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Protein

SUMO-activating enzyme subunit 1

Gene

SAE1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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
  • enzyme activator activity Source: ProtInc
  • protein C-terminus binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • ubiquitin activating enzyme activity Source: UniProtKB

GO - Biological processi

  • positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
  • protein sumoylation Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
  • regulation of mitotic cell cycle Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciZFISH:ENSG00000142230-MONOMER.
ReactomeiR-HSA-3065676. SUMO is conjugated to E1 (UBA2:SAE1).
R-HSA-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
UniPathwayiUPA00886.

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:
Gene namesi
Name:SAE1
Synonyms:AOS1, SUA1, UBLE1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:30660. SAE1.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • cytosol Source: GO_Central
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • SUMO activating enzyme complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi21R → A: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication1
Mutagenesisi24 – 26RLW → AAA: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication3

Organism-specific databases

DisGeNETi10055.
OpenTargetsiENSG00000142230.
PharmGKBiPA162402387.

Chemistry databases

ChEMBLiCHEMBL1615388.

Polymorphism and mutation databases

BioMutaiSAE1.
DMDMi42559897.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001949661 – 346SUMO-activating enzyme subunit 1Add BLAST346
Initiator methionineiRemoved; alternateCombined sources
ChainiPRO_00004232902 – 346SUMO-activating enzyme subunit 1, N-terminally processedAdd BLAST345

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei2N-acetylvaline; in SUMO-activating enzyme subunit 1, N-terminally processedCombined sources1
Modified residuei12PhosphoserineCombined sources1
Modified residuei198N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9UBE0.
MaxQBiQ9UBE0.
PaxDbiQ9UBE0.
PeptideAtlasiQ9UBE0.
PRIDEiQ9UBE0.

PTM databases

iPTMnetiQ9UBE0.
PhosphoSitePlusiQ9UBE0.
SwissPalmiQ9UBE0.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000142230.
CleanExiHS_SAE1.
ExpressionAtlasiQ9UBE0. baseline and differential.
GenevisibleiQ9UBE0. HS.

Organism-specific databases

HPAiHPA041906.
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

WithEntry#Exp.IntActNotes
UBA2Q9UBT28EBI-743154,EBI-718569

GO - Molecular functioni

  • ATP-dependent protein binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi115366. 55 interactors.
DIPiDIP-34587N.
IntActiQ9UBE0. 20 interactors.
MINTiMINT-1205002.
STRINGi9606.ENSP00000270225.

Chemistry databases

BindingDBiQ9UBE0.

Structurei

Secondary structure

1346
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 26Combined sources14
Helixi28 – 35Combined sources8
Beta strandi38 – 42Combined sources5
Helixi46 – 58Combined sources13
Beta strandi61 – 66Combined sources6
Beta strandi73 – 75Combined sources3
Helixi76 – 78Combined sources3
Helixi91 – 101Combined sources11
Beta strandi106 – 111Combined sources6
Helixi115 – 117Combined sources3
Helixi120 – 123Combined sources4
Beta strandi127 – 133Combined sources7
Helixi136 – 148Combined sources13
Beta strandi152 – 160Combined sources9
Beta strandi162 – 168Combined sources7
Beta strandi170 – 177Combined sources8
Beta strandi206 – 212Combined sources7
Helixi216 – 219Combined sources4
Helixi227 – 233Combined sources7
Helixi239 – 252Combined sources14
Beta strandi253 – 255Combined sources3
Helixi259 – 261Combined sources3
Helixi262 – 278Combined sources17
Turni279 – 281Combined sources3
Helixi284 – 286Combined sources3
Helixi289 – 293Combined sources5
Beta strandi296 – 298Combined sources3
Helixi300 – 319Combined sources20
Beta strandi327 – 332Combined sources6
Turni333 – 336Combined sources4
Beta strandi337 – 341Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y8QX-ray2.25A/C1-346[»]
1Y8RX-ray2.75A/D1-346[»]
3KYCX-ray2.45A1-346[»]
3KYDX-ray2.61A1-346[»]
DisProtiDP00485.
ProteinModelPortaliQ9UBE0.
SMRiQ9UBE0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UBE0.

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Phylogenomic databases

eggNOGiKOG2014. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00550000075007.
HOGENOMiHOG000172217.
HOVERGENiHBG080782.
InParanoidiQ9UBE0.
KOiK10684.
OMAiSEMSPVC.
OrthoDBiEOG091G0DZ1.
PhylomeDBiQ9UBE0.
TreeFamiTF315037.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
[Graphical view]
PRINTSiPR01849. UBIQUITINACT.
SUPFAMiSSF69572. 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. AlignAdd to basket

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

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

Note: No experimental confirmation available.
Show »
Length:266
Mass (Da):29,811
Checksum:i058AD8B9B2A2EEBB
GO
Isoform 3 (identifier: Q9UBE0-3) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:299
Mass (Da):33,063
Checksum:i35D1828B2957CCBA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti115I → M in BAG51064 (Ref. 6) Curated1
Sequence conflicti158V → A in AAF29104 (PubMed:11042152).Curated1
Sequence conflicti178 – 180KTK → ETD in AAF29104 (PubMed:11042152).Curated3
Sequence conflicti186Q → H in AAF29104 (PubMed:11042152).Curated1
Sequence conflicti273R → G in AAD12785 (PubMed:9920803).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_045372245 – 299VLLKF…CFSEM → GPVSAGPSSQQLLLLRWHEG EWDCGVPWPQVNSRFGSPRD ANCSMPTCIPCPLPS in isoform 3. 1 PublicationAdd BLAST55
Alternative sequenceiVSP_045373245 – 266VLLKF…YEEDS → GTASPRWPQCVRWLEGFWHR KL in isoform 2. 1 PublicationAdd BLAST22
Alternative sequenceiVSP_045374267 – 346Missing in isoform 2. 1 PublicationAdd BLAST80
Alternative sequenceiVSP_045375300 – 346Missing in isoform 3. 1 PublicationAdd BLAST47

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.
CCDSiCCDS12696.1. [Q9UBE0-1]
CCDS54284.1. [Q9UBE0-2]
CCDS54285.1. [Q9UBE0-3]
RefSeqiNP_001139185.1. NM_001145713.1. [Q9UBE0-3]
NP_001139186.1. NM_001145714.1. [Q9UBE0-2]
NP_005491.1. NM_005500.2. [Q9UBE0-1]
UniGeneiHs.515500.

Genome annotation databases

EnsembliENST00000270225; ENSP00000270225; ENSG00000142230. [Q9UBE0-1]
ENST00000392776; ENSP00000440818; ENSG00000142230. [Q9UBE0-2]
ENST00000413379; ENSP00000416557; ENSG00000142230. [Q9UBE0-3]
GeneIDi10055.
KEGGihsa:10055.
UCSCiuc002pgc.4. human. [Q9UBE0-1]

Keywords - Coding sequence diversityi

Alternative splicing

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.
CCDSiCCDS12696.1. [Q9UBE0-1]
CCDS54284.1. [Q9UBE0-2]
CCDS54285.1. [Q9UBE0-3]
RefSeqiNP_001139185.1. NM_001145713.1. [Q9UBE0-3]
NP_001139186.1. NM_001145714.1. [Q9UBE0-2]
NP_005491.1. NM_005500.2. [Q9UBE0-1]
UniGeneiHs.515500.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y8QX-ray2.25A/C1-346[»]
1Y8RX-ray2.75A/D1-346[»]
3KYCX-ray2.45A1-346[»]
3KYDX-ray2.61A1-346[»]
DisProtiDP00485.
ProteinModelPortaliQ9UBE0.
SMRiQ9UBE0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115366. 55 interactors.
DIPiDIP-34587N.
IntActiQ9UBE0. 20 interactors.
MINTiMINT-1205002.
STRINGi9606.ENSP00000270225.

Chemistry databases

BindingDBiQ9UBE0.
ChEMBLiCHEMBL1615388.

PTM databases

iPTMnetiQ9UBE0.
PhosphoSitePlusiQ9UBE0.
SwissPalmiQ9UBE0.

Polymorphism and mutation databases

BioMutaiSAE1.
DMDMi42559897.

Proteomic databases

EPDiQ9UBE0.
MaxQBiQ9UBE0.
PaxDbiQ9UBE0.
PeptideAtlasiQ9UBE0.
PRIDEiQ9UBE0.

Protocols and materials databases

DNASUi10055.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000270225; ENSP00000270225; ENSG00000142230. [Q9UBE0-1]
ENST00000392776; ENSP00000440818; ENSG00000142230. [Q9UBE0-2]
ENST00000413379; ENSP00000416557; ENSG00000142230. [Q9UBE0-3]
GeneIDi10055.
KEGGihsa:10055.
UCSCiuc002pgc.4. human. [Q9UBE0-1]

Organism-specific databases

CTDi10055.
DisGeNETi10055.
GeneCardsiSAE1.
HGNCiHGNC:30660. SAE1.
HPAiHPA041906.
HPA043552.
MIMi613294. gene.
neXtProtiNX_Q9UBE0.
OpenTargetsiENSG00000142230.
PharmGKBiPA162402387.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2014. Eukaryota.
COG0476. LUCA.
GeneTreeiENSGT00550000075007.
HOGENOMiHOG000172217.
HOVERGENiHBG080782.
InParanoidiQ9UBE0.
KOiK10684.
OMAiSEMSPVC.
OrthoDBiEOG091G0DZ1.
PhylomeDBiQ9UBE0.
TreeFamiTF315037.

Enzyme and pathway databases

UniPathwayiUPA00886.
BioCyciZFISH:ENSG00000142230-MONOMER.
ReactomeiR-HSA-3065676. SUMO is conjugated to E1 (UBA2:SAE1).
R-HSA-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).

Miscellaneous databases

EvolutionaryTraceiQ9UBE0.
GeneWikiiSAE1.
GenomeRNAii10055.
PROiQ9UBE0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000142230.
CleanExiHS_SAE1.
ExpressionAtlasiQ9UBE0. baseline and differential.
GenevisibleiQ9UBE0. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
[Graphical view]
PRINTSiPR01849. UBIQUITINACT.
SUPFAMiSSF69572. SSF69572. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSAE1_HUMAN
AccessioniPrimary (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: November 30, 2016
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.