Gene UBC - ENSG00000150991 | NCBI Gene ID: 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)
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 'on' state
(R-HSA-5632684)
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)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: thyroid follicular cell (CL0002258)
Fold Change: 5.51
Marker Score: 4317
Cell Name: CD38-negative naive B cell (CL0002102)
Fold Change: 5.13
Marker Score: 10757
Cell Name: alveolar capillary type 1 endothelial cell (CL4028002)
Fold Change: 5.12
Marker Score: 13017
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 5.1
Marker Score: 173680
Cell Name: uterine smooth muscle cell (CL0002601)
Fold Change: 5.08
Marker Score: 6611
Cell Name: mature T cell (CL0002419)
Fold Change: 5.05
Marker Score: 49992
Cell Name: mature gamma-delta T cell (CL0000800)
Fold Change: 4.63
Marker Score: 14602.5
Cell Name: IgA plasma cell (CL0000987)
Fold Change: 4.62
Marker Score: 3933
Cell Name: NKp46-positive innate lymphoid cell, human (CL0001076)
Fold Change: 4.55
Marker Score: 13294
Cell Name: activated CD8-positive, alpha-beta T cell (CL0000906)
Fold Change: 4.49
Marker Score: 3258
Cell Name: natural T-regulatory cell (CL0000903)
Fold Change: 4.43
Marker Score: 2278
Cell Name: mature alpha-beta T cell (CL0000791)
Fold Change: 4.37
Marker Score: 231078
Cell Name: alpha-beta T cell (CL0000789)
Fold Change: 4.35
Marker Score: 3292
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 4.3
Marker Score: 1028
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 4.29
Marker Score: 5186
Cell Name: acinar cell (CL0000622)
Fold Change: 4.26
Marker Score: 3004
Cell Name: alveolar capillary type 2 endothelial cell (CL4028003)
Fold Change: 4.26
Marker Score: 6164
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 4.25
Marker Score: 237584
Cell Name: radial glial cell (CL0000681)
Fold Change: 4.25
Marker Score: 1566
Cell Name: malignant cell (CL0001064)
Fold Change: 4.23
Marker Score: 56789
Cell Name: blood cell (CL0000081)
Fold Change: 4.21
Marker Score: 48885
Cell Name: CD8-positive, alpha-beta memory T cell, CD45RO-positive (CL0001203)
Fold Change: 4.16
Marker Score: 11665
Cell Name: decidual natural killer cell, human (CL0002343)
Fold Change: 4.13
Marker Score: 11412
Cell Name: glycinergic amacrine cell (CL4030028)
Fold Change: 4.11
Marker Score: 3879
Cell Name: double negative T regulatory cell (CL0011024)
Fold Change: 4.04
Marker Score: 3907
Cell Name: T-helper 22 cell (CL0001042)
Fold Change: 4.03
Marker Score: 17298
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 3.99
Marker Score: 9755
Cell Name: type I pneumocyte (CL0002062)
Fold Change: 3.98
Marker Score: 4796
Cell Name: skeletal muscle satellite stem cell (CL0008011)
Fold Change: 3.98
Marker Score: 4250
Cell Name: CD4-positive, alpha-beta memory T cell (CL0000897)
Fold Change: 3.98
Marker Score: 2333
Cell Name: fibroblast of connective tissue of nonglandular part of prostate (CL1000304)
Fold Change: 3.97
Marker Score: 3385
Cell Name: naive T cell (CL0000898)
Fold Change: 3.96
Marker Score: 2549
Cell Name: mesenchymal stem cell (CL0000134)
Fold Change: 3.95
Marker Score: 6087.5
Cell Name: foveolar cell of stomach (CL0002179)
Fold Change: 3.95
Marker Score: 25180
Cell Name: myoepithelial cell of mammary gland (CL0002324)
Fold Change: 3.92
Marker Score: 19264
Cell Name: type I NK T cell (CL0000921)
Fold Change: 3.91
Marker Score: 3071
Cell Name: supporting cell (CL0000630)
Fold Change: 3.9
Marker Score: 7331
Cell Name: theca cell (CL0000503)
Fold Change: 3.9
Marker Score: 2795
Cell Name: mucosal invariant T cell (CL0000940)
Fold Change: 3.88
Marker Score: 3455
Cell Name: chondrocyte (CL0000138)
Fold Change: 3.88
Marker Score: 1748
Cell Name: mesodermal cell (CL0000222)
Fold Change: 3.87
Marker Score: 51026
Cell Name: epithelial cell of lung (CL0000082)
Fold Change: 3.85
Marker Score: 20252
Cell Name: IgG-negative class switched memory B cell (CL0002117)
Fold Change: 3.85
Marker Score: 3793
Cell Name: intraepithelial lymphocyte (CL0002496)
Fold Change: 3.85
Marker Score: 4273
Cell Name: memory T cell (CL0000813)
Fold Change: 3.84
Marker Score: 1652
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 3.84
Marker Score: 8752
Cell Name: effector memory CD8-positive, alpha-beta T cell, terminally differentiated (CL0001062)
Fold Change: 3.84
Marker Score: 5653
Cell Name: central memory CD8-positive, alpha-beta T cell (CL0000907)
Fold Change: 3.83
Marker Score: 9348
Cell Name: pulmonary artery endothelial cell (CL1001568)
Fold Change: 3.78
Marker Score: 3257
Cell Name: endothelial cell (CL0000115)
Fold Change: 3.75
Marker Score: 3365
Cell Name: epithelial cell of uterus (CL0002149)
Fold Change: 3.75
Marker Score: 859
Cell Name: CD4-positive, alpha-beta cytotoxic T cell (CL0000934)
Fold Change: 3.74
Marker Score: 3288
Cell Name: squamous epithelial cell (CL0000076)
Fold Change: 3.74
Marker Score: 2548
Cell Name: neutrophil (CL0000775)
Fold Change: 3.74
Marker Score: 2279
Cell Name: bronchial epithelial cell (CL0002328)
Fold Change: 3.7
Marker Score: 980
Cell Name: fibroblast (CL0000057)
Fold Change: 3.69
Marker Score: 3564
Cell Name: ependymal cell (CL0000065)
Fold Change: 3.68
Marker Score: 1284
Cell Name: class switched memory B cell (CL0000972)
Fold Change: 3.67
Marker Score: 3449
Cell Name: capillary endothelial cell (CL0002144)
Fold Change: 3.66
Marker Score: 3942
Cell Name: adipocyte of epicardial fat of left ventricle (CL1000311)
Fold Change: 3.66
Marker Score: 964
Cell Name: CD4-positive helper T cell (CL0000492)
Fold Change: 3.65
Marker Score: 3975
Cell Name: effector CD8-positive, alpha-beta T cell (CL0001050)
Fold Change: 3.64
Marker Score: 3067
Cell Name: CD16-negative, CD56-bright natural killer cell, human (CL0000938)
Fold Change: 3.64
Marker Score: 2982
Cell Name: skeletal muscle satellite cell (CL0000594)
Fold Change: 3.64
Marker Score: 2434
Cell Name: unswitched memory B cell (CL0000970)
Fold Change: 3.59
Marker Score: 2102
Cell Name: endothelial tip cell (CL0000704)
Fold Change: 3.59
Marker Score: 835
Cell Name: starburst amacrine cell (CL0004232)
Fold Change: 3.58
Marker Score: 1017
Cell Name: meningeal macrophage (CL0000879)
Fold Change: 3.58
Marker Score: 1008
Cell Name: granulocyte (CL0000094)
Fold Change: 3.58
Marker Score: 1604
Cell Name: type II pneumocyte (CL0002063)
Fold Change: 3.57
Marker Score: 23248
Cell Name: CD8-positive, alpha-beta cytotoxic T cell (CL0000794)
Fold Change: 3.56
Marker Score: 3137
Cell Name: progenitor cell of endocrine pancreas (CL0002351)
Fold Change: 3.55
Marker Score: 773
Cell Name: naive B cell (CL0000788)
Fold Change: 3.55
Marker Score: 3169
Cell Name: myofibroblast cell (CL0000186)
Fold Change: 3.54
Marker Score: 4375
Cell Name: medullary thymic epithelial cell (CL0002365)
Fold Change: 3.54
Marker Score: 5806
Cell Name: enteroendocrine cell (CL0000164)
Fold Change: 3.53
Marker Score: 1827
Cell Name: epithelial cell (CL0000066)
Fold Change: 3.51
Marker Score: 5584
Cell Name: lung macrophage (CL1001603)
Fold Change: 3.51
Marker Score: 4013
Cell Name: columnar/cuboidal epithelial cell (CL0000075)
Fold Change: 3.5
Marker Score: 927
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 3.5
Marker Score: 998
Cell Name: naive thymus-derived CD4-positive, alpha-beta T cell (CL0000895)
Fold Change: 3.5
Marker Score: 5996
Cell Name: Schwann cell precursor (CL0002375)
Fold Change: 3.49
Marker Score: 868
Cell Name: common myeloid progenitor (CL0000049)
Fold Change: 3.49
Marker Score: 924
Cell Name: alternatively activated macrophage (CL0000890)
Fold Change: 3.49
Marker Score: 1453
Cell Name: club cell (CL0000158)
Fold Change: 3.48
Marker Score: 4064
Cell Name: immature B cell (CL0000816)
Fold Change: 3.48
Marker Score: 2305
Cell Name: type I enteroendocrine cell (CL0002277)
Fold Change: 3.48
Marker Score: 866
Cell Name: basal cell (CL0000646)
Fold Change: 3.48
Marker Score: 4488
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: 3.47
Marker Score: 22546
Cell Name: mesothelial cell of epicardium (CL0011019)
Fold Change: 3.46
Marker Score: 1110
Cell Name: stromal cell (CL0000499)
Fold Change: 3.46
Marker Score: 4048
Cell Name: CD8-positive, alpha-beta memory T cell (CL0000909)
Fold Change: 3.45
Marker Score: 2931
Cell Name: activated CD4-positive, alpha-beta T cell, human (CL0001043)
Fold Change: 3.45
Marker Score: 1569
Cell Name: memory B cell (CL0000787)
Fold Change: 3.45
Marker Score: 2607
Cell Name: endothelial cell of vascular tree (CL0002139)
Fold Change: 3.44
Marker Score: 4994.5
Cell Name: kidney collecting duct principal cell (CL1001431)
Fold Change: 3.44
Marker Score: 8667
Cell Name: kidney loop of Henle thick ascending limb epithelial cell (CL1001106)
Fold Change: 3.44
Marker Score: 9209.5
Cell Name: epithelial cell of proximal tubule (CL0002306)
Fold Change: 3.43
Marker Score: 12194
Cell Name: smooth muscle cell (CL0000192)
Fold Change: 3.43
Marker Score: 2257
Cell Name: stratified epithelial cell (CL0000079)
Fold Change: 3.43
Marker Score: 26780

Hover over a box to see details here...

**Key characteristics:** - Ubiquitin C is a large protein (60-80 kDa) with multiple functions. - It is a substrate for a variety of proteases and is involved in the regulation of protein turnover. - It is found in a wide range of cellular compartments, including the nucleus, cytoplasm, and cell membrane. - It plays a crucial role in the regulation of cell growth, differentiation, and apoptosis. **Pathways and functions:** - Ubiquitination: UBC protein is ubiquitinated by a variety of E1, E2, and E3 ubiquitin ligases, leading to its degradation. - Proteasomal degradation: UBC is a substrate for the proteasome, a large protein complex responsible for protein degradation. - Autophagy: UBC is involved in the regulation of autophagy, a cellular process that removes damaged or unnecessary proteins and organelles. - Apoptosis: UBC is a key regulator of apoptosis, a process that eliminates damaged or cancerous cells. - Cell cycle regulation: UBC is involved in cell cycle regulation, including the regulation of cell cycle entry and exit points. - Immune responses: UBC is a key regulator of immune responses, where it is involved in the activation of immune cells and the regulation of inflammation. **Clinical significance:** - Mutations in the UBC gene are associated with various diseases, including cancer, neurodegenerative disorders, and autoimmune diseases. - Targeting UBC has emerged as a promising therapeutic strategy for cancer and other diseases. - Inhibitors of UBC have been shown to have anti-tumor effects in preclinical models. **Additional information:** - UBC is a highly conserved protein that is found in all eukaryotic cells. - It is a ubiquitin-like protein (ULP) that is involved in the regulation of protein-protein interactions. - UBC is a highly regulated protein that plays a vital role in maintaining cellular homeostasis and preventing the accumulation of damaged or misfolded proteins.

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. 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