UBE2I | ENSG00000103275 | NCBI 7329

Details for: UBE2I

Gene ID: 7329

Symbol: UBE2I

Ensembl ID: ENSG00000103275

Description: ubiquitin conjugating enzyme E2 I

Associated with

Antiviral mechanism by ifn-stimulated genes
(R-HSA-1169410)
Cell cycle
(R-HSA-1640170)
Cell cycle, mitotic
(R-HSA-69278)
Cytokine signaling in immune system
(R-HSA-1280215)
Disease
(R-HSA-1643685)
Dna double-strand break repair
(R-HSA-5693532)
Dna double strand break response
(R-HSA-5693606)
Dna repair
(R-HSA-73894)
Epigenetic regulation of gene expression
(R-HSA-212165)
Formation of incision complex in gg-ner
(R-HSA-5696395)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Global genome nucleotide excision repair (gg-ner)
(R-HSA-5696399)
Hdr through homologous recombination (hrr) or single strand annealing (ssa)
(R-HSA-5693567)
Homology directed repair
(R-HSA-5693538)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Interferon signaling
(R-HSA-913531)
Late sars-cov-2 infection events
(R-HSA-9772573)
Maturation of nucleoprotein
(R-HSA-9694631)
Meiosis
(R-HSA-1500620)
Meiotic synapsis
(R-HSA-1221632)
Metabolism
(R-HSA-1430728)
Metabolism of lipids
(R-HSA-556833)
Metabolism of proteins
(R-HSA-392499)
Metabolism of steroids
(R-HSA-8957322)
Mitotic anaphase
(R-HSA-68882)
Mitotic metaphase and anaphase
(R-HSA-2555396)
M phase
(R-HSA-68886)
Negative regulation of activity of tfap2 (ap-2) family transcription factors
(R-HSA-8866904)
Nuclear envelope (ne) reassembly
(R-HSA-2995410)
Nucleotide excision repair
(R-HSA-5696398)
Pkr-mediated signaling
(R-HSA-9833482)
Post-translational protein modification
(R-HSA-597592)
Postmitotic nuclear pore complex (npc) reformation
(R-HSA-9615933)
Processing and activation of sumo
(R-HSA-3215018)
Processing of dna double-strand break ends
(R-HSA-5693607)
Recruitment and atm-mediated phosphorylation of repair and signaling proteins at dna double strand breaks
(R-HSA-5693565)
Regulation of endogenous retroelements
(R-HSA-9842860)
Regulation of endogenous retroelements by krab-zfp proteins
(R-HSA-9843940)
Reproduction
(R-HSA-1474165)
Rna polymerase ii transcription
(R-HSA-73857)
Sars-cov-1 infection
(R-HSA-9678108)
Sars-cov-1 targets host intracellular signalling and regulatory pathways
(R-HSA-9735871)
Sars-cov-1-host interactions
(R-HSA-9692914)
Sars-cov-2 infection
(R-HSA-9694516)
Sars-cov infections
(R-HSA-9679506)
Sumo e3 ligases sumoylate target proteins
(R-HSA-3108232)
Sumo is transferred from e1 to e2 (ube2i, ubc9)
(R-HSA-3065678)
Sumoylation
(R-HSA-2990846)
Sumoylation of chromatin organization proteins
(R-HSA-4551638)
Sumoylation of dna damage response and repair proteins
(R-HSA-3108214)
Sumoylation of dna methylation proteins
(R-HSA-4655427)
Sumoylation of dna replication proteins
(R-HSA-4615885)
Sumoylation of immune response proteins
(R-HSA-4755510)
Sumoylation of intracellular receptors
(R-HSA-4090294)
Sumoylation of nuclear envelope proteins
(R-HSA-9793242)
Sumoylation of rna binding proteins
(R-HSA-4570464)
Sumoylation of sumoylation proteins
(R-HSA-4085377)
Sumoylation of transcription cofactors
(R-HSA-3899300)
Sumoylation of transcription factors
(R-HSA-3232118)
Sumoylation of ubiquitinylation proteins
(R-HSA-3232142)
Transcriptional regulation by the ap-2 (tfap2) family of transcription factors
(R-HSA-8864260)
Translation of structural proteins
(R-HSA-9694635)
Viral infection pathways
(R-HSA-9824446)
Vitamin d (calciferol) metabolism
(R-HSA-196791)
Atp binding
(GO:0005524)
Cell division
(GO:0051301)
Chromosome segregation
(GO:0007059)
Enzyme binding
(GO:0019899)
Mitotic nuclear membrane reassembly
(GO:0007084)
Negative regulation of dna-templated transcription
(GO:0045892)
Negative regulation of transcription by rna polymerase ii
(GO:0000122)
Nuclear envelope
(GO:0005635)
Nuclear export
(GO:0051168)
Nuclear pore
(GO:0005643)
Nucleus
(GO:0005634)
Positive regulation of cell migration
(GO:0030335)
Positive regulation of sumo transferase activity
(GO:1903755)
Protein binding
(GO:0005515)
Protein modification process
(GO:0036211)
Protein sumoylation
(GO:0016925)
Ring-like zinc finger domain binding
(GO:0071535)
Rna binding
(GO:0003723)
Small protein activating enzyme binding
(GO:0044388)
Sumo conjugating enzyme activity
(GO:0061656)
Sumo transferase activity
(GO:0019789)
Synaptonemal complex
(GO:0000795)
Transcription coregulator binding
(GO:0001221)
Transcription factor binding
(GO:0008134)
Ubiquitin-dependent protein catabolic process
(GO:0006511)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 375.5821
Cell Significance Index: -58.4200
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 215.8542
Cell Significance Index: -54.7500
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 189.9028
Cell Significance Index: -78.2300
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 167.6771
Cell Significance Index: -68.1200
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 166.4186
Cell Significance Index: -78.5700
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 148.4490
Cell Significance Index: -76.3600
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 117.3434
Cell Significance Index: -78.7400
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 72.6164
Cell Significance Index: -69.3300
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 58.0394
Cell Significance Index: -71.5600
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 19.0748
Cell Significance Index: -75.2700
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 16.8318
Cell Significance Index: -45.0900
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 15.4389
Cell Significance Index: -47.4200
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 9.8328
Cell Significance Index: -21.5200
Cell Name: skeletal muscle myoblast (CL0000515)
Fold Change: 2.9812
Cell Significance Index: 32.4100
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: 2.7957
Cell Significance Index: 97.1500
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 2.7160
Cell Significance Index: 320.3000
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: 2.6888
Cell Significance Index: 56.2800
Cell Name: granulosa cell (CL0000501)
Fold Change: 2.6857
Cell Significance Index: 70.6200
Cell Name: early pro-B cell (CL0002046)
Fold Change: 2.6759
Cell Significance Index: 172.6400
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 2.3065
Cell Significance Index: 316.7500
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 2.0658
Cell Significance Index: 97.0900
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: 2.0236
Cell Significance Index: 25.9200
Cell Name: cell in vitro (CL0001034)
Fold Change: 1.8896
Cell Significance Index: 1031.9800
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 1.8847
Cell Significance Index: 51.3000
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: 1.8005
Cell Significance Index: 52.8800
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 1.7684
Cell Significance Index: 287.6100
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 1.7369
Cell Significance Index: 213.5700
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 1.7333
Cell Significance Index: 312.4700
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 1.5002
Cell Significance Index: 43.0100
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 1.4699
Cell Significance Index: 109.5500
Cell Name: odontoblast (CL0000060)
Fold Change: 1.3806
Cell Significance Index: 176.9800
Cell Name: kidney cell (CL1000497)
Fold Change: 1.3777
Cell Significance Index: 11.0000
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 1.3298
Cell Significance Index: 69.0800
Cell Name: neoplastic cell (CL0001063)
Fold Change: 1.3270
Cell Significance Index: 263.3500
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 1.3164
Cell Significance Index: 582.0000
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 1.3044
Cell Significance Index: 34.8300
Cell Name: lactocyte (CL0002325)
Fold Change: 1.2613
Cell Significance Index: 162.9500
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 1.1229
Cell Significance Index: 58.4900
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 1.0179
Cell Significance Index: 47.4600
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 0.9789
Cell Significance Index: 69.2300
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 0.7926
Cell Significance Index: 22.1500
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 0.7517
Cell Significance Index: 150.7900
Cell Name: endothelial cell of venule (CL1000414)
Fold Change: 0.6338
Cell Significance Index: 7.2000
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 0.6238
Cell Significance Index: 11.5300
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.5932
Cell Significance Index: 58.6800
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 0.3760
Cell Significance Index: 19.7400
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.3420
Cell Significance Index: 7.4100
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.3368
Cell Significance Index: 120.8200
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.3348
Cell Significance Index: 302.3100
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.2199
Cell Significance Index: 37.5600
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.1734
Cell Significance Index: 32.9900
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.1288
Cell Significance Index: 89.0500
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.1213
Cell Significance Index: 5.5000
Cell Name: mesenchymal cell (CL0008019)
Fold Change: 0.0911
Cell Significance Index: 1.5300
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: 0.0450
Cell Significance Index: 1.2100
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.0408
Cell Significance Index: 76.8500
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: 0.0177
Cell Significance Index: 13.4000
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0118
Cell Significance Index: -8.7600
Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.0169
Cell Significance Index: -31.2000
Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.0250
Cell Significance Index: -38.5300
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0334
Cell Significance Index: -3.4100
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0472
Cell Significance Index: -29.4600
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.0502
Cell Significance Index: -68.3300
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0504
Cell Significance Index: -36.9400
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: -0.0624
Cell Significance Index: -0.5800
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.0641
Cell Significance Index: -40.7300
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0760
Cell Significance Index: -42.8800
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.0987
Cell Significance Index: -44.7800
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: -0.1244
Cell Significance Index: -6.9800
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.1629
Cell Significance Index: -34.3100
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.1870
Cell Significance Index: -21.4200
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.2152
Cell Significance Index: -61.9100
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -0.2169
Cell Significance Index: -13.3300
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.2239
Cell Significance Index: -26.0900
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: -0.2621
Cell Significance Index: -9.2100
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.3080
Cell Significance Index: -35.1600
Cell Name: pro-T cell (CL0000827)
Fold Change: -0.3171
Cell Significance Index: -8.1000
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.3410
Cell Significance Index: -49.5700
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: -0.3756
Cell Significance Index: -28.8300
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -0.4514
Cell Significance Index: -28.4500
Cell Name: peg cell (CL4033014)
Fold Change: -0.6138
Cell Significance Index: -14.1800
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.6392
Cell Significance Index: -42.9800
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.6640
Cell Significance Index: -69.1400
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -0.7036
Cell Significance Index: -9.6000
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: -0.7899
Cell Significance Index: -54.6300
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.8322
Cell Significance Index: -65.9100
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.8595
Cell Significance Index: -27.5300
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.8823
Cell Significance Index: -18.7900
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: -0.8899
Cell Significance Index: -15.2500
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: -0.9100
Cell Significance Index: -24.3900
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: -0.9368
Cell Significance Index: -5.6600
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -1.0447
Cell Significance Index: -30.7700
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -1.1411
Cell Significance Index: -69.9600
Cell Name: intestinal epithelial cell (CL0002563)
Fold Change: -1.1664
Cell Significance Index: -12.0800
Cell Name: vascular lymphangioblast (CL0005022)
Fold Change: -1.1765
Cell Significance Index: -20.7900
Cell Name: luminal hormone-sensing cell of mammary gland (CL4033058)
Fold Change: -1.1943
Cell Significance Index: -7.3500
Cell Name: germ cell (CL0000586)
Fold Change: -1.2052
Cell Significance Index: -9.1000
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -1.2179
Cell Significance Index: -53.8700
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: -1.2729
Cell Significance Index: -31.8200
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -1.4782
Cell Significance Index: -55.9800

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics** UBE2I is a small ubiquitin-like modifier (SUMO) conjugating enzyme that plays a crucial role in the SUMOylation of target proteins. SUMOylation is a post-translational modification process that involves the covalent attachment of SUMO proteins to target proteins, resulting in changes to their function, localization, and stability. UBE2I is a key enzyme in the SUMOylation pathway, responsible for transferring SUMO proteins from SUMO-conjugating enzyme E1 (UBE1) to SUMO-conjugating enzyme E3 (UBE2F) or UBE2I. UBE2I is also involved in the regulation of protein degradation, transcriptional regulation, and DNA repair. **Pathways and Functions** UBE2I is involved in a wide range of cellular pathways, including: 1. **Antiviral mechanism by IFN-stimulated genes**: UBE2I is involved in the regulation of interferon signaling, which is a key component of the innate immune response against viral infections. 2. **Cell cycle**: UBE2I regulates cell cycle progression by modulating the activity of key cell cycle regulators, including cyclin-dependent kinases and cyclin-dependent kinase inhibitors. 3. **DNA repair**: UBE2I is involved in the regulation of DNA repair pathways, including non-homologous end joining and homologous recombination. 4. **Immune system**: UBE2I is significantly expressed in cells of the immune system and is involved in the regulation of immune responses, including B cell activation and T cell function. 5. **Viral infection pathways**: UBE2I is involved in the regulation of viral infection pathways, including the regulation of viral replication and transcription. **Clinical Significance** UBE2I has been implicated in various diseases, including: 1. **Cancer**: UBE2I is overexpressed in several types of cancer, including breast cancer, lung cancer, and colon cancer. 2. **Autoimmune diseases**: UBE2I has been implicated in the regulation of autoimmune diseases, including rheumatoid arthritis and lupus. 3. **Neurological disorders**: UBE2I has been implicated in the regulation of neurological disorders, including Alzheimer's disease and Parkinson's disease. 4. **Viral infections**: UBE2I is involved in the regulation of viral infections, including HIV and influenza. In summary, UBE2I is a critical component of the ubiquitin-proteasome pathway and plays a pivotal role in regulating various cellular processes, including protein degradation, cell cycle progression, and immune response. Its dysregulation has been implicated in various diseases, including cancer, autoimmune diseases, and neurological disorders.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

SUMO-conjugating enzyme UBC9
A8K503_HUMAN

Genular Protein ID: 509166672

Symbol: UBC9_HUMAN

Name: SUMO-conjugating enzyme UBC9

UniProtKB Accession Codes:

P63279 D3DU69 P50550 Q15698 Q59GX1 Q86VB3

Database IDs:

Citations:

PubMed ID: 8668529

Title: Identification of the structural and functional human homolog of the yeast ubiquitin conjugating enzyme UBC9.

PubMed ID: 8668529

DOI: 10.1093/nar/24.11.2005

PubMed ID: 9067428

Title: Assignment of the gene for a ubiquitin-conjugating enzyme (UBE2I) to human chromosome band 16p13.3 by in situ hybridization.

PubMed ID: 9067428

DOI: 10.1159/000134487

PubMed ID: 8565643

Title: 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.

PubMed ID: 8565643

DOI: 10.1159/000134169

PubMed ID: 9197546

Title: Poly(ADP-ribose) polymerase interacts with a novel human ubiquitin conjugating enzyme: hUbc9.

PubMed ID: 9197546

DOI: 10.1016/s0378-1119(97)00015-2

PubMed ID: 8610150

Title: Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes.

PubMed ID: 8610150

DOI: 10.1073/pnas.93.7.2958

PubMed ID: 8668125

Title: Two-hybrid interaction of a human UBC9 homolog with centromere proteins of Saccharomyces cerevisiae.

PubMed ID: 8668125

DOI: 10.1007/bf02172913

PubMed ID: 8798754

Title: Molecular cloning of the cDNA and chromosome localization of the gene for human ubiquitin-conjugating enzyme 9.

PubMed ID: 8798754

DOI: 10.1074/jbc.271.40.24811

PubMed ID: 9333025

Title: Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-conjugating enzyme.

PubMed ID: 9333025

DOI: 10.1038/sj.onc.1201301

PubMed ID: 11157797

Title: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16.

PubMed ID: 11157797

DOI: 10.1093/hmg/10.4.339

PubMed ID: 15616553

Title: The sequence and analysis of duplication-rich human chromosome 16.

PubMed ID: 15616553

DOI: 10.1038/nature03187

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8824223

Title: mUBC9, a novel adenovirus E1A-interacting protein that complements a yeast cell cycle defect.

PubMed ID: 8824223

DOI: 10.1074/jbc.271.42.25906

PubMed ID: 9334332

Title: Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway.

PubMed ID: 9334332

DOI: 10.1101/gad.11.20.2701

PubMed ID: 10383460

Title: Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription.

PubMed ID: 10383460

DOI: 10.1074/jbc.274.27.19441

PubMed ID: 11085938

Title: Association of FHIT (fragile histidine triad), a candidate tumour suppressor gene, with the ubiquitin-conjugating enzyme hUBC9.

PubMed ID: 11085938

DOI: 10.1042/bj3520443

PubMed ID: 11451954

Title: Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9.

PubMed ID: 11451954

DOI: 10.1074/jbc.m104214200

PubMed ID: 12072434

Title: Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo.

PubMed ID: 12072434

DOI: 10.1074/jbc.m202780200

PubMed ID: 12641448

Title: Role of two residues proximal to the active site of Ubc9 in substrate recognition by the Ubc9.SUMO-1 thiolester complex.

PubMed ID: 12641448

DOI: 10.1021/bi026861x

PubMed ID: 12573574

Title: The intracellular association of the nucleocapsid protein (NP) of hantaan virus (HTNV) with small ubiquitin-like modifier-1 (SUMO-1) conjugating enzyme 9 (Ubc9).

PubMed ID: 12573574

DOI: 10.1006/viro.2002.1767

PubMed ID: 12924945

Title: Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation.

PubMed ID: 12924945

DOI: 10.1021/bi0345283

PubMed ID: 15378033

Title: The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type.

PubMed ID: 15378033

DOI: 10.1038/nsmb834

PubMed ID: 15809060

Title: Requirement of the coiled-coil domain of PML-RARalpha oncoprotein for localization, sumoylation, and inhibition of monocyte differentiation.

PubMed ID: 15809060

DOI: 10.1016/j.bbrc.2005.03.052

PubMed ID: 15608651

Title: Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection.

PubMed ID: 15608651

DOI: 10.1038/nsmb878

PubMed ID: 16620772

Title: A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers.

PubMed ID: 16620772

DOI: 10.1016/j.abb.2006.03.002

PubMed ID: 16631117

Title: Ubc9 interacts with SOX4 and represses its transcriptional activity.

PubMed ID: 16631117

DOI: 10.1016/j.bbrc.2006.03.194

PubMed ID: 17005699

Title: Functional interaction between human herpesvirus 6 immediate-early 2 protein and ubiquitin-conjugating enzyme 9 in the absence of sumoylation.

PubMed ID: 17005699

DOI: 10.1128/jvi.00375-06

PubMed ID: 17956732

Title: RSUME, a small RWD-containing protein, enhances SUMO conjugation and stabilizes HIF-1alpha during hypoxia.

PubMed ID: 17956732

DOI: 10.1016/j.cell.2007.07.044

PubMed ID: 17704809

Title: Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response.

PubMed ID: 17704809

DOI: 10.1038/sj.onc.1210710

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19450230

Title: SUMOylation enhances DNA methyltransferase 1 activity.

PubMed ID: 19450230

DOI: 10.1042/bj20090142

PubMed ID: 19744555

Title: Sumoylation of forkhead L2 by Ubc9 is required for its activity as a transcriptional repressor of the steroidogenic acute regulatory gene.

PubMed ID: 19744555

DOI: 10.1016/j.cellsig.2009.09.001

PubMed ID: 19638400

Title: SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle.

PubMed ID: 19638400

DOI: 10.1096/fj.09-136630

PubMed ID: 19557165

Title: Ebola Zaire virus blocks type I interferon production by exploiting the host SUMO modification machinery.

PubMed ID: 19557165

DOI: 10.1371/journal.ppat.1000493

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20543865

Title: Identification of a molecular recognition feature in the E1A oncoprotein that binds the SUMO conjugase UBC9 and likely interferes with polySUMOylation.

PubMed ID: 20543865

DOI: 10.1038/onc.2010.226

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21965678

Title: SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function.

PubMed ID: 21965678

DOI: 10.1074/jbc.m111.267237

PubMed ID: 21795333

Title: Epstein-Barr virus latent membrane protein 1 (LMP1) C-terminal-activating region 3 contributes to LMP1-mediated cellular migration via its interaction with Ubc9.

PubMed ID: 21795333

DOI: 10.1128/jvi.05035-11

PubMed ID: 22214662

Title: The RAX/PACT-PKR stress response pathway promotes p53 sumoylation and activation, leading to G(1) arrest.

PubMed ID: 22214662

DOI: 10.4161/cc.11.2.18999

PubMed ID: 22509284

Title: Phosphorylation of Ubc9 by Cdk1 enhances SUMOylation activity.

PubMed ID: 22509284

DOI: 10.1371/journal.pone.0034250

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 24105744

Title: 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.

PubMed ID: 24105744

DOI: 10.1101/gad.224923.113

PubMed ID: 23404503

Title: UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3 ligase for zinc finger protein 131.

PubMed ID: 23404503

DOI: 10.1074/jbc.m112.438234

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23508108

Title: RSUME enhances glucocorticoid receptor SUMOylation and transcriptional activity.

PubMed ID: 23508108

DOI: 10.1128/mcb.01470-12

PubMed ID: 23469069

Title: In silico structural and functional characterization of the RSUME splice variants.

PubMed ID: 23469069

DOI: 10.1371/journal.pone.0057795

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 26620705

Title: The C-terminal Region and SUMOylation of Cockayne Syndrome Group B Protein Play Critical Roles in Transcription-coupled Nucleotide Excision Repair.

PubMed ID: 26620705

DOI: 10.1074/jbc.m115.683235

PubMed ID: 27068747

Title: Transcription Factor hDREF Is a Novel SUMO E3 Ligase of Mi2alpha.

PubMed ID: 27068747

DOI: 10.1074/jbc.m115.713370

PubMed ID: 27211601

Title: SUMO5, a novel poly-sumo isoform, regulates pml nuclear bodies.

PubMed ID: 27211601

DOI: 10.1038/srep26509

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 33967989

Title: Sumoylation of the Carboxy-Terminal of Human Cytomegalovirus DNA Polymerase Processivity Factor UL44 Attenuates Viral DNA Replication.

PubMed ID: 33967989

DOI: 10.3389/fmicb.2021.652719

PubMed ID: 9261152

Title: Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system.

PubMed ID: 9261152

DOI: 10.1074/jbc.272.34.21381

PubMed ID: 11853669

Title: Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1.

PubMed ID: 11853669

DOI: 10.1016/s0092-8674(02)00630-x

PubMed ID: 15931224

Title: Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex.

PubMed ID: 15931224

DOI: 10.1038/nature03588

PubMed ID: 16732283

Title: Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway.

PubMed ID: 16732283

DOI: 10.1038/nsmb1104

PubMed ID: 17466333

Title: Structure and analysis of a complex between SUMO and Ubc9 illustrates features of a conserved E2-Ubl interaction.

PubMed ID: 17466333

DOI: 10.1016/j.jmb.2007.04.006

PubMed ID: 20077568

Title: Structural basis for regulation of poly-SUMO chain by a SUMO-like domain of Nip45.

PubMed ID: 20077568

DOI: 10.1002/prot.22667

PubMed ID: 21139563

Title: Structure of Importin13-Ubc9 complex: nuclear import and release of a key regulator of sumoylation.

PubMed ID: 21139563

DOI: 10.1038/emboj.2010.320

PubMed ID: 25918163

Title: RWD domain as an E2 (Ubc9)-interaction module.

PubMed ID: 25918163

DOI: 10.1074/jbc.m115.644047

PubMed ID: 26524494

Title: Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase.

PubMed ID: 26524494

DOI: 10.1038/nsmb.3116

Sequence Information:

Length: 158
Mass: 18007
Checksum: E2C826E9C8D0683D
Sequence:

MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG TPWEGGLFKL 
RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL 
NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA QAKKFAPS

Genular Protein ID: 2985431330

Symbol: A8K503_HUMAN

Name: N/A

UniProtKB Accession Codes:

A8K503

Database IDs:

Sequence Information:

Length: 158
Mass: 18035
Checksum: E2C826EBA540683D
Sequence:

MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG TPWEGGLFKL 
RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL 
NEPNIQDPAQ AEAYTIYCRN RVEYEKRVRA QAKKFAPS

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: UBE2I

Associated with

Cells (max top 100)

Other Information

Identification of the structural and functional human homolog of the yeast ubiquitin conjugating enzyme UBC9. PubMed ID: 8668529

Assignment of the gene for a ubiquitin-conjugating enzyme (UBE2I) to human chromosome band 16p13.3 by in situ hybridization. PubMed ID: 9067428

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. PubMed ID: 8565643

Poly(ADP-ribose) polymerase interacts with a novel human ubiquitin conjugating enzyme: hUbc9. PubMed ID: 9197546

Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes. PubMed ID: 8610150

Two-hybrid interaction of a human UBC9 homolog with centromere proteins of Saccharomyces cerevisiae. PubMed ID: 8668125

Molecular cloning of the cDNA and chromosome localization of the gene for human ubiquitin-conjugating enzyme 9. PubMed ID: 8798754

Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-conjugating enzyme. PubMed ID: 9333025

Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. PubMed ID: 11157797

The sequence and analysis of duplication-rich human chromosome 16. PubMed ID: 15616553

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

mUBC9, a novel adenovirus E1A-interacting protein that complements a yeast cell cycle defect. PubMed ID: 8824223

Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway. PubMed ID: 9334332

Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription. PubMed ID: 10383460

Association of FHIT (fragile histidine triad), a candidate tumour suppressor gene, with the ubiquitin-conjugating enzyme hUBC9. PubMed ID: 11085938

Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. PubMed ID: 11451954

Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo. PubMed ID: 12072434

Role of two residues proximal to the active site of Ubc9 in substrate recognition by the Ubc9.SUMO-1 thiolester complex. PubMed ID: 12641448

The intracellular association of the nucleocapsid protein (NP) of hantaan virus (HTNV) with small ubiquitin-like modifier-1 (SUMO-1) conjugating enzyme 9 (Ubc9). PubMed ID: 12573574

Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation. PubMed ID: 12924945

The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type. PubMed ID: 15378033

Requirement of the coiled-coil domain of PML-RARalpha oncoprotein for localization, sumoylation, and inhibition of monocyte differentiation. PubMed ID: 15809060

Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection. PubMed ID: 15608651

A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers. PubMed ID: 16620772

Ubc9 interacts with SOX4 and represses its transcriptional activity. PubMed ID: 16631117

Functional interaction between human herpesvirus 6 immediate-early 2 protein and ubiquitin-conjugating enzyme 9 in the absence of sumoylation. PubMed ID: 17005699

RSUME, a small RWD-containing protein, enhances SUMO conjugation and stabilizes HIF-1alpha during hypoxia. PubMed ID: 17956732

Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response. PubMed ID: 17704809

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

SUMOylation enhances DNA methyltransferase 1 activity. PubMed ID: 19450230

Sumoylation of forkhead L2 by Ubc9 is required for its activity as a transcriptional repressor of the steroidogenic acute regulatory gene. PubMed ID: 19744555

SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle. PubMed ID: 19638400

Ebola Zaire virus blocks type I interferon production by exploiting the host SUMO modification machinery. PubMed ID: 19557165

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Identification of a molecular recognition feature in the E1A oncoprotein that binds the SUMO conjugase UBC9 and likely interferes with polySUMOylation. PubMed ID: 20543865

Initial characterization of the human central proteome. PubMed ID: 21269460

SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function. PubMed ID: 21965678

Epstein-Barr virus latent membrane protein 1 (LMP1) C-terminal-activating region 3 contributes to LMP1-mediated cellular migration via its interaction with Ubc9. PubMed ID: 21795333

The RAX/PACT-PKR stress response pathway promotes p53 sumoylation and activation, leading to G(1) arrest. PubMed ID: 22214662

Phosphorylation of Ubc9 by Cdk1 enhances SUMOylation activity. PubMed ID: 22509284

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

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. PubMed ID: 24105744

UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3 ligase for zinc finger protein 131. PubMed ID: 23404503

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

RSUME enhances glucocorticoid receptor SUMOylation and transcriptional activity. PubMed ID: 23508108

In silico structural and functional characterization of the RSUME splice variants. PubMed ID: 23469069

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Uncovering global SUMOylation signaling networks in a site-specific manner. PubMed ID: 25218447

Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli. PubMed ID: 25114211

SUMO-2 orchestrates chromatin modifiers in response to DNA damage. PubMed ID: 25772364

System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability. PubMed ID: 25755297

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

The C-terminal Region and SUMOylation of Cockayne Syndrome Group B Protein Play Critical Roles in Transcription-coupled Nucleotide Excision Repair. PubMed ID: 26620705

Transcription Factor hDREF Is a Novel SUMO E3 Ligase of Mi2alpha. PubMed ID: 27068747

SUMO5, a novel poly-sumo isoform, regulates pml nuclear bodies. PubMed ID: 27211601

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733

Sumoylation of the Carboxy-Terminal of Human Cytomegalovirus DNA Polymerase Processivity Factor UL44 Attenuates Viral DNA Replication. PubMed ID: 33967989

Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system. PubMed ID: 9261152

Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. PubMed ID: 11853669

Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. PubMed ID: 15931224

Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway. PubMed ID: 16732283

Structure and analysis of a complex between SUMO and Ubc9 illustrates features of a conserved E2-Ubl interaction. PubMed ID: 17466333

Structural basis for regulation of poly-SUMO chain by a SUMO-like domain of Nip45. PubMed ID: 20077568

Structure of Importin13-Ubc9 complex: nuclear import and release of a key regulator of sumoylation. PubMed ID: 21139563

RWD domain as an E2 (Ubc9)-interaction module. PubMed ID: 25918163

Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase. PubMed ID: 26524494