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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, 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

ATP + SUMO + protein lysine = AMP + diphosphate + protein N-SUMOyllysine.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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei93 – 931Glycyl thioester intermediate
Sitei100 – 1012Substrate binding

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: UniProtKB
  • ligase activity Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
  • RING-like zinc finger domain binding Source: UniProtKB
  • SUMO conjugating enzyme activity Source: BHF-UCL
  • SUMO transferase activity Source: Reactome
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • cellular protein modification process Source: ProtInc
  • chromosome segregation Source: UniProtKB-KW
  • global genome nucleotide-excision repair Source: Reactome
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of transcription, DNA-templated Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  • positive regulation of SUMO transferase activity Source: BHF-UCL
  • protein sumoylation Source: UniProtKB
  • ubiquitin-dependent protein catabolic process Source: ProtInc
  • 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

ReactomeiR-HSA-1221632. Meiotic synapsis.
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-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.
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:6.3.2.-1 Publication)
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
Proteomesi
  • UP000005640 Componenti: 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

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • nuclear envelope Source: Reactome
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB
  • sumoylated E2 ligase complex Source: BHF-UCL
  • synaptonemal complex Source: ProtInc
  • 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.

Chemistry

ChEMBLiCHEMBL3137290.

Polymorphism and mutation databases

BioMutaiUBE2I.
DMDMi54039791.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 158157SUMO-conjugating enzyme UBC9PRO_0000082454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Cross-linki18 – 18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki48 – 48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki49 – 49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki49 – 49Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei65 – 651N6-acetyllysineCombined sources
Modified residuei71 – 711Phosphoserine; by CDK1Combined sources1 Publication

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.
PhosphoSiteiP63279.
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.By similarityCurated31 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei4 – 41Interaction with RANBP2
Sitei25 – 251Interaction with RANBP2
Sitei57 – 571Interaction with RANBP2

Binary interactionsi

WithEntry#Exp.IntActNotes
G2XKQ03EBI-80168,EBI-10175576
P299913EBI-80168,EBI-8826488From a different organism.
BHLHE40O145033EBI-80168,EBI-711810
CHMP4BQ9H4443EBI-80168,EBI-749627
DAXXQ9UER73EBI-80168,EBI-77321
DNMT3BQ9UBC33EBI-80168,EBI-80125
E1P031162EBI-80168,EBI-7015985From a different organism.
EDARADDQ8WWZ33EBI-80168,EBI-2949647
ELK1P194197EBI-80168,EBI-726632
GMCL1Q96IK54EBI-80168,EBI-2548508
GOLGA2Q083793EBI-80168,EBI-618309
HDAC4P565243EBI-80168,EBI-308629
IPO13O948296EBI-80168,EBI-747310
LMP1P032305EBI-80168,EBI-6973030From a different organism.
PIAS2O759288EBI-80168,EBI-348555
RANGAP1P460606EBI-80168,EBI-396091
RNF111Q6ZNA45EBI-80168,EBI-2129175
RWDD3Q9Y3V25EBI-80168,EBI-1549885
SETXQ7Z3333EBI-80168,EBI-1220123
SMAD4Q134854EBI-80168,EBI-347263
SOX10P566932EBI-80168,EBI-1167533
SUMO1P631656EBI-80168,EBI-80140
SUMO2P619566EBI-80168,EBI-473220
TFAP2AP055494EBI-80168,EBI-347351
TFAP2CQ927545EBI-80168,EBI-937309
TFCP2Q128004EBI-80168,EBI-717422
UBA1P223142EBI-80168,EBI-709688
ZBTB26Q9HCK03EBI-80168,EBI-3918996
ZCCHC7Q8N3Z63EBI-80168,EBI-7265024
ZNF451Q9Y4E53EBI-80168,EBI-747230

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • RING-like zinc finger domain binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113177. 455 interactions.
DIPiDIP-29078N.
IntActiP63279. 189 interactions.
MINTiMINT-137807.
STRINGi9606.ENSP00000324897.

Chemistry

BindingDBiP63279.

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[»]
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[»]
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

eggNOGiKOG0424. Eukaryota.
COG5078. LUCA.
GeneTreeiENSGT00550000075088.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiP63279.
KOiK10577.
OMAiDLKRWEC.
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 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)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.
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.

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.
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[»]
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[»]
ProteinModelPortaliP63279.
SMRiP63279. Positions 1-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113177. 455 interactions.
DIPiDIP-29078N.
IntActiP63279. 189 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

iPTMnetiP63279.
PhosphoSiteiP63279.
SwissPalmiP63279.

Polymorphism and mutation databases

BioMutaiUBE2I.
DMDMi54039791.

Proteomic databases

EPDiP63279.
MaxQBiP63279.
PaxDbiP63279.
PeptideAtlasiP63279.
PRIDEiP63279.
TopDownProteomicsiP63279.

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.
GeneCardsiUBE2I.
HGNCiHGNC:12485. UBE2I.
HPAiCAB009021.
HPA003909.
MIMi601661. gene.
neXtProtiNX_P63279.
PharmGKBiPA37134.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0424. Eukaryota.
COG5078. LUCA.
GeneTreeiENSGT00550000075088.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiP63279.
KOiK10577.
OMAiDLKRWEC.
PhylomeDBiP63279.
TreeFamiTF101122.

Enzyme and pathway databases

UniPathwayiUPA00886.
ReactomeiR-HSA-1221632. Meiotic synapsis.
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-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.
SignaLinkiP63279.
SIGNORiP63279.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000103275.
CleanExiHS_UBE2I.
ExpressionAtlasiP63279. baseline and differential.
GenevisibleiP63279. HS.

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_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: September 7, 2016
This is version 148 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

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.