| General information | | DisProt: | DP00486 | | Name: | SUMO-activating enzyme subunit 2 | | Synonym(s): | SAE2_HUMAN
Ubiquitin-like 1-activating enzyme E1B
Anthracycline-associated resistance ARX
| | First appeared in release: | Release 3.1 (03/31/2006) | | UniProt: | Q9UBT2 | | UniGene: | Hs.631580 | | SwissProt: | SAE2_HUMAN | | TrEMBL: | | | NCBI (GI): | 42559898 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 640 | | Percent disordered: | 20% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MALSRGLPRE LAEAVAGGRV LVVGAGGIGC ELLKNLVLTG FSHIDLIDLD TIDVSNLNRQ - 60
FLFQKKHVGR SKAQVAKESV LQFYPKANIV AYHDSIMNPD YNVEFFRQFI LVMNALDNRA - 120
ARNHVNRMCL AADVPLIESG TAGYLGQVTT IKKGVTECYE CHPKPTQRTF PGCTIRNTPS - 180
EPIHCIVWAK YLFNQLFGEE DADQEVSPDR ADPEAAWEPT EAEARARASN EDGDIKRIST - 240
KEWAKSTGYD PVKLFTKLFK DDIRYLLTMD KLWRKRKPPV PLDWAEVQSQ GEETNASDQQ - 300
NEPQLGLKDQ QVLDVKSYAR LFSKSIETLR VHLAEKGDGA ELIWDKDDPS AMDFVTSAAN - 360
LRMHIFSMNM KSRFDIKSMA GNIIPAIATT NAVIAGLIVL EGLKILSGKI DQCRTIFLNK - 420
QPNPRKKLLV PCALDPPNPN CYVCASKPEV TVRLNVHKVT VLTLQDKIVK EKFAMVAPDV - 480
QIEDGKGTIL ISSEEGETEA NNHKKLSEFG IRNGSRLQAD DFLQDYTLLI NILHSEDLGK - 540
DVEFEVVGDA PEKVGPKQAE DAAKSITNGS DDGAQPSTST AQEQDDVLIV DSDEEDSSNN - 600
ADVSEEERSR KRKLDEKENL SAKRSRIEQK EELDDVIALD
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| Functional narrative |
The dimeric enzyme acts as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins and formation of a thioester with a conserved cysteine residue on SAE2.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 1 - 3 | | Length: | 3 | | Region sequence: |
MAL | | Modification type: | Complex
Engineered
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (277 K; ammonium acetate (0.1-1.0 M); ATP 10 mM; polyethylene glycerol 4000 (10-20%); sodium acetate (pH 5.6) 0.1 M)
| References:
- Lois LM, Lima CD. "Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1." Embo J. 2005; 24(3): 439-51. PubMed: 15660128
| Comments:Residues 1-158 are part of the protein's adenylation domain.
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 219 - 237 | | Length: | 19 | | Region sequence: |
PTEAEARARASNEDGDIKR | | Modification type: | Complex
Engineered
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (277 K; ammonium acetate (0.1-1.0 M); ATP 10 mM; polyethylene glycerol 4000 (10-20%); sodium acetate (pH 5.6) 0.1 M)
| References:
- Lois LM, Lima CD. "Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1." Embo J. 2005; 24(3): 439-51. PubMed: 15660128
| Comments:Residues 159-386 make up the catalytic cys domain of the protein. It contains Cys173 which is the catalytic cysteine responsible for E1-SUMO-thioester bond formation.
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| Region 3 | | Type: | Disordered | | Name: | | | Location: | 291 - 304 | | Length: | 14 | | Region sequence: |
GEETNASDQQNEPQ | | Modification type: | Complex
Engineered
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (277 K; ammonium acetate (0.1-1.0 M); ATP 10 mM; polyethylene glycerol 4000 (10-20%); sodium acetate (pH 5.6) 0.1 M)
| References:
- Lois LM, Lima CD. "Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1." Embo J. 2005; 24(3): 439-51. PubMed: 15660128
| Comments:Residues 159-386 make up the catalytic cys domain of the protein. It contains Cys173 which is the catalytic cysteine responsible for E1-SUMO-thioester bond formation.
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| Region 4 | | Type: | Disordered | | Name: | | | Location: | 551 - 640 | | Length: | 90 | | Region sequence: |
PEKVGPKQAEDAAKSITNGSDDGAQPSTSTAQEQDDVLIVDSDEEDSSNNADVSEEERSR
KRKLDEKENLSAKRSRIEQKEELDDVIALD | | Modification type: | Complex
Engineered
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Nuclear localization
| Detection methods:
- X-ray crystallography (277 K; ammonium acetate (0.1-1.0 M); ATP 10 mM; polyethylene glycerol 4000 (10-20%); sodium acetate (pH 5.6) 0.1 M)
| References:
- Lois LM, Lima CD. "Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1." Embo J. 2005; 24(3): 439-51. PubMed: 15660128
| Comments:
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| References |
- 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; 274(15): 10618-24. PubMed: 10187858
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| Comments |
E1 enzymes activate ubiquitin and ubiquitin-like proteins through adenylation, thioester transfer within E1, and thioester transfer from E1 (ubiquitin-activating) to E2 (ubiquitin-conjugating) proteins. The E1 for SUMO activation is the Sae1/Sae2 (or Ubiquitin-like 1-activating enzyme E1A/Ubiquitin-like 1-activating enzyme E1B) protein complex. Refer to DP00485 for Ubiquitin-like 1-activating enzyme E1A.
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