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Q13616

- CUL1_HUMAN

UniProt

Q13616 - CUL1_HUMAN

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Protein

Cullin-1

Gene

CUL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as a rigid scaffold that organizes the SKP1-F-box protein and RBX1 subunits. May contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and exchange of the substrate recognition component is mediated by TIP120A/CAND1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO1) directs ubiquitination of BCL6 and DTL but does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) direct ubiquitination of TTI1 and TELO2. SCF(FBXO10) directs ubiquitination of BCL2.8 Publications

Pathwayi

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. cell cycle arrest Source: ProtInc
  3. cell proliferation Source: Ensembl
  4. G1/S transition of mitotic cell cycle Source: Reactome
  5. G2/M transition of mitotic cell cycle Source: Reactome
  6. intrinsic apoptotic signaling pathway Source: ProtInc
  7. mitotic cell cycle Source: Reactome
  8. negative regulation of cell proliferation Source: ProtInc
  9. Notch signaling pathway Source: Reactome
  10. organ morphogenesis Source: Ensembl
  11. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  12. protein monoubiquitination Source: Ensembl
  13. protein ubiquitination Source: UniProtKB
  14. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  15. SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  16. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_115697. Prolactin receptor signaling.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_160305. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_22442. Interleukin-1 signaling.
REACT_24941. Circadian Clock.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_821. Cyclin D associated events in G1.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
SignaLinkiQ13616.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cullin-1
Short name:
CUL-1
Gene namesi
Name:CUL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:2551. CUL1.

Subcellular locationi

GO - Cellular componenti

  1. cullin-RING ubiquitin ligase complex Source: MGI
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. Parkin-FBXW7-Cul1 ubiquitin ligase complex Source: ParkinsonsUK-UCL
  5. SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27047.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 776776Cullin-1PRO_0000119787Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki708 – 708Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki720 – 720Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)

Post-translational modificationi

Neddylated; which enhances the ubiquitination activity of SCF and prevents binding of the inhibitor CAND1. Deneddylated via its interaction with the COP9 signalosome (CSN) complex. Deneddylated by Epstein-Barr virus BPLF1 leading to a S-phase-like environment that is required for efficient replication of the viral genome.5 Publications

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ13616.
PaxDbiQ13616.
PeptideAtlasiQ13616.
PRIDEiQ13616.

PTM databases

PhosphoSiteiQ13616.

Expressioni

Tissue specificityi

Expressed in lung fibroblasts.1 Publication

Gene expression databases

BgeeiQ13616.
CleanExiHS_CUL1.
ExpressionAtlasiQ13616. baseline and differential.
GenevestigatoriQ13616.

Organism-specific databases

HPAiCAB002676.
HPA050796.

Interactioni

Subunit structurei

Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes formed of CUL1, SKP1, RBX1 and a variable F-box domain-containing protein as substrate-specific subunit. Component of the SCF(FBXW11) complex containing FBXW11. Component of the SCF(SKP2) complex containing SKP2, in which it interacts directly with SKP1, SKP2 and RBX1. Component of the SCF(FBXW2) complex containing FBXw2. Component of the SCF(FBXO32) complex containing FBXO32. Component of the probable SCF(FBXO7) complex containing FBXO7. Component of the SCF(FBXO10) complex containing FBXO10. Component of the SCF(FBXO11) complex containing FBXO11. Component of the SCF(FBXO25) complex containing FBXO25. Component of the SCF(FBXO33) complex containing FBXO33. Component of the probable SCF(FBXO4) complex containing FBXO4. Component of the SCF(FBXO44) complex, composed of SKP1, CUL1 and FBXO44. Component of the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC. This complex binds phosphorylated NFKBIA. Part of a SCF complex consisting of CUL1, RBX1, SKP1 and FBXO2. Component of a SCF(SKP2)-like complex containing CUL1, SKP1, TRIM21 and SKP2. Component of the SCF(FBXO17) complex, composed of SKP1, CUL1 and FBXO17. Component of the SCF(FBXO27) complex, composed of SKP1, CUL1 and FBXO27. Component of the SCF(CCNF) complex consisting of CUL1, RBX1, SKP1 and CCNF. Component of the SCF(FBXL3) complex composed of CUL1, SKP1, RBX1 and FBXL3. Component of the SCF(FBXL21) complex composed of CUL1, SKP1, RBX1 and FBXL21. Component of the SCF(FBXO9) composed of CUL1, SKP1, RBX1 and FBXO9. Component of the SCF(FBXW7) composed of CUL1, SKP1, RBX1 and FBXW7. Interacts with CHEK2; mediates CHEK2 ubiquitination and regulates its function. Part of a complex with TIP120A/CAND1 and RBX1. The unneddylated form interacts with TIP120A/CAND1 and the interaction mediates the exchange of the F-box substrate-specific subunit. Can self-associate. Interacts with FBXW8. Interacts with RNF7. Interacts with CUL7; the interaction seems to be mediated by FBXW8. Interacts with TRIM21. Interacts with COPS2. Interacts with Epstein-Barr virus BPLF1. Interacts with human adenovirus early E1A protein; this interaction inhibits RBX1-CUL1-dependent elongation reaction of ubiquitin chains by the SCF(FBXW7) complex.22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARIH1Q9Y4X56EBI-359390,EBI-2514233
BTRCQ9Y2975EBI-359390,EBI-307461
CAND1Q86VP619EBI-359390,EBI-456077
CCNYQ8ND763EBI-359390,EBI-1049189
CDC34P494273EBI-359390,EBI-975634
Fbxl21Q8BFZ43EBI-359390,EBI-6898235From a different organism.
Fbxl3Q8C4V43EBI-359390,EBI-1266589From a different organism.
FBXO4Q9UKT52EBI-359390,EBI-960409
FBXW11Q9UKB12EBI-359390,EBI-355189
m005RQ837305EBI-359390,EBI-6859930From a different organism.
MDM2Q009873EBI-359390,EBI-389668
NEDD8Q158435EBI-359390,EBI-716247
RBX1P6287712EBI-359390,EBI-398523
SKP1P632089EBI-359390,EBI-307486
SKP2Q133099EBI-359390,EBI-456291
UBE2MP610812EBI-359390,EBI-1041660

Protein-protein interaction databases

BioGridi114032. 677 interactions.
DIPiDIP-17013N.
IntActiQ13616. 63 interactions.
MINTiMINT-120495.
STRINGi9606.ENSP00000326804.

Structurei

Secondary structure

1
776
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 3114
Turni32 – 343
Helixi39 – 5214
Helixi87 – 10519
Turni106 – 1094
Turni111 – 1144
Helixi115 – 13622
Helixi138 – 1436
Beta strandi144 – 1463
Helixi159 – 1657
Helixi168 – 1714
Turni172 – 1776
Helixi178 – 18710
Turni188 – 1903
Helixi199 – 21012
Turni211 – 2133
Beta strandi215 – 2195
Helixi226 – 2316
Helixi233 – 25422
Helixi261 – 27313
Turni274 – 2796
Beta strandi281 – 2844
Helixi285 – 29511
Beta strandi296 – 3005
Helixi301 – 31212
Helixi318 – 32811
Helixi333 – 35523
Helixi359 – 3613
Helixi363 – 38220
Turni383 – 3875
Helixi389 – 40416
Helixi407 – 4126
Helixi417 – 43014
Helixi439 – 45315
Helixi459 – 47517
Helixi482 – 52544
Turni526 – 5283
Beta strandi532 – 54110
Turni542 – 5443
Helixi557 – 5593
Helixi560 – 56910
Turni570 – 5734
Beta strandi579 – 5813
Helixi583 – 5853
Beta strandi589 – 5979
Beta strandi600 – 6023
Helixi605 – 6128
Helixi613 – 6153
Beta strandi616 – 6216
Helixi622 – 6287
Helixi633 – 64513
Turni646 – 6483
Beta strandi652 – 6543
Turni658 – 6603
Beta strandi668 – 6714
Beta strandi678 – 6825
Helixi691 – 70010
Helixi703 – 72220
Beta strandi723 – 7264
Helixi727 – 73812
Turni739 – 7413
Helixi746 – 75813
Beta strandi761 – 7655
Beta strandi768 – 7747

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LDJX-ray3.00A17-776[»]
1LDKX-ray3.10A15-410[»]
B411-776[»]
1U6GX-ray3.10A1-776[»]
3RTRX-ray3.21A/C/E/G411-776[»]
3TDUX-ray1.50C/D702-776[»]
3TDZX-ray2.00C/D702-776[»]
4F52X-ray3.00A/C411-690[»]
4P5OX-ray3.11A/C411-776[»]
ProteinModelPortaliQ13616.
SMRiQ13616. Positions 17-776.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13616.

Family & Domainsi

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5647.
GeneTreeiENSGT00760000119212.
HOGENOMiHOG000176713.
HOVERGENiHBG106177.
InParanoidiQ13616.
KOiK03347.
OMAiNEAFNGE.
OrthoDBiEOG7X3QQG.
PhylomeDBiQ13616.
TreeFamiTF101151.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTiSM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMiSSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEiPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q13616-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSTRSQNPH GLKQIGLDQI WDDLRAGIQQ VYTRQSMAKS RYMELYTHVY
60 70 80 90 100
NYCTSVHQSN QARGAGVPPS KSKKGQTPGG AQFVGLELYK RLKEFLKNYL
110 120 130 140 150
TNLLKDGEDL MDESVLKFYT QQWEDYRFSS KVLNGICAYL NRHWVRRECD
160 170 180 190 200
EGRKGIYEIY SLALVTWRDC LFRPLNKQVT NAVLKLIEKE RNGETINTRL
210 220 230 240 250
ISGVVQSYVE LGLNEDDAFA KGPTLTVYKE SFESQFLADT ERFYTRESTE
260 270 280 290 300
FLQQNPVTEY MKKAEARLLE EQRRVQVYLH ESTQDELARK CEQVLIEKHL
310 320 330 340 350
EIFHTEFQNL LDADKNEDLG RMYNLVSRIQ DGLGELKKLL ETHIHNQGLA
360 370 380 390 400
AIEKCGEAAL NDPKMYVQTV LDVHKKYNAL VMSAFNNDAG FVAALDKACG
410 420 430 440 450
RFINNNAVTK MAQSSSKSPE LLARYCDSLL KKSSKNPEEA ELEDTLNQVM
460 470 480 490 500
VVFKYIEDKD VFQKFYAKML AKRLVHQNSA SDDAEASMIS KLKQACGFEY
510 520 530 540 550
TSKLQRMFQD IGVSKDLNEQ FKKHLTNSEP LDLDFSIQVL SSGSWPFQQS
560 570 580 590 600
CTFALPSELE RSYQRFTAFY ASRHSGRKLT WLYQLSKGEL VTNCFKNRYT
610 620 630 640 650
LQASTFQMAI LLQYNTEDAY TVQQLTDSTQ IKMDILAQVL QILLKSKLLV
660 670 680 690 700
LEDENANVDE VELKPDTLIK LYLGYKNKKL RVNINVPMKT EQKQEQETTH
710 720 730 740 750
KNIEEDRKLL IQAAIVRIMK MRKVLKHQQL LGEVLTQLSS RFKPRVPVIK
760 770
KCIDILIEKE YLERVDGEKD TYSYLA
Length:776
Mass (Da):89,679
Last modified:August 14, 2001 - v2
Checksum:i6625A1FFA7799BBA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 8224Missing in AAC50544. (PubMed:8681378)CuratedAdd
BLAST
Sequence conflicti726 – 7261K → R in CAD97651. (PubMed:17974005)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58087 mRNA. Translation: AAC50544.1.
AF062536 mRNA. Translation: AAC36681.1.
BX537409 mRNA. Translation: CAD97651.1.
AC005229 Genomic DNA. Translation: AAM49153.1.
CH471146 Genomic DNA. Translation: EAW80074.1.
BC125119 mRNA. Translation: AAI25120.1.
BC125120 mRNA. Translation: AAI25121.1.
CCDSiCCDS34772.1.
RefSeqiNP_003583.2. NM_003592.2.
XP_005250117.1. XM_005250060.2.
UniGeneiHs.146806.

Genome annotation databases

EnsembliENST00000325222; ENSP00000326804; ENSG00000055130.
ENST00000409469; ENSP00000387160; ENSG00000055130.
ENST00000602748; ENSP00000473318; ENSG00000055130.
ENST00000617797; ENSP00000482123; ENSG00000055130.
GeneIDi8454.
KEGGihsa:8454.
UCSCiuc003wey.3. human.

Polymorphism databases

DMDMi19863257.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58087 mRNA. Translation: AAC50544.1 .
AF062536 mRNA. Translation: AAC36681.1 .
BX537409 mRNA. Translation: CAD97651.1 .
AC005229 Genomic DNA. Translation: AAM49153.1 .
CH471146 Genomic DNA. Translation: EAW80074.1 .
BC125119 mRNA. Translation: AAI25120.1 .
BC125120 mRNA. Translation: AAI25121.1 .
CCDSi CCDS34772.1.
RefSeqi NP_003583.2. NM_003592.2.
XP_005250117.1. XM_005250060.2.
UniGenei Hs.146806.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LDJ X-ray 3.00 A 17-776 [» ]
1LDK X-ray 3.10 A 15-410 [» ]
B 411-776 [» ]
1U6G X-ray 3.10 A 1-776 [» ]
3RTR X-ray 3.21 A/C/E/G 411-776 [» ]
3TDU X-ray 1.50 C/D 702-776 [» ]
3TDZ X-ray 2.00 C/D 702-776 [» ]
4F52 X-ray 3.00 A/C 411-690 [» ]
4P5O X-ray 3.11 A/C 411-776 [» ]
ProteinModelPortali Q13616.
SMRi Q13616. Positions 17-776.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114032. 677 interactions.
DIPi DIP-17013N.
IntActi Q13616. 63 interactions.
MINTi MINT-120495.
STRINGi 9606.ENSP00000326804.

PTM databases

PhosphoSitei Q13616.

Polymorphism databases

DMDMi 19863257.

Proteomic databases

MaxQBi Q13616.
PaxDbi Q13616.
PeptideAtlasi Q13616.
PRIDEi Q13616.

Protocols and materials databases

DNASUi 8454.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000325222 ; ENSP00000326804 ; ENSG00000055130 .
ENST00000409469 ; ENSP00000387160 ; ENSG00000055130 .
ENST00000602748 ; ENSP00000473318 ; ENSG00000055130 .
ENST00000617797 ; ENSP00000482123 ; ENSG00000055130 .
GeneIDi 8454.
KEGGi hsa:8454.
UCSCi uc003wey.3. human.

Organism-specific databases

CTDi 8454.
GeneCardsi GC07P148395.
HGNCi HGNC:2551. CUL1.
HPAi CAB002676.
HPA050796.
MIMi 603134. gene.
neXtProti NX_Q13616.
PharmGKBi PA27047.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5647.
GeneTreei ENSGT00760000119212.
HOGENOMi HOG000176713.
HOVERGENi HBG106177.
InParanoidi Q13616.
KOi K03347.
OMAi NEAFNGE.
OrthoDBi EOG7X3QQG.
PhylomeDBi Q13616.
TreeFami TF101151.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_115697. Prolactin receptor signaling.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_160305. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_22442. Interleukin-1 signaling.
REACT_24941. Circadian Clock.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_821. Cyclin D associated events in G1.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
SignaLinki Q13616.

Miscellaneous databases

ChiTaRSi CUL1. human.
EvolutionaryTracei Q13616.
GeneWikii CUL1.
GenomeRNAii 8454.
NextBioi 31638.
PROi Q13616.
SOURCEi Search...

Gene expression databases

Bgeei Q13616.
CleanExi HS_CUL1.
ExpressionAtlasi Q13616. baseline and differential.
Genevestigatori Q13616.

Family and domain databases

Gene3Di 1.10.10.10. 2 hits.
InterProi IPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view ]
SMARTi SM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view ]
SUPFAMi SSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEi PS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family."
    Kipreos E.T., Lander L.E., Wing J.P., He W.W., Hedgecock E.M.
    Cell 85:829-839(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Human CUL-1, but not other cullin family members, selectively interacts with SKP1 to form a complex with SKP2 and cyclin A."
    Michel J.J., Xiong Y.
    Cell Growth Differ. 9:435-449(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Endometrium.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha."
    Tan P., Fuchs S.Y., Chen A., Wu K., Gomez C., Ronai Z., Pan Z.-Q.
    Mol. Cell 3:527-533(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBX1, IDENTIFICATION IN SCF COMPLEX WITH RBX1; SKP1 AND SKP2.
  8. "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity."
    Ohta T., Michel J.J., Schottelius A.J., Xiong Y.
    Mol. Cell 3:535-541(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBX1 AND RNF7.
  9. "Covalent modification of all members of human cullin family proteins by NEDD8."
    Hori T., Osaka F., Chiba T., Miyamoto C., Okabayashi K., Shimbara N., Kato S., Tanaka K.
    Oncogene 18:6829-6834(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NEDDYLATION AT LYS-720.
  10. "Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent ubiquitination of IkappaBalpha."
    Read M.A., Brownell J.E., Gladysheva T.B., Hottelet M., Parent L.A., Coggins M.B., Pierce J.W., Podust V.N., Luo R.-S., Chau V., Palombella V.J.
    Mol. Cell. Biol. 20:2326-2333(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NEDDYLATION.
  11. "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."
    Swaroop M., Wang Y., Miller P., Duan H., Jatkoe T., Madore S.J., Sun Y.
    Oncogene 19:2855-2866(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF7.
  12. Cited for: INTERACTION WITH COPS2.
  13. "CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex."
    Zheng J., Yang X., Harrell J.M., Ryzhikov S., Shim E.-H., Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H.
    Mol. Cell 10:1519-1526(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIP120A.
  14. "TIP120A associates with cullins and modulates ubiquitin ligase activity."
    Min K.-W., Hwang J.-W., Lee J.-S., Park Y., Tamura T.-A., Yoon J.-B.
    J. Biol. Chem. 278:15905-15910(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIP120A.
  15. "Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a proline-rich region."
    Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F.
    J. Biol. Chem. 279:32592-32602(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SCF(FBXO7) COMPLEX.
  16. Cited for: RECONSTITUTION OF THE SCF(FBXO32) COMPLEX, FUNCTION IN UBIQUITINATION OF MYOD1.
  17. "FBW2 targets GCMa to the ubiquitin-proteasome degradation system."
    Yang C.S., Yu C., Chuang H.C., Chang C.W., Chang G.D., Yao T.P., Chen H.
    J. Biol. Chem. 280:10083-10090(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GCM1, FUNCTION IN UBIQUITINATION OF GCM1.
  18. "FBXO25, an F-box protein homologue of atrogin-1, is not induced in atrophying muscle."
    Maragno A.L., Baqui M.M., Gomes M.D.
    Biochim. Biophys. Acta 1760:966-972(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECONSTITUTION OF THE SCF(FBXO25) COMPLEX.
  19. "Proteasomal degradation of the multifunctional regulator YB-1 is mediated by an F-Box protein induced during programmed cell death."
    Lutz M., Wempe F., Bahr I., Zopf D., von Melchner H.
    FEBS Lett. 580:3921-3930(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SCF(FBXO33) COMPLEX WITH SKP1; RBX1 AND FBXO33.
  20. "Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein."
    Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M., Krek W.
    Mol. Cell. Biol. 26:5994-6004(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE SCF(SKP2)-LIKE COMPLEX, INTERACTION WITH TRIM21.
  21. "Characterization of cullin-based E3 ubiquitin ligases in intact mammalian cells -- evidence for cullin dimerization."
    Chew E.H., Poobalasingam T., Hawkey C.J., Hagen T.
    Cell. Signal. 19:1071-1080(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-ASSOCIATION.
  22. "FBXO11 promotes the neddylation of p53 and inhibits its transcriptional activity."
    Abida W.M., Nikolaev A., Zhao W., Zhang W., Gu W.
    J. Biol. Chem. 282:1797-1804(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SCF(FBXO11) COMPLEX WITH SKP1; RBX1 AND FBXO11.
  23. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-708 AND LYS-720.
    Tissue: Mammary cancer.
  24. "Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation."
    Duda D.M., Borg L.A., Scott D.C., Hunt H.W., Hammel M., Schulman B.A.
    Cell 134:995-1006(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NEDDYLATION AT LYS-720.
  25. "Diversity in tissue expression, substrate binding, and SCF complex formation for a lectin family of ubiquitin ligases."
    Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L.
    J. Biol. Chem. 283:12717-12729(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FBXO44; FBXO17 AND FBXO27, IDENTIFICATION IN SCF-COMPLEX.
  26. "Regulation of Chk2 ubiquitination and signaling through autophosphorylation of serine 379."
    Lovly C.M., Yan L., Ryan C.E., Takada S., Piwnica-Worms H.
    Mol. Cell. Biol. 28:5874-5885(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CHEK2 UBIQUITINATION, INTERACTION WITH CHEK2.
  27. Cited for: FUNCTION, INTERACTION WITH HUMAN ADENOVIRUS EARLY E1A PROTEIN.
  28. "A deneddylase encoded by Epstein-Barr virus promotes viral DNA replication by regulating the activity of cullin-RING ligases."
    Gastaldello S., Hildebrand S., Faridani O., Callegari S., Palmkvist M., Di Guglielmo C., Masucci M.G.
    Nat. Cell Biol. 12:351-361(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS BPLF1, DENEDDYLATION BY EPSTEIN-BARR VIRUS BPLF1.
  29. "SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation."
    D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L., Washburn M.P., Dynlacht B., Pagano M.
    Nature 466:138-142(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SCF(CCNF) COMPLEX.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-cell lymphomas."
    Duan S., Cermak L., Pagan J.K., Rossi M., Martinengo C., di Celle P.F., Chapuy B., Shipp M., Chiarle R., Pagano M.
    Nature 481:90-93(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF BCL6, IDENTIFICATION IN THE SCF(FBXO11) COMPLEX.
  32. "SCF(Fbxo9) and CK2 direct the cellular response to growth factor withdrawal via Tel2/Tti1 degradation and promote survival in multiple myeloma."
    Fernandez-Saiz V., Targosz B.S., Lemeer S., Eichner R., Langer C., Bullinger L., Reiter C., Slotta-Huspenina J., Schroeder S., Knorn A.M., Kurutz J., Peschel C., Pagano M., Kuster B., Bassermann F.
    Nat. Cell Biol. 15:72-81(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SCF(FBXO9) COMPLEX, FUNCTION.
  33. Cited for: FUNCTION IN UBIQUITINATION OF BCL2, IDENTIFICATION IN THE SCF(FBXO10) COMPLEX.
  34. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 17-776 IN COMPLEX WITH 19-108 OF RBX1, X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN SCF COMPLEX WITH RBX1; SKP1 AND SKP2.
  35. "Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases."
    Goldenberg S.J., Cascio T.C., Shumway S.D., Garbutt K.C., Liu J., Xiong Y., Zheng N.
    Cell 119:517-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CAND1 AND ROC1, NEDDYLATION AT LYS-720, SUBUNIT.
  36. "N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex."
    Scott D.C., Monda J.K., Bennett E.J., Harper J.W., Schulman B.A.
    Science 334:674-678(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 702-776 IN COMPLEX WITH DCUN1D1 AND UBE2M.

Entry informationi

Entry nameiCUL1_HUMAN
AccessioniPrimary (citable) accession number: Q13616
Secondary accession number(s): D3DWG3
, O60719, Q08AL6, Q8IYW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 14, 2001
Last modified: October 29, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3