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Protein

Cullin-1

Gene

CUL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. SCF complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins (PubMed:27565346). 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 (PubMed:25704143, PubMed:25503564). 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 BCL2.11 Publications

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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

BioCyciZFISH:ENSG00000055130-MONOMER.
ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1170546. Prolactin receptor signaling.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2644607. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-400253. Circadian Clock.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5684264. MAP3K8 (TPL2)-dependent MAPK1/3 activation.
R-HSA-69231. Cyclin D associated events in G1.
R-HSA-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ13616.
SIGNORiQ13616.
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
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:2551. CUL1.

Subcellular locationi

GO - Cellular componenti

  • cullin-RING ubiquitin ligase complex Source: MGI
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • Parkin-FBXW7-Cul1 ubiquitin ligase complex Source: ParkinsonsUK-UCL
  • SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi8454.
OpenTargetsiENSG00000055130.
PharmGKBiPA27047.

Polymorphism and mutation databases

BioMutaiCUL1.
DMDMi19863257.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001197871 – 776Cullin-1Add BLAST776

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei63Omega-N-methylarginineCombined sources1
Cross-linki720Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)3 Publications

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 (PubMed:10597293, PubMed:10713156, PubMed:15537541, PubMed:18805092).7 Publications
(Microbial infection) Deneddylated by Epstein-Barr virus BPLF1 leading to a S-phase-like environment that is required for efficient replication of the viral genome (PubMed:20190741).1 Publication

Keywords - PTMi

Isopeptide bond, Methylation, Ubl conjugation

Proteomic databases

EPDiQ13616.
MaxQBiQ13616.
PaxDbiQ13616.
PeptideAtlasiQ13616.
PRIDEiQ13616.

PTM databases

iPTMnetiQ13616.
PhosphoSitePlusiQ13616.

Expressioni

Tissue specificityi

Expressed in lung fibroblasts.1 Publication

Gene expression databases

BgeeiENSG00000055130.
CleanExiHS_CUL1.
ExpressionAtlasiQ13616. baseline and differential.
GenevisibleiQ13616. HS.

Organism-specific databases

HPAiCAB002676.
HPA050796.
HPA064584.

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 DCUN1D3. 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 (PubMed:25503564). Interacts (when neddylated) with ARIH1; leading to activate the E3 ligase activity of ARIH1 (PubMed:24076655, PubMed:27565346). Interacts with COPS9 isoform 2 (PubMed:23776465).26 Publications
(Microbial infection) 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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ARIH1Q9Y4X56EBI-359390,EBI-2514233
BTRCQ9Y2975EBI-359390,EBI-307461
CAND1Q86VP619EBI-359390,EBI-456077
CCDC22O608263EBI-359390,EBI-3943153
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
FBXW11Q9UKB13EBI-359390,EBI-355189
m005RQ837305EBI-359390,EBI-6859930From a different organism.
MDM2Q009873EBI-359390,EBI-389668
NEDD8Q158438EBI-359390,EBI-716247
RBX1P6287718EBI-359390,EBI-398523
SKP1P6320811EBI-359390,EBI-307486
SKP2Q133099EBI-359390,EBI-456291
UBE2MP610815EBI-359390,EBI-1041660

GO - Molecular functioni

Protein-protein interaction databases

BioGridi114032. 717 interactors.
DIPiDIP-17013N.
IntActiQ13616. 85 interactors.
MINTiMINT-120495.
STRINGi9606.ENSP00000326804.

Structurei

Secondary structure

1776
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi18 – 31Combined sources14
Turni32 – 34Combined sources3
Helixi39 – 52Combined sources14
Helixi87 – 105Combined sources19
Turni106 – 109Combined sources4
Turni111 – 114Combined sources4
Helixi115 – 136Combined sources22
Helixi138 – 143Combined sources6
Beta strandi144 – 146Combined sources3
Helixi159 – 165Combined sources7
Helixi168 – 171Combined sources4
Turni172 – 177Combined sources6
Helixi178 – 187Combined sources10
Turni188 – 190Combined sources3
Helixi199 – 210Combined sources12
Turni211 – 213Combined sources3
Beta strandi215 – 219Combined sources5
Helixi226 – 231Combined sources6
Helixi233 – 254Combined sources22
Helixi261 – 273Combined sources13
Turni274 – 279Combined sources6
Beta strandi281 – 284Combined sources4
Helixi285 – 295Combined sources11
Beta strandi296 – 300Combined sources5
Helixi301 – 312Combined sources12
Helixi318 – 328Combined sources11
Helixi333 – 355Combined sources23
Helixi359 – 361Combined sources3
Helixi363 – 382Combined sources20
Turni383 – 387Combined sources5
Helixi389 – 404Combined sources16
Helixi407 – 412Combined sources6
Helixi417 – 430Combined sources14
Helixi439 – 453Combined sources15
Helixi459 – 475Combined sources17
Helixi482 – 525Combined sources44
Turni526 – 528Combined sources3
Beta strandi532 – 541Combined sources10
Turni542 – 544Combined sources3
Helixi557 – 559Combined sources3
Helixi560 – 569Combined sources10
Turni570 – 573Combined sources4
Beta strandi579 – 581Combined sources3
Helixi583 – 585Combined sources3
Beta strandi589 – 597Combined sources9
Beta strandi600 – 602Combined sources3
Helixi605 – 612Combined sources8
Helixi613 – 615Combined sources3
Beta strandi616 – 621Combined sources6
Helixi622 – 628Combined sources7
Helixi633 – 645Combined sources13
Turni646 – 648Combined sources3
Beta strandi652 – 654Combined sources3
Turni658 – 660Combined sources3
Beta strandi668 – 671Combined sources4
Beta strandi678 – 682Combined sources5
Helixi691 – 700Combined sources10
Helixi703 – 722Combined sources20
Beta strandi723 – 726Combined sources4
Helixi727 – 738Combined sources12
Turni739 – 741Combined sources3
Helixi746 – 758Combined sources13
Beta strandi761 – 765Combined sources5
Beta strandi768 – 774Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13616.

Family & Domainsi

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2166. Eukaryota.
COG5647. LUCA.
GeneTreeiENSGT00760000119212.
HOGENOMiHOG000176713.
HOVERGENiHBG106177.
InParanoidiQ13616.
KOiK03347.
OMAiHIANQGL.
OrthoDBiEOG091G02WR.
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]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF74788. 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)DescriptionActionsGraphical viewLength
Sequence conflicti59 – 82Missing in AAC50544 (PubMed:8681378).CuratedAdd BLAST24
Sequence conflicti726K → R in CAD97651 (PubMed:17974005).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005250060.4.
XP_011514931.1. XM_011516629.2.
XP_011514932.1. XM_011516630.2.
XP_011514933.1. XM_011516631.2.
XP_011514934.1. XM_011516632.2.
UniGeneiHs.146806.

Genome annotation databases

EnsembliENST00000325222; ENSP00000326804; ENSG00000055130.
ENST00000409469; ENSP00000387160; ENSG00000055130.
ENST00000602748; ENSP00000473318; ENSG00000055130.
GeneIDi8454.
KEGGihsa:8454.
UCSCiuc003wey.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005250060.4.
XP_011514931.1. XM_011516629.2.
XP_011514932.1. XM_011516630.2.
XP_011514933.1. XM_011516631.2.
XP_011514934.1. XM_011516632.2.
UniGeneiHs.146806.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114032. 717 interactors.
DIPiDIP-17013N.
IntActiQ13616. 85 interactors.
MINTiMINT-120495.
STRINGi9606.ENSP00000326804.

PTM databases

iPTMnetiQ13616.
PhosphoSitePlusiQ13616.

Polymorphism and mutation databases

BioMutaiCUL1.
DMDMi19863257.

Proteomic databases

EPDiQ13616.
MaxQBiQ13616.
PaxDbiQ13616.
PeptideAtlasiQ13616.
PRIDEiQ13616.

Protocols and materials databases

DNASUi8454.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000325222; ENSP00000326804; ENSG00000055130.
ENST00000409469; ENSP00000387160; ENSG00000055130.
ENST00000602748; ENSP00000473318; ENSG00000055130.
GeneIDi8454.
KEGGihsa:8454.
UCSCiuc003wey.4. human.

Organism-specific databases

CTDi8454.
DisGeNETi8454.
GeneCardsiCUL1.
HGNCiHGNC:2551. CUL1.
HPAiCAB002676.
HPA050796.
HPA064584.
MIMi603134. gene.
neXtProtiNX_Q13616.
OpenTargetsiENSG00000055130.
PharmGKBiPA27047.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2166. Eukaryota.
COG5647. LUCA.
GeneTreeiENSGT00760000119212.
HOGENOMiHOG000176713.
HOVERGENiHBG106177.
InParanoidiQ13616.
KOiK03347.
OMAiHIANQGL.
OrthoDBiEOG091G02WR.
PhylomeDBiQ13616.
TreeFamiTF101151.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000055130-MONOMER.
ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1170546. Prolactin receptor signaling.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2644607. Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-400253. Circadian Clock.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5684264. MAP3K8 (TPL2)-dependent MAPK1/3 activation.
R-HSA-69231. Cyclin D associated events in G1.
R-HSA-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ13616.
SIGNORiQ13616.

Miscellaneous databases

ChiTaRSiCUL1. human.
EvolutionaryTraceiQ13616.
GeneWikiiCUL1.
GenomeRNAii8454.
PROiQ13616.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000055130.
CleanExiHS_CUL1.
ExpressionAtlasiQ13616. baseline and differential.
GenevisibleiQ13616. HS.

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]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEiPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 167 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.