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Protein

SUMO-activating enzyme subunit 1

Gene

SAE1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Caution

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: CAFA
  • small protein activating enzyme binding Source: CAFA
  • 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

Keywordsi

Molecular functionLigase
Biological processUbl conjugation pathway

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000142230.11
HGNCiHGNC:30660 SAE1
MIMi613294 gene
neXtProtiNX_Q9UBE0

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 sources1 Publication
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 Publication1
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

Show more details

GO - Molecular functioni

  • ATP-dependent protein binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein heterodimerization activity Source: CAFA
  • small protein activating enzyme binding Source: CAFA

Protein-protein interaction databases

BioGridi11536660 interactors.
CORUMiQ9UBE0
DIPiDIP-34587N
IntActiQ9UBE0 28 interactors.
MINTiQ9UBE0
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
OMAiSYCFSEM
OrthoDBiEOG091G0DZ1
PhylomeDBiQ9UBE0
TreeFamiTF315037

Family and domain databases

InterProiView protein in InterPro
IPR000594 ThiF_NAD_FAD-bd
IPR035985 Ubiquitin-activating_enz
IPR000011 UBQ/SUMO-activ_enz_E1-like
PfamiView protein in Pfam
PF00899 ThiF, 1 hit
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

Similar proteinsi

Entry informationi

Entry nameiSAE1_HUMAN
AccessioniPrimary (citable) accession number: Q9UBE0
Secondary accession number(s): B2RDP5
, B3KMQ2, F5GXX7, G3XAK6, O95717, Q9P020
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: May 1, 2000
Last modified: March 28, 2018
This is version 164 of the entry and version 1 of the sequence. See 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