PDBsum entry: 1fbv

Ligase

PDB-id

1fbv


	Asymmetric unit

Contents

Description

Header details

Protein chains

Ligands

SER-ASP-GLY-PTR-
THR-PRO-GLU-PRO-
ALA

SO4 ×5

Metal ions

_ZN ×2

* Residue conservation analysis

Tools

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Clefts Calculation

		Biological unit, hexamer (as deduced by PQS)

PDB id:

1fbv

Name:

Ligase

Title:

Structure of a cbl-ubch7 complex: ring domain function in ubiquitin-protein ligases

Structure:

Signal transduction protein cbl. Chain: a. Engineered: yes. Zap-70 peptide. Chain: b. Engineered: yes. Ubiquitin-conjugating enzyme e12-18 kda ubch7. Chain: c. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: the peptide was chemically synthesized. Expression_system_taxid: 562

Biological unit:

Hexamer (from PQS)

UniProt:

Chain A: P22681 (CBL_HUMAN)

Seq:

Struc:


Seq:

Struc:


Seq:

Struc:


Seq:				906 a.a.

Struc:				388 a.a.

Chain C: P68036 (UB2L3_HUMAN)

Seq:

154 a.a.

Struc:

144 a.a.

Key:		PfamA domain
		Secondary structure			CATH domain

Enzyme class:

Chain C: E.C.6.3.2.19 [IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine (see diagram below)

Resolution:

2.90Å

R-factor:

0.227

R-free:

0.262

Authors:

N.Zheng,P.Wang,P.D.Jeffrey,N.P.Pavletich

Key ref:

N.Zheng et al. (2000). Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases.. Cell, 102, 533-539. [PubMed id: 10966114] [DOI: 10.1016/S0092-8674(00)00057-X]

Date:

17-Jul-00

Release date:

30-Aug-00

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Clefts

Surface

Enzyme reaction for E.C.6.3.2.19

ATP	+	ubiquitin	+	protein lysine	=	AMP	+	diphosphate	+	protein N-ubiquityllysine

Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Key reference

DOI no: 10.1016/S0092-8674(00)00057-X Cell 102:533-539 (2000)

PubMed id: 10966114

Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases.

N.Zheng, P.Wang, P.D.Jeffrey, N.P.Pavletich.

ABSTRACT

Ubiquitin-protein ligases (E3s) regulate diverse cellular processes by mediating protein ubiquitination. The c-Cbl proto-oncogene is a RING family E3 that recognizes activated receptor tyrosine kinases, promotes their ubiquitination by a ubiquitin-conjugating enzyme (E2) and terminates signaling. The crystal structure of c-Cbl bound to a cognate E2 and a kinase peptide shows how the RING domain recruits the E2. A comparison with a HECT family E3-E2 complex indicates that a common E2 motif is recognized by the two E3 families. The structure reveals a rigid coupling between the peptide binding and the E2 binding domains and a conserved surface channel leading from the peptide to the E2 active site, suggesting that RING E3s may function as scaffolds that position the substrate and the E2 optimally for ubiquitin transfer.

Selected figure(s)

Figure 4.
Figure 4. The RING Domain of c-Cbl and the HECT Domain of E6AP Recognize the Same Structural Elements of UbcH7The H1 helix, L1, and L2 loops of UbcH7 are colored in green, red, and yellow, respectively. Portions of the molecular surfaces of the RING domain of c-Cbl (left) and the HECT domain of E6AP (right) are shown as a white net. The Phe-63 residue of UbcH7 inserts its side chain into a groove formed by the E3 in both cases. (Prepared with the program GRASP; [25]) Figure 5.
Figure 5. c-Cbl Has a Conserved Surface Channel Leading from the Peptide to the E2 Active SiteOne side of the c-Cbl–UbcH7 complex is characterized by a surface channel formed by residues that are solvent exposed and generally conserved (Lys-78, Asn-79, Ser-80, Arg-148, Arg-149, Lys-153, Asp-275, Glu-276, Lys-278, Ala-279, Arg-280, Gln-267, Leu-370, Glu-373, Met-374, and Lys-382). The molecular surfaces of c-Cbl and UbcH7 are colored in green and blue, respectively. On c-Cbl, the surface of the residues completely conserved in human c-Cbl, human cbl-b, human cbl-c, C. elegans sli-1, and Drosophila cbl are colored in yellow. The surface of the UbcH7 active-site cysteine is colored orange. The channel is outlined by three solid red lines. The right panel shows that the molecular surface of the complex opposite to the side containing the channel is not conserved. The view on the left has an orientation similar to that of Figure 1A.

The above figures are reprinted by permission from Cell Press: Cell (2000, 102, 533-539) copyright 2000.

Figures were selected by an automated process.

Literature references that cite this PDB file's key reference

PubMed id Reference

19557013 A.G.Eldridge, and T.O'Brien (2010).
Therapeutic strategies within the ubiquitin proteasome system.

Cell Death Differ, 17, 4.

20133640 I.Levin, C.Eakin, M.P.Blanc, R.E.Klevit, S.I.Miller, and P.S.Brzovic (2010).
Identification of an unconventional E3 binding surface on the UbcH5 ~ Ub conjugate recognized by a pathogenic bacterial E3 ligase.

Proc Natl Acad Sci U S A, 107, 2848-2853.

19740377 C.Simkus, A.Bhattacharyya, M.Zhou, T.D.Veenstra, and J.M.Jones (2009).
Correlation between recombinase activating gene 1 ubiquitin ligase activity and V(D)J recombination.

Immunology, 128, 206-217.

19712108 D.E.Christensen, and R.E.Klevit (2009).
Dynamic interactions of proteins in complex networks: identifying the complete set of interacting E2s for functional investigation of E3-dependent protein ubiquitination.

FEBS J, 276, 5381-5389.

19664228 E.A.Whitcomb, and A.Taylor (2009).
Ubiquitin control of S phase: a new role for the ubiquitin conjugating enzyme, UbcH7.

Cell Div, 4, 17.

18946090 E.A.Whitcomb, E.J.Dudek, Q.Liu, and A.Taylor (2009).
Novel control of S phase of the cell cycle by ubiquitin-conjugating enzyme H7.

Mol Biol Cell, 20, 1-9.

19101823 G.Liu, F.Forouhar, A.Eletsky, H.S.Atreya, J.M.Aramini, R.Xiao, Y.J.Huang, M.Abashidze, J.Seetharaman, J.Liu, B.Rost, T.Acton, G.T.Montelione, J.F.Hunt, and T.Szyperski (2009).
NMR and X-RAY structures of human E2-like ubiquitin-fold modifier conjugating enzyme 1 (UFC1) reveal structural and functional conservation in the metazoan UFM1-UBA5-UFC1 ubiquination pathway.

J Struct Funct Genomics, 10, 127-136.

PDB codes: 2k07 3e2g 3evx

19956605 I.Alchanati, C.Teicher, G.Cohen, V.Shemesh, H.M.Barr, P.Nakache, D.Ben-Avraham, A.Idelevich, I.Angel, N.Livnah, S.Tuvia, Y.Reiss, D.Taglicht, and O.Erez (2009).
The E3 ubiquitin-ligase Bmi1/Ring1A controls the proteasomal degradation of Top2alpha cleavage complex - a potentially new drug target.

PLoS One, 4, e8104.

19798438 J.Liu, and R.Nussinov (2009).
The mechanism of ubiquitination in the cullin-RING E3 ligase machinery: conformational control of substrate orientation.

PLoS Comput Biol, 5, e1000527.

19333736 J.M.Jones, and C.Simkus (2009).
The roles of the RAG1 and RAG2 "non-core" regions in V(D)J recombination and lymphocyte development.

Arch Immunol Ther Exp (Warsz), 57, 105-116.

18615712 J.Scheper, B.Oliva, J.Villà-Freixa, and T.M.Thomson (2009).
Analysis of electrostatic contributions to the selectivity of interactions between RING-finger domains and ubiquitin-conjugating enzymes.

Proteins, 74, 92.

19252184 M.E.French, B.R.Kretzmann, and L.Hicke (2009).
Regulation of the RSP5 Ubiquitin Ligase by an Intrinsic Ubiquitin-binding Site.

J Biol Chem, 284, 12071-12079.

19571318 M.L.Loh, D.S.Sakai, C.Flotho, M.Kang, M.Fliegauf, S.Archambeault, C.G.Mullighan, L.Chen, E.Bergstraesser, C.E.Bueso-Ramos, P.D.Emanuel, H.Hasle, J.P.Issa, M.M.van den Heuvel-Eibrink, F.Locatelli, J.Stary, M.Trebo, M.Wlodarski, M.Zecca, K.M.Shannon, and C.M.Niemeyer (2009).
Mutations in CBL occur frequently in juvenile myelomonocytic leukemia.

Blood, 114, 1859-1863.

19887645 M.Mo, S.B.Fleming, and A.A.Mercer (2009).
Cell cycle deregulation by a poxvirus partial mimic of anaphase-promoting complex subunit 11.

Proc Natl Acad Sci U S A, 106, 19527-19532.

19620960 M.Sanada, T.Suzuki, L.Y.Shih, M.Otsu, M.Kato, S.Yamazaki, A.Tamura, H.Honda, M.Sakata-Yanagimoto, K.Kumano, H.Oda, T.Yamagata, J.Takita, N.Gotoh, K.Nakazaki, N.Kawamata, M.Onodera, M.Nobuyoshi, Y.Hayashi, H.Harada, M.Kurokawa, S.Chiba, H.Mori, K.Ozawa, M.Omine, H.Hirai, H.Nakauchi, H.P.Koeffler, and S.Ogawa (2009).
Gain-of-function of mutated C-CBL tumour suppressor in myeloid neoplasms.

Nature, 460, 904-908.

19465916 Q.Yin, S.C.Lin, B.Lamothe, M.Lu, Y.C.Lo, G.Hura, L.Zheng, R.L.Rich, A.D.Campos, D.G.Myszka, M.J.Lenardo, B.G.Darnay, and H.Wu (2009).
E2 interaction and dimerization in the crystal structure of TRAF6.

Nat Struct Mol Biol, 16, 658-666.

PDB codes: 3hcs 3hct 3hcu

19531064 R.A.Herr, J.Harris, S.Fang, X.Wang, and T.H.Hansen (2009).
Role of the RING-CH domain of viral ligase mK3 in ubiquitination of non-lysine and lysine MHC I residues.

Traffic, 10, 1301-1317.

19690564 S.J.van Wijk, S.J.de Vries, P.Kemmeren, A.Huang, R.Boelens, A.M.Bonvin, and H.T.Timmers (2009).
A comprehensive framework of E2-RING E3 interactions of the human ubiquitin-proteasome system.

Mol Syst Biol, 5, 295.

20011534 W.Lee, Y.Zhang, K.Mukhyala, R.A.Lazarus, and Z.Zhang (2009).
Bi-directional SIFT predicts a subset of activating mutations.

PLoS One, 4, e8311.

19223579 W.Li, D.Tu, L.Li, T.Wollert, R.Ghirlando, A.T.Brunger, and Y.Ye (2009).
Mechanistic insights into active site-associated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2.

Proc Natl Acad Sci U S A, 106, 3722-3727.

PDB code: 3fsh

19851334 Y.Ye, and M.Rape (2009).
Building ubiquitin chains: E2 enzymes at work.

Nat Rev Mol Cell Biol, 10, 755-764.

18826954 A.Y.Kim, C.C.Bommeljé, B.E.Lee, Y.Yonekawa, L.Choi, L.G.Morris, G.Huang, A.Kaufman, R.J.Ryan, B.Hao, Y.Ramanathan, and B.Singh (2008).
SCCRO (DCUN1D1) Is an Essential Component of the E3 Complex for Neddylation.

J Biol Chem, 283, 33211-33220.

18304007 C.Kiel, P.Beltrao, and L.Serrano (2008).
Analyzing protein interaction networks using structural information.

Annu Rev Biochem, 77, 415-441.

18282298 D.R.Bosu, and E.T.Kipreos (2008).
Cullin-RING ubiquitin ligases: global regulation and activation cycles.

Cell Div, 3, 7.

18264111 D.T.Huang, M.Zhuang, O.Ayrault, and B.A.Schulman (2008).
Identification of conjugation specificity determinants unmasks vestigial preference for ubiquitin within the NEDD8 E2.

Nat Struct Mol Biol, 15, 280-287.

18410486 J.A.Nathan, S.Sengupta, S.A.Wood, A.Admon, G.Markson, C.Sanderson, and P.J.Lehner (2008).
The ubiquitin E3 ligase MARCH7 is differentially regulated by the deubiquitylating enzymes USP7 and USP9X.

Traffic, 9, 1130-1145.

18219319 K.Linke, P.D.Mace, C.A.Smith, D.L.Vaux, J.Silke, and C.L.Day (2008).
Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans.

Cell Death Differ, 15, 841-848.

PDB codes: 2vje 2vjf

18508924 K.Umebayashi, H.Stenmark, and T.Yoshimori (2008).
Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation.

Mol Biol Cell, 19, 3454-3462.

18583345 L.A.Durfee, M.L.Kelley, and J.M.Huibregtse (2008).
The Basis for Selective E1-E2 Interactions in the ISG15 Conjugation System.

J Biol Chem, 283, 23895-23902.

18398435 L.Micale, C.Fusco, B.Augello, L.M.Napolitano, E.T.Dermitzakis, G.Meroni, G.Merla, and A.Reymond (2008).
Williams-Beuren syndrome TRIM50 encodes an E3 ubiquitin ligase.

Eur J Hum Genet, 16, 1038-1049.

18958179 L.Volpon, M.J.Osborne, and K.L.Borden (2008).
NMR assignment of the arenaviral protein Z from Lassa fever virus.

Biomol NMR Assign, 2, 81-84.

18508925 O.Santt, T.Pfirrmann, B.Braun, J.Juretschke, P.Kimmig, H.Scheel, K.Hofmann, M.Thumm, and D.H.Wolf (2008).
The yeast GID complex, a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism.

Mol Biol Cell, 19, 3323-3333.

18784070 P.D.Mace, K.Linke, R.Feltham, F.R.Schumacher, C.A.Smith, D.L.Vaux, J.Silke, and C.L.Day (2008).
Structures of the cIAP2 RING Domain Reveal Conformational Changes Associated with Ubiquitin-conjugating Enzyme (E2) Recruitment.

J Biol Chem, 283, 31633-31640.

PDB codes: 3eb5 3eb6

18698375 P.J.Reynolds, J.R.Simms, and R.J.Duronio (2008).
Identifying determinants of cullin binding specificity among the three functionally different Drosophila melanogaster Roc proteins via domain swapping.

PLoS ONE, 3, e2918.

18316398 S.Pennock, and Z.Wang (2008).
A tale of two Cbls: interplay of c-Cbl and Cbl-b in epidermal growth factor receptor downregulation.

Mol Cell Biol, 28, 3020-3037.

18284575 T.Kubori, A.Hyakutake, and H.Nagai (2008).
Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes with distinct functions.

Mol Microbiol, 67, 1307-1319.

18344614 T.Omura, M.Kaneko, M.Onoguchi, S.Koizumi, M.Itami, M.Ueyama, Y.Okuma, and Y.Nomura (2008).
Novel functions of ubiquitin ligase HRD1 with transmembrane and proline-rich domains.

J Pharmacol Sci, 106, 512-519.

18241051 T.Omura, M.Kaneko, N.Tabei, Y.Okuma, and Y.Nomura (2008).
Immunohistochemical localization of a ubiquitin ligase HRD1 in murine brain.

J Neurosci Res, 86, 1577-1587.

19043414 Y.Sheng, R.C.Laister, A.Lemak, B.Wu, E.Tai, S.Duan, J.Lukin, M.Sunnerhagen, S.Srisailam, M.Karra, S.Benchimol, and C.H.Arrowsmith (2008).
Molecular basis of Pirh2-mediated p53 ubiquitylation.

Nat Struct Mol Biol, 15, 1334-1342.

PDB codes: 2jrj 2k2c 2k2d

18997779 Y.Zhu, H.Li, L.Hu, J.Wang, Y.Zhou, Z.Pang, L.Liu, and F.Shao (2008).
Structure of a Shigella effector reveals a new class of ubiquitin ligases.

Nat Struct Mol Biol, 15, 1302-1308.

PDB code: 3cvr

18492068 Z.Tang, C.M.Hecker, A.Scheschonka, and H.Betz (2008).
Protein interactions in the sumoylation cascade: lessons from X-ray structures.

FEBS J, 275, 3003-3015.

18485199 Z.Xu, E.Kohli, K.I.Devlin, M.Bold, J.C.Nix, and S.Misra (2008).
Interactions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymes.

BMC Struct Biol, 8, 26.

PDB code: 2oxq

17016439 A.Brauweiler, K.L.Lorick, J.P.Lee, Y.C.Tsai, D.Chan, A.M.Weissman, H.A.Drabkin, and R.M.Gemmill (2007).
RING-dependent tumor suppression and G2/M arrest induced by the TRC8 hereditary kidney cancer gene.

Oncogene, 26, 2263-2271.

17477837 B.T.Dye, and B.A.Schulman (2007).
Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins.

Annu Rev Biophys Biomol Struct, 36, 131-150.

17873885 D.E.Christensen, P.S.Brzovic, and R.E.Klevit (2007).
E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages.

Nat Struct Mol Biol, 14, 941-948.

17475278 D.M.Duda, R.C.van Waardenburg, L.A.Borg, S.McGarity, A.Nourse, M.B.Waddell, M.A.Bjornsti, and B.A.Schulman (2007).
Structure of a SUMO-binding-motif mimic bound to Smt3p-Ubc9p: conservation of a non-covalent ubiquitin-like protein-E2 complex as a platform for selective interactions within a SUMO pathway.

J Mol Biol, 369, 619-630.

PDB code: 2eke

17890322 D.Tu, W.Li, Y.Ye, and A.T.Brunger (2007).
Inaugural Article: Structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p.

Proc Natl Acad Sci U S A, 104, 15599-15606.

PDB codes: 2qiz 2qj0

17329252 E.S.Wong, J.M.Tan, C.Wang, Z.Zhang, S.P.Tay, N.Zaiden, H.S.Ko, V.L.Dawson, T.M.Dawson, and K.L.Lim (2007).
Relative sensitivity of parkin and other cysteine-containing enzymes to stress-induced solubility alterations.

J Biol Chem, 282, 12310-12318.

17206147 E.Sakata, Y.Yamaguchi, Y.Miyauchi, K.Iwai, T.Chiba, Y.Saeki, N.Matsuda, K.Tanaka, and K.Kato (2007).
Direct interactions between NEDD8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity.

Nat Struct Mol Biol, 14, 167-168.

17521420 J.L.Jiménez, B.Hegemann, J.R.Hutchins, J.M.Peters, and R.Durbin (2007).
A systematic comparative and structural analysis of protein phosphorylation sites based on the mtcPTM database.

Genome Biol, 8, R90.

17220175 K.Dreher, and J.Callis (2007).
Ubiquitin, hormones and biotic stress in plants.

Ann Bot, 99, 787-822.

17562869 K.M.Scaglione, P.K.Bansal, A.E.Deffenbaugh, A.Kiss, J.M.Moore, S.Korolev, R.Cocklin, M.Goebl, K.Kitagawa, and D.Skowyra (2007).
SCF E3-mediated autoubiquitination negatively regulates activity of Cdc34 E2 but plays a nonessential role in the catalytic cycle in vitro and in vivo.

Mol Cell Biol, 27, 5860-5870.

17728242 K.Uzunova, K.Göttsche, M.Miteva, S.R.Weisshaar, C.Glanemann, M.Schnellhardt, M.Niessen, H.Scheel, K.Hofmann, E.S.Johnson, G.J.Praefcke, and R.J.Dohmen (2007).
Ubiquitin-dependent proteolytic control of SUMO conjugates.

J Biol Chem, 282, 34167-34175.

17475912 M.A.Caligiuri, R.Briesewitz, J.Yu, L.Wang, M.Wei, K.J.Arnoczky, T.B.Marburger, J.Wen, D.Perrotti, C.D.Bloomfield, and S.P.Whitman (2007).
Novel c-CBL and CBL-b ubiquitin ligase mutations in human acute myeloid leukemia.

Blood, 110, 1022-1024.

17938210 M.Siatecka, L.Xue, and J.J.Bieker (2007).
Sumoylation of EKLF promotes transcriptional repression and is involved in inhibition of megakaryopoiesis.

Mol Cell Biol, 27, 8547-8560.

17170710 M.V.Poyurovsky, C.Priest, A.Kentsis, K.L.Borden, Z.Q.Pan, N.Pavletich, and C.Prives (2007).
The Mdm2 RING domain C-terminus is required for supramolecular assembly and ubiquitin ligase activity.

EMBO J, 26, 90.

17327397 P.Mercier, M.J.Lewis, D.D.Hau, L.F.Saltibus, W.Xiao, and L.Spyracopoulos (2007).
Structure, interactions, and dynamics of the RING domain from human TRAF6.

Protein Sci, 16, 602-614.

PDB code: 2jmd

17301054 R.K.Singh, S.Iyappan, and M.Scheffner (2007).
Hetero-oligomerization with MdmX rescues the ubiquitin/Nedd8 ligase activity of RING finger mutants of Mdm2.

J Biol Chem, 282, 10901-10907.

17389369 T.Mizushima, Y.Yoshida, T.Kumanomidou, Y.Hasegawa, A.Suzuki, T.Yamane, and K.Tanaka (2007).
Structural basis for the selection of glycosylated substrates by SCF(Fbs1) ubiquitin ligase.

Proc Natl Acad Sci U S A, 104, 5777-5781.

PDB codes: 2e31 2e32 2e33

17720710 V.Notenboom, R.G.Hibbert, S.E.van Rossum-Fikkert, J.V.Olsen, M.Mann, and T.K.Sixma (2007).
Functional characterization of Rad18 domains for Rad6, ubiquitin, DNA binding and PCNA modification.

Nucleic Acids Res, 35, 5819-5830.

17597076 X.Yang, J.Zhou, L.Sun, Z.Wei, J.Gao, W.Gong, R.M.Xu, Z.Rao, and Y.Liu (2007).
Structural basis for the function of DCN-1 in protein Neddylation.

J Biol Chem, 282, 24490-24494.

PDB code: 2is9

16732283 A.A.Yunus, and C.D.Lima (2006).
Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway.

Nat Struct Mol Biol, 13, 491-499.

PDB codes: 2grn 2gro 2grp 2grq 2grr

16474167 A.M.Gurtan, P.Stuckert, and A.D.D'Andrea (2006).
The WD40 repeats of FANCL are required for Fanconi anemia core complex assembly.

J Biol Chem, 281, 10896-10905.

16601699 C.Stroupe, K.M.Collins, R.A.Fratti, and W.Wickner (2006).
Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p.

EMBO J, 25, 1579-1589.

16571805 F.He, B.J.Fenner, A.K.Godwin, and J.Kwang (2006).
White spot syndrome virus open reading frame 222 encodes a viral E3 ligase and mediates degradation of a host tumor suppressor via ubiquitination.

J Virol, 80, 3884-3892.

16710298 G.Buchwald, P.van der Stoop, O.Weichenrieder, A.Perrakis, M.van Lohuizen, and T.K.Sixma (2006).
Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b.

EMBO J, 25, 2465-2474.

PDB code: 2ckl

16741904 G.Swaminathan, and A.Y.Tsygankov (2006).
The Cbl family proteins: ring leaders in regulation of cell signaling.

J Cell Physiol, 209, 21-43.

17108083 I.Unk, I.Hajdú, K.Fátyol, B.Szakál, A.Blastyák, V.Bermudez, J.Hurwitz, L.Prakash, S.Prakash, and L.Haracska (2006).
Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen.

Proc Natl Acad Sci U S A, 103, 18107-18112.

16931876 J.Kadlec, D.Guilligay, R.B.Ravelli, and S.Cusack (2006).
Crystal structure of the UPF2-interacting domain of nonsense-mediated mRNA decay factor UPF1.

RNA, 12, 1817-1824.

PDB code: 2iyk

16557337 M.Serrano, S.Parra, L.D.Alcaraz, and P.Guzmán (2006).
The ATL gene family from Arabidopsis thaliana and Oryza sativa comprises a large number of putative ubiquitin ligases of the RING-H2 type.

J Mol Evol, 62, 434-445.

16601690 M.Wang, D.Cheng, J.Peng, and C.M.Pickart (2006).
Molecular determinants of polyubiquitin linkage selection by an HECT ubiquitin ligase.

EMBO J, 25, 1710-1719.

17035235 O.A.Bazirgan, R.M.Garza, and R.Y.Hampton (2006).
Determinants of RING-E2 fidelity for Hrd1p, a membrane-anchored ubiquitin ligase.

J Biol Chem, 281, 38989-39001.

16757944 P.Knipscheer, and T.K.Sixma (2006).
Divide and conquer: the E2 active site.

Nat Struct Mol Biol, 13, 474-476.

16582478 R.Arai, S.Yoshikawa, K.Murayama, Y.Imai, R.Takahashi, M.Shirouzu, and S.Yokoyama (2006).
Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7).

Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 330-334.

PDB code: 2cyx

16373536 R.Janjusevic, R.B.Abramovitch, G.B.Martin, and C.E.Stebbins (2006).
A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase.

Science, 311, 222-226.

PDB code: 2fd4

16462746 S.Lee, Y.C.Tsai, R.Mattera, W.J.Smith, M.S.Kostelansky, A.M.Weissman, J.S.Bonifacino, and J.H.Hurley (2006).
Structural basis for ubiquitin recognition and autoubiquitination by Rabex-5.

Nat Struct Mol Biol, 13, 264-271.

PDB codes: 2fid 2fif

16735510 S.Oved, Y.Mosesson, Y.Zwang, E.Santonico, K.Shtiegman, M.D.Marmor, B.S.Kochupurakkal, M.Katz, S.Lavi, G.Cesareni, and Y.Yarden (2006).
Conjugation to Nedd8 instigates ubiquitylation and down-regulation of activated receptor tyrosine kinases.

J Biol Chem, 281, 21640-21651.

17059562 T.Omura, M.Kaneko, Y.Okuma, Y.Orba, K.Nagashima, R.Takahashi, N.Fujitani, S.Matsumura, A.Hata, K.Kubota, K.Murahashi, T.Uehara, and Y.Nomura (2006).
A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of Parkin.

J Neurochem, 99, 1456-1469.

16908531 V.Gangavarapu, L.Haracska, I.Unk, R.E.Johnson, S.Prakash, and L.Prakash (2006).
Mms2-Ubc13-dependent and -independent roles of Rad5 ubiquitin ligase in postreplication repair and translesion DNA synthesis in Saccharomyces cerevisiae.

Mol Cell Biol, 26, 7783-7790.

16714294 Z.Li, R.Cao, M.Wang, M.P.Myers, Y.Zhang, and R.M.Xu (2006).
Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex.

J Biol Chem, 281, 20643-20649.

PDB code: 2h0d

15882441 A.d'Azzo, A.Bongiovanni, and T.Nastasi (2005).
E3 ubiquitin ligases as regulators of membrane protein trafficking and degradation.

Traffic, 6, 429-441.

15701717 C.A.Dangelmaier, P.G.Quinter, J.Jin, A.Y.Tsygankov, S.P.Kunapuli, and J.L.Daniel (2005).
Rapid ubiquitination of Syk following GPVI activation in platelets.

Blood, 105, 3918-3924.

15917799 C.G.Vinuesa, M.C.Cook, C.Angelucci, V.Athanasopoulos, L.Rui, K.M.Hill, D.Yu, H.Domaschenz, B.Whittle, T.Lambe, I.S.Roberts, R.R.Copley, J.I.Bell, R.J.Cornall, and C.C.Goodnow (2005).
A RING-type ubiquitin ligase family member required to repress follicular helper T cells and autoimmunity.

Nature, 435, 452-458.

15816865 C.Wang, J.M.Tan, M.W.Ho, N.Zaiden, S.H.Wong, C.L.Chew, P.W.Eng, T.M.Lim, T.M.Dawson, and K.L.Lim (2005).
Alterations in the solubility and intracellular localization of parkin by several familial Parkinson's disease-linked point mutations.

J Neurochem, 93, 422-431.

15790571 E.Kellenberger, C.Dominguez, S.Fribourg, E.Wasielewski, D.Moras, A.Poterszman, R.Boelens, and B.Kieffer (2005).
Solution structure of the C-terminal domain of TFIIH P44 subunit reveals a novel type of C4C4 ring domain involved in protein-protein interactions.

J Biol Chem, 280, 20785-20792.

PDB code: 1z60

16365295 E.Ozkan, H.Yu, and J.Deisenhofer (2005).
Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases.

Proc Natl Acad Sci U S A, 102, 18890-18895.

PDB codes: 2esk 2eso 2esp 2esq

15635092 F.Huang, and A.Sorkin (2005).
Growth factor receptor binding protein 2-mediated recruitment of the RING domain of Cbl to the epidermal growth factor receptor is essential and sufficient to support receptor endocytosis.

Mol Biol Cell, 16, 1268-1281.

16237670 G.Meroni, and G.Diez-Roux (2005).
TRIM/RBCC, a novel class of 'single protein RING finger' E3 ubiquitin ligases.

Bioessays, 27, 1147-1157.

15837792 H.Xiong, H.Li, H.J.Kong, Y.Chen, J.Zhao, S.Xiong, B.Huang, H.Gu, L.Mayer, K.Ozato, and J.C.Unkeless (2005).
Ubiquitin-dependent degradation of interferon regulatory factor-8 mediated by Cbl down-regulates interleukin-12 expression.

J Biol Chem, 280, 23531-23539.

15659549 I.Alroy, S.Tuvia, T.Greener, D.Gordon, H.M.Barr, D.Taglicht, R.Mandil-Levin, D.Ben-Avraham, D.Konforty, A.Nir, O.Levius, V.Bicoviski, M.Dori, S.Cohen, L.Yaar, O.Erez, O.Propheta-Meiran, M.Koskas, E.Caspi-Bachar, I.Alchanati, A.Sela-Brown, H.Moskowitz, U.Tessmer, U.Schubert, and Y.Reiss (2005).
The trans-Golgi network-associated human ubiquitin-protein ligase POSH is essential for HIV type 1 production.

Proc Natl Acad Sci U S A, 102, 1478-1483.

15964842 J.Hennig, L.Ottosson, C.Andrésen, L.Horvath, V.K.Kuchroo, K.Broo, M.Wahren-Herlenius, and M.Sunnerhagen (2005).
Structural organization and Zn2+-dependent subdomain interactions involving autoantigenic epitopes in the Ring-B-box-coiled-coil (RBCC) region of Ro52.

J Biol Chem, 280, 33250-33261.

15965468 M.Dentice, A.Bandyopadhyay, B.Gereben, I.Callebaut, M.A.Christoffolete, B.W.Kim, S.Nissim, J.P.Mornon, A.M.Zavacki, A.Zeöld, L.P.Capelo, C.Curcio-Morelli, R.Ribeiro, J.W.Harney, C.J.Tabin, and A.C.Bianco (2005).
The Hedgehog-inducible ubiquitin ligase subunit WSB-1 modulates thyroid hormone activation and PTHrP secretion in the developing growth plate.

Nat Cell Biol, 7, 698-705.

15592428 M.H.Kagey, T.A.Melhuish, S.E.Powers, and D.Wotton (2005).
Multiple activities contribute to Pc2 E3 function.

EMBO J, 24, 108-119.

15608651 M.H.Tatham, S.Kim, E.Jaffray, J.Song, Y.Chen, and R.T.Hay (2005).
Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection.

Nat Struct Mol Biol, 12, 67-74.

15649886 M.J.Bottomley, G.Stier, D.Pennacchini, G.Legube, B.Simon, A.Akhtar, M.Sattler, and G.Musco (2005).
NMR structure of the first PHD finger of autoimmune regulator protein (AIRE1). Insights into autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy (APECED) disease.

J Biol Chem, 280, 11505-11512.

PDB code: 1xwh

15781449 M.Kobayashi, A.Takaori-Kondo, Y.Miyauchi, K.Iwai, and T.Uchiyama (2005).
Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function.

J Biol Chem, 280, 18573-18578.

15930137 M.S.Gentry, C.A.Worby, and J.E.Dixon (2005).
Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin.

Proc Natl Acad Sci U S A, 102, 8501-8506.

16341092 M.Wang, and C.M.Pickart (2005).
Different HECT domain ubiquitin ligases employ distinct mechanisms of polyubiquitin chain synthesis.

EMBO J, 24, 4324-4333.

16014632 N.Merkley, K.R.Barber, and G.S.Shaw (2005).
Ubiquitin manipulation by an E2 conjugating enzyme using a novel covalent intermediate.

J Biol Chem, 280, 31732-31738.

16207353 P.J.Stogios, G.S.Downs, J.J.Jauhal, S.K.Nandra, and G.G.Privé (2005).
Sequence and structural analysis of BTB domain proteins.

Genome Biol, 6, R82.

16207360 R.Riley, C.Lee, C.Sabatti, and D.Eisenberg (2005).
Inferring protein domain interactions from databases of interacting proteins.

Genome Biol, 6, R89.

15964836 S.K.Elkin, D.Ivanov, M.Ewalt, C.G.Ferguson, S.G.Hyberts, Z.Y.Sun, G.D.Prestwich, J.Yuan, G.Wagner, M.A.Oettinger, and O.P.Gozani (2005).
A PHD finger motif in the C terminus of RAG2 modulates recombination activity.

J Biol Chem, 280, 28701-28710.

PDB codes: 2a23 2jwo

16186120 S.Katoh, Y.Tsunoda, K.Murata, E.Minami, and E.Katoh (2005).
Active site residues and amino acid specificity of the ubiquitin carrier protein-binding RING-H2 finger domain.

J Biol Chem, 280, 41015-41024.

16219697 S.Matsuzawa, M.Cuddy, T.Fukushima, and J.C.Reed (2005).
Method for targeting protein destruction by using a ubiquitin-independent, proteasome-mediated degradation pathway.

Proc Natl Acad Sci U S A, 102, 14982-14987.

15838520 X.L.Ang, and J.Wade Harper (2005).
SCF-mediated protein degradation and cell cycle control.

Oncogene, 24, 2860-2870.

16142244 Z.M.Eletr, D.T.Huang, D.M.Duda, B.A.Schulman, and B.Kuhlman (2005).
E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer.

Nat Struct Mol Biol, 12, 933-934.

15078868 A.Dasgupta, K.L.Ramsey, J.S.Smith, and D.T.Auble (2004).
Sir Antagonist 1 (San1) is a ubiquitin ligase.

J Biol Chem, 279, 26830-26838.

15208330 A.K.Ghosh, A.L.Reddi, N.L.Rao, L.Duan, V.Band, and H.Band (2004).
Biochemical basis for the requirement of kinase activity for Cbl-dependent ubiquitinylation and degradation of a target tyrosine kinase.

J Biol Chem, 279, 36132-36141.

14747994 B.M.Kus, C.E.Caldon, R.Andorn-Broza, and A.M.Edwards (2004).
Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro.

Proteins, 54, 455-467.

15117950 C.K.Kassenbrock, and S.M.Anderson (2004).
Regulation of ubiquitin protein ligase activity in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations.

J Biol Chem, 279, 28017-28027.

15361859 D.T.Huang, D.W.Miller, R.Mathew, R.Cassell, J.M.Holton, M.F.Roussel, and B.A.Schulman (2004).
A unique E1-E2 interaction required for optimal conjugation of the ubiquitin-like protein NEDD8.

Nat Struct Mol Biol, 11, 927-935.

PDB code: 1tt5

15252205 D.Yao, Z.Gu, T.Nakamura, Z.Q.Shi, Y.Ma, B.Gaston, L.A.Palmer, E.M.Rockenstein, Z.Zhang, E.Masliah, T.Uehara, and S.A.Lipton (2004).
Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity.

Proc Natl Acad Sci U S A, 101, 10810-10814.

14612447 F.M.Townsley, B.Thompson, and M.Bienz (2004).
Pygopus residues required for its binding to Legless are critical for transcription and development.

J Biol Chem, 279, 5177-5183.

15496420 J.Huang, Q.Huang, X.Zhou, M.M.Shen, A.Yen, S.X.Yu, G.Dong, K.Qu, P.Huang, E.M.Anderson, S.Daniel-Issakani, R.M.Buller, D.G.Payan, and H.H.Lu (2004).
The poxvirus p28 virulence factor is an E3 ubiquitin ligase.

J Biol Chem, 279, 54110-54116.

14990566 J.Nie, S.S.Li, and C.J.McGlade (2004).
A novel PTB-PDZ domain interaction mediates isoform-specific ubiquitylation of mammalian Numb.

J Biol Chem, 279, 20807-20815.

15377232 J.Smalle, and R.D.Vierstra (2004).
The ubiquitin 26S proteasome proteolytic pathway.

Annu Rev Plant Biol, 55, 555-590.

15113913 K.J.Oh, A.Kalinina, J.Wang, K.Nakayama, K.I.Nakayama, and S.Bagchi (2004).
The papillomavirus E7 oncoprotein is ubiquitinated by UbcH7 and Cullin 1- and Skp2-containing E3 ligase.

J Virol, 78, 5338-5346.

15226437 K.L.Ramsey, J.J.Smith, A.Dasgupta, N.Maqani, P.Grant, and D.T.Auble (2004).
The NEF4 complex regulates Rad4 levels and utilizes Snf2/Swi2-related ATPase activity for nucleotide excision repair.

Mol Cell Biol, 24, 6362-6378.

14769789 M.Donnini, A.Lapucci, L.Papucci, E.Witort, A.Jacquier, G.Brewer, A.Nicolin, S.Capaccioli, and N.Schiavone (2004).
Identification of TINO: a new evolutionarily conserved BCL-2 AU-rich element RNA-binding protein.

J Biol Chem, 279, 20154-20166.

15328341 N.Merkley, and G.S.Shaw (2004).
Solution structure of the flexible class II ubiquitin-conjugating enzyme Ubc1 provides insights for polyubiquitin chain assembly.

J Biol Chem, 279, 47139-47147.

PDB code: 1tte

15231834 P.Andersen, B.B.Kragelund, A.N.Olsen, F.H.Larsen, N.H.Chua, F.M.Poulsen, and K.Skriver (2004).
Structure and biochemical function of a prototypical Arabidopsis U-box domain.

J Biol Chem, 279, 40053-40061.

PDB code: 1t1h

15242397 P.De, and K.K.Rodgers (2004).
Putting the pieces together: identification and characterization of structural domains in the V(D)J recombination protein RAG1.

Immunol Rev, 200, 70-82.

15123609 P.Peschard, N.Ishiyama, T.Lin, S.Lipkowitz, and M.Park (2004).
A conserved DpYR motif in the juxtamembrane domain of the Met receptor family forms an atypical c-Cbl/Cbl-b tyrosine kinase binding domain binding site required for suppression of oncogenic activation.

J Biol Chem, 279, 29565-29571.

15465811 R.B.Dodd, M.D.Allen, S.E.Brown, C.M.Sanderson, L.M.Duncan, P.J.Lehner, M.Bycroft, and R.J.Read (2004).
Solution structure of the Kaposi's sarcoma-associated herpesvirus K3 N-terminal domain reveals a Novel E2-binding C4HC3-type RING domain.

J Biol Chem, 279, 53840-53847.

PDB code: 1vyx

14755799 R.Moore, and L.Boyd (2004).
Analysis of RING finger genes required for embryogenesis in C. elegans.

Genesis, 38, 1.

15247280 R.Rajendra, D.Malegaonkar, P.Pungaliya, H.Marshall, Z.Rasheed, J.Brownell, L.F.Liu, S.Lutzker, A.Saleem, and E.H.Rubin (2004).
Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53.

J Biol Chem, 279, 36440-36444.

15075914 S.Rome, E.Meugnier, and H.Vidal (2004).
The ubiquitin-proteasome pathway is a new partner for the control of insulin signaling.

Curr Opin Clin Nutr Metab Care, 7, 249-254.

15340381 T.Cardozo, and M.Pagano (2004).
The SCF ubiquitin ligase: insights into a molecular machine.

Nat Rev Mol Cell Biol, 5, 739-751.

15280476 X.Wang, L.Lybarger, R.Connors, M.R.Harris, and T.H.Hansen (2004).
Model for the interaction of gammaherpesvirus 68 RING-CH finger protein mK3 with major histocompatibility complex class I and the peptide-loading complex.

J Virol, 78, 8673-8686.

15032575 Y.C.Liu (2004).
Ubiquitin ligases and the immune response.

Annu Rev Immunol, 22, 81.

12626763 C.M.House, I.J.Frew, H.L.Huang, G.Wiche, N.Traficante, E.Nice, B.Catimel, and D.D.Bowtell (2003).
A binding motif for Siah ubiquitin ligase.

Proc Natl Acad Sci U S A, 100, 3101-3106.

12829707 H.A.Alwan, E.J.van Zoelen, and J.E.van Leeuwen (2003).
Ligand-induced lysosomal epidermal growth factor receptor (EGFR) degradation is preceded by proteasome-dependent EGFR de-ubiquitination.

J Biol Chem, 278, 35781-35790.

12496280 H.D.Ulrich (2003).
Protein-protein interactions within an E2-RING finger complex. Implications for ubiquitin-dependent DNA damage repair.

J Biol Chem, 278, 7051-7058.

12520055 J.Chen, J.B.Anderson, C.DeWeese-Scott, N.D.Fedorova, L.Y.Geer, S.He, D.I.Hurwitz, J.D.Jackson, A.R.Jacobs, C.J.Lanczycki, C.A.Liebert, C.Liu, T.Madej, A.Marchler-Bauer, G.H.Marchler, R.Mazumder, A.N.Nikolskaya, B.S.Rao, A.R.Panchenko, B.A.Shoemaker, V.Simonyan, J.S.Song, P.A.Thiessen, S.Vasudevan, Y.Wang, R.A.Yamashita, J.J.Yin, and S.H.Bryant (2003).
MMDB: Entrez's 3D-structure database.

Nucleic Acids Res, 31, 474-477.

14671314 J.M.Jones, and M.Gellert (2003).
Autoubiquitylation of the V(D)J recombinase protein RAG1.

Proc Natl Acad Sci U S A, 100, 15446-15451.

12754251 L.Duan, Y.Miura, M.Dimri, B.Majumder, I.L.Dodge, A.L.Reddi, A.Ghosh, N.Fernandes, P.Zhou, K.Mullane-Robinson, N.Rao, S.Donoghue, R.A.Rogers, D.Bowtell, M.Naramura, H.Gu, V.Band, and H.Band (2003).
Cbl-mediated ubiquitinylation is required for lysosomal sorting of epidermal growth factor receptor but is dispensable for endocytosis.

J Biol Chem, 278, 28950-28960.

12627222 M.D.Ohi, C.W.Vander Kooi, J.A.Rosenberg, W.J.Chazin, and K.L.Gould (2003).
Structural insights into the U-box, a domain associated with multi-ubiquitination.

Nat Struct Biol, 10, 250-255.

PDB code: 1n87

12773374 M.Harkiolaki, M.Lewitzky, R.J.Gilbert, E.Y.Jones, R.P.Bourette, G.Mouchiroud, H.Sondermann, I.Moarefi, and S.M.Feller (2003).
Structural basis for SH3 domain-mediated high-affinity binding between Mona/Gads and SLP-76.

EMBO J, 22, 2571-2582.

PDB code: 1oeb

12621021 N.Finney, F.Walther, P.Y.Mantel, D.Stauffer, G.Rovelli, and K.K.Dev (2003).
The cellular protein level of parkin is regulated by its ubiquitin-like domain.

J Biol Chem, 278, 16054-16058.

12502808 N.Imai, N.Matsuda, K.Tanaka, A.Nakano, S.Matsumoto, and W.Kang (2003).
Ubiquitin ligase activities of Bombyx mori nucleopolyhedrovirus RING finger proteins.

J Virol, 77, 923-930.

12732733 P.S.Brzovic, J.R.Keeffe, H.Nishikawa, K.Miyamoto, D.Fox, M.Fukuda, T.Ohta, and R.Klevit (2003).
Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex.

Proc Natl Acad Sci U S A, 100, 5646-5651.

14517261 P.Y.Wu, M.Hanlon, M.Eddins, C.Tsui, R.S.Rogers, J.P.Jensen, M.J.Matunis, A.M.Weissman, A.M.Weisman, A.M.Weissman, C.Wolberger, C.P.Wolberger, and C.M.Pickart (2003).
A conserved catalytic residue in the ubiquitin-conjugating enzyme family.

EMBO J, 22, 5241-5250.

12588869 S.Katoh, C.Hong, Y.Tsunoda, K.Murata, R.Takai, E.Minami, T.Yamazaki, and E.Katoh (2003).
High precision NMR structure and function of the RING-H2 finger domain of EL5, a rice protein whose expression is increased upon exposure to pathogen-derived oligosaccharides.

J Biol Chem, 278, 15341-15348.

PDB code: 1iym

12569095 S.McKenna, T.Moraes, L.Pastushok, C.Ptak, W.Xiao, L.Spyracopoulos, and M.J.Ellison (2003).
An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2.Ubc13. The structural basis for lysine 63 chain catalysis.

J Biol Chem, 278, 13151-13158.

12881521 Y.Miura-Shimura, L.Duan, N.L.Rao, A.L.Reddi, H.Shimura, R.Rottapel, B.J.Druker, A.Tsygankov, V.Band, and H.Band (2003).
Cbl-mediated ubiquitinylation and negative regulation of Vav.

J Biol Chem, 278, 38495-38504.

12431996 Y.Xia, G.M.Pao, H.W.Chen, I.M.Verma, and T.Hunter (2003).
Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein.

J Biol Chem, 278, 5255-5263.

11927591 A.Chen, F.E.Kleiman, J.L.Manley, T.Ouchi, and Z.Q.Pan (2002).
Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase.

J Biol Chem, 277, 22085-22092.

12438698 A.Kentsis, R.E.Gordon, and K.L.Borden (2002).
Control of biochemical reactions through supramolecular RING domain self-assembly.

Proc Natl Acad Sci U S A, 99, 15404-15409.

11959851 A.Sasaki, Y.Masuda, K.Iwai, K.Ikeda, and K.Watanabe (2002).
A RING finger protein Praja1 regulates Dlx5-dependent transcription through its ubiquitin ligase activity for the Dlx/Msx-interacting MAGE/Necdin family protein, Dlxin-1.

J Biol Chem, 277, 22541-22546.

11997436 A.Wong, B.Lamothe, A.Lee, J.Schlessinger, I.Lax, and A.Li (2002).
FRS2 alpha attenuates FGF receptor signaling by Grb2-mediated recruitment of the ubiquitin ligase Cbl.

Proc Natl Acad Sci U S A, 99, 6684-6689.

11752173 C.Boutell, S.Sadis, and R.D.Everett (2002).
Herpes simplex virus type 1 immediate-early protein ICP0 and is isolated RING finger domain act as ubiquitin E3 ligases in vitro.

J Virol, 76, 841-850.

11994282 C.K.Kassenbrock, S.Hunter, P.Garl, G.L.Johnson, and S.M.Anderson (2002).
Inhibition of Src family kinases blocks epidermal growth factor (EGF)-induced activation of Akt, phosphorylation of c-Cbl, and ubiquitination of the EGF receptor.

J Biol Chem, 277, 24967-24975.

12466024 C.Yi, H.Wang, N.Wei, and X.W.Deng (2002).
An initial biochemical and cell biological characterization of the mammalian homologue of a central plant developmental switch, COP1.

BMC Cell Biol, 3, 30.

11807090 D.Kang, J.Chen, J.Wong, and G.Fang (2002).
The checkpoint protein Chfr is a ligase that ubiquitinates Plk1 and inhibits Cdc2 at the G2 to M transition.

J Cell Biol, 156, 249-259.

12234920 E.S.Wong, C.W.Fong, J.Lim, P.Yusoff, B.C.Low, W.Y.Langdon, and G.R.Guy (2002).
Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling.

EMBO J, 21, 4796-4808.

12006494 E.W.Hewitt, L.Duncan, D.Mufti, J.Baker, P.G.Stevenson, and P.J.Lehner (2002).
Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation.

EMBO J, 21, 2418-2429.

11742346 G.Polekhina, C.M.House, N.Traficante, J.P.Mackay, F.Relaix, D.A.Sassoon, M.W.Parker, and D.D.Bowtell (2002).
Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-alpha signaling.

Nat Struct Biol, 9, 68-75.

PDB code: 1k2f

12393902 J.C.Badciong, and A.L.Haas (2002).
MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination.

J Biol Chem, 277, 49668-49675.

12021772 J.P.Wing, B.A.Schreader, T.Yokokura, Y.Wang, P.S.Andrews, N.Huseinovic, C.K.Dong, J.L.Ogdahl, L.M.Schwartz, K.White, and J.R.Nambu (2002).
Drosophila Morgue is an F box/ubiquitin conjugase domain protein important for grim-reaper mediated apoptosis.

Nat Cell Biol, 4, 451-456.

12354763 K.P.Bencsath, M.S.Podgorski, V.R.Pagala, C.A.Slaughter, and B.A.Schulman (2002).
Identification of a multifunctional binding site on Ubc9p required for Smt3p conjugation.

J Biol Chem, 277, 47938-47945.

11675391 K.Wu, A.Chen, P.Tan, and Z.Q.Pan (2002).
The Nedd8-conjugated ROC1-CUL1 core ubiquitin ligase utilizes Nedd8 charged surface residues for efficient polyubiquitin chain assembly catalyzed by Cdc34.

J Biol Chem, 277, 516-527.

12438443 L.K.Phan, F.Lin, C.A.LeDuc, W.K.Chung, and R.L.Leibel (2002).
The mouse mahoganoid coat color mutation disrupts a novel C3HC4 RING domain protein.

J Clin Invest, 110, 1449-1459.

11861641 M.Furukawa, T.Ohta, and Y.Xiong (2002).
Activation of UBC5 ubiquitin-conjugating enzyme by the RING finger of ROC1 and assembly of active ubiquitin ligases by all cullins.

J Biol Chem, 277, 15758-15765.

12024036 M.P.Loreto, D.M.Berry, and C.J.McGlade (2002).
Functional cooperation between c-Cbl and Src-like adaptor protein 2 in the negative regulation of T-cell receptor signaling.

Mol Cell Biol, 22, 4241-4255.

12077349 N.Kotaja, U.Karvonen, O.A.Jänne, and J.J.Palvimo (2002).
PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases.

Mol Cell Biol, 22, 5222-5234.

12006492 O.Pornillos, S.L.Alam, R.L.Rich, D.G.Myszka, D.R.Davis, and W.I.Sundquist (2002).
Structure and functional interactions of the Tsg101 UEV domain.

EMBO J, 21, 2397-2406.

PDB codes: 1kpp 1kpq

12016299 R.C.Conaway, C.S.Brower, and J.W.Conaway (2002).
Emerging roles of ubiquitin in transcription regulation.

Science, 296, 1254-1258.

12215542 S.Li, C.Xu, and R.W.Carthew (2002).
Phyllopod acts as an adaptor protein to link the sina ubiquitin ligase to the substrate protein tramtrack.

Mol Cell Biol, 22, 6854-6865.

11823428 T.K.Albert, H.Hanzawa, Y.I.Legtenberg, M.J.de Ruwe, F.A.van den Heuvel, M.A.Collart, R.Boelens, and H.T.Timmers (2002).
Identification of a ubiquitin-protein ligase subunit within the CCR4-NOT transcription repressor complex.

EMBO J, 21, 355-364.

12411582 X.B.Qiu, and A.L.Goldberg (2002).
Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and degradation of the epidermal growth factor receptor family member, ErbB3.

Proc Natl Acad Sci U S A, 99, 14843-14848.

11927573 Y.Lin, W.C.Hwang, and R.Basavappa (2002).
Structural and functional analysis of the human mitotic-specific ubiquitin-conjugating enzyme, UbcH10.

J Biol Chem, 277, 21913-21921.

PDB code: 1i7k

11514605 A.Magnan, V.Di Bartolo, A.M.Mura, C.Boyer, M.Richelme, Y.L.Lin, A.Roure, A.Gillet, C.Arrieumerlou, O.Acuto, B.Malissen, and M.Malissen (2001).
T cell development and T cell responses in mice with mutations affecting tyrosines 292 or 315 of the ZAP-70 protein tyrosine kinase.

J Exp Med, 194, 491-505.

11395416 C.M.Pickart (2001).
Mechanisms underlying ubiquitination.

Annu Rev Biochem, 70, 503-533.

11533242 C.Ptak, C.Gwozd, J.T.Huzil, T.J.Gwozd, G.Garen, and M.J.Ellison (2001).
Creation of a pluripotent ubiquitin-conjugating enzyme.

Mol Cell Biol, 21, 6537-6548.

11905825 G.A.Koretzky, and P.S.Myung (2001).
Positive and negative regulation of T-cell activation by adaptor proteins.

Nat Rev Immunol, 1, 95.

11722579 G.Martinez-Noel, U.Müller, and K.Harbers (2001).
Identification of molecular determinants required for interaction of ubiquitin-conjugating enzymes and RING finger proteins.

Eur J Biochem, 268, 5912-5919.

11557750 J.Jiang, C.A.Ballinger, Y.Wu, Q.Dai, D.M.Cyr, J.Höhfeld, and C.Patterson (2001).
CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation.

J Biol Chem, 276, 42938-42944.

11410931 J.Myung, K.B.Kim, and C.M.Crews (2001).
The ubiquitin-proteasome pathway and proteasome inhibitors.

Med Res Rev, 21, 245-273.

11322894 K.Ito, S.Adachi, R.Iwakami, H.Yasuda, Y.Muto, N.Seki, and Y.Okano (2001).
N-Terminally extended human ubiquitin-conjugating enzymes (E2s) mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8.

Eur J Biochem, 268, 2725-2732.

11742985 N.Rao, A.K.Ghosh, S.Ota, P.Zhou, A.L.Reddi, K.Hakezi, B.K.Druker, J.Wu, and H.Band (2001).
The non-receptor tyrosine kinase Syk is a target of Cbl-mediated ubiquitylation upon B-cell receptor stimulation.

EMBO J, 20, 7085-7095.

11292843 N.V.Grishin (2001).
Treble clef finger--a functionally diverse zinc-binding structural motif.

Nucleic Acids Res, 29, 1703-1714.

11573085 P.S.Brzovic, P.Rajagopal, D.W.Hoyt, M.C.King, and R.E.Klevit (2001).
Structure of a BRCA1-BARD1 heterodimeric RING-RING complex.

Nat Struct Biol, 8, 833-837.

PDB code: 1jm7

11573079 R.Baer (2001).
With the ends in sight: images from the BRCA1 tumor suppressor.

Nat Struct Biol, 8, 822-824.

11390656 R.G.Gardner, A.G.Shearer, and R.Y.Hampton (2001).
In vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation.

Mol Cell Biol, 21, 4276-4291.

11641273 R.Swanson, M.Locher, and M.Hochstrasser (2001).
A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation.

Genes Dev, 15, 2660-2674.

11724934 S.Fang, M.Ferrone, C.Yang, J.P.Jensen, S.Tiwari, and A.M.Weissman (2001).
The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum.

Proc Natl Acad Sci U S A, 98, 14422-14427.

11602710 Y.Xu, J.H.Ahn, M.Cheng, C.M.apRhys, C.J.Chiou, J.Zong, M.J.Matunis, and G.S.Hayward (2001).
Proteasome-independent disruption of PML oncogenic domains (PODs), but not covalent modification by SUMO-1, is required for human cytomegalovirus immediate-early protein IE1 to inhibit PML-mediated transcriptional repression.

J Virol, 75, 10683-10695.

11739784 Z.Tang, B.Li, R.Bharadwaj, H.Zhu, E.Ozkan, K.Hakala, J.Deisenhofer, and H.Yu (2001).
APC2 Cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex.

Mol Biol Cell, 12, 3839-3851.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.