≡

Ubiquitin Like Modifier Activating Enzyme 2 (UBA2)

[Edit]

SAE2; ARX; SUMO1 Activating Enzyme Subunit 2; Anthracycline-associated resistance ARX; Ubiquitin-like 1-activating enzyme E1B; SUMO-activating enzyme subunit 2

Ubiquitin Like Modifier Activating Enzyme 2 (UBA2)
CCC G158
HGNC 30661
MGI 1858313
PubMed 15837425
RGD 1312023
UniProt Q9UBT2
Wiki SAE2
Posttranslational modification of proteins by the addition of the small protein SUMO, or sumoylation, regulates protein structure and intracellular localization. SAE1 and UBA2 form a heterodimer that functions as a SUMO-activating enzyme for the sumoylation of proteins.
The deduced SAE1 and SAE2 proteins contain 347 and 640 amino acids, respectively. SAE1 shares sequence similarity with the N terminus of ubiquitin-activating E1 enzymes, and SAE2 share sequence similarity with the C terminus of E1 enzymes. Both SAE subunits contain a conserved nucleotide-binding motif, and SAE2 contains an E1-like active-site cysteine. SAE2 has a calculated molecular mass of 72 kD. It had an apparent molecular mass of 90 kD by SDS-PAGE.

Organism species: Homo sapiens (Human)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPG158Hu01 Recombinant Ubiquitin Like Modifier Activating Enzyme 2 (UBA2) Positive Control; Immunogen; SDS-PAGE; WB.
Antibodies PAG158Hu01 Polyclonal Antibody to Ubiquitin Like Modifier Activating Enzyme 2 (UBA2) WB; IHC; ICC; IP.
Assay Kits SEG158Hu ELISA Kit for Ubiquitin Like Modifier Activating Enzyme 2 (UBA2) Enzyme-linked immunosorbent assay for Antigen Detection.

Organism species: Mus musculus (Mouse)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPG158Mu01 Recombinant Ubiquitin Like Modifier Activating Enzyme 2 (UBA2) Positive Control; Immunogen; SDS-PAGE; WB.
Antibodies n/a Monoclonal Antibody to Ubiquitin Like Modifier Activating Enzyme 2 (UBA2) Monoclonal Antibody Customized Service Offer
n/a Polyclonal Antibody to Ubiquitin Like Modifier Activating Enzyme 2 (UBA2) Polyclonal Antibody Customized Service Offer
Assay Kits n/a CLIA Kit for Ubiquitin Like Modifier Activating Enzyme 2 (UBA2) CLIA Kit Customized Service Offer
n/a ELISA Kit for Ubiquitin Like Modifier Activating Enzyme 2 (UBA2) ELISA Kit Customized Service Offer

Organism species: Rattus norvegicus (Rat)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins n/a Recombinant Ubiquitin Like Modifier Activating Enzyme 2 (UBA2) Recombinant Protein Customized Service Offer
Antibodies n/a Monoclonal Antibody to Ubiquitin Like Modifier Activating Enzyme 2 (UBA2) Monoclonal Antibody Customized Service Offer
n/a Polyclonal Antibody to Ubiquitin Like Modifier Activating Enzyme 2 (UBA2) Polyclonal Antibody Customized Service Offer
Assay Kits n/a CLIA Kit for Ubiquitin Like Modifier Activating Enzyme 2 (UBA2) CLIA Kit Customized Service Offer
n/a ELISA Kit for Ubiquitin Like Modifier Activating Enzyme 2 (UBA2) ELISA Kit Customized Service Offer
  1. "In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2."Biochem. Biophys. Res. Commun. 254:693-698(1999) [PubMed] [Europe PMC] [Abstract]
  2. "Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin-activating enzyme complex."FEBS Lett. 448:185-189(1999) [PubMed] [Europe PMC] [Abstract]
  3. "Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1."J. Biol. Chem. 274:10618-10624(1999) [PubMed] [Europe PMC] [Abstract]
  4. "Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs." Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
  6. "The DNA sequence and biology of human chromosome 19." Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
  8. "Selection system for genes encoding nuclear-targeted proteins."Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
  9. "Expression and regulation of the mammalian SUMO-1 E1 enzyme."FASEB J. 15:1825-1827(2001) [PubMed] [Europe PMC] [Abstract]
  10. "Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9."J. Biol. Chem. 276:35368-35374(2001) [PubMed] [Europe PMC] [Abstract]
  11. "A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers."Arch. Biochem. Biophys. 453:70-74(2006) [PubMed] [Europe PMC] [Abstract]
  12. "A quantitative atlas of mitotic phosphorylation."Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
  14. "Conformational transition associated with E1-E2 interaction in small ubiquitin-like modifications."J. Biol. Chem. 284:20340-20348(2009) [PubMed] [Europe PMC] [Abstract]
  15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
  17. "Initial characterization of the human central proteome."BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
  18. "Small ubiquitin-like modifier (SUMO) modification of E1 Cys domain inhibits E1 Cys domain enzymatic activity."J. Biol. Chem. 287:15154-15163(2012) [PubMed] [Europe PMC] [Abstract]
  19. "Sumoylation of SAE2 C terminus regulates SAE nuclear localization."J. Biol. Chem. 287:42611-42619(2012) [PubMed] [Europe PMC] [Abstract]
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
  21. "Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1."EMBO J. 24:439-451(2005) [PubMed] [Europe PMC] [Abstract]
  22. "The intrinsic affinity between E2 and the Cys domain of E1 in ubiquitin-like modifications."Mol. Cell 27:228-237(2007) [PubMed] [Europe PMC] [Abstract]
  23. "Active site remodelling accompanies thioester bond formation in the SUMO E1."Nature 463:906-912(2010) [PubMed] [Europe PMC] [Abstract]