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Identification
HMDB Protein ID HMDBP00601
Secondary Accession Numbers
  • 5873
Name Ubiquitin-conjugating enzyme E2 L3
Synonyms
  1. L-UBC
  2. UbcH7
  3. Ubiquitin carrier protein L3
  4. Ubiquitin-conjugating enzyme E2-F1
  5. Ubiquitin-protein ligase L3
Gene Name UBE2L3
Protein Type Enzyme
Biological Properties
General Function Involved in acid-amino acid ligase activity
Specific Function Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis.
Pathways
  • Parkinson's disease
  • protein ubiquitination
  • Ubiquitin mediated proteolysis
Reactions
Adenosine triphosphate + ubiquitin + protein lysine → Adenosine monophosphate + Pyrophosphate + protein N-ubiquityllysine details
GO Classification
Biological Process
cell proliferation
ubiquitin-dependent protein catabolic process
protein K11-linked ubiquitination
regulation of S phase of mitotic cell cycle
cellular response to glucocorticoid stimulus
regulation of transcription, DNA-dependent
transcription, DNA-dependent
Cellular Component
cytoplasm
nucleus
ubiquitin ligase complex
Function
catalytic activity
small conjugating protein ligase activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
acid-amino acid ligase activity
Molecular Function
ubiquitin-protein ligase activity
ATP binding
transcription coactivator activity
enzyme binding
acid-amino acid ligase activity
Process
metabolic process
regulation of protein metabolic process
macromolecule metabolic process
biological regulation
regulation of biological process
regulation of metabolic process
regulation of macromolecule metabolic process
post-translational protein modification
macromolecule modification
protein modification process
Cellular Location
  1. Nucleus
  2. Cytoplasm
Gene Properties
Chromosome Location 22
Locus 22q11.21
SNPs UBE2L3
Gene Sequence
>465 bp
ATGGCGGCCAGCAGGAGGCTGATGAAGGAGCTTGAAGAAATCCGCAAATGTGGGATGAAA
AACTTCCGTAACATCCAGGTTGATGAAGCTAATTTATTGACTTGGCAAGGGCTTATTGTT
CCTGACAACCCTCCATATGATAAGGGAGCCTTCAGAATCGAAATCAACTTTCCAGCAGAG
TACCCATTCAAACCACCGAAGATCACATTTAAAACAAAGATCTATCACCCAAACATCGAC
GAAAAGGGGCAGGTCTGTCTGCCAGTAATTAGTGCCGAAAACTGGAAGCCAGCAACCAAA
ACCGACCAAGTAATCCAGTCCCTCATAGCACTGGTGAATGACCCCCAGCCTGAGCACCCG
CTTCGGGCTGACCTAGCTGAAGAATACTCTAAGGACCGTAAAAAATTCTGTAAGAATGCT
GAAGAGTTTACAAAGAAATATGGGGAAAAGCGACCTGTGGACTAA
Protein Properties
Number of Residues 154
Molecular Weight 24003.385
Theoretical pI 8.742
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Ubiquitin-conjugating enzyme E2 L3
MAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINFPAE
YPFKPPKITFKTKIYHPNIDEKGQVCLPVISAENWKPATKTDQVIQSLIALVNDPQPEHP
LRADLAEEYSKDRKKFCKNAEEFTKKYGEKRPVD
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P68036
UniProtKB/Swiss-Prot Entry Name UB2L3_HUMAN
PDB IDs
GenBank Gene ID S81003
GeneCard ID UBE2L3
GenAtlas ID UBE2L3
HGNC ID HGNC:12488
References
General References
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  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Verma S, Ismail A, Gao X, Fu G, Li X, O'Malley BW, Nawaz Z: The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator for steroid hormone receptors. Mol Cell Biol. 2004 Oct;24(19):8716-26. [PubMed:15367689 ]
  5. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed:15461802 ]
  6. David Y, Ziv T, Admon A, Navon A: The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines. J Biol Chem. 2010 Mar 19;285(12):8595-604. doi: 10.1074/jbc.M109.089003. Epub 2010 Jan 8. [PubMed:20061386 ]
  7. Niwa J, Ishigaki S, Doyu M, Suzuki T, Tanaka K, Sobue G: A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity. Biochem Biophys Res Commun. 2001 Mar 2;281(3):706-13. [PubMed:11237715 ]
  8. Huang J, Xu LG, Liu T, Zhai Z, Shu HB: The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis. FEBS Lett. 2006 Feb 6;580(3):940-7. Epub 2006 Jan 18. [PubMed:16427630 ]
  9. Fortier JM, Kornbluth J: NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase. J Immunol. 2006 Jun 1;176(11):6454-63. [PubMed:16709802 ]
  10. Robinson PA, Leek JP, Thompson J, Carr IM, Bailey A, Moynihan TP, Coletta PL, Lench NJ, Markham AF: A human ubiquitin conjugating enzyme, L-UBC, maps in the Alzheimer's disease locus on chromosome 14q24.3. Mamm Genome. 1995 Oct;6(10):725-31. [PubMed:8563171 ]
  11. Nuber U, Schwarz S, Kaiser P, Schneider R, Scheffner M: Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5. J Biol Chem. 1996 Feb 2;271(5):2795-800. [PubMed:8576257 ]
  12. Moynihan TP, Cole CG, Dunham I, O'Neil L, Markham AF, Robinson PA: Fine-mapping, genomic organization, and transcript analysis of the human ubiquitin-conjugating enzyme gene UBE2L3. Genomics. 1998 Jul 1;51(1):124-7. [PubMed:9693040 ]
  13. Blumenfeld N, Gonen H, Mayer A, Smith CE, Siegel NR, Schwartz AL, Ciechanover A: Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-"N-end rule" protein substrates. J Biol Chem. 1994 Apr 1;269(13):9574-81. [PubMed:8144544 ]
  14. Ardley HC, Moynihan TP, Markham AF, Robinson PA: Promoter analysis of the human ubiquitin-conjugating enzyme gene family UBE2L1-4, including UBE2L3 which encodes UbcH7. Biochim Biophys Acta. 2000 Apr 25;1491(1-3):57-64. [PubMed:10760570 ]
  15. Shimura H, Hattori N, Kubo Si, Mizuno Y, Asakawa S, Minoshima S, Shimizu N, Iwai K, Chiba T, Tanaka K, Suzuki T: Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat Genet. 2000 Jul;25(3):302-5. [PubMed:10888878 ]
  16. Ardley HC, Tan NG, Rose SA, Markham AF, Robinson PA: Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7. J Biol Chem. 2001 Jun 1;276(22):19640-7. Epub 2001 Mar 13. [PubMed:11278816 ]
  17. Toby GG, Gherraby W, Coleman TR, Golemis EA: A novel RING finger protein, human enhancer of invasion 10, alters mitotic progression through regulation of cyclin B levels. Mol Cell Biol. 2003 Mar;23(6):2109-22. [PubMed:12612082 ]
  18. Garside H, Waters C, Berry A, Rice L, Ardley HC, White A, Robinson PA, Ray D: UbcH7 interacts with the glucocorticoid receptor and mediates receptor autoregulation. J Endocrinol. 2006 Sep;190(3):621-9. [PubMed:17003263 ]
  19. Marteijn JA, van der Meer LT, Smit JJ, Noordermeer SM, Wissink W, Jansen P, Swarts HG, Hibbert RG, de Witte T, Sixma TK, Jansen JH, van der Reijden BA: The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains. Leukemia. 2009 Aug;23(8):1480-9. doi: 10.1038/leu.2009.57. Epub 2009 Apr 2. [PubMed:19340006 ]
  20. Whitcomb EA, Dudek EJ, Liu Q, Taylor A: Novel control of S phase of the cell cycle by ubiquitin-conjugating enzyme H7. Mol Biol Cell. 2009 Jan;20(1):1-9. doi: 10.1091/mbc.E08-01-0036. Epub 2008 Oct 22. [PubMed:18946090 ]
  21. Huang L, Kinnucan E, Wang G, Beaudenon S, Howley PM, Huibregtse JM, Pavletich NP: Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science. 1999 Nov 12;286(5443):1321-6. [PubMed:10558980 ]
  22. Zheng N, Wang P, Jeffrey PD, Pavletich NP: Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell. 2000 Aug 18;102(4):533-9. [PubMed:10966114 ]