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Showing Protein Ubiquitin-conjugating enzyme E2 D2 (HMDBP00587)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 5 metabolites
Identification
HMDB Protein ID HMDBP00587
Secondary Accession Numbers
  • 5859
Name Ubiquitin-conjugating enzyme E2 D2
Synonyms
  1. Ubiquitin carrier protein D2
  2. Ubiquitin-conjugating enzyme E2(17)KB 2
  3. Ubiquitin-conjugating enzyme E2-17 kDa 2
  4. Ubiquitin-protein ligase D2
  5. p53-regulated ubiquitin-conjugating enzyme 1
Gene Name UBE2D2
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. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by DDX58/RIG-I in response to viral infection. Essential for viral activation of IRF3.
Pathways
  • Protein processing in endoplasmic reticulum
  • protein ubiquitination
  • Shigellosis
  • Ubiquitin mediated proteolysis
Reactions
Adenosine triphosphate + ubiquitin + protein lysine → Adenosine monophosphate + Pyrophosphate + protein N-ubiquityllysine details
GO Classification
Biological Process
protein K48-linked ubiquitination
ubiquitin-dependent protein catabolic process
regulation of transcription from RNA polymerase II promoter in response to hypoxia
Cellular Component
cytosol
nucleoplasm
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 Not Available
Gene Properties
Chromosome Location 5
Locus 5q31.2
SNPs UBE2D2
Gene Sequence 
>444 bp
ATGGCTCTGAAGAGAATCCACAAGGAATTGAATGATCTGGCACGGGACCCTCCAGCACAG
TGTTCAGCAGGTCCTGTTGGAGATGATATGTTCCATTGGCAAGCTACAATAATGGGGCCA
AATGACAGTCCCTATCAGGGTGGAGTATTTTTCTTGACAATTCATTTCCCAACAGATTAC
CCCTTCAAACCACCTAAGGTTGCATTTACAACAAGAATTTATCATCCAAATATTAACAGT
AATGGCAGCATTTGTCTTGATATTCTACGATCACAGTGGTCTCCAGCACTAACTATTTCA
AAAGTACTCTTGTCCATCTGTTCTCTGTTGTGTGATCCCAATCCAGATGATCCTTTAGTG
CCTGAGATTGCTCGGATCTACAAAACAGATAGAGAAAAGTACAACAGAATAGCTCGGGAA
TGGACTCAGAAGTATGCGATGTAA
Protein Properties
Number of Residues 147
Molecular Weight 16735.06
Theoretical pI 7.823
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Ubiquitin-conjugating enzyme E2 D2
MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDY
PFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLV
PEIARIYKTDREKYNRIAREWTQKYAM
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P62837
UniProtKB/Swiss-Prot Entry Name UB2D2_HUMAN
PDB IDs
GenBank Gene ID U39317
GeneCard ID UBE2D2
GenAtlas ID UBE2D2
HGNC ID HGNC:12475
References
General References
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  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. 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. Windheim M, Peggie M, Cohen P: Two different classes of E2 ubiquitin-conjugating enzymes are required for the mono-ubiquitination of proteins and elongation by polyubiquitin chains with a specific topology. Biochem J. 2008 Feb 1;409(3):723-9. [PubMed:18042044 ]
  6. Grou CP, Carvalho AF, Pinto MP, Wiese S, Piechura H, Meyer HE, Warscheid B, Sa-Miranda C, Azevedo JE: Members of the E2D (UbcH5) family mediate the ubiquitination of the conserved cysteine of Pex5p, the peroxisomal import receptor. J Biol Chem. 2008 May 23;283(21):14190-7. doi: 10.1074/jbc.M800402200. Epub 2008 Mar 22. [PubMed:18359941 ]
  7. Zeng W, Xu M, Liu S, Sun L, Chen ZJ: Key role of Ubc5 and lysine-63 polyubiquitination in viral activation of IRF3. Mol Cell. 2009 Oct 23;36(2):315-25. doi: 10.1016/j.molcel.2009.09.037. [PubMed:19854139 ]
  8. Jensen JP, Bates PW, Yang M, Vierstra RD, Weissman AM: Identification of a family of closely related human ubiquitin conjugating enzymes. J Biol Chem. 1995 Dec 22;270(51):30408-14. [PubMed:8530467 ]
  9. Rolfe M, Beer-Romero P, Glass S, Eckstein J, Berdo I, Theodoras A, Pagano M, Draetta G: Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP). Proc Natl Acad Sci U S A. 1995 Apr 11;92(8):3264-8. [PubMed:7724550 ]
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  13. Saville MK, Sparks A, Xirodimas DP, Wardrop J, Stevenson LF, Bourdon JC, Woods YL, Lane DP: Regulation of p53 by the ubiquitin-conjugating enzymes UbcH5B/C in vivo. J Biol Chem. 2004 Oct 1;279(40):42169-81. Epub 2004 Jul 26. [PubMed:15280377 ]
  14. Winkler GS, Albert TK, Dominguez C, Legtenberg YI, Boelens R, Timmers HT: An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair. J Mol Biol. 2004 Mar 12;337(1):157-65. [PubMed:15001359 ]
  15. Chiang MH, Chen LF, Chen H: Ubiquitin-conjugating enzyme UBE2D2 is responsible for FBXW2 (F-box and WD repeat domain containing 2)-mediated human GCM1 (glial cell missing homolog 1) ubiquitination and degradation. Biol Reprod. 2008 Nov;79(5):914-20. doi: 10.1095/biolreprod.108.071407. Epub 2008 Aug 13. [PubMed:18703417 ]
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