Cul1

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. SCF complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins. 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(BTRC) and/or SCF(FBXW11) direct ubiquitination of CEP68. 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) directs ubiquitination of TTI1 and TELO2. SCF(FBXO10) directs ubiquitination of BCL2.By similarity

Pathwayⁱ: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functionⁱ

ubiquitin protein ligase binding Source: GO_Central
ubiquitin-protein transferase activity Source: MGI

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

animal organ morphogenesis
Source: MGI
Inferred from mutant phenotypeⁱ
- 10508527
apoptotic process
Source: MGI
Inferred from mutant phenotypeⁱ
- 10508527
cell proliferation
Source: MGI
Inferred from mutant phenotypeⁱ
- 10508527
protein monoubiquitination
Source: MGI
Inferred from genetic interactionⁱ
- 21343341
protein ubiquitination Source: MGI
SCF-dependent proteasomal ubiquitin-dependent protein catabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 12140560
ubiquitin-dependent protein catabolic process
Source: MGI
Inferred by curatorⁱ
- 12665572
viral process Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Host-virus interaction, Ubl conjugation pathway

Biological process

Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

Reactomeⁱ	R-MMU-1169091 Activation of NF-kappaB in B cells R-MMU-1170546 Prolactin receptor signaling R-MMU-174113 SCF-beta-TrCP mediated degradation of Emi1 R-MMU-187577 SCF(Skp2)-mediated degradation of p27/p21 R-MMU-195253 Degradation of beta-catenin by the destruction complex R-MMU-202424 Downstream TCR signaling R-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition R-MMU-2871837 FCERI mediated NF-kB activation R-MMU-5607761 Dectin-1 mediated noncanonical NF-kB signaling R-MMU-5607764 CLEC7A (Dectin-1) signaling R-MMU-5610780 Degradation of GLI1 by the proteasome R-MMU-5610785 GLI3 is processed to GLI3R by the proteasome R-MMU-5676590 NIK-->noncanonical NF-kB signaling R-MMU-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation R-MMU-68949 Orc1 removal from chromatin R-MMU-69231 Cyclin D associated events in G1 R-MMU-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis R-MMU-8939902 Regulation of RUNX2 expression and activity R-MMU-8951664 Neddylation R-MMU-9020702 Interleukin-1 signaling R-MMU-917937 Iron uptake and transport R-MMU-983168 Antigen processing: Ubiquitination & Proteasome degradation
UniPathwayⁱ	UPA00143

Reactomeⁱ

R-MMU-1169091 Activation of NF-kappaB in B cells
R-MMU-1170546 Prolactin receptor signaling
R-MMU-174113 SCF-beta-TrCP mediated degradation of Emi1
R-MMU-187577 SCF(Skp2)-mediated degradation of p27/p21
R-MMU-195253 Degradation of beta-catenin by the destruction complex
R-MMU-202424 Downstream TCR signaling
R-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition
R-MMU-2871837 FCERI mediated NF-kB activation
R-MMU-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-MMU-5607764 CLEC7A (Dectin-1) signaling
R-MMU-5610780 Degradation of GLI1 by the proteasome
R-MMU-5610785 GLI3 is processed to GLI3R by the proteasome
R-MMU-5676590 NIK-->noncanonical NF-kB signaling
R-MMU-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-MMU-68949 Orc1 removal from chromatin
R-MMU-69231 Cyclin D associated events in G1
R-MMU-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-MMU-8939902 Regulation of RUNX2 expression and activity
R-MMU-8951664 Neddylation
R-MMU-9020702 Interleukin-1 signaling
R-MMU-917937 Iron uptake and transport
R-MMU-983168 Antigen processing: Ubiquitination & Proteasome degradation

UniPathwayⁱ

UPA00143

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Cullin-1 Short name: CUL-1
Gene namesⁱ	Name:Cul1
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 6

Organism-specific databases

MGIⁱ	MGI:1349658 Cul1

Subcellular locationⁱ

GO - Cellular component

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000119788	1 – 776	Cullin-1Add BLAST		776

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	63	Omega-N-methylarginineCombined sources		1
Cross-linkⁱ	720	Glycyl 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.1 Publication

(Microbial infection) Deneddylated by murine cytomegalovirus M48 leading to a S-phase-like environment that is required for efficient replication of the viral genome.1 Publication

Keywords - PTMⁱ

Isopeptide bond, Methylation, Ubl conjugation

Proteomic databases

EPDⁱ	Q9WTX6
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9WTX6
PaxDbⁱ	Q9WTX6
PeptideAtlas More...PeptideAtlasⁱ	Q9WTX6
PRIDEⁱ	Q9WTX6

PTM databases

iPTMnetⁱ	Q9WTX6
PhosphoSitePlusⁱ	Q9WTX6

Expressionⁱ

Tissue specificityⁱ

Embryo fibroblasts and embryo preadipocytes.1 Publication

Gene expression databases

Bgeeⁱ	ENSMUSG00000029686
CleanExⁱ	MM_CUL1
ExpressionAtlasⁱ	Q9WTX6 baseline and differential
Genevisibleⁱ	Q9WTX6 MM

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 DCUN1D3 (By similarity). Interacts with COPS2. Interacts with CEP68 as part of the SCF(FBXW11) complex; the interaction is probably mediated by FBXW11 and the complex also contains CDK5RAP2 and PCNT (By similarity). Interacts (when neddylated) with ARIH1; leading to activate the E3 ligase activity of ARIH1 (By similarity). Interacts with COPS9 (By similarity). Interacts with KAT7, probably as part of an SCF complex; the interaction mediates KAT7 ubiquitination (PubMed:23319590). Interacts with NOTCH2 (By similarity).By similarity8 Publications

(Microbial infection) Interacts with murine cytomegalovirus M48.1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
UBXN7	O94888	3	EBI-1551052,EBI-1993627	From Homo sapiens.
VCP	P55072	2	EBI-1551052,EBI-355164	From Homo sapiens.

Show more details

GO - Molecular functionⁱ

ubiquitin protein ligase binding Source: GO_Central

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	205088, 60 interactors
CORUMⁱ	Q9WTX6
Database of interacting proteins More...DIPⁱ	DIP-39799N
IntActⁱ	Q9WTX6, 41 interactors
Molecular INTeraction database More...MINTⁱ	Q9WTX6
STRINGⁱ	10090.ENSMUSP00000031697

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q9WTX6
SMRⁱ	Q9WTX6
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGⁱ	KOG2166 Eukaryota COG5647 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000119212
HOGENOMⁱ	HOG000176713
HOVERGENⁱ	HBG106177
InParanoidⁱ	Q9WTX6
KEGG Orthology (KO) More...KOⁱ	K03347
OMAⁱ	TTHKHIE
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G02WR
PhylomeDBⁱ	Q9WTX6
TreeFamⁱ	TF101151

Family and domain databases

Gene3Dⁱ	1.10.10.10, 2 hits
InterProⁱ	View protein in InterPro IPR016157 Cullin_CS IPR016158 Cullin_homology IPR036317 Cullin_homology_sf IPR001373 Cullin_N IPR019559 Cullin_neddylation_domain IPR016159 Cullin_repeat-like_dom_sf IPR036388 WH-like_DNA-bd_sf IPR036390 WH_DNA-bd_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00888 Cullin, 1 hit PF10557 Cullin_Nedd8, 1 hit
SMARTⁱ	View protein in SMART SM00182 CULLIN, 1 hit SM00884 Cullin_Nedd8, 1 hit
SUPFAMⁱ	SSF46785 SSF46785, 1 hit SSF74788 SSF74788, 1 hit SSF75632 SSF75632, 1 hit
PROSITEⁱ	View protein in PROSITE PS01256 CULLIN_1, 1 hit PS50069 CULLIN_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q9WTX6-1 [UniParc]FASTA Add 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 key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	74	K → R in AAD34471 (Ref. 2) Curated	1
Sequence conflictⁱ	249	T → S in AAD34471 (Ref. 2) Curated	1
Sequence conflictⁱ	308	Q → H in AAD34471 (Ref. 2) Curated	1
Sequence conflictⁱ	334	G → R in AAD34471 (Ref. 2) Curated	1
Sequence conflictⁱ	640 – 663	LQILL…DEVEL → YRFTEVEIAGLRDEMPMLMR WM in AAD34471 (Ref. 2) CuratedAdd BLAST	24

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF083216 mRNA Translation: AAD16038.1 AF176910 mRNA Translation: AAD52657.1 AF136441 mRNA Translation: AAD34471.1 BC029260 mRNA Translation: AAH29260.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS20095.1
NCBI Reference Sequences More...RefSeqⁱ	NP_036172.1, NM_012042.3 XP_006506251.1, XM_006506188.3 XP_006506252.1, XM_006506189.3 XP_006506253.1, XM_006506190.3
UniGeneⁱ	Mm.87611

Genome annotation databases

Ensemblⁱ	ENSMUST00000031697; ENSMUSP00000031697; ENSMUSG00000029686
GeneIDⁱ	26965
KEGGⁱ	mmu:26965
UCSC genome browser More...UCSCⁱ	uc009bsz.1 mouse

Protein	Similar proteins		Species	Score	Length
Q9WTX6	cullin-1		MESAU		776
Cul1 protein		RAT		776
cullin-1		ALLSI		776
Cullin 1		TAEGU		776
Cullin 1		CHICK		776
+4

Protein	Similar proteins		Species	Score	Length
Q9WTX6	Cullin-1	)	HUMAN		776
Cullin-1		PONAB		776
CUL1 isoform 1		PANTR		776
Cullin-1		CALJA		776
Cullin-1		MACMU		776
+237

Protein	Similar proteins		Species	Score	Length
Q9WTX6	Cullin-1	)	HUMAN		776
Cullin-1		PONAB		776
CUL1 isoform 1		PANTR		776
Cullin-1		CALJA		776
Cullin-1		MACMU		776
+615

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF083216 mRNA Translation: AAD16038.1 AF176910 mRNA Translation: AAD52657.1 AF136441 mRNA Translation: AAD34471.1 BC029260 mRNA Translation: AAH29260.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS20095.1
NCBI Reference Sequences More...RefSeqⁱ	NP_036172.1, NM_012042.3 XP_006506251.1, XM_006506188.3 XP_006506252.1, XM_006506189.3 XP_006506253.1, XM_006506190.3
UniGeneⁱ	Mm.87611

3D structure databases

ProteinModelPortalⁱ	Q9WTX6
SMRⁱ	Q9WTX6
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	205088, 60 interactors
CORUMⁱ	Q9WTX6
Database of interacting proteins More...DIPⁱ	DIP-39799N
IntActⁱ	Q9WTX6, 41 interactors
Molecular INTeraction database More...MINTⁱ	Q9WTX6
STRINGⁱ	10090.ENSMUSP00000031697

PTM databases

iPTMnetⁱ	Q9WTX6
PhosphoSitePlusⁱ	Q9WTX6

Proteomic databases

EPDⁱ	Q9WTX6
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9WTX6
PaxDbⁱ	Q9WTX6
PeptideAtlas More...PeptideAtlasⁱ	Q9WTX6
PRIDEⁱ	Q9WTX6

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000031697; ENSMUSP00000031697; ENSMUSG00000029686
GeneIDⁱ	26965
KEGGⁱ	mmu:26965
UCSC genome browser More...UCSCⁱ	uc009bsz.1 mouse

Organism-specific databases

CTDⁱ	8454
MGIⁱ	MGI:1349658 Cul1

Phylogenomic databases

eggNOGⁱ	KOG2166 Eukaryota COG5647 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000119212
HOGENOMⁱ	HOG000176713
HOVERGENⁱ	HBG106177
InParanoidⁱ	Q9WTX6
KEGG Orthology (KO) More...KOⁱ	K03347
OMAⁱ	TTHKHIE
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G02WR
PhylomeDBⁱ	Q9WTX6
TreeFamⁱ	TF101151

Enzyme and pathway databases

UniPathwayⁱ	UPA00143
Reactomeⁱ	R-MMU-1169091 Activation of NF-kappaB in B cells R-MMU-1170546 Prolactin receptor signaling R-MMU-174113 SCF-beta-TrCP mediated degradation of Emi1 R-MMU-187577 SCF(Skp2)-mediated degradation of p27/p21 R-MMU-195253 Degradation of beta-catenin by the destruction complex R-MMU-202424 Downstream TCR signaling R-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition R-MMU-2871837 FCERI mediated NF-kB activation R-MMU-5607761 Dectin-1 mediated noncanonical NF-kB signaling R-MMU-5607764 CLEC7A (Dectin-1) signaling R-MMU-5610780 Degradation of GLI1 by the proteasome R-MMU-5610785 GLI3 is processed to GLI3R by the proteasome R-MMU-5676590 NIK-->noncanonical NF-kB signaling R-MMU-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation R-MMU-68949 Orc1 removal from chromatin R-MMU-69231 Cyclin D associated events in G1 R-MMU-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis R-MMU-8939902 Regulation of RUNX2 expression and activity R-MMU-8951664 Neddylation R-MMU-9020702 Interleukin-1 signaling R-MMU-917937 Iron uptake and transport R-MMU-983168 Antigen processing: Ubiquitination & Proteasome degradation

UniPathwayⁱ

UPA00143

Reactomeⁱ

R-MMU-1169091 Activation of NF-kappaB in B cells
R-MMU-1170546 Prolactin receptor signaling
R-MMU-174113 SCF-beta-TrCP mediated degradation of Emi1
R-MMU-187577 SCF(Skp2)-mediated degradation of p27/p21
R-MMU-195253 Degradation of beta-catenin by the destruction complex
R-MMU-202424 Downstream TCR signaling
R-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition
R-MMU-2871837 FCERI mediated NF-kB activation
R-MMU-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-MMU-5607764 CLEC7A (Dectin-1) signaling
R-MMU-5610780 Degradation of GLI1 by the proteasome
R-MMU-5610785 GLI3 is processed to GLI3R by the proteasome
R-MMU-5676590 NIK-->noncanonical NF-kB signaling
R-MMU-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-MMU-68949 Orc1 removal from chromatin
R-MMU-69231 Cyclin D associated events in G1
R-MMU-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-MMU-8939902 Regulation of RUNX2 expression and activity
R-MMU-8951664 Neddylation
R-MMU-9020702 Interleukin-1 signaling
R-MMU-917937 Iron uptake and transport
R-MMU-983168 Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

ChiTaRSⁱ	Cul1 mouse
Protein Ontology More...PROⁱ	PR:Q9WTX6
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000029686
CleanExⁱ	MM_CUL1
ExpressionAtlasⁱ	Q9WTX6 baseline and differential
Genevisibleⁱ	Q9WTX6 MM

Family and domain databases

Gene3Dⁱ	1.10.10.10, 2 hits
InterProⁱ	View protein in InterPro IPR016157 Cullin_CS IPR016158 Cullin_homology IPR036317 Cullin_homology_sf IPR001373 Cullin_N IPR019559 Cullin_neddylation_domain IPR016159 Cullin_repeat-like_dom_sf IPR036388 WH-like_DNA-bd_sf IPR036390 WH_DNA-bd_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00888 Cullin, 1 hit PF10557 Cullin_Nedd8, 1 hit
SMARTⁱ	View protein in SMART SM00182 CULLIN, 1 hit SM00884 Cullin_Nedd8, 1 hit
SUPFAMⁱ	SSF46785 SSF46785, 1 hit SSF74788 SSF74788, 1 hit SSF75632 SSF75632, 1 hit
PROSITEⁱ	View protein in PROSITE PS01256 CULLIN_1, 1 hit PS50069 CULLIN_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CUL1_MOUSE
Accessionⁱ	Q9WTX6Primary (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:	May 23, 2018
	This is version 148 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9WTX6 (CUL1_MOUSE)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Cullin-1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

Pathwayⁱ: protein ubiquitination

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ