gomez C, Ronai Z, Pan ZQ (1999) Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha. Mol. Cell 3(4), 527–33.
- Watanabe N, Arai H, Nishihara Y, Taniguchi M, Watanabe N, Hunter T, Osada H (2004) M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCFbeta-TrCP. Proc. Natl. Acad. Sci. U.S.A. 101(13), 4419–24.
- Busino L, Donzelli M, Chiesa M, Guardavaccaro D, Ganoth D, Dorrello NV, Hershko A, Pagano M, Draetta GF (2003) Degradation of Cdc25A by beta-TrCP during S phase and in response to DNA damage. Nature 426(6962), 87–91.
- Liu C, Kato Y, Zhang Z, Do VM, Yankner BA, He X (1999) beta-Trcp couples beta-catenin phosphorylation-degradation and regulates Xenopus axis formation. Proc. Natl. Acad. Sci. U.S.A. 96(11), 6273–8.
- Koepp DM, Schaefer LK, Ye X, Keyomarsi K, Chu C, Harper JW, Elledge SJ (2001) Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase. Science 294(5540), 173–7.
- Welcker M, Orian A, Jin J, Grim JE, Grim JA, Harper JW, Eisenman RN, Clurman BE (2004) The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation. Proc. Natl. Acad. Sci. U.S.A. 101(24), 9085–90.
- Wei W, Jin J, Schlisio S, Harper JW, Kaelin WG (2005) The v-Jun point mutation allows c-Jun to escape GSK3-dependent recognition and destruction by the Fbw7 ubiquitin ligase. Cancer Cell 8(1), 25–33.
- Huang H, Regan KM, Wang F, Wang D, Smith DI, van Deursen JM, Tindall DJ (2005) Skp2 inhibits FOXO1 in tumor suppression through ubiquitin-mediated degradation. Proc. Natl. Acad. Sci. U.S.A. 102(5), 1649–54.
- Carrano AC, Eytan E, Hershko A, Pagano M (1999) SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat. Cell Biol. 1(4), 193–9.
- Motegi A, Liaw HJ, Lee KY, Roest HP, Maas A, Wu X, Moinova H, Markowitz SD, Ding H, Hoeijmakers JH, Myung K (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. 105(34), 12411–6.
- Fukushima T, Zapata JM, Singha NC, Thomas M, Kress CL, Krajewska M, Krajewski S, Ronai Z, Reed JC, Matsuzawa S (2006) Critical function for SIP, a ubiquitin E3 ligase component of the beta-catenin degradation pathway, for thymocyte development and G1 checkpoint. Immunity 24(1), 29–39.
- Wen YY, Yang ZQ, Song M, Li BL, Zhu JJ, Wang EH (2010) SIAH1 induced apoptosis by activation of the JNK pathway and inhibited invasion by inactivation of the ERK pathway in breast cancer cells. Cancer Sci. 101(1), 73–9.
- Zhou Y, Li L, Liu Q, Xing G, Kuai X, Sun J, Yin X, Wang J, Zhang L, He F (2008) E3 ubiquitin ligase SIAH1 mediates ubiquitination and degradation of TRB3. Cell. Signal. 20(5), 942–8.
- Calzado MA, de la Vega L, Möller A, Bowtell DD, Schmitz ML (2009) An inducible autoregulatory loop between HIPK2 and Siah2 at the apex of the hypoxic response. Nat. Cell Biol. 11(1), 85–91.
- Nakayama K, Frew IJ, Hagensen M, Skals M, Habelhah H, Bhoumik A, Kadoya T, Erdjument-Bromage H, Tempst P, Frappell PB, Bowtell DD, Ronai Z (2004) Siah2 regulates stability of prolyl-hydroxylases, controls HIF1alpha abundance, and modulates physiological responses to hypoxia. Cell 117(7), 941–52.
- Zhu H, Kavsak P, Abdollah S, Wrana JL, Thomsen GH (1999) A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation. Nature 400(6745), 687–93.
- Yamashita M, Ying SX, Zhang GM, Li C, Cheng SY, Deng CX, Zhang YE (2005) Ubiquitin ligase Smurf1 controls osteoblast activity and bone homeostasis by targeting MEKK2 for degradation. Cell 121(1), 101–13.
- Zhang Y, Chang C, Gehling DJ, Hemmati-Brivanlou A, Derynck R (2001) Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase. Proc. Natl. Acad. Sci. U.S.A. 98(3), 974–9.
- Osmundson EC, Ray D, Moore FE, Gao Q, Thomsen GH, Kiyokawa H (2008) The HECT E3 ligase Smurf2 is required for Mad2-dependent spindle assembly checkpoint. J. Cell Biol. 183(2), 267–77.
- Yang X, Li H, Zhou Z, Wang WH, Deng A, Andrisani O, Liu X (2009) Plk1-mediated phosphorylation of Topors regulates p53 stability. J. Biol. Chem. 284(28), 18588–92.
- Guan B, Pungaliya P, Li X, Uquillas C, Mutton LN, Rubin EH, Bieberich CJ (2008) Ubiquitination by TOPORS regulates the prostate tumor suppressor NKX3.1. J. Biol. Chem. 283(8), 4834–40.
- Yang WL, Wang J, Chan CH, Lee SW, Campos AD, Lamothe B, Hur L, Grabiner BC, Lin X, Darnay BG, Lin HK (2009) The E3 ligase TRAF6 regulates Akt ubiquitination and activation. Science 325(5944), 1134–8.
- Deng L, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen ZJ (2000) Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 103(2), 351–61.
- Xu LG, Li LY, Shu HB (2004) TRAF7 potentiates MEKK3-induced AP1 and CHOP activation and induces apoptosis. J. Biol. Chem. 279(17), 17278–82.
- Cohen S, Brault JJ, Gygi SP, Glass DJ, Valenzuela DM, Gartner C, Latres E, Goldberg AL (2009) During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation. J. Cell Biol. 185(6), 1083–95.
- Gong TW, Huang L, Warner SJ, Lomax MI (2003) Characterization of the human UBE3B gene: structure, expression, evolution, and alternative splicing. Genomics 82(2), 143–52.
- You J, Wang M, Aoki T, Tamura TA, Pickart CM (2003) Proteolytic targeting of transcriptional regulator TIP120B by a HECT domain E3 ligase. J. Biol. Chem. 278(26), 23369–75.
- Eisele F, Wolf DH (2008) Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1. FEBS Lett. 582(30), 4143–6.
- Tasaki T, Kwon YT (2007) The mammalian N-end rule pathway: new insights into its components and physiological roles. Trends Biochem. Sci. 32(11), 520–8.
- An JY, Kim EA, Jiang Y, Zakrzewska A, Kim DE, Lee MJ, Mook-Jung I, Zhang Y, Kwon YT (2010) UBR2 mediates transcriptional silencing during spermatogenesis via histone ubiquitination. Proc. Natl. Acad. Sci. U.S.A. 107(5), 1912–7.
- Tasaki T, Zakrzewska A, Dudgeon DD, Jiang Y, Lazo JS, Kwon YT (2009) The substrate recognition domains of the N-end rule pathway. J. Biol. Chem. 284(3), 1884–95.
- Li Y, Mori T, Hata H, Homma Y, Kochi H (2004) NIRF induces G1 arrest and associates with Cdk2. Biochem. Biophys. Res. Commun. 319(2), 464–8.
- Mori T, Li Y, Hata H, Kochi H (2004) NIRF is a ubiquitin ligase that is capable of ubiquitinating PCNP, a PEST-containing nuclear protein. FEBS Lett. 557(1-3), 209–14.
- Iwata A, Nagashima Y, Matsumoto L, Suzuki T, Yamanaka T, Date H, Deoka K, Nukina N, Tsuji S (2009) Intranuclear degradation of polyglutamine aggregates by the ubiquitin-proteasome system. J. Biol. Chem. 284(15), 9796–803.
- Ivan M, Kondo K, Yang H, Kim W, Valiando J, Ohh M, Salic A, Asara JM, Lane WS, Kaelin WG (2001) HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing. Science 292(5516), 464–8.
- Li Y, Zhou Z, Alimandi M, Chen C (2009) WW domain containing E3 ubiquitin protein ligase 1 targets the full-length ErbB4 for ubiquitin-mediated degradation in breast cancer. Oncogene 28(33), 2948–58.
- Carrano AC, Liu Z, Dillin A, Hunter T (2009) A conserved ubiquitination pathway determines longevity in response to diet restriction. Nature 460(7253), 396–9.
- Xu H, Wang W, Li C, Yu H, Yang A, Wang B, Jin Y (2009) WWP2 promotes degradation of transcription factor OCT4 in human embryonic stem cells. Cell Res. 19(5), 561–73.
- Chen A, Gao B, Zhang J, McEwen T, Ye SQ, Zhang D, Fang D (2009) The HECT-type E3 ubiquitin ligase AIP2 inhibits activation-induced T-cell death by catalyzing EGR2 ubiquitination. Mol. Cell. Biol. 29(19), 5348–56.
- Araki T, Milbrandt J (2003) ZNRF proteins constitute a family of presynaptic E3 ubiquitin ligases. J. Neurosci. 23(28), 9385–94.
created November 2010