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Q9WTX6

- CUL1_MOUSE

UniProt

Q9WTX6 - CUL1_MOUSE

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Protein

Cullin-1

Gene

Cul1

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

Pathwayi

GO - Molecular functioni

  1. ubiquitin-protein transferase activity Source: MGI

GO - Biological processi

  1. apoptotic process Source: MGI
  2. cell proliferation Source: MGI
  3. organ morphogenesis Source: MGI
  4. protein monoubiquitination Source: MGI
  5. SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  6. ubiquitin-dependent protein catabolic process Source: MGI
  7. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_196604. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_198561. Prolactin receptor signaling.
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_224208. Interleukin-1 signaling.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cullin-1
Short name:
CUL-1
Gene namesi
Name:Cul1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1349658. Cul1.

Subcellular locationi

GO - Cellular componenti

  1. SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 776776Cullin-1PRO_0000119788Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Neddylated; which enhances the ubiquitination activity of SCF. Deneddylated via its interaction with the COP9 signalosome (CSN) complex. Deneddylated by murine cytomegalovirus M48 leading to a S-phase-like environment that is required for efficient replication of the viral genome.

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ9WTX6.
PaxDbiQ9WTX6.
PRIDEiQ9WTX6.

PTM databases

PhosphoSiteiQ9WTX6.

Expressioni

Tissue specificityi

Embryo fibroblasts and embryo preadipocytes.1 Publication

Gene expression databases

BgeeiQ9WTX6.
CleanExiMM_CUL1.
ExpressionAtlasiQ9WTX6. baseline and differential.
GenevestigatoriQ9WTX6.

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(FBXO11) complex containing FBXO11. Component of the SCF(FBXO10) complex containing FBXO10. 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 murine cytomegalovirus M48.8 Publications

Protein-protein interaction databases

BioGridi205088. 21 interactions.
DIPiDIP-39799N.
IntActiQ9WTX6. 5 interactions.
MINTiMINT-4092624.

Structurei

3D structure databases

ProteinModelPortaliQ9WTX6.
SMRiQ9WTX6. Positions 17-776.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5647.
GeneTreeiENSGT00760000119212.
HOGENOMiHOG000176713.
HOVERGENiHBG106177.
InParanoidiQ9WTX6.
KOiK03347.
OMAiNEAFNGE.
PhylomeDBiQ9WTX6.
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.

Q9WTX6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSNRSQNPH 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):89,692
Last modified:November 1, 1999 - v1
Checksum:i3E1F8B63C6E498F4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741K → R in AAD34471. 1 PublicationCurated
Sequence conflicti249 – 2491T → S in AAD34471. 1 PublicationCurated
Sequence conflicti308 – 3081Q → H in AAD34471. 1 PublicationCurated
Sequence conflicti334 – 3341G → R in AAD34471. 1 PublicationCurated
Sequence conflicti640 – 66324LQILL…DEVEL → YRFTEVEIAGLRDEMPMLMR WM in AAD34471. 1 PublicationCuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF083216 mRNA. Translation: AAD16038.1.
AF176910 mRNA. Translation: AAD52657.1.
AF136441 mRNA. Translation: AAD34471.1.
BC029260 mRNA. Translation: AAH29260.1.
CCDSiCCDS20095.1.
RefSeqiNP_036172.1. NM_012042.3.
XP_006506251.1. XM_006506188.1.
XP_006506252.1. XM_006506189.1.
XP_006506253.1. XM_006506190.1.
UniGeneiMm.87611.

Genome annotation databases

EnsembliENSMUST00000031697; ENSMUSP00000031697; ENSMUSG00000029686.
GeneIDi26965.
KEGGimmu:26965.
UCSCiuc009bsz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF083216 mRNA. Translation: AAD16038.1 .
AF176910 mRNA. Translation: AAD52657.1 .
AF136441 mRNA. Translation: AAD34471.1 .
BC029260 mRNA. Translation: AAH29260.1 .
CCDSi CCDS20095.1.
RefSeqi NP_036172.1. NM_012042.3.
XP_006506251.1. XM_006506188.1.
XP_006506252.1. XM_006506189.1.
XP_006506253.1. XM_006506190.1.
UniGenei Mm.87611.

3D structure databases

ProteinModelPortali Q9WTX6.
SMRi Q9WTX6. Positions 17-776.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 205088. 21 interactions.
DIPi DIP-39799N.
IntActi Q9WTX6. 5 interactions.
MINTi MINT-4092624.

PTM databases

PhosphoSitei Q9WTX6.

Proteomic databases

MaxQBi Q9WTX6.
PaxDbi Q9WTX6.
PRIDEi Q9WTX6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031697 ; ENSMUSP00000031697 ; ENSMUSG00000029686 .
GeneIDi 26965.
KEGGi mmu:26965.
UCSCi uc009bsz.1. mouse.

Organism-specific databases

CTDi 8454.
MGIi MGI:1349658. Cul1.

Phylogenomic databases

eggNOGi COG5647.
GeneTreei ENSGT00760000119212.
HOGENOMi HOG000176713.
HOVERGENi HBG106177.
InParanoidi Q9WTX6.
KOi K03347.
OMAi NEAFNGE.
PhylomeDBi Q9WTX6.
TreeFami TF101151.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_196604. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_198561. Prolactin receptor signaling.
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_224208. Interleukin-1 signaling.

Miscellaneous databases

ChiTaRSi CUL1. mouse.
NextBioi 304903.
PROi Q9WTX6.
SOURCEi Search...

Gene expression databases

Bgeei Q9WTX6.
CleanExi MM_CUL1.
ExpressionAtlasi Q9WTX6. baseline and differential.
Genevestigatori Q9WTX6.

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. "Ubiquitin-dependent degradation of IkappaBalpha is mediated by a ubiquitin ligase Skp1/Cul 1/F-box protein FWD1."
    Hatakeyama S., Kitagawa M., Nakayama K., Shirane M., Matsumoto M., Hattori K., Higashi H., Nakano H., Okumura K., Onoe K., Good R.A., Nakayama K.
    Proc. Natl. Acad. Sci. U.S.A. 96:3859-3863(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN A COMPLEX WITH PHOSPHORYLATED NFKBIA; SKP1 AND BTRC.
    Strain: C57BL/6J.
    Tissue: Brain.
  2. Filippov V., Filippova M., Gill S.S.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Loss of Cul1 results in early embryonic lethality and dysregulation of cyclin E."
    Dealy M.J., Nguyen K.V.T., Lo J., Gstaiger M., Krek W., Elson D., Arbeit J., Kipreos E.T., Johnson R.S.
    Nat. Genet. 23:245-248(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: NIH Swiss.
    Tissue: Embryo.
  4. "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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  5. "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: TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  6. "Characterization of a mouse gene (Fbxw6) that encodes a homologue of Caenorhabditis elegans SEL-10."
    Maruyama S., Hatakeyama S., Nakayama K., Ishida N., Kawakami K., Nakayama K.
    Genomics 78:214-222(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH BTRC AND SKP1.
  7. "The COP9 signalosome inhibits p27(kip1) degradation and impedes G1-S phase progression via deneddylation of SCF Cul1."
    Yang X., Menon S., Lykke-Andersen K., Tsuge T., Xiao D., Wang X., Rodriguez-Suarez R.J., Zhang H., Wei N.
    Curr. Biol. 12:667-672(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COPS2.
  8. Cited for: FUNCTION, SUBUNIT.
  9. "Fbxw8 is essential for Cul1-Cul7 complex formation and for placental development."
    Tsunematsu R., Nishiyama M., Kotoshiba S., Saiga T., Kamura T., Nakayama K.I.
    Mol. Cell. Biol. 26:6157-6169(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CUL7 AND FBXW8.
  10. "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 MURINE CYTOMEGALOVIRUS M48, DENEDDYLATION BY MURINE CYTOMEGALOVIRUS M48.
  11. "Competing E3 ubiquitin ligases govern circadian periodicity by degradation of CRY in nucleus and cytoplasm."
    Yoo S.H., Mohawk J.A., Siepka S.M., Shan Y., Huh S.K., Hong H.K., Kornblum I., Kumar V., Koike N., Xu M., Nussbaum J., Liu X., Chen Z., Chen Z.J., Green C.B., Takahashi J.S.
    Cell 152:1091-1105(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SCF(FBXL3) COMPLEX, FUNCTION.
  12. "FBXL21 regulates oscillation of the circadian clock through ubiquitination and stabilization of cryptochromes."
    Hirano A., Yumimoto K., Tsunematsu R., Matsumoto M., Oyama M., Kozuka-Hata H., Nakagawa T., Lanjakornsiripan D., Nakayama K.I., Fukada Y.
    Cell 152:1106-1118(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SCF(FBXL21) COMPLEX, FUNCTION.

Entry informationi

Entry nameiCUL1_MOUSE
AccessioniPrimary (citable) accession number: Q9WTX6
Secondary accession number(s): Q9WUI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3