UniProtKB - P63279 (UBC9_HUMAN)
SUMO-conjugating enzyme UBC9
UBE2I
Functioni
: protein sumoylation Pathwayi
This protein is involved in the pathway protein sumoylation, which is part of Protein modification.1 PublicationView all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 93 | Glycyl thioester intermediate | 1 | |
Sitei | 100 – 101 | Substrate binding | 2 |
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 cofactor binding Source: ARUK-UCL
- transcription factor binding Source: UniProtKB
GO - Biological processi
- cell cycle Source: UniProtKB-KW
- cell division Source: UniProtKB-KW
- cellular protein modification process Source: ProtInc
- chromosome segregation Source: UniProtKB-KW
- negative regulation of transcription, DNA-templated Source: BHF-UCL
- negative regulation of transcription by RNA polymerase II 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
Keywordsi
Molecular function | Transferase |
Biological process | Cell cycle, Cell division, Chromosome partition, Host-virus interaction, Mitosis, Ubl conjugation pathway |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
PathwayCommonsi | P63279 |
Reactomei | R-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-3108232, SUMO E3 ligases SUMOylate target proteins R-HSA-3232118, SUMOylation of transcription factors R-HSA-3232142, SUMOylation of ubiquitinylation proteins R-HSA-3899300, SUMOylation of transcription cofactors R-HSA-4085377, SUMOylation of SUMOylation proteins R-HSA-4090294, SUMOylation of intracellular receptors 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-4655427, SUMOylation of DNA methylation proteins R-HSA-4755510, SUMOylation of immune response 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 R-HSA-9615933, Postmitotic nuclear pore complex (NPC) reformation R-HSA-9683610, Maturation of nucleoprotein |
SignaLinki | P63279 |
SIGNORi | P63279 |
UniPathwayi | UPA00886 |
Protein family/group databases
MoonDBi | P63279, Predicted |
TCDBi | 3.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 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000103275.18 |
HGNCi | HGNC:12485, UBE2I |
MIMi | 601661, gene |
neXtProti | NX_P63279 |
Subcellular locationi
Cytosol
- cytosol Source: Reactome
Nucleus
- nuclear envelope Source: Reactome
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKB
- PML body Source: UniProtKB
- synaptonemal complex Source: ProtInc
Other locations
- cytoplasm Source: MGI
- sumoylated E2 ligase complex Source: CAFA
- transferase complex Source: BHF-UCL
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 13 – 14 | RK → AA: Impairs binding to SUMO1 and catalytic activity. 1 Publication | 2 | |
Mutagenesisi | 17 – 18 | RK → AA: Impairs binding to SUMO1 and catalytic activity. 1 Publication | 2 | |
Mutagenesisi | 22 | F → A: Impairs binding to RANBP2. 1 Publication | 1 | |
Mutagenesisi | 25 | V → A: Impairs binding to RANBP2. 1 Publication | 1 | |
Mutagenesisi | 27 | V → A: Impairs binding to RANBP2. 1 Publication | 1 | |
Mutagenesisi | 42 | E → A: Slightly impairs binding to RANBP2. 1 Publication | 1 | |
Mutagenesisi | 48 | K → A: Slightly impairs binding to RANBP2. 1 Publication | 1 | |
Mutagenesisi | 54 | E → A: Slightly impairs binding to RANBP2. 1 Publication | 1 | |
Mutagenesisi | 57 | L → A: Impairs binding to RANBP2. 1 Publication | 1 | |
Mutagenesisi | 59 | K → A: Impairs binding to RANBP2. 1 Publication | 1 | |
Mutagenesisi | 61 | R → A: Slightly impairs binding to RANBP2. 1 Publication | 1 | |
Mutagenesisi | 85 | N → Q: Impairs catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 87 | Y → A: Impairs catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 93 | C → S: Loss of enhancement of sumoylation by RWDD3. No effect on RWDD3 protein levels. | 1 | |
Mutagenesisi | 100 – 101 | DK → AA: Impairs catalytic activity. 1 Publication | 2 | |
Mutagenesisi | 127 | D → A: Impairs catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 127 | D → S: No effect on catalytic activity. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 7329 |
OpenTargetsi | ENSG00000103275 |
PharmGKBi | PA37134 |
Miscellaneous databases
Pharosi | P63279, Tbio |
Chemistry databases
ChEMBLi | CHEMBL1741191 |
Polymorphism and mutation databases
BioMutai | UBE2I |
DMDMi | 54039791 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000082454 | 2 – 158 | SUMO-conjugating enzyme UBC9Add BLAST | 157 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineCombined sources | 1 | |
Cross-linki | 18 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources | ||
Cross-linki | 18 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||
Cross-linki | 48 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 49 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources | ||
Cross-linki | 49 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources | ||
Modified residuei | 65 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 71 | Phosphoserine; by CDK1Combined sources1 Publication | 1 | |
Cross-linki | 101 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
CPTACi | CPTAC-1469 CPTAC-1470 CPTAC-1471 CPTAC-3261 CPTAC-711 |
EPDi | P63279 |
jPOSTi | P63279 |
MassIVEi | P63279 |
MaxQBi | P63279 |
PaxDbi | P63279 |
PeptideAtlasi | P63279 |
PRIDEi | P63279 |
ProteomicsDBi | 12715 57517 |
TopDownProteomicsi | P63279 |
PTM databases
iPTMneti | P63279 |
PhosphoSitePlusi | P63279 |
SwissPalmi | P63279 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000103275, Expressed in oocyte and 245 other tissues |
ExpressionAtlasi | P63279, baseline and differential |
Genevisiblei | P63279, HS |
Organism-specific databases
HPAi | ENSG00000103275, Low tissue specificity |
Interactioni
Subunit structurei
Forms a complex with SENP6 and UBE2I in response to UV irradiation (PubMed:17704809).
Forms a tight complex with RANGAP1 and RANBP2 (PubMed:15378033, PubMed:15608651, PubMed:11853669, PubMed:15931224, PubMed:16732283).
Identified in a complex with SUMO2 and UBE2I, where one ZNF451 interacts with one UBE2I and two SUMO2 chains, one bound to the UBE2I active site and the other to another region of the same UBE2I molecule (PubMed:12924945, PubMed:26524494).
Interacts with SETX (PubMed:24105744).
Interacts with HIPK1 and HIPK2 (By similarity).
Interacts with PPM1J (By similarity).
Interacts with RASD2 (By similarity).
Interacts with TCF3 (By similarity).
Interacts with NR2C1; the interaction promotes its sumoylation (By similarity).
Interacts with SIAH1 (PubMed:9334332).
Interacts with PARP (PubMed:9197546).
Interacts with various transcription factors such as TFAP2A, TFAP2B, and TFAP2C (PubMed:12072434).
Interacts with AR (PubMed:10383460).
Interacts with ETS1 (PubMed:9333025).
Interacts with SOX4 (PubMed:16631117).
Interacts with RWDD3; the interaction enhances the sumoylation of a number of proteins such as HIF1A and I-kappa-B (PubMed:17956732, PubMed:23469069).
Interacts with FOXL2 (PubMed:19744555).
Interacts with DNM1l (via its GTPase and B domains); the interaction promotes sumoylation of DNM1L, mainly in its B domain (PubMed:19638400).
Interacts with NFATC2IP; this inhibits formation of poly-SUMO chains (PubMed:20077568).
Interacts with FHIT (PubMed:11085938).
Interacts with PRKRA and p53/TP53 (By similarity).
Interacts with UHRF2 (PubMed:23404503).
Interacts with NR3C1 and this interaction is enhanced in the presence of RWDD3 (PubMed:23508108, PubMed:25918163).
Interacts with MTA1 (PubMed:21965678).
Interacts with ZNF451 (PubMed:26524494).
Interacts with CPEB3 (By similarity).
Interacts with SUMO1, SUMO2 and SUMO3 (PubMed:17466333).
Interacts with IPO13 (PubMed:21139563).
Interacts with DNMT1 (PubMed:19450230).
Interacts with SUMO1P1/SUMO5 (PubMed:27211601).
Interacts with PML-RARA oncoprotein (via the coiled-colied domain); the interaction is required for sumoylation of the PML-RARA oncoprotein (PubMed:15809060).
Interacts with ZBED1/hDREF (PubMed:27068747).
By similarityCurated31 Publications(Microbial infection) Interacts with human herpesvirus 6 IE2.
1 Publication(Microbial infection) Interacts with human adenovirus early E1A protein; this interaction interferes with polysumoylation.
2 Publications(Microbial infection) Interacts with Epstein-barr virus protein LMP1.
1 PublicationSites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 4 | Interaction with RANBP2 | 1 | |
Sitei | 25 | Interaction with RANBP2 | 1 | |
Sitei | 57 | Interaction with RANBP2 | 1 |
Binary interactionsi
Hide detailsP63279
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 cofactor binding Source: ARUK-UCL
- transcription factor binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 113177, 625 interactors |
ComplexPortali | CPX-3043, sumoylated E2 ligase complex (SUMO1) CPX-3049, sumoylated E2 ligase complex (SUMO2) CPX-3050, sumoylated E2 ligase complex (SUMO3) CPX-3051, sumoylated E2 ligase complex (SUMO4) |
CORUMi | P63279 |
DIPi | DIP-29078N |
ELMi | P63279 |
IntActi | P63279, 206 interactors |
MINTi | P63279 |
STRINGi | 9606.ENSP00000348056 |
Chemistry databases
BindingDBi | P63279 |
Miscellaneous databases
RNActi | P63279, protein |
Structurei
Secondary structure
3D structure databases
BMRBi | P63279 |
SMRi | P63279 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P63279 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 4 – 157 | UBC corePROSITE-ProRule annotationAdd BLAST | 154 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 13 – 18 | Interaction with SUMO1 | 6 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0424, Eukaryota |
GeneTreei | ENSGT00550000075088 |
InParanoidi | P63279 |
OMAi | QEPAWRA |
OrthoDBi | 1110467at2759 |
PhylomeDBi | P63279 |
TreeFami | TF101122 |
Family and domain databases
CDDi | cd00195, UBCc, 1 hit |
Gene3Di | 3.10.110.10, 1 hit |
InterProi | View protein in InterPro IPR000608, UBQ-conjugat_E2 IPR023313, UBQ-conjugating_AS IPR016135, UBQ-conjugating_enzyme/RWD |
Pfami | View protein in Pfam PF00179, UQ_con, 1 hit |
SUPFAMi | SSF54495, SSF54495, 1 hit |
PROSITEi | View protein in PROSITE PS00183, UBC_1, 1 hit PS50127, UBC_2, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All
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
Computationally mapped potential isoform sequencesi
There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketB0QYN7 | B0QYN7_HUMAN | SUMO-conjugating enzyme UBC9 | UBE2I | 184 | Annotation score: | ||
H3BQQ9 | H3BQQ9_HUMAN | SUMO-conjugating enzyme UBC9 | UBE2I | 137 | Annotation score: | ||
H3BPC4 | H3BPC4_HUMAN | SUMO-conjugating enzyme UBC9 | UBE2I | 70 | Annotation score: | ||
H3BRD1 | H3BRD1_HUMAN | SUMO-conjugating enzyme UBC9 | UBE2I | 29 | Annotation score: |
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 18 | K → P in AAC50603 (PubMed:8668125).Curated | 1 | |
Sequence conflicti | 86 – 89 | VYPS → GVPF in AAC50603 (PubMed:8668125).Curated | 4 |
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. |
CCDSi | CCDS10433.1 |
PIRi | JC6056 |
RefSeqi | NP_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 |
Genome annotation databases
Similar proteinsi
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 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. |
CCDSi | CCDS10433.1 |
PIRi | JC6056 |
RefSeqi | NP_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 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1A3S | X-ray | 2.80 | A | 1-158 | [»] | |
1KPS | X-ray | 2.50 | A/C | 1-158 | [»] | |
1Z5Q | model | - | A | 1-158 | [»] | |
1Z5S | X-ray | 3.01 | A | 1-158 | [»] | |
2GRN | X-ray | 1.80 | A | 1-158 | [»] | |
2GRO | X-ray | 1.70 | A | 1-158 | [»] | |
2GRP | X-ray | 2.05 | A | 1-158 | [»] | |
2GRQ | X-ray | 1.70 | A | 1-158 | [»] | |
2GRR | X-ray | 1.30 | A | 1-158 | [»] | |
2O25 | X-ray | 2.60 | C/D | 1-158 | [»] | |
2PE6 | X-ray | 2.40 | A | 1-158 | [»] | |
2PX9 | NMR | - | B | 1-158 | [»] | |
2XWU | X-ray | 2.80 | A | 1-158 | [»] | |
3A4S | X-ray | 2.70 | A/B | 1-158 | [»] | |
3UIN | X-ray | 2.60 | A | 1-158 | [»] | |
3UIO | X-ray | 2.60 | A | 1-158 | [»] | |
3UIP | X-ray | 2.29 | A | 1-158 | [»] | |
4W5V | X-ray | 2.50 | A | 1-158 | [»] | |
4Y1L | X-ray | 2.70 | A/B | 1-158 | [»] | |
5D2M | X-ray | 2.40 | A/D | 1-158 | [»] | |
5F6D | X-ray | 1.55 | A | 2-158 | [»] | |
5F6E | X-ray | 1.12 | A | 2-158 | [»] | |
5F6U | X-ray | 1.55 | A | 2-158 | [»] | |
5F6V | X-ray | 1.49 | A | 2-158 | [»] | |
5F6W | X-ray | 1.70 | A | 2-158 | [»] | |
5F6X | X-ray | 1.56 | A | 2-158 | [»] | |
5F6Y | X-ray | 1.14 | A | 2-158 | [»] | |
5FQ2 | X-ray | 2.20 | A | 1-158 | [»] | |
6SYF | X-ray | 1.90 | A/B/C/D | 2-158 | [»] | |
BMRBi | P63279 | |||||
SMRi | P63279 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 113177, 625 interactors |
ComplexPortali | CPX-3043, sumoylated E2 ligase complex (SUMO1) CPX-3049, sumoylated E2 ligase complex (SUMO2) CPX-3050, sumoylated E2 ligase complex (SUMO3) CPX-3051, sumoylated E2 ligase complex (SUMO4) |
CORUMi | P63279 |
DIPi | DIP-29078N |
ELMi | P63279 |
IntActi | P63279, 206 interactors |
MINTi | P63279 |
STRINGi | 9606.ENSP00000348056 |
Chemistry databases
BindingDBi | P63279 |
ChEMBLi | CHEMBL1741191 |
Protein family/group databases
MoonDBi | P63279, Predicted |
TCDBi | 3.A.20.1.1, the peroxisomal protein importer (ppi) family |
PTM databases
iPTMneti | P63279 |
PhosphoSitePlusi | P63279 |
SwissPalmi | P63279 |
Polymorphism and mutation databases
BioMutai | UBE2I |
DMDMi | 54039791 |
Proteomic databases
CPTACi | CPTAC-1469 CPTAC-1470 CPTAC-1471 CPTAC-3261 CPTAC-711 |
EPDi | P63279 |
jPOSTi | P63279 |
MassIVEi | P63279 |
MaxQBi | P63279 |
PaxDbi | P63279 |
PeptideAtlasi | P63279 |
PRIDEi | P63279 |
ProteomicsDBi | 12715 57517 |
TopDownProteomicsi | P63279 |
Protocols and materials databases
ABCDi | P63279, 1 sequenced antibody |
Antibodypediai | 1138, 503 antibodies |
CPTCi | P63279, 1 antibody |
DNASUi | 7329 |
Genome annotation databases
Organism-specific databases
CTDi | 7329 |
DisGeNETi | 7329 |
EuPathDBi | HostDB:ENSG00000103275.18 |
GeneCardsi | UBE2I |
HGNCi | HGNC:12485, UBE2I |
HPAi | ENSG00000103275, Low tissue specificity |
MIMi | 601661, gene |
neXtProti | NX_P63279 |
OpenTargetsi | ENSG00000103275 |
PharmGKBi | PA37134 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0424, Eukaryota |
GeneTreei | ENSGT00550000075088 |
InParanoidi | P63279 |
OMAi | QEPAWRA |
OrthoDBi | 1110467at2759 |
PhylomeDBi | P63279 |
TreeFami | TF101122 |
Enzyme and pathway databases
UniPathwayi | UPA00886 |
PathwayCommonsi | P63279 |
Reactomei | R-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-3108232, SUMO E3 ligases SUMOylate target proteins R-HSA-3232118, SUMOylation of transcription factors R-HSA-3232142, SUMOylation of ubiquitinylation proteins R-HSA-3899300, SUMOylation of transcription cofactors R-HSA-4085377, SUMOylation of SUMOylation proteins R-HSA-4090294, SUMOylation of intracellular receptors 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-4655427, SUMOylation of DNA methylation proteins R-HSA-4755510, SUMOylation of immune response 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 R-HSA-9615933, Postmitotic nuclear pore complex (NPC) reformation R-HSA-9683610, Maturation of nucleoprotein |
SignaLinki | P63279 |
SIGNORi | P63279 |
Miscellaneous databases
BioGRID-ORCSi | 7329, 756 hits in 852 CRISPR screens |
ChiTaRSi | UBE2I, human |
EvolutionaryTracei | P63279 |
GeneWikii | UBE2I |
GenomeRNAii | 7329 |
Pharosi | P63279, Tbio |
PROi | PR:P63279 |
RNActi | P63279, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000103275, Expressed in oocyte and 245 other tissues |
ExpressionAtlasi | P63279, baseline and differential |
Genevisiblei | P63279, HS |
Family and domain databases
CDDi | cd00195, UBCc, 1 hit |
Gene3Di | 3.10.110.10, 1 hit |
InterProi | View protein in InterPro IPR000608, UBQ-conjugat_E2 IPR023313, UBQ-conjugating_AS IPR016135, UBQ-conjugating_enzyme/RWD |
Pfami | View protein in Pfam PF00179, UQ_con, 1 hit |
SUPFAMi | SSF54495, SSF54495, 1 hit |
PROSITEi | View protein in PROSITE PS00183, UBC_1, 1 hit PS50127, UBC_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | UBC9_HUMAN | |
Accessioni | P63279Primary (citable) accession number: P63279 Secondary accession number(s): D3DU69 Q86VB3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 11, 2004 |
Last sequence update: | October 11, 2004 | |
Last modified: | December 2, 2020 | |
This is version 187 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Reference proteomeDocuments
- MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 16
Human chromosome 16: entries, gene names and cross-references to MIM