CUL1 | ENSG00000055130 | NCBI 8454

Details for: CUL1

Gene ID: 8454

Symbol: CUL1

Ensembl ID: ENSG00000055130

Description: cullin 1

Associated with

Activation of nf-kappab in b cells
(R-HSA-1169091)
Adaptive immune system
(R-HSA-1280218)
Antigen processing: ubiquitination & proteasome degradation
(R-HSA-983168)
Apc/c-mediated degradation of cell cycle proteins
(R-HSA-174143)
C-type lectin receptors (clrs)
(R-HSA-5621481)
Cell cycle
(R-HSA-1640170)
Cell cycle, mitotic
(R-HSA-69278)
Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Cellular response to chemical stress
(R-HSA-9711123)
Circadian clock
(R-HSA-400253)
Class i mhc mediated antigen processing & presentation
(R-HSA-983169)
Clec7a (dectin-1) signaling
(R-HSA-5607764)
Constitutive signaling by notch1 hd+pest domain mutants
(R-HSA-2894862)
Constitutive signaling by notch1 pest domain mutants
(R-HSA-2644606)
Cyclin a:cdk2-associated events at s phase entry
(R-HSA-69656)
Cyclin d associated events in g1
(R-HSA-69231)
Cyclin e associated events during g1/s transition
(R-HSA-69202)
Cytokine signaling in immune system
(R-HSA-1280215)
Dectin-1 mediated noncanonical nf-kb signaling
(R-HSA-5607761)
Degradation of beta-catenin by the destruction complex
(R-HSA-195253)
Degradation of gli1 by the proteasome
(R-HSA-5610780)
Degradation of gli2 by the proteasome
(R-HSA-5610783)
Disease
(R-HSA-1643685)
Diseases of signal transduction by growth factor receptors and second messengers
(R-HSA-5663202)
Dna replication
(R-HSA-69306)
Downstream signaling events of b cell receptor (bcr)
(R-HSA-1168372)
Downstream tcr signaling
(R-HSA-202424)
Fbxl7 down-regulates aurka during mitotic entry and in early mitosis
(R-HSA-8854050)
Fbxw7 mutants and notch1 in cancer
(R-HSA-2644605)
Fc epsilon receptor (fceri) signaling
(R-HSA-2454202)
Fceri mediated nf-kb activation
(R-HSA-2871837)
G1 phase
(R-HSA-69236)
G1/s transition
(R-HSA-69206)
G2/m transition
(R-HSA-69275)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Gli3 is processed to gli3r by the proteasome
(R-HSA-5610785)
Hedgehog 'off' state
(R-HSA-5610787)
Immune system
(R-HSA-168256)
Innate immune system
(R-HSA-168249)
Interleukin-1 family signaling
(R-HSA-446652)
Interleukin-1 signaling
(R-HSA-9020702)
Interleukin-17 signaling
(R-HSA-448424)
Iron uptake and transport
(R-HSA-917937)
Keap1-nfe2l2 pathway
(R-HSA-9755511)
Loss of function of fbxw7 in cancer and notch1 signaling
(R-HSA-2644607)
Metabolism of proteins
(R-HSA-392499)
Mitotic g1 phase and g1/s transition
(R-HSA-453279)
Mitotic g2-g2/m phases
(R-HSA-453274)
Myd88 cascade initiated on plasma membrane
(R-HSA-975871)
Myd88 dependent cascade initiated on endosome
(R-HSA-975155)
Myd88-independent tlr4 cascade
(R-HSA-166166)
Myd88:mal(tirap) cascade initiated on plasma membrane
(R-HSA-166058)
Neddylation
(R-HSA-8951664)
Negative regulation of notch4 signaling
(R-HSA-9604323)
Nik-->noncanonical nf-kb signaling
(R-HSA-5676590)
Notch1 intracellular domain regulates transcription
(R-HSA-2122947)
Nuclear events mediated by nfe2l2
(R-HSA-9759194)
Nuclear events stimulated by alk signaling in cancer
(R-HSA-9725371)
Post-translational protein modification
(R-HSA-597592)
Prolactin receptor signaling
(R-HSA-1170546)
Regulation of apc/c activators between g1/s and early anaphase
(R-HSA-176408)
Regulation of bach1 activity
(R-HSA-9708530)
Regulation of mitotic cell cycle
(R-HSA-453276)
Regulation of plk1 activity at g2/m transition
(R-HSA-2565942)
Regulation of runx2 expression and activity
(R-HSA-8939902)
Rna polymerase ii transcription
(R-HSA-73857)
Scf(skp2)-mediated degradation of p27/p21
(R-HSA-187577)
Scf-beta-trcp mediated degradation of emi1
(R-HSA-174113)
Signaling by alk fusions and activated point mutants
(R-HSA-9725370)
Signaling by alk in cancer
(R-HSA-9700206)
Signaling by hedgehog
(R-HSA-5358351)
Signaling by interleukins
(R-HSA-449147)
Signaling by notch
(R-HSA-157118)
Signaling by notch1
(R-HSA-1980143)
Signaling by notch1 hd+pest domain mutants in cancer
(R-HSA-2894858)
Signaling by notch1 in cancer
(R-HSA-2644603)
Signaling by notch1 pest domain mutants in cancer
(R-HSA-2644602)
Signaling by notch4
(R-HSA-9013694)
Signaling by the b cell receptor (bcr)
(R-HSA-983705)
Signaling by wnt
(R-HSA-195721)
Signal transduction
(R-HSA-162582)
S phase
(R-HSA-69242)
Switching of origins to a post-replicative state
(R-HSA-69052)
Synthesis of dna
(R-HSA-69239)
Tcr signaling
(R-HSA-202403)
Tnfr2 non-canonical nf-kb pathway
(R-HSA-5668541)
Toll-like receptor cascades
(R-HSA-168898)
Toll like receptor 2 (tlr2) cascade
(R-HSA-181438)
Toll like receptor 3 (tlr3) cascade
(R-HSA-168164)
Toll like receptor 4 (tlr4) cascade
(R-HSA-166016)
Toll like receptor 5 (tlr5) cascade
(R-HSA-168176)
Toll like receptor 7/8 (tlr7/8) cascade
(R-HSA-168181)
Toll like receptor 9 (tlr9) cascade
(R-HSA-168138)
Toll like receptor 10 (tlr10) cascade
(R-HSA-168142)
Toll like receptor tlr1:tlr2 cascade
(R-HSA-168179)
Toll like receptor tlr6:tlr2 cascade
(R-HSA-168188)
Transcriptional regulation by runx2
(R-HSA-8878166)
Transport of small molecules
(R-HSA-382551)

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: 328.1682
Cell Significance Index: -51.0500
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 201.9765
Cell Significance Index: -51.2300
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 132.8446
Cell Significance Index: -54.7300
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 116.8129
Cell Significance Index: -55.1500
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 114.2626
Cell Significance Index: -46.4200
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 101.2860
Cell Significance Index: -52.1000
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 82.2626
Cell Significance Index: -55.2000
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 48.6623
Cell Significance Index: -46.4600
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 43.9594
Cell Significance Index: -54.2000
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 18.9782
Cell Significance Index: -50.8400
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 14.9050
Cell Significance Index: -45.7800
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 13.8886
Cell Significance Index: -54.8100
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 13.6846
Cell Significance Index: -29.9500
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 2.0995
Cell Significance Index: 421.1600
Cell Name: neoplastic cell (CL0001063)
Fold Change: 2.0369
Cell Significance Index: 404.2300
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: 1.6830
Cell Significance Index: 196.1400
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 1.4740
Cell Significance Index: 528.6800
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 1.3975
Cell Significance Index: 78.4200
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 1.3557
Cell Significance Index: 36.2000
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 1.3098
Cell Significance Index: 1182.6600
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: 1.2706
Cell Significance Index: 32.6600
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 0.9908
Cell Significance Index: 27.6900
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 0.9493
Cell Significance Index: 72.8500
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.8935
Cell Significance Index: 617.9600
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 0.8653
Cell Significance Index: 51.9500
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.8527
Cell Significance Index: 138.6900
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: 0.7469
Cell Significance Index: 50.2200
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: 0.7264
Cell Significance Index: 32.1300
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: 0.7172
Cell Significance Index: 27.1600
Cell Name: preadipocyte (CL0002334)
Fold Change: 0.6748
Cell Significance Index: 13.1700
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: 0.6418
Cell Significance Index: 39.4500
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.6145
Cell Significance Index: 60.7900
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 0.5704
Cell Significance Index: 70.1400
Cell Name: leptomeningeal cell (CL0000708)
Fold Change: 0.5567
Cell Significance Index: 11.9000
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 0.5370
Cell Significance Index: 96.8100
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: 0.4868
Cell Significance Index: 30.6800
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 0.4388
Cell Significance Index: 10.9700
Cell Name: centrilobular region hepatocyte (CL0019029)
Fold Change: 0.4096
Cell Significance Index: 6.9000
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 0.3387
Cell Significance Index: 23.4200
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: 0.3305
Cell Significance Index: 8.8600
Cell Name: retinal rod cell (CL0000604)
Fold Change: 0.3246
Cell Significance Index: 3.8700
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.2492
Cell Significance Index: 136.1200
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.2480
Cell Significance Index: 466.9300
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.2423
Cell Significance Index: 107.1100
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.2308
Cell Significance Index: 5.0000
Cell Name: hippocampal pyramidal neuron (CL1001571)
Fold Change: 0.2201
Cell Significance Index: 6.2800
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: 0.2148
Cell Significance Index: 97.5000
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: 0.2089
Cell Significance Index: 132.6600
Cell Name: GABAergic amacrine cell (CL4030027)
Fold Change: 0.1991
Cell Significance Index: 2.4700
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.1912
Cell Significance Index: 26.2600
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: 0.1246
Cell Significance Index: 2.1400
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.1165
Cell Significance Index: 22.1700
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 0.1118
Cell Significance Index: 172.1400
Cell Name: anterior lens cell (CL0002223)
Fold Change: 0.0837
Cell Significance Index: 154.4400
Cell Name: cortical interneuron (CL0008031)
Fold Change: 0.0621
Cell Significance Index: 1.4900
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 0.0473
Cell Significance Index: 5.5800
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.0233
Cell Significance Index: 0.6700
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 0.0015
Cell Significance Index: 2.0200
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: -0.0031
Cell Significance Index: -0.1100
Cell Name: type I muscle cell (CL0002211)
Fold Change: -0.0193
Cell Significance Index: -0.4700
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0251
Cell Significance Index: -15.6900
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0282
Cell Significance Index: -20.9000
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: -0.0369
Cell Significance Index: -6.3000
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0414
Cell Significance Index: -30.3400
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0529
Cell Significance Index: -40.0400
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0570
Cell Significance Index: -32.1500
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: -0.0697
Cell Significance Index: -3.6200
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.0795
Cell Significance Index: -1.3300
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: -0.0890
Cell Significance Index: -4.1900
Cell Name: lactocyte (CL0002325)
Fold Change: -0.0955
Cell Significance Index: -12.3400
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: -0.0978
Cell Significance Index: -4.5600
Cell Name: odontoblast (CL0000060)
Fold Change: -0.1003
Cell Significance Index: -12.8600
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: -0.1262
Cell Significance Index: -3.4400
Cell Name: cardiac endothelial cell (CL0010008)
Fold Change: -0.1342
Cell Significance Index: -1.9300
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.1473
Cell Significance Index: -15.0500
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.1652
Cell Significance Index: -47.5200
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.1661
Cell Significance Index: -24.1400
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.1679
Cell Significance Index: -35.3600
Cell Name: sebum secreting cell (CL0000317)
Fold Change: -0.2254
Cell Significance Index: -15.9400
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: -0.2303
Cell Significance Index: -10.4400
Cell Name: glycinergic neuron (CL1001509)
Fold Change: -0.2427
Cell Significance Index: -12.7500
Cell Name: early pro-B cell (CL0002046)
Fold Change: -0.2468
Cell Significance Index: -15.9300
Cell Name: fibroblast of cardiac tissue (CL0002548)
Fold Change: -0.2678
Cell Significance Index: -3.8500
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.2874
Cell Significance Index: -29.9300
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.3512
Cell Significance Index: -7.4800
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.3594
Cell Significance Index: -41.1800
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.3745
Cell Significance Index: -42.7500
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: -0.3891
Cell Significance Index: -29.0000
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: -0.4717
Cell Significance Index: -2.8500
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: -0.4786
Cell Significance Index: -13.7200
Cell Name: granulosa cell (CL0000501)
Fold Change: -0.4794
Cell Significance Index: -12.6100
Cell Name: lung endothelial cell (CL1001567)
Fold Change: -0.4892
Cell Significance Index: -25.4800
Cell Name: Purkinje cell (CL0000121)
Fold Change: -0.5046
Cell Significance Index: -11.0500
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -0.5710
Cell Significance Index: -7.7900
Cell Name: periportal region hepatocyte (CL0019026)
Fold Change: -0.5752
Cell Significance Index: -8.4900
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.5785
Cell Significance Index: -45.8200
Cell Name: skeletal muscle fibroblast (CL0011027)
Fold Change: -0.6214
Cell Significance Index: -4.2100
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: -0.6403
Cell Significance Index: -22.2500
Cell Name: cardiac muscle cell (CL0000746)
Fold Change: -0.7143
Cell Significance Index: -10.5500
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.7446
Cell Significance Index: -23.8500

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** Cullin 1 is a 72-kDa protein that belongs to the Cullin family of proteins. It is a component of the SCF (SKP1-CUL1-F-box protein) complex, which is a type of E3 ubiquitin ligase. CUL1 is characterized by its high specificity for targeting proteins for degradation through the ubiquitin-proteasome pathway. It is also known for its ability to regulate cell cycle progression, apoptosis, and immune responses. **Pathways and Functions** CUL1 is involved in various signaling pathways, including: 1. **NF-κB signaling**: CUL1 regulates the degradation of IκBα, allowing NF-κB to translocate to the nucleus and activate transcription of target genes. 2. **Notch signaling**: CUL1 regulates the degradation of Notch receptors, which is essential for the development and maintenance of tissues. 3. **Wnt/β-catenin signaling**: CUL1 regulates the degradation of β-catenin, which is involved in cell proliferation, differentiation, and survival. 4. **Cell cycle regulation**: CUL1 regulates the degradation of cell cycle regulators, such as p27 and p21, to promote cell cycle progression. 5. **Apoptosis**: CUL1 regulates the degradation of pro-apoptotic proteins, such as Bax and Bak, to promote cell survival. **Clinical Significance** Dysregulation of CUL1 has been implicated in various diseases, including: 1. **Cancer**: Overexpression of CUL1 has been observed in various types of cancer, including breast, lung, and colon cancer. 2. **Autoimmune disorders**: Dysregulation of CUL1 has been implicated in autoimmune disorders, such as rheumatoid arthritis and multiple sclerosis. 3. **Neurological conditions**: CUL1 has been implicated in neurological conditions, such as Alzheimer's disease and Parkinson's disease. 4. **Infectious diseases**: CUL1 has been implicated in the regulation of immune responses to infections, such as HIV and tuberculosis. In conclusion, CUL1 is a critical regulator of various cellular processes, including cell cycle regulation, protein degradation, and signaling pathways. Its dysregulation has been implicated in various diseases, highlighting the importance of CUL1 in maintaining cellular homeostasis.

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.

Cullin-1
B3KTW0_HUMAN

Genular Protein ID: 3086156254

Symbol: CUL1_HUMAN

Name: Cullin-1

UniProtKB Accession Codes:

Q13616 D3DWG3 O60719 Q08AL6 Q8IYW1

Database IDs:

Citations:

PubMed ID: 8681378

Title: cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family.

PubMed ID: 8681378

DOI: 10.1016/s0092-8674(00)81267-2

PubMed ID: 9663463

Title: Human CUL-1, but not other cullin family members, selectively interacts with SKP1 to form a complex with SKP2 and cyclin A.

PubMed ID: 9663463

PubMed ID: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

PubMed ID: 12853948

Title: The DNA sequence of human chromosome 7.

PubMed ID: 12853948

DOI: 10.1038/nature01782

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: 10230406

Title: Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha.

PubMed ID: 10230406

DOI: 10.1016/s1097-2765(00)80481-5

PubMed ID: 10230407

Title: ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity.

PubMed ID: 10230407

DOI: 10.1016/s1097-2765(00)80482-7

PubMed ID: 10597293

Title: Covalent modification of all members of human cullin family proteins by NEDD8.

PubMed ID: 10597293

DOI: 10.1038/sj.onc.1203093

PubMed ID: 10713156

Title: Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent ubiquitination of IkappaBalpha.

PubMed ID: 10713156

DOI: 10.1128/mcb.20.7.2326-2333.2000

PubMed ID: 10851089

Title: Yeast homolog of human SAG/ROC2/Rbx2/Hrt2 is essential for cell growth, but not for germination: chip profiling implicates its role in cell cycle regulation.

PubMed ID: 10851089

DOI: 10.1038/sj.onc.1203635

PubMed ID: 11337588

Title: Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome.

PubMed ID: 11337588

DOI: 10.1126/science.1059780

PubMed ID: 12504026

Title: CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex.

PubMed ID: 12504026

DOI: 10.1016/s1097-2765(02)00784-0

PubMed ID: 12609982

Title: TIP120A associates with cullins and modulates ubiquitin ligase activity.

PubMed ID: 12609982

DOI: 10.1074/jbc.m213070200

PubMed ID: 15145941

Title: Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a proline-rich region.

PubMed ID: 15145941

DOI: 10.1074/jbc.m404950200

PubMed ID: 15531760

Title: Degradation of MyoD mediated by the SCF (MAFbx) ubiquitin ligase.

PubMed ID: 15531760

DOI: 10.1074/jbc.m411346200

PubMed ID: 15640526

Title: FBW2 targets GCMa to the ubiquitin-proteasome degradation system.

PubMed ID: 15640526

DOI: 10.1074/jbc.m413986200

PubMed ID: 16714087

Title: FBXO25, an F-box protein homologue of atrogin-1, is not induced in atrophying muscle.

PubMed ID: 16714087

DOI: 10.1016/j.bbagen.2006.03.020

PubMed ID: 16797541

Title: Proteasomal degradation of the multifunctional regulator YB-1 is mediated by an F-Box protein induced during programmed cell death.

PubMed ID: 16797541

DOI: 10.1016/j.febslet.2006.06.023

PubMed ID: 16880511

Title: Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein.

PubMed ID: 16880511

DOI: 10.1128/mcb.01630-05

PubMed ID: 17254749

Title: Characterization of cullin-based E3 ubiquitin ligases in intact mammalian cells -- evidence for cullin dimerization.

PubMed ID: 17254749

DOI: 10.1016/j.cellsig.2006.12.002

PubMed ID: 17098746

Title: FBXO11 promotes the neddylation of p53 and inhibits its transcriptional activity.

PubMed ID: 17098746

DOI: 10.1074/jbc.m609001200

PubMed ID: 18805092

Title: Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation.

PubMed ID: 18805092

DOI: 10.1016/j.cell.2008.07.022

PubMed ID: 18203720

Title: Diversity in tissue expression, substrate binding, and SCF complex formation for a lectin family of ubiquitin ligases.

PubMed ID: 18203720

DOI: 10.1074/jbc.m709508200

PubMed ID: 18644861

Title: Regulation of Chk2 ubiquitination and signaling through autophosphorylation of serine 379.

PubMed ID: 18644861

DOI: 10.1128/mcb.00821-08

PubMed ID: 19679664

Title: Adenovirus E1A inhibits SCF(Fbw7) ubiquitin ligase.

PubMed ID: 19679664

DOI: 10.1074/jbc.m109.006809

PubMed ID: 20190741

Title: A deneddylase encoded by Epstein-Barr virus promotes viral DNA replication by regulating the activity of cullin-RING ligases.

PubMed ID: 20190741

DOI: 10.1038/ncb2035

PubMed ID: 20596027

Title: SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation.

PubMed ID: 20596027

DOI: 10.1038/nature09140

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22017875

Title: mTOR drives its own activation via SCF(betaTrCP)-dependent degradation of the mTOR inhibitor DEPTOR.

PubMed ID: 22017875

DOI: 10.1016/j.molcel.2011.08.030

PubMed ID: 22017877

Title: mTOR generates an auto-amplification loop by triggering the betaTrCP- and CK1alpha-dependent degradation of DEPTOR.

PubMed ID: 22017877

DOI: 10.1016/j.molcel.2011.09.005

PubMed ID: 22405651

Title: The glomuvenous malformation protein Glomulin binds Rbx1 and regulates cullin RING ligase-mediated turnover of Fbw7.

PubMed ID: 22405651

DOI: 10.1016/j.molcel.2012.02.005

PubMed ID: 22113614

Title: FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-cell lymphomas.

PubMed ID: 22113614

DOI: 10.1038/nature10688

PubMed ID: 24076655

Title: TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes.

PubMed ID: 24076655

DOI: 10.1038/emboj.2013.209

PubMed ID: 23263282

Title: SCF(Fbxo9) and CK2 direct the cellular response to growth factor withdrawal via Tel2/Tti1 degradation and promote survival in multiple myeloma.

PubMed ID: 23263282

DOI: 10.1038/ncb2651

PubMed ID: 23776465

Title: Myeloma overexpressed 2 (Myeov2) regulates L11 subnuclear localization through Nedd8 modification.

PubMed ID: 23776465

DOI: 10.1371/journal.pone.0065285

PubMed ID: 23431138

Title: Related F-box proteins control cell death in Caenorhabditis elegans and human lymphoma.

PubMed ID: 23431138

DOI: 10.1073/pnas.1217271110

PubMed ID: 23201271

Title: Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes.

PubMed ID: 23201271

DOI: 10.1016/j.str.2012.10.013

PubMed ID: 24192928

Title: Oncogenic function of SCCRO5/DCUN1D5 requires its Neddylation E3 activity and nuclear localization.

PubMed ID: 24192928

DOI: 10.1158/1078-0432.ccr-13-1252

PubMed ID: 25349211

Title: SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of SCCRO (DCUN1D1).

PubMed ID: 25349211

DOI: 10.1074/jbc.m114.585505

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: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 25704143

Title: Cep68 can be regulated by Nek2 and SCF complex.

PubMed ID: 25704143

DOI: 10.1016/j.ejcb.2015.01.004

PubMed ID: 25503564

Title: Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM to allow centriole separation, disengagement and licensing.

PubMed ID: 25503564

DOI: 10.1038/ncb3076

PubMed ID: 27565346

Title: Two distinct types of E3 ligases work in unison to regulate substrate ubiquitylation.

PubMed ID: 27565346

DOI: 10.1016/j.cell.2016.07.027

PubMed ID: 26906416

Title: Characterization of the mammalian family of DCN-type NEDD8 E3 ligases.

PubMed ID: 26906416

DOI: 10.1242/jcs.181784

PubMed ID: 26818844

Title: SCF(Cyclin F)-dependent degradation of CDC6 suppresses DNA re-replication.

PubMed ID: 26818844

DOI: 10.1038/ncomms10530

PubMed ID: 29149593

Title: NOTCH2 Hajdu-Cheney mutations escape SCFFBW7-dependent proteolysis to promote osteoporosis.

PubMed ID: 29149593

DOI: 10.1016/j.molcel.2017.10.018

PubMed ID: 28152074

Title: Multiple UBXN family members inhibit retrovirus and lentivirus production and canonical NFkappaBeta signaling by stabilizing IkappaBalpha.

PubMed ID: 28152074

DOI: 10.1371/journal.ppat.1006187

PubMed ID: 29444943

Title: Vaccinia Virus C9 Ankyrin Repeat/F-Box Protein Is a Newly Identified Antagonist of the Type I Interferon-Induced Antiviral State.

PubMed ID: 29444943

DOI: 10.1128/jvi.00053-18

PubMed ID: 34319780

Title: Suppression of JAK-STAT Signaling by Epstein-Barr Virus Tegument Protein BGLF2 through Recruitment of SHP1 Phosphatase and Promotion of STAT2 Degradation.

PubMed ID: 34319780

DOI: 10.1128/jvi.01027-21

PubMed ID: 35982156

Title: Structure of CRL7FBXW8 reveals coupling with CUL1-RBX1/ROC1 for multi-cullin-RING E3-catalyzed ubiquitin ligation.

PubMed ID: 35982156

DOI: 10.1038/s41594-022-00815-6

PubMed ID: 38225265

Title: The phosphatase DUSP22 inhibits UBR2-mediated K63-ubiquitination and activation of Lck downstream of TCR signalling.

PubMed ID: 38225265

DOI: 10.1038/s41467-024-44843-w

PubMed ID: 11961546

Title: Structure of the Cul1-Rbx1-Skp1-F box Skp2 SCF ubiquitin ligase complex.

PubMed ID: 11961546

DOI: 10.1038/416703a

PubMed ID: 15537541

Title: Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases.

PubMed ID: 15537541

DOI: 10.1016/j.cell.2004.10.019

PubMed ID: 21940857

Title: N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex.

PubMed ID: 21940857

DOI: 10.1126/science.1209307

PubMed ID: 22748924

Title: Structure of a glomulin-RBX1-CUL1 complex: inhibition of a RING E3 ligase through masking of its E2-binding surface.

PubMed ID: 22748924

DOI: 10.1016/j.molcel.2012.05.044

PubMed ID: 28581483

Title: Blocking an N-terminal acetylation-dependent protein interaction inhibits an E3 ligase.

PubMed ID: 28581483

DOI: 10.1038/nchembio.2386

Sequence Information:

Length: 776
Mass: 89679
Checksum: 6625A1FFA7799BBA
Sequence:

MSSTRSQNPH GLKQIGLDQI WDDLRAGIQQ VYTRQSMAKS RYMELYTHVY NYCTSVHQSN 
QARGAGVPPS KSKKGQTPGG AQFVGLELYK RLKEFLKNYL TNLLKDGEDL MDESVLKFYT 
QQWEDYRFSS KVLNGICAYL NRHWVRRECD EGRKGIYEIY SLALVTWRDC LFRPLNKQVT 
NAVLKLIEKE RNGETINTRL ISGVVQSYVE LGLNEDDAFA KGPTLTVYKE SFESQFLADT 
ERFYTRESTE FLQQNPVTEY MKKAEARLLE EQRRVQVYLH ESTQDELARK CEQVLIEKHL 
EIFHTEFQNL LDADKNEDLG RMYNLVSRIQ DGLGELKKLL ETHIHNQGLA AIEKCGEAAL 
NDPKMYVQTV LDVHKKYNAL VMSAFNNDAG FVAALDKACG RFINNNAVTK MAQSSSKSPE 
LLARYCDSLL KKSSKNPEEA ELEDTLNQVM VVFKYIEDKD VFQKFYAKML AKRLVHQNSA 
SDDAEASMIS KLKQACGFEY TSKLQRMFQD IGVSKDLNEQ FKKHLTNSEP LDLDFSIQVL 
SSGSWPFQQS CTFALPSELE RSYQRFTAFY ASRHSGRKLT WLYQLSKGEL VTNCFKNRYT 
LQASTFQMAI LLQYNTEDAY TVQQLTDSTQ IKMDILAQVL QILLKSKLLV LEDENANVDE 
VELKPDTLIK LYLGYKNKKL RVNINVPMKT EQKQEQETTH KNIEEDRKLL IQAAIVRIMK 
MRKVLKHQQL LGEVLTQLSS RFKPRVPVIK KCIDILIEKE YLERVDGEKD TYSYLA

Genular Protein ID: 579746978

Symbol: B3KTW0_HUMAN

Name: N/A

UniProtKB Accession Codes:

B3KTW0

Database IDs:

Citations:

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

Sequence Information:

Length: 607
Mass: 69886
Checksum: B03AA71184726313
Sequence:

MELYTHVYNY CTSVHQSNQA RGAGVPPSKS KKGQTPGGAQ FVGLELYKRL KEFLKNYLTN 
LLKDGEDLMD ESVLKFYTQQ WEDYRFSSKV LNGICAYLNR HWVRRECDEG RKGIYEIYSL 
ALVTWRDCLF RPLNKQVTNA VLKLIEKERN GETINTRLIS GVVQSYVELG LNEDDAFAKG 
PTLTVYKESF ESQFLADTER FYTRESTEFL QQNPVTEYMK KAEARLLEEQ RRVQVYLHES 
TQDELARKCE QVLIEKHLEI FHTEFQNLLD ADKNEDLGRM YNLVSRIQDG LGELKKLLET 
HIHNQGLAAI EKCGEAALND PKMYVQTVLD VHKKYNALVM SAFNNDAGFV AALDKACGRF 
INNNAVTKMA QSSSKSPELL ARYCDSLLKK SSKNPEEAEL EDTLNQVMVV FKYIEDKDVF 
QKFYAKMLAK RLVHQNSASD DAEASMISKL KQACGFEYTS KLQRMFQDIG VSKDLNEQFK 
KHLTNSEPLD LDFSIQVLSS GSWPFQQSCT FALPSELERS YQRFTAFYAS RHSGRKLTWL 
YQLSKGELVT NCFKNRYTLQ ASTFQMAILL QYNTEDAYTV QQLTDSTQIK MDILAQVLQI 
LLKSKLL

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: CUL1

Associated with

Cells (max top 100)

Other Information

cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family. PubMed ID: 8681378

Human CUL-1, but not other cullin family members, selectively interacts with SKP1 to form a complex with SKP2 and cyclin A. PubMed ID: 9663463

The full-ORF clone resource of the German cDNA consortium. PubMed ID: 17974005

The DNA sequence of human chromosome 7. PubMed ID: 12853948

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

Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha. PubMed ID: 10230406

ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity. PubMed ID: 10230407

Covalent modification of all members of human cullin family proteins by NEDD8. PubMed ID: 10597293

Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent ubiquitination of IkappaBalpha. PubMed ID: 10713156

Yeast homolog of human SAG/ROC2/Rbx2/Hrt2 is essential for cell growth, but not for germination: chip profiling implicates its role in cell cycle regulation. PubMed ID: 10851089

Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome. PubMed ID: 11337588

CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. PubMed ID: 12504026

TIP120A associates with cullins and modulates ubiquitin ligase activity. PubMed ID: 12609982

Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a proline-rich region. PubMed ID: 15145941

Degradation of MyoD mediated by the SCF (MAFbx) ubiquitin ligase. PubMed ID: 15531760

FBW2 targets GCMa to the ubiquitin-proteasome degradation system. PubMed ID: 15640526

FBXO25, an F-box protein homologue of atrogin-1, is not induced in atrophying muscle. PubMed ID: 16714087

Proteasomal degradation of the multifunctional regulator YB-1 is mediated by an F-Box protein induced during programmed cell death. PubMed ID: 16797541

Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein. PubMed ID: 16880511

Characterization of cullin-based E3 ubiquitin ligases in intact mammalian cells -- evidence for cullin dimerization. PubMed ID: 17254749

FBXO11 promotes the neddylation of p53 and inhibits its transcriptional activity. PubMed ID: 17098746

Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. PubMed ID: 18805092

Diversity in tissue expression, substrate binding, and SCF complex formation for a lectin family of ubiquitin ligases. PubMed ID: 18203720

Regulation of Chk2 ubiquitination and signaling through autophosphorylation of serine 379. PubMed ID: 18644861

Adenovirus E1A inhibits SCF(Fbw7) ubiquitin ligase. PubMed ID: 19679664

A deneddylase encoded by Epstein-Barr virus promotes viral DNA replication by regulating the activity of cullin-RING ligases. PubMed ID: 20190741

SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation. PubMed ID: 20596027

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

mTOR drives its own activation via SCF(betaTrCP)-dependent degradation of the mTOR inhibitor DEPTOR. PubMed ID: 22017875

mTOR generates an auto-amplification loop by triggering the betaTrCP- and CK1alpha-dependent degradation of DEPTOR. PubMed ID: 22017877

The glomuvenous malformation protein Glomulin binds Rbx1 and regulates cullin RING ligase-mediated turnover of Fbw7. PubMed ID: 22405651

FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-cell lymphomas. PubMed ID: 22113614

TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes. PubMed ID: 24076655

SCF(Fbxo9) and CK2 direct the cellular response to growth factor withdrawal via Tel2/Tti1 degradation and promote survival in multiple myeloma. PubMed ID: 23263282

Myeloma overexpressed 2 (Myeov2) regulates L11 subnuclear localization through Nedd8 modification. PubMed ID: 23776465

Related F-box proteins control cell death in Caenorhabditis elegans and human lymphoma. PubMed ID: 23431138

Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes. PubMed ID: 23201271

Oncogenic function of SCCRO5/DCUN1D5 requires its Neddylation E3 activity and nuclear localization. PubMed ID: 24192928

SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of SCCRO (DCUN1D1). PubMed ID: 25349211

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

Immunoaffinity enrichment and mass spectrometry analysis of protein methylation. PubMed ID: 24129315

Cep68 can be regulated by Nek2 and SCF complex. PubMed ID: 25704143

Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM to allow centriole separation, disengagement and licensing. PubMed ID: 25503564

Two distinct types of E3 ligases work in unison to regulate substrate ubiquitylation. PubMed ID: 27565346

Characterization of the mammalian family of DCN-type NEDD8 E3 ligases. PubMed ID: 26906416

SCF(Cyclin F)-dependent degradation of CDC6 suppresses DNA re-replication. PubMed ID: 26818844

NOTCH2 Hajdu-Cheney mutations escape SCFFBW7-dependent proteolysis to promote osteoporosis. PubMed ID: 29149593

Multiple UBXN family members inhibit retrovirus and lentivirus production and canonical NFkappaBeta signaling by stabilizing IkappaBalpha. PubMed ID: 28152074

Vaccinia Virus C9 Ankyrin Repeat/F-Box Protein Is a Newly Identified Antagonist of the Type I Interferon-Induced Antiviral State. PubMed ID: 29444943

Suppression of JAK-STAT Signaling by Epstein-Barr Virus Tegument Protein BGLF2 through Recruitment of SHP1 Phosphatase and Promotion of STAT2 Degradation. PubMed ID: 34319780

Structure of CRL7FBXW8 reveals coupling with CUL1-RBX1/ROC1 for multi-cullin-RING E3-catalyzed ubiquitin ligation. PubMed ID: 35982156

The phosphatase DUSP22 inhibits UBR2-mediated K63-ubiquitination and activation of Lck downstream of TCR signalling. PubMed ID: 38225265

Structure of the Cul1-Rbx1-Skp1-F box Skp2 SCF ubiquitin ligase complex. PubMed ID: 11961546

Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases. PubMed ID: 15537541

N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex. PubMed ID: 21940857

Structure of a glomulin-RBX1-CUL1 complex: inhibition of a RING E3 ligase through masking of its E2-binding surface. PubMed ID: 22748924

Blocking an N-terminal acetylation-dependent protein interaction inhibits an E3 ligase. PubMed ID: 28581483

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039