UniProt Accession

 SAE1_HUMAN; Q9UBE0; B2RDP5; B3KMQ2; F5GXX7; G3XAK6; O95717; Q9P020 

Genbank Protein ID

 AF090385; AF046025; AF110956; AF161489; AL560234; BT007290; AK021978; AK315624; AC008532; AC008755; CH471126; CH471126; BC000344; BC003611; BC018271 

Genbank Nucleotide ID

 AAD12785.2; AAD23902.2; AAD24433.1; AAF29104.1; AAP35954.1; BAG51064.1; BAG37992.1; EAW57461.1; EAW57463.1; AAH00344.1; AAH03611.1; AAH18271.1 

Protein Name

 SUMO-activating enzyme subunit 1 

Protein Synonyms/Alias

 Ubiquitin-like 1-activating enzyme E1A; SUMO-activating enzyme subunit 1, N-terminally processed 

Gene Name

 SAE1 

Gene Synonyms/Alias

 AOS1; SUA1; UBLE1A 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
32	LWGLEAQKRLRASRV	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
45	RVLLVGLKGLGAEIA	ubiquitination	[2, 3, 5]
53	GLGAEIAKNLILAGV	ubiquitination	[1, 2, 3, 5, 7]
61	NLILAGVKGLTMLDH	ubiquitination	[2, 5]
109	LNPMVDVKVDTEDIE	ubiquitination	[2]
141	CSRDVIVKVDQICHK	ubiquitination	[5]
148	KVDQICHKNSIKFFT	ubiquitination	[5]
152	ICHKNSIKFFTGDVF	ubiquitination	[5]
180	EFVEEKTKVAKVSQG	ubiquitination	[5]
183	EEKTKVAKVSQGVED	ubiquitination	[2, 5, 6]
195	VEDGPDTKRAKLDSS	ubiquitination	[2, 3, 5, 6]
198	GPDTKRAKLDSSETT	ubiquitination	[5]
208	SSETTMVKKKVVFCP	ubiquitination	[2, 3, 5, 6]
209	SETTMVKKKVVFCPV	ubiquitination	[5]
210	ETTMVKKKVVFCPVK	ubiquitination	[5]
217	KVVFCPVKEALEVDW	ubiquitination	[5, 8]
228	EVDWSSEKAKAALKR	ubiquitination	[2, 5, 6]
230	DWSSEKAKAALKRTT	ubiquitination	[5]
335	FFFFDGMKGNGIVEC	ubiquitination	[3, 5]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 

Functional Description

 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. 

Sequence Annotation

 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 2 2 N-acetylvaline; in SUMO-activating enzyme  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Ligase; Nucleus; Reference proteome; Ubl conjugation pathway. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 346 AA 

Protein Sequence

Gene Ontology

 GO:0005634; C:nucleus; NAS:UniProtKB.
 GO:0043008; F:ATP-dependent protein binding; IDA:UniProtKB.
 GO:0008047; F:enzyme activator activity; TAS:ProtInc.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0008022; F:protein C-terminus binding; IDA:UniProtKB.
 GO:0046982; F:protein heterodimerization activity; TAS:UniProtKB.
 GO:0004839; F:ubiquitin activating enzyme activity; TAS:UniProtKB.
 GO:0016925; P:protein sumoylation; IDA:UniProtKB.
 GO:0016567; P:protein ubiquitination; TAS:UniProtKB. 

Interpro

 IPR009036; Molybdenum_cofac_synth_MoeB.
 IPR016040; NAD(P)-bd_dom.
 IPR000594; ThiF_NAD_FAD-bd.
 IPR000011; UBQ/SUMO-activ_enz_E1-like. 

Pfam

 PF00899; ThiF 

SMART

  

PROSITE

  

PRINTS

 PR01849; UBIQUITINACT.