Details for: SAE1
Associated with
Other Information
Genular Protein ID: 2546153082
Symbol: SAE1_HUMAN
Name: SUMO-activating enzyme subunit 1
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 9920803
Title: In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2.
PubMed ID: 9920803
PubMed ID: 10217437
Title: Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin-activating enzyme complex.
PubMed ID: 10217437
PubMed ID: 10187858
Title: Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1.
PubMed ID: 10187858
PubMed ID: 11042152
Title: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells.
PubMed ID: 11042152
DOI: 10.1101/gr.140200
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 15057824
Title: The DNA sequence and biology of human chromosome 19.
PubMed ID: 15057824
DOI: 10.1038/nature02399
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 11481243
Title: Expression and regulation of the mammalian SUMO-1 E1 enzyme.
PubMed ID: 11481243
PubMed ID: 11451954
Title: Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9.
PubMed ID: 11451954
PubMed ID: 16620772
Title: A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers.
PubMed ID: 16620772
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 25489052
Title: Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-acetylation defects.
PubMed ID: 25489052
DOI: 10.1093/hmg/ddu611
PubMed ID: 15660128
Title: Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1.
PubMed ID: 15660128
PubMed ID: 20164921
Title: Active site remodelling accompanies thioester bond formation in the SUMO E1.
PubMed ID: 20164921
DOI: 10.1038/nature08765
Sequence Information:
- Length: 346
- Mass: 38450
- Checksum: E2B10A69FF2ED746
- Sequence:
MVEKEEAGGG ISEEEAAQYD RQIRLWGLEA QKRLRASRVL LVGLKGLGAE IAKNLILAGV KGLTMLDHEQ VTPEDPGAQF LIRTGSVGRN RAEASLERAQ NLNPMVDVKV DTEDIEKKPE SFFTQFDAVC LTCCSRDVIV KVDQICHKNS IKFFTGDVFG YHGYTFANLG EHEFVEEKTK VAKVSQGVED GPDTKRAKLD SSETTMVKKK VVFCPVKEAL EVDWSSEKAK AALKRTTSDY FLLQVLLKFR TDKGRDPSSD TYEEDSELLL QIRNDVLDSL GISPDLLPED FVRYCFSEMA PVCAVVGGIL AQEIVKALSQ RDPPHNNFFF FDGMKGNGIV ECLGPK
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.