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Q9WTX6 (CUL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cullin-1

Short name=CUL-1
Gene names
Name:Cul1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length776 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.9 Ref.12 Ref.13

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.1 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Tissue specificity

Embryo fibroblasts and embryo preadipocytes. Ref.6

Post-translational modification

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.

Sequence similarities

Belongs to the cullin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 776776Cullin-1
PRO_0000119788

Amino acid modifications

Cross-link708Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link720Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) By similarity

Experimental info

Sequence conflict741K → R in AAD34471. Ref.3
Sequence conflict2491T → S in AAD34471. Ref.3
Sequence conflict3081Q → H in AAD34471. Ref.3
Sequence conflict3341G → R in AAD34471. Ref.3
Sequence conflict640 – 66324LQILL…DEVEL → YRFTEVEIAGLRDEMPMLMR WM in AAD34471. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9WTX6 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 3E1F8B63C6E498F4

FASTA77689,692
        10         20         30         40         50         60 
MSSNRSQNPH GLKQIGLDQI WDDLRAGIQQ VYTRQSMAKS RYMELYTHVY NYCTSVHQSN 

        70         80         90        100        110        120 
QARGAGVPPS KSKKGQTPGG AQFVGLELYK RLKEFLKNYL TNLLKDGEDL MDESVLKFYT 

       130        140        150        160        170        180 
QQWEDYRFSS KVLNGICAYL NRHWVRRECD EGRKGIYEIY SLALVTWRDC LFRPLNKQVT 

       190        200        210        220        230        240 
NAVLKLIEKE RNGETINTRL ISGVVQSYVE LGLNEDDAFA KGPTLTVYKE SFESQFLADT 

       250        260        270        280        290        300 
ERFYTRESTE FLQQNPVTEY MKKAEARLLE EQRRVQVYLH ESTQDELARK CEQVLIEKHL 

       310        320        330        340        350        360 
EIFHTEFQNL LDADKNEDLG RMYNLVSRIQ DGLGELKKLL ETHIHNQGLA AIEKCGEAAL 

       370        380        390        400        410        420 
NDPKMYVQTV LDVHKKYNAL VMSAFNNDAG FVAALDKACG RFINNNAVTK MAQSSSKSPE 

       430        440        450        460        470        480 
LLARYCDSLL KKSSKNPEEA ELEDTLNQVM VVFKYIEDKD VFQKFYAKML AKRLVHQNSA 

       490        500        510        520        530        540 
SDDAEASMIS KLKQACGFEY TSKLQRMFQD IGVSKDLNEQ FKKHLTNSEP LDLDFSIQVL 

       550        560        570        580        590        600 
SSGSWPFQQS CTFALPSELE RSYQRFTAFY ASRHSGRKLT WLYQLSKGEL VTNCFKNRYT 

       610        620        630        640        650        660 
LQASTFQMAI LLQYNTEDAY TVQQLTDSTQ IKMDILAQVL QILLKSKLLV LEDENANVDE 

       670        680        690        700        710        720 
VELKPDTLIK LYLGYKNKKL RVNINVPMKT EQKQEQETTH KNIEEDRKLL IQAAIVRIMK 

       730        740        750        760        770 
MRKVLKHQQL LGEVLTQLSS RFKPRVPVIK KCIDILIEKE YLERVDGEKD TYSYLA 

« Hide

References

« Hide 'large scale' references
[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]Erratum
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. 96:6571-6571(1999)
[3]Filippov V., Filippova M., Gill S.S.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"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.
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"E3 ubiquitin ligase that recognizes sugar chains."
Yoshida Y., Chiba T., Tokunaga F., Kawasaki H., Iwai K., Suzuki T., Ito Y., Matsuoka K., Yoshida M., Tanaka K., Tai T.
Nature 418:438-442(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF083216 mRNA. Translation: AAD16038.1.
AF176910 mRNA. Translation: AAD52657.1.
AF136441 mRNA. Translation: AAD34471.1.
BC029260 mRNA. Translation: AAH29260.1.
CCDSCCDS20095.1.
RefSeqNP_036172.1. NM_012042.3.
XP_006506251.1. XM_006506188.1.
XP_006506252.1. XM_006506189.1.
XP_006506253.1. XM_006506190.1.
UniGeneMm.87611.

3D structure databases

ProteinModelPortalQ9WTX6.
SMRQ9WTX6. Positions 17-776.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid205088. 21 interactions.
DIPDIP-39799N.
IntActQ9WTX6. 5 interactions.
MINTMINT-4092624.

PTM databases

PhosphoSiteQ9WTX6.

Proteomic databases

MaxQBQ9WTX6.
PaxDbQ9WTX6.
PRIDEQ9WTX6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031697; ENSMUSP00000031697; ENSMUSG00000029686.
GeneID26965.
KEGGmmu:26965.
UCSCuc009bsz.1. mouse.

Organism-specific databases

CTD8454.
MGIMGI:1349658. Cul1.

Phylogenomic databases

eggNOGCOG5647.
GeneTreeENSGT00730000110820.
HOGENOMHOG000176713.
HOVERGENHBG106177.
InParanoidQ9WTX6.
KOK03347.
OMANEAFNGE.
PhylomeDBQ9WTX6.
TreeFamTF101151.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9WTX6.
BgeeQ9WTX6.
CleanExMM_CUL1.
GenevestigatorQ9WTX6.

Family and domain databases

Gene3D1.10.10.10. 2 hits.
InterProIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTSM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMSSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCUL1. mouse.
NextBio304903.
PROQ9WTX6.
SOURCESearch...

Entry information

Entry nameCUL1_MOUSE
AccessionPrimary (citable) accession number: Q9WTX6
Secondary accession number(s): Q9WUI7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot