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Identification
HMDB Protein ID HMDBP09256
Secondary Accession Numbers
  • 15084
Name SUMO-activating enzyme subunit 2
Synonyms
  1. Anthracycline-associated resistance ARX
  2. Ubiquitin-like 1-activating enzyme E1B
Gene Name UBA2
Protein Type Enzyme
Biological Properties
General Function Involved in catalytic activity
Specific Function The heterodimer acts as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
catalytic activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
small protein activating enzyme activity
Process
metabolic process
macromolecule metabolic process
macromolecule modification
protein modification process
Cellular Location
  1. Nucleus
Gene Properties
Chromosome Location Chromosome:1
Locus 19q12
SNPs UBA2
Gene Sequence
>1923 bp
ATGGCACTGTCGCGGGGGCTGCCCCGGGAGCTGGCTGAGGCGGTGGCCGGGGGCCGGGTG
CTGGTGGTGGGGGCGGGCGGCATCGGCTGCGAGCTCCTCAAGAATCTCGTGCTCACCGGT
TTCTCCCACATCGACCTGATTGATCTGGATACTATTGATGTAAGCAACCTCAACAGACAG
TTTTTGTTTCAAAAGAAACATGTTGGAAGATCAAAGGCACAGGTTGCCAAGGAAAGTGTA
CTGCAGTTTTACCCGAAAGCTAATATCGTTGCCTACCATGACAGCATCATGAACCCTGAC
TATAATGTGGAATTTTTCCGACAGTTTATACTGGTTATGAATGCTTTAGATAACAGAGCT
GCCCGAAACCATGTTAATAGAATGTGCCTGGCAGCTGATGTTCCTCTTATTGAAAGTGGA
ACAGCTGGGTATCTTGGACAAGTAACTACTATCAAAAAGGGTGTGACCGAGTGTTATGAG
TGTCATCCTAAGCCGACCCAGAGAACCTTTCCTGGCTGTACAATTCGTAACACACCTTCA
GAACCTATACATTGCATCGTTTGGGCAAAGTACTTGTTCAACCAGTTGTTTGGGGAAGAA
GATGCTGATCAAGAAGTATCTCCTGACAGAGCTGACCCTGAAGCTGCCTGGGAACCAACG
GAAGCCGAAGCCAGAGCTAGAGCATCTAATGAAGATGGTGACATTAAACGTATTTCTACT
AAGGAATGGGCTAAATCAACTGGATATGATCCAGTTAAACTTTTTACCAAGCTTTTTAAA
GATGACATCAGGTATCTGTTGACAATGGACAAACTATGGCGGAAAAGGAAACCTCCAGTT
CCGTTGGACTGGGCTGAAGTACAAAGTCAAGGAGAAGAAACGAATGCATCAGATCAACAG
AATGAACCCCAGTTAGGCCTGAAAGACCAGCAGGTTCTAGATGTAAAGAGCTATGCACGT
CTTTTTTCAAAGAGCATCGAGACTTTGAGAGTTCATTTAGCAGAAAAGGGGGATGGAGCT
GAGCTCATATGGGATAAGGATGACCCATCTGCAATGGATTTTGTCACCTCTGCTGCAAAC
CTCAGGATGCATATTTTCAGTATGAATATGAAGAGTAGATTTGATATCAAATCAATGGCA
GGGAACATTATTCCTGCTATTGCTACTACTAATGCAGTAATTGCTGGGTTGATAGTATTG
GAAGGATTGAAGATTTTATCAGGAAAAATAGACCAGTGCAGAACAATTTTTTTGAATAAA
CAACCAAACCCAAGAAAGAAGCTTCTTGTGCCTTGTGCACTGGATCCTCCCAACCCCAAT
TGTTATGTATGTGCCAGCAAGCCAGAGGTGACTGTGCGGCTGAATGTCCATAAAGTGACT
GTTCTCACCTTACAAGACAAGATAGTGAAAGAAAAATTTGCTATGGTAGCACCAGATGTC
CAAATTGAAGATGGGAAAGGAACAATCCTAATATCTTCCGAAGAGGGAGAGACGGAAGCT
AATAATCACAAGAAGTTGTCAGAATTTGGAATTAGAAATGGCAGCCGGCTTCAAGCAGAT
GACTTCCTCCAGGACTATACTTTATTGATCAACATCCTTCATAGTGAAGACCTAGGAAAG
GACGTTGAATTTGAAGTTGTTGGTGATGCCCCGGAAAAAGTGGGGCCCAAACAAGCTGAA
GATGCTGCCAAAAGCATAACCAATGGCAGTGATGATGGAGCTCAGCCCTCCACCTCCACA
GCTCAAGAGCAAGATGACGTTCTCATAGTTGATTCAGATGAAGAAGATTCTTCAAATAAT
GCCGACGTCAGTGAAGAAGAGAGAAGCCGCAAGAGGAAATTAGATGAGAAAGAGAATCTC
AGTGCAAAGAGGTCACGTATAGAACAGAAGGAAGAGCTTGATGATGTCATAGCATTAGAT
TGA
Protein Properties
Number of Residues 640
Molecular Weight 71222.9
Theoretical pI 4.91
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>SUMO-activating enzyme subunit 2
MALSRGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQ
FLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMNPDYNVEFFRQFILVMNALDNRA
ARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRTFPGCTIRNTPS
EPIHCIVWAKYLFNQLFGEEDADQEVSPDRADPEAAWEPTEAEARARASNEDGDIKRIST
KEWAKSTGYDPVKLFTKLFKDDIRYLLTMDKLWRKRKPPVPLDWAEVQSQGEETNASDQQ
NEPQLGLKDQQVLDVKSYARLFSKSIETLRVHLAEKGDGAELIWDKDDPSAMDFVTSAAN
LRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSGKIDQCRTIFLNK
QPNPRKKLLVPCALDPPNPNCYVCASKPEVTVRLNVHKVTVLTLQDKIVKEKFAMVAPDV
QIEDGKGTILISSEEGETEANNHKKLSEFGIRNGSRLQADDFLQDYTLLINILHSEDLGK
DVEFEVVGDAPEKVGPKQAEDAAKSITNGSDDGAQPSTSTAQEQDDVLIVDSDEEDSSNN
ADVSEEERSRKRKLDEKENLSAKRSRIEQKEELDDVIALD
GenBank ID Protein 4885649
UniProtKB/Swiss-Prot ID Q9UBT2
UniProtKB/Swiss-Prot Entry Name SAE2_HUMAN
PDB IDs
GenBank Gene ID NM_005499.2
GeneCard ID UBA2
GenAtlas ID UBA2
HGNC ID HGNC:30661
References
General References
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  2. 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 ]
  3. 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 ]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  5. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed:11230166 ]
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  7. Li T, Santockyte R, Shen RF, Tekle E, Wang G, Yang DC, Chock PB: A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers. Arch Biochem Biophys. 2006 Sep 1;453(1):70-4. Epub 2006 Mar 20. [PubMed:16620772 ]
  8. Ueki N, Oda T, Kondo M, Yano K, Noguchi T, Muramatsu M: Selection system for genes encoding nuclear-targeted proteins. Nat Biotechnol. 1998 Dec;16(13):1338-42. [PubMed:9853615 ]
  9. Okuma T, Honda R, Ichikawa G, Tsumagari N, Yasuda H: In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2. Biochem Biophys Res Commun. 1999 Jan 27;254(3):693-8. [PubMed:9920803 ]
  10. Gong L, Li B, Millas S, Yeh ET: Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin-activating enzyme complex. FEBS Lett. 1999 Apr 1;448(1):185-9. [PubMed:10217437 ]
  11. Desterro JM, Rodriguez MS, Kemp GD, Hay RT: Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1. J Biol Chem. 1999 Apr 9;274(15):10618-24. [PubMed:10187858 ]
  12. Azuma Y, Tan SH, Cavenagh MM, Ainsztein AM, Saitoh H, Dasso M: Expression and regulation of the mammalian SUMO-1 E1 enzyme. FASEB J. 2001 Aug;15(10):1825-7. [PubMed:11481243 ]
  13. Wang J, Lee B, Cai S, Fukui L, Hu W, Chen Y: Conformational transition associated with E1-E2 interaction in small ubiquitin-like modifications. J Biol Chem. 2009 Jul 24;284(30):20340-8. doi: 10.1074/jbc.M109.000257. Epub 2009 May 14. [PubMed:19443651 ]
  14. Lois LM, Lima CD: Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1. EMBO J. 2005 Feb 9;24(3):439-51. Epub 2005 Jan 20. [PubMed:15660128 ]
  15. Wang J, Hu W, Cai S, Lee B, Song J, Chen Y: The intrinsic affinity between E2 and the Cys domain of E1 in ubiquitin-like modifications. Mol Cell. 2007 Jul 20;27(2):228-37. [PubMed:17643372 ]
  16. Olsen SK, Capili AD, Lu X, Tan DS, Lima CD: Active site remodelling accompanies thioester bond formation in the SUMO E1. Nature. 2010 Feb 18;463(7283):906-12. doi: 10.1038/nature08765. [PubMed:20164921 ]