SAE1

Functionⁱ

The heterodimer acts as an 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/SAE2.7 Publications

Pathwayⁱ: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

GO - Molecular functionⁱ

ATP-dependent protein binding
Source: UniProtKB
Inferred from direct assayⁱ
- 10187858
enzyme activator activity
Source: ProtInc
Traceable author statementⁱ
- 9920803
protein C-terminus binding
Source: UniProtKB
Inferred from direct assayⁱ
- 10187858
protein heterodimerization activity
Source: CAFA
Inferred from direct assayⁱ
- 15660128
small protein activating enzyme binding
Source: CAFA
Inferred from physical interactionⁱ
- 15660128
ubiquitin activating enzyme activity
Source: UniProtKB
Traceable author statementⁱ
- 10187858

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

positive regulation of protein targeting to mitochondrion
Source: ParkinsonsUK-UCL
Inferred from high throughput mutant phenotypeⁱ
- 24270810
protein sumoylation
Source: UniProtKB
Inferred from direct assayⁱ
- 20164921
protein ubiquitination
Source: UniProtKB
Traceable author statementⁱ
- 10187858

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Ligase
Biological process	Ubl conjugation pathway

Enzyme and pathway databases

Reactomeⁱ	R-HSA-3065676 SUMO is conjugated to E1 (UBA2:SAE1) R-HSA-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9)
UniPathwayⁱ	UPA00886

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: SUMO-activating enzyme subunit 1 Alternative name(s): Ubiquitin-like 1-activating enzyme E1A Cleaved into the following chain: SUMO-activating enzyme subunit 1, N-terminally processed
Gene namesⁱ	Name:SAE1 Synonyms:AOS1, SUA1, UBLE1A
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 19

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000142230.11
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:30660 SAE1
MIMⁱ	613294 gene
neXtProtⁱ	NX_Q9UBE0

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	21	R → A: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication		1
Mutagenesisⁱ	24 – 26	RLW → AAA: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication		3

Organism-specific databases

DisGeNET More...DisGeNETⁱ	10055
Open Targets More...OpenTargetsⁱ	ENSG00000142230
PharmGKBⁱ	PA162402387

Chemistry databases

ChEMBLⁱ	CHEMBL1615388

ChEMBLⁱ

CHEMBL1615388

Polymorphism and mutation databases

BioMutaⁱ	SAE1
DMDMⁱ	42559897

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
ChainⁱPRO_0000194966	1 – 346	SUMO-activating enzyme subunit 1Add BLAST	346
Initiator methionineⁱ		Removed; alternateCombined sources1 Publication
ChainⁱPRO_0000423290	2 – 346	SUMO-activating enzyme subunit 1, N-terminally processedAdd BLAST	345

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	1	N-acetylmethionineCombined sources	1
Modified residueⁱ	2	N-acetylvaline; in SUMO-activating enzyme subunit 1, N-terminally processedCombined sources1 Publication	1
Modified residueⁱ	12	PhosphoserineCombined sources	1
Modified residueⁱ	198	N6-acetyllysineBy similarity	1

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

EPDⁱ	Q9UBE0
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9UBE0
PaxDbⁱ	Q9UBE0
PeptideAtlas More...PeptideAtlasⁱ	Q9UBE0
PRIDEⁱ	Q9UBE0
ProteomicsDBⁱ	83952

PTM databases

iPTMnetⁱ	Q9UBE0
PhosphoSitePlusⁱ	Q9UBE0
SwissPalmⁱ	Q9UBE0

Expressionⁱ

Tissue specificityⁱ

Expression level increases during S phase and drops in G2 phase (at protein level).1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000142230 Expressed in 225 organ(s), highest expression level in muscle layer of sigmoid colon
CleanExⁱ	HS_SAE1
ExpressionAtlasⁱ	Q9UBE0 baseline and differential
Genevisibleⁱ	Q9UBE0 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA041906 HPA043552

HPAⁱ

HPA041906
HPA043552

Interactionⁱ

Subunit structureⁱ

Heterodimer of SAE1 and UBA2/SAE2. The heterodimer corresponds to the two domains that are encoded on a single polypeptide chain in ubiquitin-activating enzyme E1. Interacts with UBE2I.2 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
UBA2	Q9UBT2	11	EBI-743154,EBI-718569

With

Entry

#Exp.

IntAct

Notes

UBA2

Q9UBT2

11

EBI-743154,EBI-718569

GO - Molecular functionⁱ

ATP-dependent protein binding
Source: UniProtKB
Inferred from direct assayⁱ
- 10187858
protein C-terminus binding
Source: UniProtKB
Inferred from direct assayⁱ
- 10187858
protein heterodimerization activity
Source: CAFA
Inferred from direct assayⁱ
- 15660128
small protein activating enzyme binding
Source: CAFA
Inferred from physical interactionⁱ
- 15660128

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	115366, 61 interactors
ComplexPortalⁱ	CPX-2161 SUMO activating enzyme complex CPX-3042 activated SUMO1-E1 ligase complex CPX-3044 activated SUMO2-E1 ligase complex CPX-3045 activated SUMO3-E1 ligase complex CPX-3076 activated SUMO4-E1 ligase complex
CORUMⁱ	Q9UBE0
Database of interacting proteins More...DIPⁱ	DIP-34587N
IntActⁱ	Q9UBE0, 28 interactors
Molecular INTeraction database More...MINTⁱ	Q9UBE0
STRINGⁱ	9606.ENSP00000270225

Chemistry databases

BindingDBⁱ

Q9UBE0

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	13 – 26	Combined sources	14
Helixⁱ	28 – 35	Combined sources	8
Beta strandⁱ	38 – 42	Combined sources	5
Helixⁱ	46 – 58	Combined sources	13
Beta strandⁱ	61 – 66	Combined sources	6
Beta strandⁱ	73 – 75	Combined sources	3
Helixⁱ	76 – 78	Combined sources	3
Helixⁱ	91 – 101	Combined sources	11
Beta strandⁱ	106 – 111	Combined sources	6
Helixⁱ	115 – 117	Combined sources	3
Helixⁱ	120 – 123	Combined sources	4
Beta strandⁱ	127 – 133	Combined sources	7
Helixⁱ	136 – 148	Combined sources	13
Beta strandⁱ	152 – 160	Combined sources	9
Beta strandⁱ	162 – 168	Combined sources	7
Beta strandⁱ	170 – 177	Combined sources	8
Beta strandⁱ	206 – 212	Combined sources	7
Helixⁱ	216 – 219	Combined sources	4
Helixⁱ	227 – 233	Combined sources	7
Helixⁱ	239 – 252	Combined sources	14
Beta strandⁱ	253 – 255	Combined sources	3
Helixⁱ	259 – 261	Combined sources	3
Helixⁱ	262 – 278	Combined sources	17
Turnⁱ	279 – 281	Combined sources	3
Helixⁱ	284 – 286	Combined sources	3
Helixⁱ	289 – 293	Combined sources	5
Beta strandⁱ	296 – 298	Combined sources	3
Helixⁱ	300 – 319	Combined sources	20
Beta strandⁱ	327 – 332	Combined sources	6
Turnⁱ	333 – 336	Combined sources	4
Beta strandⁱ	337 – 341	Combined sources	5

Show more details

3D structure databases

Database of protein disorder More...DisProtⁱ	DP00485
ProteinModelPortalⁱ	Q9UBE0
SMRⁱ	Q9UBE0
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q9UBE0

EvolutionaryTraceⁱ

Q9UBE0

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the ubiquitin-activating E1 family.Curated

Phylogenomic databases

eggNOGⁱ	KOG2014 Eukaryota COG0476 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00550000075007
HOGENOMⁱ	HOG000172217
HOVERGENⁱ	HBG080782
InParanoidⁱ	Q9UBE0
KEGG Orthology (KO) More...KOⁱ	K10684
OMAⁱ	SYCFSEM
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0DZ1
PhylomeDBⁱ	Q9UBE0
TreeFamⁱ	TF315037

Family and domain databases

InterProⁱ	View protein in InterPro IPR000594 ThiF_NAD_FAD-bd IPR035985 Ubiquitin-activating_enz IPR000011 UBQ/SUMO-activ_enz_E1-like
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00899 ThiF, 1 hit
PRINTSⁱ	PR01849 UBIQUITINACT
SUPFAMⁱ	SSF69572 SSF69572, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 8 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q9UBE0-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVEKEEAGGG ISEEEAAQYD RQIRLWGLEA QKRLRASRVL LVGLKGLGAE 
        60         70         80         90        100
IAKNLILAGV KGLTMLDHEQ VTPEDPGAQF LIRTGSVGRN RAEASLERAQ 
       110        120        130        140        150
NLNPMVDVKV DTEDIEKKPE SFFTQFDAVC LTCCSRDVIV KVDQICHKNS 
       160        170        180        190        200
IKFFTGDVFG YHGYTFANLG EHEFVEEKTK VAKVSQGVED GPDTKRAKLD 
       210        220        230        240        250
SSETTMVKKK VVFCPVKEAL EVDWSSEKAK AALKRTTSDY FLLQVLLKFR 
       260        270        280        290        300
TDKGRDPSSD TYEEDSELLL QIRNDVLDSL GISPDLLPED FVRYCFSEMA 
       310        320        330        340 
PVCAVVGGIL AQEIVKALSQ RDPPHNNFFF FDGMKGNGIV ECLGPK

Length:346

Mass (Da):38,450

Last modified:May 1, 2000 - v1

Checksum:ⁱE2B10A69FF2ED746

GO

Isoform 2 (identifier: Q9UBE0-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
245-266: VLLKFRTDKGRDPSSDTYEEDS → GTASPRWPQCVRWLEGFWHRKL
267-346: Missing.

« Hide

        10         20         30         40         50
MVEKEEAGGG ISEEEAAQYD RQIRLWGLEA QKRLRASRVL LVGLKGLGAE 
        60         70         80         90        100
IAKNLILAGV KGLTMLDHEQ VTPEDPGAQF LIRTGSVGRN RAEASLERAQ 
       110        120        130        140        150
NLNPMVDVKV DTEDIEKKPE SFFTQFDAVC LTCCSRDVIV KVDQICHKNS 
       160        170        180        190        200
IKFFTGDVFG YHGYTFANLG EHEFVEEKTK VAKVSQGVED GPDTKRAKLD 
       210        220        230        240        250
SSETTMVKKK VVFCPVKEAL EVDWSSEKAK AALKRTTSDY FLLQGTASPR 
       260 
WPQCVRWLEG FWHRKL

Note: No experimental confirmation available.

Show »

Length:266

Mass (Da):29,811

Checksum:ⁱ058AD8B9B2A2EEBB

GO

Isoform 3 (identifier: Q9UBE0-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
245-299: VLLKFRTDKG...DFVRYCFSEM → GPVSAGPSSQ...PTCIPCPLPS
300-346: Missing.

« Hide

        10         20         30         40         50
MVEKEEAGGG ISEEEAAQYD RQIRLWGLEA QKRLRASRVL LVGLKGLGAE 
        60         70         80         90        100
IAKNLILAGV KGLTMLDHEQ VTPEDPGAQF LIRTGSVGRN RAEASLERAQ 
       110        120        130        140        150
NLNPMVDVKV DTEDIEKKPE SFFTQFDAVC LTCCSRDVIV KVDQICHKNS 
       160        170        180        190        200
IKFFTGDVFG YHGYTFANLG EHEFVEEKTK VAKVSQGVED GPDTKRAKLD 
       210        220        230        240        250
SSETTMVKKK VVFCPVKEAL EVDWSSEKAK AALKRTTSDY FLLQGPVSAG 
       260        270        280        290 
PSSQQLLLLR WHEGEWDCGV PWPQVNSRFG SPRDANCSMP TCIPCPLPS

Note: No experimental confirmation available.

Show »

Length:299

Mass (Da):33,063

Checksum:ⁱ35D1828B2957CCBA

GO

Computationally mapped potential isoform sequencesⁱ

There are 8 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

B3KNJ4	B3KNJ4_HUMAN	SUMO-1 activating enzyme subunit 1,... SUMO-1 activating enzyme subunit 1, isoform CRA_a (SUMO-activating enzyme subunit 1) (cDNA FLJ14689 fis, clone NT2RP2005204, highly similar to Ubiquitin-like 1-activating enzyme E1A)	SAE1 hCG_20373	299	Annotation score:
M0QX65	M0QX65_HUMAN	SUMO-activating enzyme subunit 1 SUMO-activating enzyme subunit 1	SAE1	205	Annotation score:
M0R054	M0R054_HUMAN	SUMO-activating enzyme subunit 1 SUMO-activating enzyme subunit 1	SAE1	157	Annotation score:
M0QYP2	M0QYP2_HUMAN	SUMO-activating enzyme subunit 1 SUMO-activating enzyme subunit 1	SAE1	71	Annotation score:
M0QZS6	M0QZS6_HUMAN	SUMO-activating enzyme subunit 1 SUMO-activating enzyme subunit 1	SAE1	265	Annotation score:
M0R286	M0R286_HUMAN	SUMO-activating enzyme subunit 1 SUMO-activating enzyme subunit 1	SAE1	98	Annotation score:
M0QYM8	M0QYM8_HUMAN	SUMO-activating enzyme subunit 1 SUMO-activating enzyme subunit 1	SAE1	133	Annotation score:
M0R375	M0R375_HUMAN	SUMO-activating enzyme subunit 1 SUMO-activating enzyme subunit 1	SAE1	50	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	115	I → M in BAG51064 (Ref. 6) Curated	1
Sequence conflictⁱ	158	V → A in AAF29104 (PubMed:11042152).Curated	1
Sequence conflictⁱ	178 – 180	KTK → ETD in AAF29104 (PubMed:11042152).Curated	3
Sequence conflictⁱ	186	Q → H in AAF29104 (PubMed:11042152).Curated	1
Sequence conflictⁱ	273	R → G in AAD12785 (PubMed:9920803).Curated	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_045372	245 – 299	VLLKF…CFSEM → GPVSAGPSSQQLLLLRWHEG EWDCGVPWPQVNSRFGSPRD ANCSMPTCIPCPLPS in isoform 3. 1 PublicationAdd BLAST	55
Alternative sequenceⁱVSP_045373	245 – 266	VLLKF…YEEDS → GTASPRWPQCVRWLEGFWHR KL in isoform 2. 1 PublicationAdd BLAST	22
Alternative sequenceⁱVSP_045374	267 – 346	Missing in isoform 2. 1 PublicationAdd BLAST	80
Alternative sequenceⁱVSP_045375	300 – 346	Missing in isoform 3. 1 PublicationAdd BLAST	47

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF090385 mRNA Translation: AAD12785.2 AF046025 mRNA Translation: AAD23902.2 AF110956 mRNA Translation: AAD24433.1 AF161489 mRNA Translation: AAF29104.1 AL560234 mRNA No translation available. BT007290 mRNA Translation: AAP35954.1 AK021978 mRNA Translation: BAG51064.1 AK315624 mRNA Translation: BAG37992.1 AC008532 Genomic DNA No translation available. AC008755 Genomic DNA No translation available. CH471126 Genomic DNA Translation: EAW57461.1 CH471126 Genomic DNA Translation: EAW57463.1 BC000344 mRNA Translation: AAH00344.1 BC003611 mRNA Translation: AAH03611.1 BC018271 mRNA Translation: AAH18271.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS12696.1 [Q9UBE0-1] CCDS54284.1 [Q9UBE0-2] CCDS54285.1 [Q9UBE0-3]
NCBI Reference Sequences More...RefSeqⁱ	NP_001139185.1, NM_001145713.1 [Q9UBE0-3] NP_001139186.1, NM_001145714.1 [Q9UBE0-2] NP_005491.1, NM_005500.2 [Q9UBE0-1]
UniGeneⁱ	Hs.515500

Genome annotation databases

Ensemblⁱ	ENST00000270225; ENSP00000270225; ENSG00000142230 [Q9UBE0-1] ENST00000392776; ENSP00000440818; ENSG00000142230 [Q9UBE0-2] ENST00000413379; ENSP00000416557; ENSG00000142230 [Q9UBE0-3]
GeneIDⁱ	10055
KEGGⁱ	hsa:10055
UCSC genome browser More...UCSCⁱ	uc002pgc.4 human [Q9UBE0-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Protein	Similar proteins		Species	Score	Length	Source
Q9UBE0	SUMO-activating enzyme subunit 1		PONAB		346	UniRef100_Q9UBE0
SUMO-activating enzyme subunit 1 (Fragment)		HUMAN		157
SAE1 isoform 1 (Fragment)		PANTR		157
SUMO1 activating enzyme subunit 1		GORGO		346
SUMO-activating enzyme subunit 1		PONAB		382
+11
Q9UBE0-2	SAE1 isoform 11		PANTR		266	UniRef100_K7B2W5
SUMO1 activating enzyme subunit 1		GORGO		266

Protein	Similar proteins		Species	Score	Length	Source
Q9UBE0	SUMO-activating enzyme subunit 1		PONAB		346	UniRef90_Q9UBE0
SUMO-activating enzyme subunit 1		MOUSE		350
SUMO-activating enzyme subunit 1		RAT		349
SUMO-activating enzyme subunit 1 (Fragment)		HUMAN		157
SAE1 isoform 1 (Fragment)		PANTR		157
+38
Q9UBE0-2	SAE1 isoform 11		PANTR		266	UniRef90_K7B2W5
SUMO1 activating enzyme subunit 1		GORGO		266
SUMO-activating enzyme subunit 1 isoform c		CALJA		266
SAE1 isoform 11		PONAB		266
UPI0007625584		MARMA		332
Q9UBE0-3	SAE1 isoform 4		PANTR		299	UniRef90_Q9UBE0-3
Uncharacterized protein		RHIRO		299
Uncharacterized protein		Cebus capucinus imitator		299
SAE1 isoform 4		PONAB		299
Uncharacterized protein		RHIBE		299
+4

Protein	Similar proteins		Species	Score	Length	Source
Q9UBE0	SUMO-activating enzyme subunit 1		PONAB		346	UniRef50_Q9UBE0
SUMO-activating enzyme subunit 1		MOUSE		350
SUMO-activating enzyme subunit 1		RAT		349
SUMO-activating enzyme subunit 1		XENTR		347
SUMO-activating enzyme subunit 1		XENLA		344
+233
Q9UBE0-2	Isoform 2 of SUMO-activating enzyme subunit 1		MOUSE		328	UniRef50_Q9R1T2-2
Uncharacterized protein		MACFA		299
Uncharacterized protein		MACNE		299
Uncharacterized protein		AOTNA		300
Uncharacterized protein		PANTR		328
+90

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF090385 mRNA Translation: AAD12785.2 AF046025 mRNA Translation: AAD23902.2 AF110956 mRNA Translation: AAD24433.1 AF161489 mRNA Translation: AAF29104.1 AL560234 mRNA No translation available. BT007290 mRNA Translation: AAP35954.1 AK021978 mRNA Translation: BAG51064.1 AK315624 mRNA Translation: BAG37992.1 AC008532 Genomic DNA No translation available. AC008755 Genomic DNA No translation available. CH471126 Genomic DNA Translation: EAW57461.1 CH471126 Genomic DNA Translation: EAW57463.1 BC000344 mRNA Translation: AAH00344.1 BC003611 mRNA Translation: AAH03611.1 BC018271 mRNA Translation: AAH18271.1
CCDSⁱ	CCDS12696.1 [Q9UBE0-1] CCDS54284.1 [Q9UBE0-2] CCDS54285.1 [Q9UBE0-3]
RefSeqⁱ	NP_001139185.1, NM_001145713.1 [Q9UBE0-3] NP_001139186.1, NM_001145714.1 [Q9UBE0-2] NP_005491.1, NM_005500.2 [Q9UBE0-1]
UniGeneⁱ	Hs.515500

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1Y8Q	X-ray	2.25	A/C	1-346	[»]
	1Y8R	X-ray	2.75	A/D	1-346	[»]
	3KYC	X-ray	2.45	A	1-346	[»]
	3KYD	X-ray	2.61	A	1-346	[»]
DisProtⁱ	DP00485
ProteinModelPortalⁱ	Q9UBE0
SMRⁱ	Q9UBE0
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	115366, 61 interactors
ComplexPortalⁱ	CPX-2161 SUMO activating enzyme complex CPX-3042 activated SUMO1-E1 ligase complex CPX-3044 activated SUMO2-E1 ligase complex CPX-3045 activated SUMO3-E1 ligase complex CPX-3076 activated SUMO4-E1 ligase complex
CORUMⁱ	Q9UBE0
DIPⁱ	DIP-34587N
IntActⁱ	Q9UBE0, 28 interactors
MINTⁱ	Q9UBE0
STRINGⁱ	9606.ENSP00000270225

Chemistry databases

BindingDBⁱ	Q9UBE0
ChEMBLⁱ	CHEMBL1615388

PTM databases

iPTMnetⁱ	Q9UBE0
PhosphoSitePlusⁱ	Q9UBE0
SwissPalmⁱ	Q9UBE0

Polymorphism and mutation databases

BioMutaⁱ	SAE1
DMDMⁱ	42559897

Proteomic databases

EPDⁱ	Q9UBE0
MaxQBⁱ	Q9UBE0
PaxDbⁱ	Q9UBE0
PeptideAtlasⁱ	Q9UBE0
PRIDEⁱ	Q9UBE0
ProteomicsDBⁱ	83952

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	10055
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000270225; ENSP00000270225; ENSG00000142230 [Q9UBE0-1] ENST00000392776; ENSP00000440818; ENSG00000142230 [Q9UBE0-2] ENST00000413379; ENSP00000416557; ENSG00000142230 [Q9UBE0-3]
GeneIDⁱ	10055
KEGGⁱ	hsa:10055
UCSCⁱ	uc002pgc.4 human [Q9UBE0-1]

Organism-specific databases

CTDⁱ	10055
DisGeNETⁱ	10055
EuPathDBⁱ	HostDB:ENSG00000142230.11
GeneCardsⁱ	SAE1
HGNCⁱ	HGNC:30660 SAE1
HPAⁱ	HPA041906 HPA043552
MIMⁱ	613294 gene
neXtProtⁱ	NX_Q9UBE0
OpenTargetsⁱ	ENSG00000142230
PharmGKBⁱ	PA162402387
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2014 Eukaryota COG0476 LUCA
GeneTreeⁱ	ENSGT00550000075007
HOGENOMⁱ	HOG000172217
HOVERGENⁱ	HBG080782
InParanoidⁱ	Q9UBE0
KOⁱ	K10684
OMAⁱ	SYCFSEM
OrthoDBⁱ	EOG091G0DZ1
PhylomeDBⁱ	Q9UBE0
TreeFamⁱ	TF315037

Enzyme and pathway databases

UniPathwayⁱ	UPA00886
Reactomeⁱ	R-HSA-3065676 SUMO is conjugated to E1 (UBA2:SAE1) R-HSA-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9)

Miscellaneous databases

ChiTaRSⁱ	SAE1 human
EvolutionaryTraceⁱ	Q9UBE0
GeneWikiⁱ	SAE1
GenomeRNAiⁱ	10055
Protein Ontology More...PROⁱ	PR:Q9UBE0
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000142230 Expressed in 225 organ(s), highest expression level in muscle layer of sigmoid colon
CleanExⁱ	HS_SAE1
ExpressionAtlasⁱ	Q9UBE0 baseline and differential
Genevisibleⁱ	Q9UBE0 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR000594 ThiF_NAD_FAD-bd IPR035985 Ubiquitin-activating_enz IPR000011 UBQ/SUMO-activ_enz_E1-like
Pfamⁱ	View protein in Pfam PF00899 ThiF, 1 hit
PRINTSⁱ	PR01849 UBIQUITINACT
SUPFAMⁱ	SSF69572 SSF69572, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	SAE1_HUMAN
Accessionⁱ	Q9UBE0Primary (citable) accession number: Q9UBE0 Secondary accession number(s): B2RDP5 , B3KMQ2, F5GXX7, G3XAK6, O95717, Q9P020
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 16, 2004
	Last sequence update:	May 1, 2000
	Last modified:	October 10, 2018
	This is version 169 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 19
Human chromosome 19: entries, gene names and cross-references to MIM
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9UBE0 (SAE1_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

SUMO-activating enzyme subunit 1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein sumoylation

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

Pathwayⁱ: protein sumoylation

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ