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Protein

SUMO-conjugating enzyme UBC9

Gene

UBE2I

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 or CBX4. 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'.7 Publications

Catalytic activityi

ATP + SUMO + protein lysine = AMP + diphosphate + protein N-SUMOyllysine.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei4 – 41Interaction with RANBP2
Sitei25 – 251Interaction with RANBP2
Sitei57 – 571Interaction with RANBP2
Active sitei93 – 931Glycyl thioester intermediate
Sitei100 – 1012Substrate binding

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. enzyme binding Source: UniProtKB
  3. ligase activity Source: UniProtKB-KW
  4. poly(A) RNA binding Source: UniProtKB
  5. RING-like zinc finger domain binding Source: UniProtKB
  6. SUMO conjugating enzyme activity Source: BHF-UCL
  7. transcription factor binding Source: UniProtKB
  8. ubiquitin-protein transferase activity Source: Ensembl

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. cellular protein metabolic process Source: Reactome
  3. cellular protein modification process Source: ProtInc
  4. chromosome segregation Source: UniProtKB-KW
  5. mitotic nuclear division Source: UniProtKB-KW
  6. negative regulation of transcription, DNA-templated Source: BHF-UCL
  7. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  8. positive regulation of intracellular steroid hormone receptor signaling pathway Source: Ensembl
  9. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
  10. positive regulation of SUMO transferase activity Source: BHF-UCL
  11. post-translational protein modification Source: Reactome
  12. proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
  13. protein sumoylation Source: BHF-UCL
  14. protein ubiquitination Source: GO_Central
  15. regulation of receptor activity Source: Ensembl
  16. ubiquitin-dependent protein catabolic process Source: ProtInc
  17. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Host-virus interaction, Mitosis, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_163646. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
REACT_75792. Meiotic synapsis.
SignaLinkiP63279.
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:6.3.2.-)
Alternative name(s):
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
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:12485. UBE2I.

Subcellular locationi

Nucleus. Cytoplasm
Note: Mainly nuclear. In spermatocytes, localizes in synaptonemal complexes. Recruited by BCL11A into the nuclear body (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. dendrite Source: Ensembl
  3. fibrillar center Source: Ensembl
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
  6. PML body Source: UniProtKB
  7. sumoylated E2 ligase complex Source: BHF-UCL
  8. synapse Source: Ensembl
  9. synaptonemal complex Source: ProtInc
  10. transferase complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 142RK → AA: Impairs binding to SUMO1 and catalytic activity. 1 Publication
Mutagenesisi17 – 182RK → AA: Impairs binding to SUMO1 and catalytic activity. 1 Publication
Mutagenesisi22 – 221F → A: Impairs binding to RANBP2. 1 Publication
Mutagenesisi25 – 251V → A: Impairs binding to RANBP2. 1 Publication
Mutagenesisi27 – 271V → A: Impairs binding to RANBP2. 1 Publication
Mutagenesisi42 – 421E → A: Slightly impairs binding to RANBP2. 1 Publication
Mutagenesisi48 – 481K → A: Slightly impairs binding to RANBP2. 1 Publication
Mutagenesisi54 – 541E → A: Slightly impairs binding to RANBP2. 1 Publication
Mutagenesisi57 – 571L → A: Impairs binding to RANBP2. 1 Publication
Mutagenesisi59 – 591K → A: Impairs binding to RANBP2. 1 Publication
Mutagenesisi61 – 611R → A: Slightly impairs binding to RANBP2. 1 Publication
Mutagenesisi85 – 851N → Q: Impairs catalytic activity. 1 Publication
Mutagenesisi87 – 871Y → A: Impairs catalytic activity. 1 Publication
Mutagenesisi93 – 931C → S: Loss of enhancement of sumoylation by RWDD3. No effect on RWDD3 protein levels.
Mutagenesisi100 – 1012DK → AA: Impairs catalytic activity. 1 Publication
Mutagenesisi127 – 1271D → A: Impairs catalytic activity. 1 Publication
Mutagenesisi127 – 1271D → S: No effect on catalytic activity. 1 Publication

Organism-specific databases

PharmGKBiPA37134.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 158157SUMO-conjugating enzyme UBC9PRO_0000082454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Cross-linki18 – 18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei65 – 651N6-acetyllysine1 Publication
Modified residuei71 – 711Phosphoserine; by CDK11 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP63279.
PaxDbiP63279.
PeptideAtlasiP63279.
PRIDEiP63279.

PTM databases

PhosphoSiteiP63279.

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

BgeeiP63279.
CleanExiHS_UBE2I.
ExpressionAtlasiP63279. baseline and differential.
GenevestigatoriP63279.

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.By similarity28 PublicationsCurated

Binary interactionsi

WithEntry#Exp.IntActNotes
P299913EBI-80168,EBI-8826488From a different organism.
BHLHE40O145033EBI-80168,EBI-711810
DAXXQ9UER73EBI-80168,EBI-77321
DNMT3BQ9UBC33EBI-80168,EBI-80125
E1P031162EBI-80168,EBI-7015985From a different organism.
ELK1P194197EBI-80168,EBI-726632
HDAC4P565243EBI-80168,EBI-308629
IPO13O948296EBI-80168,EBI-747310
LMP1P032305EBI-80168,EBI-6973030From a different organism.
PIAS2O759285EBI-80168,EBI-348555
RANGAP1P460605EBI-80168,EBI-396091
RWDD3Q9Y3V25EBI-80168,EBI-1549885
SMAD4Q134854EBI-80168,EBI-347263
SOX10P566932EBI-80168,EBI-1167533
SUMO1P631655EBI-80168,EBI-80140
SUMO2P619566EBI-80168,EBI-473220
TFAP2AP055494EBI-80168,EBI-347351
TFAP2CQ927545EBI-80168,EBI-937309
UBA1P223142EBI-80168,EBI-709688
ZNF451Q9Y4E53EBI-80168,EBI-747230

Protein-protein interaction databases

BioGridi113177. 321 interactions.
DIPiDIP-29078N.
IntActiP63279. 147 interactions.
MINTiMINT-137807.
STRINGi9606.ENSP00000324897.

Structurei

Secondary structure

1
158
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1816Combined sources
Beta strandi25 – 306Combined sources
Beta strandi32 – 343Combined sources
Beta strandi36 – 4611Combined sources
Turni52 – 554Combined sources
Beta strandi57 – 637Combined sources
Turni66 – 694Combined sources
Beta strandi74 – 796Combined sources
Beta strandi90 – 923Combined sources
Helixi95 – 973Combined sources
Turni99 – 1024Combined sources
Helixi109 – 12113Combined sources
Helixi131 – 1399Combined sources
Helixi141 – 15414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP63279.
SMRiP63279. Positions 1-157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63279.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni13 – 186Interaction with SUMO1

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00550000075088.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiP63279.
KOiK10577.
OMAiWEGGVYK.
OrthoDBiEOG7B8S5F.
PhylomeDBiP63279.
TreeFamiTF101122.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR027230. Ubc9.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PANTHERiPTHR24067:SF51. PTHR24067:SF51. 1 hit.
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

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 AAH51289.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAD92225.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181K → P in AAC50603 (PubMed:8668125).Curated
Sequence conflicti86 – 894VYPS → GVPF in AAC50603 (PubMed:8668125).Curated

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. Translation: CAB45853.1.
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_006721002.1. XM_006720939.1.
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.

Polymorphism databases

DMDMi54039791.

Cross-referencesi

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. Translation: CAB45853.1.
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_006721002.1. XM_006720939.1.
UniGeneiHs.302903.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP63279.
SMRiP63279. Positions 1-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113177. 321 interactions.
DIPiDIP-29078N.
IntActiP63279. 147 interactions.
MINTiMINT-137807.
STRINGi9606.ENSP00000324897.

Chemistry

BindingDBiP63279.
ChEMBLiCHEMBL3137290.

Protein family/group databases

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

PTM databases

PhosphoSiteiP63279.

Polymorphism databases

DMDMi54039791.

Proteomic databases

MaxQBiP63279.
PaxDbiP63279.
PeptideAtlasiP63279.
PRIDEiP63279.

Protocols and materials databases

DNASUi7329.
Structural Biology KnowledgebaseSearch...

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.

Organism-specific databases

CTDi7329.
GeneCardsiGC16P001359.
HGNCiHGNC:12485. UBE2I.
HPAiCAB009021.
HPA003909.
MIMi601661. gene.
neXtProtiNX_P63279.
PharmGKBiPA37134.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00550000075088.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiP63279.
KOiK10577.
OMAiWEGGVYK.
OrthoDBiEOG7B8S5F.
PhylomeDBiP63279.
TreeFamiTF101122.

Enzyme and pathway databases

UniPathwayiUPA00886.
ReactomeiREACT_163646. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
REACT_75792. Meiotic synapsis.
SignaLinkiP63279.

Miscellaneous databases

ChiTaRSiUBE2I. human.
EvolutionaryTraceiP63279.
GeneWikiiUBE2I.
GenomeRNAii7329.
NextBioi28682.
PROiP63279.
SOURCEiSearch...

Gene expression databases

BgeeiP63279.
CleanExiHS_UBE2I.
ExpressionAtlasiP63279. baseline and differential.
GenevestigatoriP63279.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR027230. Ubc9.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PANTHERiPTHR24067:SF51. PTHR24067:SF51. 1 hit.
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the structural and functional human homolog of the yeast ubiquitin conjugating enzyme UBC9."
    Yasugi T., Howley P.M.
    Nucleic Acids Res. 24:2005-2010(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "Assignment of the gene for a ubiquitin-conjugating enzyme (UBE2I) to human chromosome band 16p13.3 by in situ hybridization."
    Tachibana M., Iwata N., Watanabe A., Nobukuni Y., Ploplis B., Kajigaya S.
    Cytogenet. Cell Genet. 75:222-223(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning, expression, and mapping of UBE2I, a novel gene encoding a human homologue of yeast ubiquitin-conjugating enzymes which are critical for regulating the cell cycle."
    Watanabe T.K., Fujiwara T., Kawai A., Shimizu F., Takami S., Hirano H., Okuno S., Ozaki K., Takeda S., Shimada Y., Nagata M., Takaichi A., Takahashi E., Nakamura Y., Shin S.
    Cytogenet. Cell Genet. 72:86-89(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal brain.
  4. "Poly(ADP-ribose) polymerase interacts with a novel human ubiquitin conjugating enzyme: hUbc9."
    Masson M., Menissier-de Murcia J., Mattei M.-G., de Murcia G.M., Niedergang C.P.
    Gene 190:287-296(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PARP.
  5. "Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes."
    Kovalenko O.V., Plug A.W., Haaf T., Gonda D.K., Ashley T., Ward D.C., Radding C.M., Golub E.I.
    Proc. Natl. Acad. Sci. U.S.A. 93:2958-2963(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  6. "Two-hybrid interaction of a human UBC9 homolog with centromere proteins of Saccharomyces cerevisiae."
    Jiang W., Koltin Y.
    Mol. Gen. Genet. 251:153-160(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  7. "Molecular cloning of the cDNA and chromosome localization of the gene for human ubiquitin-conjugating enzyme 9."
    Wang Z.-Y., Qiu Q., Seufert W., Taguchi T., Testa J.R., Whitmore S.A., Callen D.F., Welsh D., Shenk T., Deuel T.F.
    J. Biol. Chem. 271:24811-24816(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  8. Shen Z.
    Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  9. "Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-conjugating enzyme."
    Hahn S.L., Criqui-Filipe P., Wasylyk B.
    Oncogene 15:1489-1495(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  10. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  11. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  12. "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
    Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
    Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  14. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  15. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  16. "mUBC9, a novel adenovirus E1A-interacting protein that complements a yeast cell cycle defect."
    Hateboer G., Hijmans E.M., Nooij J.B.D., Schlenker S., Jentsch S., Bernards R.
    J. Biol. Chem. 271:25906-25911(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADENOVIRUS E1A.
  17. "Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway."
    Hu G., Zhang S., Vidal M., Baer J.L., Xu T., Fearon E.R.
    Genes Dev. 11:2701-2714(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIAH1.
  18. "Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription."
    Poukka H., Aarnisalo P., Karvonen U., Palvimo J.J., Jaenne O.A.
    J. Biol. Chem. 274:19441-19446(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AR.
  19. "Association of FHIT (fragile histidine triad), a candidate tumour suppressor gene, with the ubiquitin-conjugating enzyme hUBC9."
    Shi Y., Zou M., Farid N.R., Paterson M.C.
    Biochem. J. 352:443-448(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FHIT.
  20. "Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9."
    Tatham M.H., Jaffray E., Vaughan O.A., Desterro J.M.P., Botting C.H., Naismith J.H., Hay R.T.
    J. Biol. Chem. 276:35368-35374(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo."
    Eloranta J.J., Hurst H.C.
    J. Biol. Chem. 277:30798-30804(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TFAP2A; TFAP2B AND TFAP2C.
  22. "Role of two residues proximal to the active site of Ubc9 in substrate recognition by the Ubc9.SUMO-1 thiolester complex."
    Tatham M.H., Chen Y., Hay R.T.
    Biochemistry 42:3168-3179(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 100-ASP-LYS-101.
  23. "Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation."
    Tatham M.H., Kim S., Yu B., Jaffray E., Song J., Zheng J., Rodriguez M.S., Hay R.T., Chen Y.
    Biochemistry 42:9959-9969(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUMO1; SUMO2; SUMO3 AND THE UBLE1A-UBLE1B E1 COMPLEX, MUTAGENESIS OF 13-ARG-LYS-14 AND 17-ARG-LYS-18.
  24. Cited for: INTERACTION WITH RANBP2.
  25. "Requirement of the coiled-coil domain of PML-RARalpha oncoprotein for localization, sumoylation, and inhibition of monocyte differentiation."
    Kim Y.E., Kim D.Y., Lee J.M., Kim S.T., Han T.H., Ahn J.H.
    Biochem. Biophys. Res. Commun. 330:746-754(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE PML-RARALPHA ONCOPROTEIN, FUNCTION.
  26. "Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection."
    Tatham M.H., Kim S., Jaffray E., Song J., Chen Y., Hay R.T.
    Nat. Struct. Mol. Biol. 12:67-74(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RANBP2, MUTAGENESIS OF PHE-22; VAL-25; VAL-27; GLU-42; LYS-48; GLU-54; LEU-57; LYS-59 AND ARG-61.
  27. "A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers."
    Li T., Santockyte R., Shen R.-F., Tekle E., Wang G., Yang D.C.H., Chock P.B.
    Arch. Biochem. Biophys. 453:70-74(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
  28. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SOX4.
  29. "Functional interaction between human herpesvirus 6 immediate-early 2 protein and ubiquitin-conjugating enzyme 9 in the absence of sumoylation."
    Tomoiu A., Gravel A., Tanguay R.M., Flamand L.
    J. Virol. 80:10218-10228(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HERPESVIRUS 6 IE2.
  30. "RSUME, a small RWD-containing protein, enhances SUMO conjugation and stabilizes HIF-1alpha during hypoxia."
    Carbia-Nagashima A., Gerez J., Perez-Castro C., Paez-Pereda M., Silberstein S., Stalla G.K., Holsboer F., Arzt E.
    Cell 131:309-323(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RWDD3, SUBCELLULAR LOCATION.
  31. "Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response."
    Cheng Z., Ke Y., Ding X., Wang F., Wang H., Wang W., Ahmed K., Liu Z., Xu Y., Aikhionbare F., Yan H., Liu J., Xue Y., Yu J., Powell M., Liang S., Wu Q., Reddy S.E.
    , Hu R., Huang H., Jin C., Yao X.
    Oncogene 27:931-941(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION OF KAT5-UBE2I-SENP6 COMPLEX.
  32. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  33. "SUMOylation enhances DNA methyltransferase 1 activity."
    Lee B., Muller M.T.
    Biochem. J. 421:449-461(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNMT1.
  34. "Sumoylation of forkhead L2 by Ubc9 is required for its activity as a transcriptional repressor of the steroidogenic acute regulatory gene."
    Kuo F.T., Bentsi-Barnes I.K., Barlow G.M., Bae J., Pisarska M.D.
    Cell. Signal. 21:1935-1944(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FOXL2, ROLE IN FOXL2 SUMOYLATION, SUBCELLULAR LOCATION.
  35. "SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle."
    Figueroa-Romero C., Iniguez-Lluhi J.A., Stadler J., Chang C.R., Arnoult D., Keller P.J., Hong Y., Blackstone C., Feldman E.L.
    FASEB J. 23:3917-3927(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNM1L, FUNCTION IN DNM1L SUMOYLATION.
  36. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "Identification of a molecular recognition feature in the E1A oncoprotein that binds the SUMO conjugase UBC9 and likely interferes with polySUMOylation."
    Yousef A.F., Fonseca G.J., Pelka P., Ablack J.N., Walsh C., Dick F.A., Bazett-Jones D.P., Shaw G.S., Mymryk J.S.
    Oncogene 29:4693-4704(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN.
  38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function."
    Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.
    J. Biol. Chem. 286:43793-43808(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MTA1.
  40. "The RAX/PACT-PKR stress response pathway promotes p53 sumoylation and activation, leading to G(1) arrest."
    Bennett R.L., Pan Y., Christian J., Hui T., May W.S. Jr.
    Cell Cycle 11:407-417(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  41. "Phosphorylation of Ubc9 by Cdk1 enhances SUMOylation activity."
    Su Y.F., Yang T., Huang H., Liu L.F., Hwang J.
    PLoS ONE 7:E34250-E34250(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-71.
  42. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  43. "A SUMO-dependent interaction between Senataxin and the exosome, disrupted in the neurodegenerative disease AOA2, targets the exosome to sites of transcription-induced DNA damage."
    Richard P., Feng S., Manley J.L.
    Genes Dev. 27:2227-2232(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SETX.
  44. "UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3 ligase for zinc finger protein 131."
    Oh Y., Chung K.C.
    J. Biol. Chem. 288:9102-9111(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UHRF2.
  45. Cited for: INTERACTION WITH NR3C1.
  46. "In silico structural and functional characterization of the RSUME splice variants."
    Gerez J., Fuertes M., Tedesco L., Silberstein S., Sevlever G., Paez-Pereda M., Holsboer F., Turjanski A.G., Arzt E.
    PLoS ONE 8:E57795-E57795(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RWDD3.
  47. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  48. "Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system."
    Tong H., Hateboer G., Perrakis A., Bernards R., Sixma T.K.
    J. Biol. Chem. 272:21381-21387(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  49. "Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1."
    Bernier-Villamor V., Sampson D.A., Matunis M.J., Lima C.D.
    Cell 108:345-356(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH RANGAP1.
  50. "Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex."
    Reverter D., Lima C.D.
    Nature 435:687-692(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH SUMO1; RANGAP1 AND RANBP2.
  51. "Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway."
    Yunus A.A., Lima C.D.
    Nat. Struct. Mol. Biol. 13:491-499(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH RANGAP1, MUTAGENESIS OF ASN-85; TYR-87 AND ASP-127.
  52. "Structure and analysis of a complex between SUMO and Ubc9 illustrates features of a conserved E2-Ubl interaction."
    Capili A.D., Lima C.D.
    J. Mol. Biol. 369:608-618(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH SUMO1, INTERACTION WITH SUMO1; SUMO2 AND SUMO3, FUNCTION.
  53. "Structural basis for regulation of poly-SUMO chain by a SUMO-like domain of Nip45."
    Sekiyama N., Arita K., Ikeda Y., Hashiguchi K., Ariyoshi M., Tochio H., Saitoh H., Shirakawa M.
    Proteins 78:1491-1502(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH NFATC2IP/NIP45, INTERACTION WITH NFATC2IP, FUNCTION.
  54. "Structure of Importin13-Ubc9 complex: nuclear import and release of a key regulator of sumoylation."
    Grunwald M., Bono F.
    EMBO J. 30:427-438(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH IPO13.

Entry informationi

Entry nameiUBC9_HUMAN
AccessioniPrimary (citable) accession number: P63279
Secondary accession number(s): D3DU69
, P50550, Q15698, Q59GX1, Q86VB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: March 4, 2015
This is version 131 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, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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

External Data

Dasty 3

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 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.