Hmdb loader
Survey
Identification
HMDB Protein ID HMDBP09326
Secondary Accession Numbers
  • 15163
Name Ubiquitin-conjugating enzyme E2 Q2
Synonyms
  1. Ubiquitin carrier protein Q2
  2. Ubiquitin-protein ligase Q2
Gene Name UBE2Q2
Protein Type Enzyme
Biological Properties
General Function Involved in acid-amino acid ligase activity
Specific Function Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination.
Pathways
  • protein ubiquitination
  • Ubiquitin mediated proteolysis
Reactions
Adenosine triphosphate + ubiquitin + protein lysine → Adenosine monophosphate + Pyrophosphate + protein N-ubiquityllysine details
GO Classification
Biological Process
protein K48-linked ubiquitination
Cellular Component
cytoplasm
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
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. Cytoplasm
Gene Properties
Chromosome Location 15
Locus 15q24.2
SNPs UBE2Q2
Gene Sequence
>1128 bp
ATGTCCGTGTCAGGGCTCAAGGCCGAGCTGAAGTTCCTGGCGTCCATCTTCGACAAGAAC
CACGAGCGATTCCGCATCGTCAGTTGGAAGCTGGACGAGCTGCACTGCCAGTTCCTGGTG
CCGCAGCAGGGCAGCCCGCACTCGCTGCCGCCGCCACTCACGCTCCACTGCAACATCACG
GAATCCTATCCATCTTCTTCACCGATATGGTTTGTGGATTCTGAAGACCCAAATCTGACA
TCAGTTCTGGAACGTCTAGAAGATACTAAGAACAACAATTTGCTTCGTCAGCAATTGAAG
TGGTTGATATGTGAACTCTGCAGTTTATATAACCTTCCTAAGCACCTGGATGTTGAGATG
CTAGATCAACCACTACCCACGGGTCAGAATGGGACAACAGAAGAAGTGACTTCAGAAGAA
GAGGAAGAAGAAGAAGAGATGGCTGAAGATATAGAAGACTTAGATCACTATGAGATGAAG
GAAGAAGAGCCTATTAGTGGGAAAAAGTCAGAGGATGAAGGAATTGAAAAAGAAAATTTG
GCAATATTAGAGAAAATTAGGAAGACTCAAAGGCAAGACCATTTAAATGGTGCAGTGTCT
GGGTCAGTGCAAGCTTCAGATAGACTTATGAAAGAGCTCAGGGACATATACAGATCACAG
AGTTATAAAACAGGGATTTATTCAGTGGAACTCATAAATGACAGTTTATATGACTGGCAT
GTTAAACTGCAGAAGGTTGACCCTGATAGTCCTTTGCACAGTGATCTTCAGATCTTAAAA
GAAAAAGAAGGCATAGAATATATTTTGCTTAACTTCTCTTTTAAGGATAACTTTCCATTT
GATCCTCCATTTGTTCGAGTGGTGTTACCTGTTCTCTCAGGAGGGTATGTATTGGGTGGA
GGAGCATTATGTATGGAACTTCTCACAAAACAGGGCTGGAGCAGTGCCTACTCAATAGAA
TCGGTCATCATGCAAATAAATGCCACCTTAGTCAAAGGCAAAGCCAGAGTGCAGTTTGGA
GCAAATAAGAATCAATATAATCTAGCAAGAGCCCAACAATCCTATAATTCCATTGTACAG
ATACATGAGAAAAATGGCTGGTACACCCCTCCAAAGGAAGATGGCTAA
Protein Properties
Number of Residues 375
Molecular Weight 40955.82
Theoretical pI 4.785
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Ubiquitin-conjugating enzyme E2 Q2
MSVSGLKAELKFLASIFDKNHERFRIVSWKLDELHCQFLVPQQGSPHSLPPPLTLHCNIT
ESYPSSSPIWFVDSEDPNLTSVLERLEDTKNNNLLRQQLKWLICELCSLYNLPKHLDVEM
LDQPLPTGQNGTTEEVTSEEEEEEEEMAEDIEDLDHYEMKEEEPISGKKSEDEGIEKENL
AILEKIRKTQRQDHLNGAVSGSVQASDRLMKELRDIYRSQSYKTGIYSVELINDSLYDWH
VKLQKVDPDSPLHSDLQILKEKEGIEYILLNFSFKDNFPFDPPFVRVVLPVLSGGYVLGG
GALCMELLTKQGWSSAYSIESVIMQINATLVKGKARVQFGANKNQYNLARAQQSYNSIVQ
IHEKNGWYTPPKEDG
GenBank ID Protein 50949459
UniProtKB/Swiss-Prot ID Q8WVN8
UniProtKB/Swiss-Prot Entry Name UB2Q2_HUMAN
PDB IDs
GenBank Gene ID AL832429
GeneCard ID UBE2Q2
GenAtlas ID UBE2Q2
HGNC ID HGNC:19248
References
General References
  1. 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 ]
  2. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  4. 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 ]
  5. Seghatoleslam A, Zambrano A, Millon R, Ganguli G, Argentini M, Cromer A, Abecassis J, Wasylyk B: Analysis of a novel human gene, LOC92912, over-expressed in hypopharyngeal tumours. Biochem Biophys Res Commun. 2006 Jan 6;339(1):422-9. Epub 2005 Nov 14. [PubMed:16300736 ]