UBC | ENSG00000150991 | NCBI 7316

Details for: UBC

Gene ID: 7316

Symbol: UBC

Ensembl ID: ENSG00000150991

Description: ubiquitin C

Associated with

Abc-family proteins mediated transport
(R-HSA-382556)
Abc transporter disorders
(R-HSA-5619084)
Adaptive immune system
(R-HSA-1280218)
Aerobic respiration and respiratory electron transport
(R-HSA-1428517)
Amyloid fiber formation
(R-HSA-977225)
Apoptosis
(R-HSA-109581)
Asparagine n-linked glycosylation
(R-HSA-446203)
Auf1 (hnrnp d0) binds and destabilizes mrna
(R-HSA-450408)
Autophagy
(R-HSA-9612973)
Axon guidance
(R-HSA-422475)
Beta-catenin independent wnt signaling
(R-HSA-3858494)
C-type lectin receptors (clrs)
(R-HSA-5621481)
Cell cycle
(R-HSA-1640170)
Cell cycle, mitotic
(R-HSA-69278)
Cell cycle checkpoints
(R-HSA-69620)
Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Cellular response to hypoxia
(R-HSA-1234174)
Cellular senescence
(R-HSA-2559583)
Chaperone mediated autophagy
(R-HSA-9613829)
Circadian clock
(R-HSA-400253)
Cytokine signaling in immune system
(R-HSA-1280215)
Cytosolic sensors of pathogen-associated dna
(R-HSA-1834949)
Ddx58/ifih1-mediated induction of interferon-alpha/beta
(R-HSA-168928)
Death receptor signaling
(R-HSA-73887)
Degradation of beta-catenin by the destruction complex
(R-HSA-195253)
Developmental biology
(R-HSA-1266738)
Disease
(R-HSA-1643685)
Diseases of metabolism
(R-HSA-5668914)
Diseases of signal transduction by growth factor receptors and second messengers
(R-HSA-5663202)
Disorders of transmembrane transporters
(R-HSA-5619115)
Dna damage bypass
(R-HSA-73893)
Dna double-strand break repair
(R-HSA-5693532)
Dna repair
(R-HSA-73894)
Dna replication
(R-HSA-69306)
Dna replication pre-initiation
(R-HSA-69002)
Fanconi anemia pathway
(R-HSA-6783310)
Fc epsilon receptor (fceri) signaling
(R-HSA-2454202)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Hedgehog 'off' state
(R-HSA-5610787)
Hedgehog ligand biogenesis
(R-HSA-5358346)
Hh mutants abrogate ligand secretion
(R-HSA-5387390)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Innate immune system
(R-HSA-168249)
Intracellular signaling by second messengers
(R-HSA-9006925)
Ion channel transport
(R-HSA-983712)
Iron uptake and transport
(R-HSA-917937)
Late endosomal microautophagy
(R-HSA-9615710)
Macroautophagy
(R-HSA-1632852)
Mapk family signaling cascades
(R-HSA-5683057)
Membrane trafficking
(R-HSA-199991)
Metabolism
(R-HSA-1430728)
Metabolism of carbohydrates
(R-HSA-71387)
Metabolism of proteins
(R-HSA-392499)
Metabolism of rna
(R-HSA-8953854)
Mitotic g1 phase and g1/s transition
(R-HSA-453279)
Mitotic g2-g2/m phases
(R-HSA-453274)
Nervous system development
(R-HSA-9675108)
Nucleotide-binding domain, leucine rich repeat containing receptor (nlr) signaling pathways
(R-HSA-168643)
Nucleotide excision repair
(R-HSA-5696398)
P75 ntr receptor-mediated signalling
(R-HSA-193704)
Peroxisomal protein import
(R-HSA-9033241)
Pip3 activates akt signaling
(R-HSA-1257604)
Plasma lipoprotein assembly, remodeling, and clearance
(R-HSA-174824)
Post-translational protein modification
(R-HSA-597592)
Programmed cell death
(R-HSA-5357801)
Protein localization
(R-HSA-9609507)
Recognition of dna damage by pcna-containing replication complex
(R-HSA-110314)
Regulated necrosis
(R-HSA-5218859)
Regulation of apoptosis
(R-HSA-169911)
Regulation of mitotic cell cycle
(R-HSA-453276)
Regulation of mrna stability by proteins that bind au-rich elements
(R-HSA-450531)
Ripk1-mediated regulated necrosis
(R-HSA-5213460)
Rna polymerase ii transcription
(R-HSA-73857)
Signaling by egfr
(R-HSA-177929)
Signaling by egfr in cancer
(R-HSA-1643713)
Signaling by erbb2
(R-HSA-1227986)
Signaling by erbb4
(R-HSA-1236394)
Signaling by fgfr
(R-HSA-190236)
Signaling by hedgehog
(R-HSA-5358351)
Signaling by interleukins
(R-HSA-449147)
Signaling by non-receptor tyrosine kinases
(R-HSA-9006927)
Signaling by notch
(R-HSA-157118)
Signaling by notch1
(R-HSA-1980143)
Signaling by notch1 in cancer
(R-HSA-2644603)
Signaling by notch2
(R-HSA-1980145)
Signaling by receptor tyrosine kinases
(R-HSA-9006934)
Signaling by tgf-beta receptor complex
(R-HSA-170834)
Signaling by tgfb family members
(R-HSA-9006936)
Signaling by wnt
(R-HSA-195721)
Signal transduction
(R-HSA-162582)
Stimuli-sensing channels
(R-HSA-2672351)
Tcf dependent signaling in response to wnt
(R-HSA-201681)
Tcr signaling
(R-HSA-202403)
Toll-like receptor cascades
(R-HSA-168898)
Translesion synthesis by y family dna polymerases bypasses lesions on dna template
(R-HSA-110313)
Transport of small molecules
(R-HSA-382551)
Vesicle-mediated transport
(R-HSA-5653656)

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: 1445.2388
Cell Significance Index: -224.8000
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 883.9576
Cell Significance Index: -224.2100
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 589.7595
Cell Significance Index: -242.9500
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 528.7609
Cell Significance Index: -249.6400
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 478.8046
Cell Significance Index: -246.2900
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 373.5048
Cell Significance Index: -250.6300
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 198.1255
Cell Significance Index: -244.2800
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 65.4984
Cell Significance Index: -258.4600
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 60.9158
Cell Significance Index: -187.1000
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 47.5426
Cell Significance Index: -127.3600
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 41.3828
Cell Significance Index: -90.5700
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 13.0229
Cell Significance Index: 373.3100
Cell Name: vascular lymphangioblast (CL0005022)
Fold Change: 10.8413
Cell Significance Index: 191.5800
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 10.3082
Cell Significance Index: 280.5800
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 9.0032
Cell Significance Index: 472.7000
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 8.9919
Cell Significance Index: 419.2500
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 8.5879
Cell Significance Index: 403.6300
Cell Name: odontoblast (CL0000060)
Fold Change: 7.1567
Cell Significance Index: 917.4500
Cell Name: lactocyte (CL0002325)
Fold Change: 5.9737
Cell Significance Index: 771.7600
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 5.6692
Cell Significance Index: 422.5200
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 5.5814
Cell Significance Index: 766.4800
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 5.2411
Cell Significance Index: 2317.2000
Cell Name: early pro-B cell (CL0002046)
Fold Change: 5.2069
Cell Significance Index: 335.9300
Cell Name: granulosa cell (CL0000501)
Fold Change: 5.0599
Cell Significance Index: 133.0500
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 5.0507
Cell Significance Index: 93.3500
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 5.0121
Cell Significance Index: 616.2800
Cell Name: cell in vitro (CL0001034)
Fold Change: 4.6866
Cell Significance Index: 2559.4400
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 4.6258
Cell Significance Index: 833.9000
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: 4.0804
Cell Significance Index: 1174.0600
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 4.0367
Cell Significance Index: 285.4900
Cell Name: endothelial cell of venule (CL1000414)
Fold Change: 3.6856
Cell Significance Index: 41.8700
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 3.6560
Cell Significance Index: 189.9200
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 3.2484
Cell Significance Index: 383.0900
Cell Name: peg cell (CL4033014)
Fold Change: 2.6399
Cell Significance Index: 60.9900
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: 1.7462
Cell Significance Index: 36.5500
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 1.7068
Cell Significance Index: 291.4400
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: 1.6002
Cell Significance Index: 55.6100
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: 1.5610
Cell Significance Index: 14.3800
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 1.4138
Cell Significance Index: 37.7500
Cell Name: retinal rod cell (CL0000604)
Fold Change: 1.1770
Cell Significance Index: 14.0300
Cell Name: colon goblet cell (CL0009039)
Fold Change: 1.1597
Cell Significance Index: 114.7200
Cell Name: neoplastic cell (CL0001063)
Fold Change: 1.0367
Cell Significance Index: 205.7400
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: 0.9403
Cell Significance Index: 107.3400
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 0.7236
Cell Significance Index: 145.1600
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: 0.3759
Cell Significance Index: 284.5000
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.3109
Cell Significance Index: 111.5200
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: 0.2140
Cell Significance Index: 156.8700
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: 0.1634
Cell Significance Index: 10.3000
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.1604
Cell Significance Index: 301.9800
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: 0.1116
Cell Significance Index: 70.8700
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.0941
Cell Significance Index: 3.3100
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 0.0740
Cell Significance Index: 113.9700
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 0.0718
Cell Significance Index: 97.6000
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0194
Cell Significance Index: -1.9800
Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.0263
Cell Significance Index: -48.4500
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.1073
Cell Significance Index: -79.4600
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.1618
Cell Significance Index: -73.4500
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.1993
Cell Significance Index: -3.3400
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.2231
Cell Significance Index: -139.3000
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: -0.2555
Cell Significance Index: -7.1400
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: -0.2877
Cell Significance Index: -54.7600
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.3204
Cell Significance Index: -180.7100
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.5461
Cell Significance Index: -115.0200
Cell Name: theca cell (CL0000503)
Fold Change: -0.5566
Cell Significance Index: -3.2700
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.9164
Cell Significance Index: -133.2100
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: -1.0589
Cell Significance Index: -172.2200
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: -1.1682
Cell Significance Index: -127.0600
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -1.2040
Cell Significance Index: -137.9400
Cell Name: type I muscle cell (CL0002211)
Fold Change: -1.2554
Cell Significance Index: -30.6300
Cell Name: basal cell of epidermis (CL0002187)
Fold Change: -1.2596
Cell Significance Index: -19.1300
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -1.4431
Cell Significance Index: -168.1800
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: -1.4824
Cell Significance Index: -18.9900
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: -1.6087
Cell Significance Index: -72.9200
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -1.6367
Cell Significance Index: -129.6300
Cell Name: cone retinal bipolar cell (CL0000752)
Fold Change: -1.7982
Cell Significance Index: -13.8600
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -1.8103
Cell Significance Index: -111.2700
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -1.8580
Cell Significance Index: -25.3500
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: -2.0263
Cell Significance Index: -155.5000
Cell Name: gut absorptive cell (CL0000677)
Fold Change: -2.1598
Cell Significance Index: -129.6600
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -2.3245
Cell Significance Index: -242.0400
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: -2.3575
Cell Significance Index: -67.9300
Cell Name: pro-T cell (CL0000827)
Fold Change: -2.3623
Cell Significance Index: -60.3500
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: -2.4032
Cell Significance Index: -166.1900
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -2.4855
Cell Significance Index: -66.4900
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -2.5171
Cell Significance Index: -80.6200
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -2.7161
Cell Significance Index: -182.6300
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: -3.5249
Cell Significance Index: -197.8000
Cell Name: paneth cell of colon (CL0009009)
Fold Change: -3.5651
Cell Significance Index: -53.4200
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: -3.9640
Cell Significance Index: -23.9500
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: -4.0155
Cell Significance Index: -117.9300
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -4.0464
Cell Significance Index: -248.0800
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: -4.2733
Cell Significance Index: -92.5800
Cell Name: luminal hormone-sensing cell of mammary gland (CL4033058)
Fold Change: -4.4287
Cell Significance Index: -27.2600
Cell Name: prostate gland microvascular endothelial cell (CL2000059)
Fold Change: -4.7355
Cell Significance Index: -34.0100
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: -4.8824
Cell Significance Index: -130.8300
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: -4.8830
Cell Significance Index: -83.6800
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -4.9395
Cell Significance Index: -145.4900
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: -5.5521
Cell Significance Index: -142.7200
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -5.5936
Cell Significance Index: -247.4200
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: -5.6462
Cell Significance Index: -141.1400

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:** 1. **Ubiquitin C**: UBC is a protein component of the ubiquitin-proteasome system (UPS), which is essential for protein degradation and quality control. 2. **Polyubiquitin chain formation**: UBC participates in the formation of polyubiquitin chains, which govern protein degradation and signaling. 3. **Antigen presentation**: UBC has been implicated in the processing and presentation of antigens to T-cells, a critical step in the adaptive immune response. 4. **Signal transduction**: UBC is involved in various signaling pathways, including those mediated by growth factor receptors, cytokines, and chemokines. **Pathways and Functions:** 1. **Adaptive immune response**: UBC is crucial for the processing and presentation of antigens to T-cells, facilitating the activation of immune cells. 2. **Antigen presentation**: UBC is involved in the formation of MHC class II molecules, which present antigens to CD4+ T-cells. 3. **Immune cell activation**: UBC regulates the activation of immune cells, including T-cells and B-cells, through signal transduction pathways. 4. **Innate immune response**: UBC is involved in the recognition of pathogen-associated molecular patterns (PAMPs) by pattern recognition receptors (PRRs), such as NLRP3. 5. **Cytokine signaling**: UBC regulates cytokine signaling pathways, including those mediated by IL-2, IL-6, and TNF-α. **Clinical Significance:** 1. **Autoimmune diseases**: Dysregulation of UBC has been implicated in autoimmune diseases, such as rheumatoid arthritis and lupus. 2. **Cancer**: UBC is overexpressed in various cancers, including breast, lung, and colon cancer, and is associated with poor prognosis. 3. **Infectious diseases**: UBC plays a critical role in the recognition and response to pathogens, and its dysregulation can contribute to the development of infectious diseases. 4. **Neurological disorders**: UBC has been implicated in neurological disorders, such as Alzheimer's disease and Parkinson's disease, where it regulates protein degradation and aggregation. In conclusion, the ubiquitin C gene is a critical regulator of various cellular processes, including protein degradation, immune response, and signal transduction. Its dysregulation has been implicated in various diseases, highlighting the importance of understanding the mechanisms of UBC in the context of immunology.

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.

Polyubiquitin-C

Genular Protein ID: 447828744

Symbol: UBC_HUMAN

Name: Polyubiquitin-C

UniProtKB Accession Codes:

P0CG48 P02248 P02249 P02250 P62988 Q29120 Q6LBL4 Q6LDU5 Q8WYN8 Q91887 Q91888 Q9BWD6 Q9BX98 Q9UEF2 Q9UEG1 Q9UEK8 Q9UPK7

Database IDs:

Citations:

PubMed ID: 2988935

Title: The human ubiquitin multigene family: some genes contain multiple directly repeated ubiquitin coding sequences.

PubMed ID: 2988935

DOI: 10.1002/j.1460-2075.1985.tb03693.x

PubMed ID: 9644242

Title: Cloning of human polyubiquitin cDNAs and a ubiquitin-binding assay involving its in vitro translation product.

PubMed ID: 9644242

DOI: 10.1093/oxfordjournals.jbchem.a022093

PubMed ID: 14745543

Title: Lineage-specific homogenization of the polyubiquitin gene among human and great apes.

PubMed ID: 14745543

DOI: 10.1007/s00239-003-2532-4

PubMed ID: 16541075

Title: The finished DNA sequence of human chromosome 12.

PubMed ID: 16541075

DOI: 10.1038/nature04569

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: 8917096

Title: Heterogeneous structure of the polyubiquitin gene UbC of HeLa S3 cells.

PubMed ID: 8917096

DOI: 10.1016/0378-1119(96)00145-x

PubMed ID: 1128706

Title: Molecular conservation of 74 amino acid sequence of ubiquitin between cattle and man.

PubMed ID: 1128706

DOI: 10.1038/255423a0

PubMed ID: 16443603

Title: Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation.

PubMed ID: 16443603

DOI: 10.1074/jbc.m512786200

PubMed ID: 9504932

Title: Higher frequency of concerted evolutionary events in rodents than in man at the polyubiquitin gene VNTR locus.

PubMed ID: 9504932

DOI: 10.1093/genetics/148.2.867

PubMed ID: 2820408

Title: Cloning and sequence analysis of a cDNA encoding poly-ubiquitin in human ovarian granulosa cells.

PubMed ID: 2820408

DOI: 10.1016/0006-291x(87)90970-3

PubMed ID: 16543144

Title: Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain.

PubMed ID: 16543144

DOI: 10.1016/j.molcel.2006.02.018

PubMed ID: 15466860

Title: Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B contributes to neuritogenesis.

PubMed ID: 15466860

DOI: 10.1074/jbc.m402916200

PubMed ID: 18719106

Title: Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks.

PubMed ID: 18719106

DOI: 10.1073/pnas.0805685105

PubMed ID: 19754430

Title: The emerging complexity of protein ubiquitination.

PubMed ID: 19754430

DOI: 10.1042/bst0370937

PubMed ID: 24660806

Title: Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65.

PubMed ID: 24660806

DOI: 10.1042/bj20140334

PubMed ID: 24751536

Title: PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity.

PubMed ID: 24751536

DOI: 10.1083/jcb.201402104

PubMed ID: 24784582

Title: Ubiquitin is phosphorylated by PINK1 to activate parkin.

PubMed ID: 24784582

DOI: 10.1038/nature13392

PubMed ID: 28525742

Title: Ubiquitin Modification by the E3 Ligase/ADP-Ribosyltransferase Dtx3L/Parp9.

PubMed ID: 28525742

DOI: 10.1016/j.molcel.2017.04.028

PubMed ID: 34239127

Title: K29-linked ubiquitin signaling regulates proteotoxic stress response and cell cycle.

PubMed ID: 34239127

DOI: 10.1038/s41589-021-00823-5

PubMed ID: 3041007

Title: Structure of ubiquitin refined at 1.8-A resolution.

PubMed ID: 3041007

DOI: 10.1016/0022-2836(87)90679-6

PubMed ID: 8166633

Title: Synthetic, structural and biological studies of the ubiquitin system: the total chemical synthesis of ubiquitin.

PubMed ID: 8166633

DOI: 10.1042/bj2990151

PubMed ID: 8107144

Title: Structure of tetraubiquitin shows how multiubiquitin chains can be formed.

PubMed ID: 8107144

DOI: 10.1006/jmbi.1994.1169

PubMed ID: 11173499

Title: Structure of a new crystal form of tetraubiquitin.

PubMed ID: 11173499

DOI: 10.1107/s090744490001800x

PubMed ID: 12507430

Title: Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde.

PubMed ID: 12507430

DOI: 10.1016/s0092-8674(02)01199-6

PubMed ID: 21399617

Title: Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21.

PubMed ID: 21399617

DOI: 10.1038/embor.2011.17

PubMed ID: 20622874

Title: Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne.

PubMed ID: 20622874

DOI: 10.1038/nsmb.1873

PubMed ID: 23827681

Title: OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis.

PubMed ID: 23827681

DOI: 10.1016/j.cell.2013.05.046

PubMed ID: 25527291

Title: Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis.

PubMed ID: 25527291

DOI: 10.15252/embj.201489847

PubMed ID: 25752573

Title: K29-selective ubiquitin binding domain reveals structural basis of specificity and heterotypic nature of K29 polyubiquitin.

PubMed ID: 25752573

DOI: 10.1016/j.molcel.2015.01.041

PubMed ID: 25752577

Title: Assembly and specific recognition of K29- and K33-linked polyubiquitin.

PubMed ID: 25752577

DOI: 10.1016/j.molcel.2015.01.042

PubMed ID: 32330457

Title: Threonine ADP-ribosylation of ubiquitin by a bacterial effector family blocks host ubiquitination.

PubMed ID: 32330457

DOI: 10.1016/j.molcel.2020.03.016

Sequence Information:

Length: 685
Mass: 77039
Checksum: B6E7BC06FEE77196
Sequence:

MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN 
IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE NVKAKIQDKE GIPPDQQRLI 
FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE PSDTIENVKA 
KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT 
ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR 
LRGGMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL 
SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ 
QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE 
NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL 
TGKTITLEVE PSDTIENVKA KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH 
LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED 
GRTLSDYNIQ KESTLHLVLR LRGGV

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: UBC

Associated with

Cells (max top 100)

Other Information

The human ubiquitin multigene family: some genes contain multiple directly repeated ubiquitin coding sequences. PubMed ID: 2988935

Cloning of human polyubiquitin cDNAs and a ubiquitin-binding assay involving its in vitro translation product. PubMed ID: 9644242

Lineage-specific homogenization of the polyubiquitin gene among human and great apes. PubMed ID: 14745543

The finished DNA sequence of human chromosome 12. PubMed ID: 16541075

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

Heterogeneous structure of the polyubiquitin gene UbC of HeLa S3 cells. PubMed ID: 8917096

Molecular conservation of 74 amino acid sequence of ubiquitin between cattle and man. PubMed ID: 1128706

Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation. PubMed ID: 16443603

Higher frequency of concerted evolutionary events in rodents than in man at the polyubiquitin gene VNTR locus. PubMed ID: 9504932

Cloning and sequence analysis of a cDNA encoding poly-ubiquitin in human ovarian granulosa cells. PubMed ID: 2820408

Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain. PubMed ID: 16543144

Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B contributes to neuritogenesis. PubMed ID: 15466860

Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks. PubMed ID: 18719106

The emerging complexity of protein ubiquitination. PubMed ID: 19754430

Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65. PubMed ID: 24660806

PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity. PubMed ID: 24751536

Ubiquitin is phosphorylated by PINK1 to activate parkin. PubMed ID: 24784582

Ubiquitin Modification by the E3 Ligase/ADP-Ribosyltransferase Dtx3L/Parp9. PubMed ID: 28525742

K29-linked ubiquitin signaling regulates proteotoxic stress response and cell cycle. PubMed ID: 34239127

Structure of ubiquitin refined at 1.8-A resolution. PubMed ID: 3041007

Synthetic, structural and biological studies of the ubiquitin system: the total chemical synthesis of ubiquitin. PubMed ID: 8166633

Structure of tetraubiquitin shows how multiubiquitin chains can be formed. PubMed ID: 8107144

Structure of a new crystal form of tetraubiquitin. PubMed ID: 11173499

Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. PubMed ID: 12507430

Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21. PubMed ID: 21399617

Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne. PubMed ID: 20622874

OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis. PubMed ID: 23827681

Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis. PubMed ID: 25527291

K29-selective ubiquitin binding domain reveals structural basis of specificity and heterotypic nature of K29 polyubiquitin. PubMed ID: 25752573

Assembly and specific recognition of K29- and K33-linked polyubiquitin. PubMed ID: 25752577

Threonine ADP-ribosylation of ubiquitin by a bacterial effector family blocks host ubiquitination. PubMed ID: 32330457