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Protein

SUMO-activating enzyme subunit 2

Gene

UBA2

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/SAE2.6 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei48ATP1 Publication1
Binding sitei72ATP1 Publication1
Metal bindingi158Zinc1
Metal bindingi161Zinc1
Active sitei173Glycyl thioester intermediatePROSITE-ProRule annotation2 Publications1
Metal bindingi441Zinc1
Metal bindingi444Zinc1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi24 – 29ATP1 Publication6
Nucleotide bindingi56 – 59ATP1 Publication4
Nucleotide bindingi95 – 96ATP1 Publication2
Nucleotide bindingi117 – 122ATP1 Publication6

GO - Molecular functioni

  • acid-amino acid ligase activity Source: InterPro
  • ATP binding Source: CAFA
  • enzyme activator activity Source: ProtInc
  • magnesium ion binding Source: CAFA
  • protein heterodimerization activity Source: CAFA
  • small protein activating enzyme binding Source: CAFA
  • SUMO activating enzyme activity Source: UniProtKB
  • SUMO binding Source: CAFA
  • transcription factor binding Source: Ensembl
  • transferase activity Source: UniProtKB-KW
  • ubiquitin-like protein conjugating enzyme binding Source: CAFA

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processUbl conjugation pathway
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

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)
UniPathwayi
UPA00886

Names & Taxonomyi

Protein namesi
Recommended name:
SUMO-activating enzyme subunit 2 (EC:2.3.2.-)
Alternative name(s):
Anthracycline-associated resistance ARX
Ubiquitin-like 1-activating enzyme E1B
Ubiquitin-like modifier-activating enzyme 2
Gene namesi
Name:UBA2
Synonyms:SAE2, UBLE1B
ORF Names:HRIHFB2115
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000126261.12
HGNCiHGNC:30661 UBA2
MIMi613295 gene
neXtProtiNX_Q9UBT2

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

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi56N → A: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication1
Mutagenesisi57L → A: Strongly reduces ATP-dependent activation of SUMO proteins. 1 Publication1
Mutagenesisi59R → A: Strongly reduces ATP-dependent activation of SUMO proteins. 1 Publication1
Mutagenesisi72K → A: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication1
Mutagenesisi117D → A: Abolishes ATP-dependent activation of SUMO proteins. 1 Publication1
Mutagenesisi173C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi174T → A: Slightly reduced enzyme activity. 1 Publication1
Mutagenesisi184H → Q: No effect on enzyme activity. 1 Publication1
Mutagenesisi235I → A: Strongly reduced interaction with UBE2I; when associated with A-238. 1 Publication1
Mutagenesisi238I → A: Strongly reduced interaction with UBE2I; when associated with A-235. 1 Publication1
Mutagenesisi484Missing : Strongly reduced interaction with UBE2I. 1 Publication1
Mutagenesisi485G → GGGG: Strongly reduced interaction with UBE2I. 1 Publication1

Organism-specific databases

DisGeNETi10054
OpenTargetsiENSG00000126261
PharmGKBiPA162407583

Chemistry databases

ChEMBLiCHEMBL3137290

Polymorphism and mutation databases

BioMutaiUBA2
DMDMi42559898

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001949681 – 640SUMO-activating enzyme subunit 2Add BLAST640

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki190Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei207PhosphoserineCombined sources1
Cross-linki236Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-linki236Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei271N6-acetyllysine; alternateCombined sources1
Cross-linki271Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki371Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki420Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki420Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei507PhosphoserineCombined sources1
Cross-linki540Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei592PhosphoserineCombined sources1
Cross-linki611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei613N6-acetyllysine; alternateBy similarity1
Cross-linki613Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki617Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki623Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modificationi

Sumoylated with SUMO1 and SUMO2/3 and by UBC9. Sumoylation at Lys-236 inhibits enzymatic activity. Sumoylation at the C-terminal lysine cluster plays an essential role in nuclear trafficking.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9UBT2
PaxDbiQ9UBT2
PeptideAtlasiQ9UBT2
PRIDEiQ9UBT2
ProteomicsDBi84055

PTM databases

iPTMnetiQ9UBT2
PhosphoSitePlusiQ9UBT2
SwissPalmiQ9UBT2

Expressioni

Gene expression databases

BgeeiENSG00000126261 Expressed in 158 organ(s), highest expression level in kidney
CleanExiHS_UBA2
ExpressionAtlasiQ9UBT2 baseline and differential
GenevisibleiQ9UBT2 HS

Organism-specific databases

HPAiHPA041436

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.4 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi115365, 84 interactors
ComplexPortaliCPX-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
CORUMiQ9UBT2
DIPiDIP-35136N
IntActiQ9UBT2, 18 interactors
MINTiQ9UBT2
STRINGi9606.ENSP00000246548

Chemistry databases

BindingDBiQ9UBT2

Structurei

Secondary structure

1640
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

DisProtiDP00486
ProteinModelPortaliQ9UBT2
SMRiQ9UBT2
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UBT2

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Phylogenomic databases

eggNOGiKOG2013 Eukaryota
COG0476 LUCA
GeneTreeiENSGT00550000074924
HOGENOMiHOG000216514
HOVERGENiHBG060266
InParanoidiQ9UBT2
KOiK10685
OMAiYPGCTIR
OrthoDBiEOG091G07PV
PhylomeDBiQ9UBT2
TreeFamiTF300765

Family and domain databases

Gene3Di1.10.10.520, 1 hit
InterProiView protein in InterPro
IPR000594 ThiF_NAD_FAD-bd
IPR028077 UAE_UbL_dom
IPR023318 Ub_act_enz_dom_a_sf
IPR030661 Uba2
IPR032426 UBA2_C
IPR035985 Ubiquitin-activating_enz
IPR018074 UBQ-activ_enz_E1_CS
IPR033127 UBQ-activ_enz_E1_Cys_AS
PANTHERiPTHR10953:SF5 PTHR10953:SF5, 1 hit
PfamiView protein in Pfam
PF00899 ThiF, 1 hit
PF14732 UAE_UbL, 1 hit
PF16195 UBA2_C, 1 hit
PIRSFiPIRSF039133 SUMO_E1B, 1 hit
SUPFAMiSSF69572 SSF69572, 2 hits
PROSITEiView protein in PROSITE
PS00536 UBIQUITIN_ACTIVAT_1, 1 hit
PS00865 UBIQUITIN_ACTIVAT_2, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9UBT2-1) [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
MALSRGLPRE LAEAVAGGRV LVVGAGGIGC ELLKNLVLTG FSHIDLIDLD
60 70 80 90 100
TIDVSNLNRQ FLFQKKHVGR SKAQVAKESV LQFYPKANIV AYHDSIMNPD
110 120 130 140 150
YNVEFFRQFI LVMNALDNRA ARNHVNRMCL AADVPLIESG TAGYLGQVTT
160 170 180 190 200
IKKGVTECYE CHPKPTQRTF PGCTIRNTPS EPIHCIVWAK YLFNQLFGEE
210 220 230 240 250
DADQEVSPDR ADPEAAWEPT EAEARARASN EDGDIKRIST KEWAKSTGYD
260 270 280 290 300
PVKLFTKLFK DDIRYLLTMD KLWRKRKPPV PLDWAEVQSQ GEETNASDQQ
310 320 330 340 350
NEPQLGLKDQ QVLDVKSYAR LFSKSIETLR VHLAEKGDGA ELIWDKDDPS
360 370 380 390 400
AMDFVTSAAN LRMHIFSMNM KSRFDIKSMA GNIIPAIATT NAVIAGLIVL
410 420 430 440 450
EGLKILSGKI DQCRTIFLNK QPNPRKKLLV PCALDPPNPN CYVCASKPEV
460 470 480 490 500
TVRLNVHKVT VLTLQDKIVK EKFAMVAPDV QIEDGKGTIL ISSEEGETEA
510 520 530 540 550
NNHKKLSEFG IRNGSRLQAD DFLQDYTLLI NILHSEDLGK DVEFEVVGDA
560 570 580 590 600
PEKVGPKQAE DAAKSITNGS DDGAQPSTST AQEQDDVLIV DSDEEDSSNN
610 620 630 640
ADVSEEERSR KRKLDEKENL SAKRSRIEQK EELDDVIALD
Length:640
Mass (Da):71,224
Last modified:February 16, 2004 - v2
Checksum:iC12D15293BBF90EB
GO
Isoform 2 (identifier: Q9UBT2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-96: Missing.

Note: No experimental confirmation available.
Show »
Length:544
Mass (Da):60,839
Checksum:i24F5E43AB6FA2B05
GO

Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7EPL2K7EPL2_HUMAN
SUMO-activating enzyme subunit 2
UBA2
262Annotation score:
U3KQ93U3KQ93_HUMAN
SUMO-activating enzyme subunit 2
UBA2
166Annotation score:
K7ESK7K7ESK7_HUMAN
SUMO-activating enzyme subunit 2
UBA2
215Annotation score:
U3KQ55U3KQ55_HUMAN
SUMO-activating enzyme subunit 2
UBA2
54Annotation score:
K7ES38K7ES38_HUMAN
SUMO-activating enzyme subunit 2
UBA2
74Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti229S → C in AAD12784 (PubMed:9920803).Curated1
Sequence conflicti229S → C in AAD23914 (PubMed:10217437).Curated1
Sequence conflicti341E → G in CAB66839 (PubMed:11230166).Curated1
Sequence conflicti456V → L in BAD92109 (Ref. 11) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_017689307L → R2 PublicationsCorresponds to variant dbSNP:rs1043062Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0561641 – 96Missing in isoform 2. 1 PublicationAdd BLAST96

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF090384 mRNA Translation: AAD12784.1
AF079566 mRNA Translation: AAD23914.1
AF110957 mRNA Translation: AAD24434.1
U35832 mRNA Translation: AAC99992.1
AL136905 mRNA Translation: CAB66839.1
AK124730 mRNA Translation: BAG54081.1
BT009781 mRNA Translation: AAP88783.1
CR456756 mRNA Translation: CAG33037.1
AC008747 Genomic DNA No translation available.
BC003153 mRNA Translation: AAH03153.1
AB208872 mRNA Translation: BAD92109.1
AB015337 mRNA Translation: BAA34795.1
CCDSiCCDS12439.1 [Q9UBT2-1]
PIRiT46936
RefSeqiNP_005490.1, NM_005499.2 [Q9UBT2-1]
UniGeneiHs.631580

Genome annotation databases

EnsembliENST00000246548; ENSP00000246548; ENSG00000126261 [Q9UBT2-1]
ENST00000439527; ENSP00000437484; ENSG00000126261 [Q9UBT2-2]
GeneIDi10054
KEGGihsa:10054
UCSCiuc002nvk.4 human [Q9UBT2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF090384 mRNA Translation: AAD12784.1
AF079566 mRNA Translation: AAD23914.1
AF110957 mRNA Translation: AAD24434.1
U35832 mRNA Translation: AAC99992.1
AL136905 mRNA Translation: CAB66839.1
AK124730 mRNA Translation: BAG54081.1
BT009781 mRNA Translation: AAP88783.1
CR456756 mRNA Translation: CAG33037.1
AC008747 Genomic DNA No translation available.
BC003153 mRNA Translation: AAH03153.1
AB208872 mRNA Translation: BAD92109.1
AB015337 mRNA Translation: BAA34795.1
CCDSiCCDS12439.1 [Q9UBT2-1]
PIRiT46936
RefSeqiNP_005490.1, NM_005499.2 [Q9UBT2-1]
UniGeneiHs.631580

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y8QX-ray2.25B/D1-640[»]
1Y8RX-ray2.75B/E1-640[»]
2PX9NMR-A166-382[»]
3KYCX-ray2.45B1-640[»]
3KYDX-ray2.61B1-549[»]
4W5VX-ray2.50B445-561[»]
5FQ2X-ray2.20B446-547[»]
DisProtiDP00486
ProteinModelPortaliQ9UBT2
SMRiQ9UBT2
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115365, 84 interactors
ComplexPortaliCPX-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
CORUMiQ9UBT2
DIPiDIP-35136N
IntActiQ9UBT2, 18 interactors
MINTiQ9UBT2
STRINGi9606.ENSP00000246548

Chemistry databases

BindingDBiQ9UBT2
ChEMBLiCHEMBL3137290

PTM databases

iPTMnetiQ9UBT2
PhosphoSitePlusiQ9UBT2
SwissPalmiQ9UBT2

Polymorphism and mutation databases

BioMutaiUBA2
DMDMi42559898

Proteomic databases

EPDiQ9UBT2
PaxDbiQ9UBT2
PeptideAtlasiQ9UBT2
PRIDEiQ9UBT2
ProteomicsDBi84055

Protocols and materials databases

DNASUi10054
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000246548; ENSP00000246548; ENSG00000126261 [Q9UBT2-1]
ENST00000439527; ENSP00000437484; ENSG00000126261 [Q9UBT2-2]
GeneIDi10054
KEGGihsa:10054
UCSCiuc002nvk.4 human [Q9UBT2-1]

Organism-specific databases

CTDi10054
DisGeNETi10054
EuPathDBiHostDB:ENSG00000126261.12
GeneCardsiUBA2
HGNCiHGNC:30661 UBA2
HPAiHPA041436
MIMi613295 gene
neXtProtiNX_Q9UBT2
OpenTargetsiENSG00000126261
PharmGKBiPA162407583
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2013 Eukaryota
COG0476 LUCA
GeneTreeiENSGT00550000074924
HOGENOMiHOG000216514
HOVERGENiHBG060266
InParanoidiQ9UBT2
KOiK10685
OMAiYPGCTIR
OrthoDBiEOG091G07PV
PhylomeDBiQ9UBT2
TreeFamiTF300765

Enzyme and pathway databases

UniPathwayi
UPA00886

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

Miscellaneous databases

ChiTaRSiUBA2 human
EvolutionaryTraceiQ9UBT2
GeneWikiiUBA2
GenomeRNAii10054
PROiPR:Q9UBT2
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000126261 Expressed in 158 organ(s), highest expression level in kidney
CleanExiHS_UBA2
ExpressionAtlasiQ9UBT2 baseline and differential
GenevisibleiQ9UBT2 HS

Family and domain databases

Gene3Di1.10.10.520, 1 hit
InterProiView protein in InterPro
IPR000594 ThiF_NAD_FAD-bd
IPR028077 UAE_UbL_dom
IPR023318 Ub_act_enz_dom_a_sf
IPR030661 Uba2
IPR032426 UBA2_C
IPR035985 Ubiquitin-activating_enz
IPR018074 UBQ-activ_enz_E1_CS
IPR033127 UBQ-activ_enz_E1_Cys_AS
PANTHERiPTHR10953:SF5 PTHR10953:SF5, 1 hit
PfamiView protein in Pfam
PF00899 ThiF, 1 hit
PF14732 UAE_UbL, 1 hit
PF16195 UBA2_C, 1 hit
PIRSFiPIRSF039133 SUMO_E1B, 1 hit
SUPFAMiSSF69572 SSF69572, 2 hits
PROSITEiView protein in PROSITE
PS00536 UBIQUITIN_ACTIVAT_1, 1 hit
PS00865 UBIQUITIN_ACTIVAT_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSAE2_HUMAN
AccessioniPrimary (citable) accession number: Q9UBT2
Secondary accession number(s): B3KWB9
, O95605, Q59H87, Q6IBP6, Q9NTJ1, Q9UED2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: February 16, 2004
Last modified: September 12, 2018
This is version 173 of the entry and version 2 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, Reference proteome

Documents

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