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Protein

SUMO-conjugating enzyme UBC9

Gene

UBE2I

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

Functioni

Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3 and SUMO4 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Sumoylates p53/TP53 at 'Lys-386'.8 Publications

Catalytic activityi

SUMOyl-[E2 SUMO-conjugating enzyme]-L-cysteine + [acceptor-protein]-L-lysine = [E2 SUMO-conjugating enzyme]-L-cysteine + N6-SUMOyl-[acceptor protein]-L-lysine.1 Publication

Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.1 Publication
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
Active sitei93Glycyl thioester intermediate1
Sitei100 – 101Substrate binding2

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: UniProtKB
  • HLH domain binding Source: Ensembl
  • RING-like zinc finger domain binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • small protein activating enzyme binding Source: CAFA
  • SUMO conjugating enzyme activity Source: BHF-UCL
  • SUMO transferase activity Source: Reactome
  • transcription factor binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: Ensembl

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processCell cycle, Cell division, Chromosome partition, Host-virus interaction, Mitosis, Ubl conjugation pathway
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-1221632 Meiotic synapsis
R-HSA-196791 Vitamin D (calciferol) metabolism
R-HSA-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9)
R-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-3232118 SUMOylation of transcription factors
R-HSA-3899300 SUMOylation of transcription cofactors
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-4570464 SUMOylation of RNA binding proteins
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-5696395 Formation of Incision Complex in GG-NER
R-HSA-8866904 Negative regulation of activity of TFAP2 (AP-2) family transcription factors
SignaLinkiP63279
SIGNORiP63279
UniPathwayiUPA00886

Protein family/group databases

TCDBi3.A.20.1.1 the peroxisomal protein importer (ppi) family

Names & Taxonomyi

Protein namesi
Recommended name:
SUMO-conjugating enzyme UBC9 (EC:2.3.2.-1 Publication)
Alternative name(s):
RING-type E3 SUMO transferase UBC9
SUMO-protein ligase
Ubiquitin carrier protein 9
Ubiquitin carrier protein I
Ubiquitin-conjugating enzyme E2 I
Ubiquitin-protein ligase I
p18
Gene namesi
Name:UBE2I
Synonyms:UBC9, UBCE9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

EuPathDBiHostDB:ENSG00000103275.18
HGNCiHGNC:12485 UBE2I
MIMi601661 gene
neXtProtiNX_P63279

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
Mutagenesisi13 – 14RK → AA: Impairs binding to SUMO1 and catalytic activity. 1 Publication2
Mutagenesisi17 – 18RK → AA: Impairs binding to SUMO1 and catalytic activity. 1 Publication2
Mutagenesisi22F → A: Impairs binding to RANBP2. 1 Publication1
Mutagenesisi25V → A: Impairs binding to RANBP2. 1 Publication1
Mutagenesisi27V → A: Impairs binding to RANBP2. 1 Publication1
Mutagenesisi42E → A: Slightly impairs binding to RANBP2. 1 Publication1
Mutagenesisi48K → A: Slightly impairs binding to RANBP2. 1 Publication1
Mutagenesisi54E → A: Slightly impairs binding to RANBP2. 1 Publication1
Mutagenesisi57L → A: Impairs binding to RANBP2. 1 Publication1
Mutagenesisi59K → A: Impairs binding to RANBP2. 1 Publication1
Mutagenesisi61R → A: Slightly impairs binding to RANBP2. 1 Publication1
Mutagenesisi85N → Q: Impairs catalytic activity. 1 Publication1
Mutagenesisi87Y → A: Impairs catalytic activity. 1 Publication1
Mutagenesisi93C → S: Loss of enhancement of sumoylation by RWDD3. No effect on RWDD3 protein levels. 1
Mutagenesisi100 – 101DK → AA: Impairs catalytic activity. 1 Publication2
Mutagenesisi127D → A: Impairs catalytic activity. 1 Publication1
Mutagenesisi127D → S: No effect on catalytic activity. 1 Publication1

Organism-specific databases

DisGeNETi7329
OpenTargetsiENSG00000103275
PharmGKBiPA37134

Chemistry databases

ChEMBLiCHEMBL1741191

Polymorphism and mutation databases

BioMutaiUBE2I
DMDMi54039791

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000824542 – 158SUMO-conjugating enzyme UBC9Add BLAST157

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Cross-linki18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Cross-linki48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei65N6-acetyllysineCombined sources1
Modified residuei71Phosphoserine; by CDK1Combined sources1 Publication1
Cross-linki101Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Post-translational modificationi

Phosphorylation at Ser-71 significantly enhances SUMOylation activity.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP63279
MaxQBiP63279
PaxDbiP63279
PeptideAtlasiP63279
PRIDEiP63279
TopDownProteomicsiP63279

PTM databases

iPTMnetiP63279
PhosphoSitePlusiP63279
SwissPalmiP63279

Expressioni

Tissue specificityi

Expressed in heart, skeletal muscle, pancreas, kidney, liver, lung, placenta and brain. Also expressed in testis and thymus.1 Publication

Gene expression databases

BgeeiENSG00000103275
CleanExiHS_UBE2I
ExpressionAtlasiP63279 baseline and differential
GenevisibleiP63279 HS

Organism-specific databases

HPAiCAB009021
HPA003909

Interactioni

Subunit structurei

Interacts with SETX (PubMed:24105744). Interacts with HIPK1, HIPK2, PPM1J, RASD2 and TCF3 Interacts with NR2C1; the interaction promotes its sumoylation (By similarity). Forms a tight complex with RANGAP1 and RANBP2. Interacts with SIAH1 and PARP. Interacts with various transcription factors such as TFAP2A, TFAP2B, TFAP2C, AR, ETS1 and SOX4. Interacts with RWDD3; the interaction enhances the sumoylation of a number of proteins such as HIF1A and I-kappa-B. Interacts with DNMT1. Interacts with FOXL2. Forms a complex with SENP6 and UBE2I in response to UV irradiation. Interacts with human herpesvirus 6 IE2. Interacts with human adenovirus early E1A protein; this interaction interferes with polysumoylation (Probable). Interacts with DNM1l (via its GTPase and B domains); the interaction promotes sumoylation of DNM1L, mainly in its B domain. Interacts with PML-RARA oncoprotein (via the coiled-colied domain); the interaction is required for sumoylation of the PML-RARA oncoprotein. Interacts with IPO13. Interacts with NFATC2IP; this inhibits formation of poly-SUMO chains. Interacts with FHIT. Interacts with PRKRA and p53/TP53 (By similarity). Interacts with UHRF2. Interacts with NR3C1 and this interaction is enhanced in the presence of RWDD3. Interacts with MTA1. Interacts with ZNF451. Identified in a complex with SUMO2 and UBC9, where one ZNF451 interacts with one UBC9 and two SUMO2 chains, one bound to the UBC9 active site and the other to another region of the same UBC9 molecule. Interacts with Epstein-barr virus protein LMP1. Interacts with CPEB3 (By similarity).By similarityCurated31 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei4Interaction with RANBP21
Sitei25Interaction with RANBP21
Sitei57Interaction with RANBP21

Binary interactionsi

Show more details

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • HLH domain binding Source: Ensembl
  • RING-like zinc finger domain binding Source: UniProtKB
  • small protein activating enzyme binding Source: CAFA
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113177, 464 interactors
CORUMiP63279
DIPiDIP-29078N
ELMiP63279
IntActiP63279, 195 interactors
MINTiP63279
STRINGi9606.ENSP00000324897

Chemistry databases

BindingDBiP63279

Structurei

Secondary structure

1158
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 18Combined sources16
Beta strandi25 – 30Combined sources6
Beta strandi32 – 34Combined sources3
Beta strandi36 – 46Combined sources11
Turni52 – 55Combined sources4
Beta strandi57 – 63Combined sources7
Turni66 – 69Combined sources4
Beta strandi74 – 79Combined sources6
Beta strandi90 – 92Combined sources3
Helixi95 – 97Combined sources3
Turni99 – 102Combined sources4
Helixi109 – 121Combined sources13
Helixi131 – 139Combined sources9
Helixi141 – 154Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A3SX-ray2.80A1-158[»]
1KPSX-ray2.50A/C1-158[»]
1Z5Qmodel-A1-158[»]
1Z5SX-ray3.01A1-158[»]
2GRNX-ray1.80A1-158[»]
2GROX-ray1.70A1-158[»]
2GRPX-ray2.05A1-158[»]
2GRQX-ray1.70A1-158[»]
2GRRX-ray1.30A1-158[»]
2O25X-ray2.60C/D1-158[»]
2PE6X-ray2.40A1-158[»]
2PX9NMR-B1-158[»]
2XWUX-ray2.80A1-158[»]
3A4SX-ray2.70A/B1-158[»]
3UINX-ray2.60A1-158[»]
3UIOX-ray2.60A1-158[»]
3UIPX-ray2.29A1-158[»]
4W5VX-ray2.50A1-158[»]
4Y1LX-ray2.70A/B1-158[»]
5D2MX-ray2.40A/D1-158[»]
5F6DX-ray1.55A2-158[»]
5F6EX-ray1.12A2-158[»]
5F6UX-ray1.55A2-158[»]
5F6VX-ray1.49A2-158[»]
5F6WX-ray1.70A2-158[»]
5F6XX-ray1.56A2-158[»]
5F6YX-ray1.14A2-158[»]
5FQ2X-ray2.20A1-158[»]
ProteinModelPortaliP63279
SMRiP63279
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63279

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni13 – 18Interaction with SUMO16

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0424 Eukaryota
COG5078 LUCA
GeneTreeiENSGT00550000075088
HOGENOMiHOG000233454
HOVERGENiHBG063308
InParanoidiP63279
KOiK10577
OMAiKCKFTPP
PhylomeDBiP63279
TreeFamiTF101122

Family and domain databases

CDDicd00195 UBCc, 1 hit
Gene3Di3.10.110.10, 1 hit
InterProiView protein in InterPro
IPR027230 Ubc9
IPR000608 UBQ-conjugat_E2
IPR023313 UBQ-conjugating_AS
IPR016135 UBQ-conjugating_enzyme/RWD
PANTHERiPTHR43927 PTHR43927, 1 hit
PfamiView protein in Pfam
PF00179 UQ_con, 1 hit
SUPFAMiSSF54495 SSF54495, 1 hit
PROSITEiView protein in PROSITE
PS00183 UBIQUITIN_CONJUGAT_1, 1 hit
PS50127 UBIQUITIN_CONJUGAT_2, 1 hit

Sequencei

Sequence statusi: Complete.

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

P63279-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG
60 70 80 90 100
TPWEGGLFKL RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED
110 120 130 140 150
KDWRPAITIK QILLGIQELL NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA

QAKKFAPS
Length:158
Mass (Da):18,007
Last modified:October 11, 2004 - v1
Checksum:iE2C826E9C8D0683D
GO

Sequence cautioni

The sequence AAH51289 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAD92225 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti18K → P in AAC50603 (PubMed:8668125).Curated1
Sequence conflicti86 – 89VYPS → GVPF in AAC50603 (PubMed:8668125).Curated4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96427 mRNA Translation: CAA65287.1
U45328 mRNA Translation: AAA86662.1
D45050 mRNA Translation: BAA08091.1
U29092 mRNA Translation: AAC51361.1
U31933 mRNA Translation: AAB02181.1
U31882 mRNA Translation: AAC50603.1
U66867 mRNA Translation: AAC50716.1
U66818 mRNA Translation: AAC50715.1
U38785 mRNA Translation: AAB09410.1
AJ002385 mRNA Translation: CAA05359.1
BT006932 mRNA Translation: AAP35578.1
AB208988 mRNA Translation: BAD92225.1 Different initiation.
AE006466 Genomic DNA Translation: AAK61274.1
AL031714 Genomic DNA No translation available.
CH471112 Genomic DNA Translation: EAW85673.1
CH471112 Genomic DNA Translation: EAW85676.1
CH471112 Genomic DNA Translation: EAW85677.1
CH471112 Genomic DNA Translation: EAW85678.1
CH471112 Genomic DNA Translation: EAW85679.1
BC000427 mRNA Translation: AAH00427.1
BC004429 mRNA Translation: AAH04429.1
BC051289 mRNA Translation: AAH51289.3 Different initiation.
CCDSiCCDS10433.1
PIRiJC6056
RefSeqiNP_003336.1, NM_003345.4
NP_919235.1, NM_194259.2
NP_919236.1, NM_194260.2
NP_919237.1, NM_194261.2
XP_016879129.1, XM_017023640.1
UniGeneiHs.302903

Genome annotation databases

EnsembliENST00000325437; ENSP00000324897; ENSG00000103275
ENST00000355803; ENSP00000348056; ENSG00000103275
ENST00000397514; ENSP00000380649; ENSG00000103275
ENST00000397515; ENSP00000380650; ENSG00000103275
ENST00000403747; ENSP00000385009; ENSG00000103275
ENST00000406620; ENSP00000384568; ENSG00000103275
ENST00000566587; ENSP00000457064; ENSG00000103275
GeneIDi7329
KEGGihsa:7329
UCSCiuc002clc.2 human

Similar proteinsi

Entry informationi

Entry nameiUBC9_HUMAN
AccessioniPrimary (citable) accession number: P63279
Secondary accession number(s): D3DU69
, P50550, Q15698, Q59GX1, Q86VB3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 23, 2018
This is version 165 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, Reference proteome

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