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Protein

SUMO-conjugating enzyme UBC9

Gene

Ube2i

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3 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. Essential for nuclear architecture and chromosome segregation (By similarity). Necessary for sumoylation of FOXL2 and KAT5. Sumoylates p53/TP53 at 'Lys-386' (By similarity).By similarity

Catalytic activityi

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

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
Active sitei93Glycyl thioester intermediatePROSITE-ProRule annotation1
Sitei100 – 101Substrate bindingBy similarity2

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • bHLH transcription factor binding Source: RGD
  • ligase activity Source: UniProtKB-KW
  • protein C-terminus binding Source: RGD
  • SUMO transferase activity Source: RGD
  • ubiquitin-protein transferase activity Source: RGD

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • chromosome segregation Source: UniProtKB-KW
  • mitotic nuclear division Source: UniProtKB-KW
  • positive regulation of intracellular steroid hormone receptor signaling pathway Source: RGD
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: RGD
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: RGD
  • protein sumoylation Source: RGD
  • regulation of receptor activity Source: RGD
  • ubiquitin-dependent protein catabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Cell division, Chromosome partition, Mitosis, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
R-RNO-3108214. SUMOylation of DNA damage response and repair proteins.
R-RNO-3232118. SUMOylation of transcription factors.
R-RNO-4570464. SUMOylation of RNA binding proteins.
R-RNO-4615885. SUMOylation of DNA replication proteins.
R-RNO-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-RNO-8866904. Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
UniPathwayiUPA00886.

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-conjugating enzyme UbcE2A1 Publication
Ubiquitin-protein ligase I
Gene namesi
Name:Ube2i
Synonyms:Ubce9
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi3926. Ube2i.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • dendrite Source: RGD
  • fibrillar center Source: RGD
  • nuclear body Source: RGD
  • nuclear envelope Source: RGD
  • nucleus Source: RGD
  • synapse Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000824572 – 158SUMO-conjugating enzyme UBC9Add BLAST157

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Cross-linki18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei65N6-acetyllysineBy similarity1
Modified residuei71Phosphoserine; by CDK1By similarity1

Post-translational modificationi

Phosphorylation at Ser-71 significantly enhances SUMOylation activity.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP63281.
PRIDEiP63281.

PTM databases

iPTMnetiP63281.
PhosphoSitePlusiP63281.

Expressioni

Tissue specificityi

Broadly expressed, with highest levels in spleen and lung (at protein level).1 Publication

Gene expression databases

BgeeiENSRNOG00000017907.
GenevisibleiP63281. RN.

Interactioni

Subunit structurei

Interacts with RASD2 (PubMed:19498170). Interacts with TCF3 (PubMed:9013644). Forms a tight complex with RANGAP1 and RANBP2. Interacts with SIAH1, PARP, HIPK1, HIPK2 and PPM1J. 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 FOXL. Forms a complex with SENP6 and UBE2I in response to UV irradiation. Interacts with DNM1l; the interaction Interacts with DNM1l (via its GTPase and B domains); the interaction promotes sumoylation of DNM1L, mainly in its B domain. Interacts with NFATC2IP; this inhibits formation of poly-SUMO chains. Interacts with FHIT. Interacts with PRKRA and p53/TP53. 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 SETX (By similarity). Interacts with CPEB3 (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei4Interaction with RANBP2By similarity1
Sitei25Interaction with RANBP2By similarity1
Sitei57Interaction with RANBP2By similarity1

GO - Molecular functioni

  • bHLH transcription factor binding Source: RGD
  • protein C-terminus binding Source: RGD

Protein-protein interaction databases

BioGridi247604. 13 interactors.
DIPiDIP-47657N.
IntActiP63281. 1 interactor.
MINTiMINT-4568236.
STRINGi10116.ENSRNOP00000024406.

Structurei

3D structure databases

ProteinModelPortaliP63281.
SMRiP63281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni13 – 18Interaction with SUMO1By similarity6

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0424. Eukaryota.
COG5078. LUCA.
GeneTreeiENSGT00550000075088.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiP63281.
KOiK10577.
OMAiDLKRWEC.
OrthoDBiEOG091G0NAK.
PhylomeDBiP63281.
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.

P63281-1 [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 databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54632 mRNA. Translation: AAC98704.1.
BC086324 mRNA. Translation: AAH86324.1.
BC086592 mRNA. Translation: AAH86592.1.
RefSeqiNP_037182.1. NM_013050.1.
XP_006245980.2. XM_006245918.3.
XP_006245981.1. XM_006245919.3.
XP_006245982.1. XM_006245920.3.
XP_008765771.2. XM_008767549.2.
XP_017452533.1. XM_017597044.1.
UniGeneiRn.2274.

Genome annotation databases

EnsembliENSRNOT00000024406; ENSRNOP00000024406; ENSRNOG00000017907.
GeneIDi25573.
KEGGirno:25573.
UCSCiRGD:3926. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54632 mRNA. Translation: AAC98704.1.
BC086324 mRNA. Translation: AAH86324.1.
BC086592 mRNA. Translation: AAH86592.1.
RefSeqiNP_037182.1. NM_013050.1.
XP_006245980.2. XM_006245918.3.
XP_006245981.1. XM_006245919.3.
XP_006245982.1. XM_006245920.3.
XP_008765771.2. XM_008767549.2.
XP_017452533.1. XM_017597044.1.
UniGeneiRn.2274.

3D structure databases

ProteinModelPortaliP63281.
SMRiP63281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247604. 13 interactors.
DIPiDIP-47657N.
IntActiP63281. 1 interactor.
MINTiMINT-4568236.
STRINGi10116.ENSRNOP00000024406.

PTM databases

iPTMnetiP63281.
PhosphoSitePlusiP63281.

Proteomic databases

PaxDbiP63281.
PRIDEiP63281.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000024406; ENSRNOP00000024406; ENSRNOG00000017907.
GeneIDi25573.
KEGGirno:25573.
UCSCiRGD:3926. rat.

Organism-specific databases

CTDi7329.
RGDi3926. Ube2i.

Phylogenomic databases

eggNOGiKOG0424. Eukaryota.
COG5078. LUCA.
GeneTreeiENSGT00550000075088.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiP63281.
KOiK10577.
OMAiDLKRWEC.
OrthoDBiEOG091G0NAK.
PhylomeDBiP63281.
TreeFamiTF101122.

Enzyme and pathway databases

UniPathwayiUPA00886.
ReactomeiR-RNO-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
R-RNO-3108214. SUMOylation of DNA damage response and repair proteins.
R-RNO-3232118. SUMOylation of transcription factors.
R-RNO-4570464. SUMOylation of RNA binding proteins.
R-RNO-4615885. SUMOylation of DNA replication proteins.
R-RNO-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-RNO-8866904. Negative regulation of activity of TFAP2 (AP-2) family transcription factors.

Miscellaneous databases

PROiP63281.

Gene expression databases

BgeeiENSRNOG00000017907.
GenevisibleiP63281. RN.

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...

Entry informationi

Entry nameiUBC9_RAT
AccessioniPrimary (citable) accession number: P63281
Secondary accession number(s): P50550, Q15698, Q86VB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 30, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.