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Protein

F-box/WD repeat-containing protein 7

Gene

FBXW7

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

Functioni

Substrate recognition component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and binds phosphorylated sites/phosphodegrons within target proteins and thereafter bring them to the SCF complex for ubiquitination (PubMed:17434132). Identified substrates include cyclin-E (CCNE1 or CCNE2), JUN, MYC, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1 (PubMed:11565034, PubMed:12354302, PubMed:11585921, PubMed:15103331, PubMed:14739463, PubMed:17558397, PubMed:17873522, PubMed:22608923). Acts as a negative regulator of JNK signaling by binding to phosphorylated JUN and promoting its ubiquitination and subsequent degradation (PubMed:14739463).1 Publication8 Publications

GO - Molecular functioni

  • cyclin binding Source: ParkinsonsUK-UCL
  • identical protein binding Source: IntAct
  • protein binding, bridging Source: ParkinsonsUK-UCL
  • sequence-specific DNA binding transcription factor activity Source: Ensembl
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
  • ubiquitin-protein transferase activator activity Source: ParkinsonsUK-UCL

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to UV Source: UniProtKB
  • lipid homeostasis Source: BHF-UCL
  • lung development Source: Ensembl
  • negative regulation of DNA endoreduplication Source: BHF-UCL
  • negative regulation of hepatocyte proliferation Source: BHF-UCL
  • negative regulation of Notch signaling pathway Source: BHF-UCL
  • negative regulation of SREBP signaling pathway Source: BHF-UCL
  • negative regulation of triglyceride biosynthetic process Source: BHF-UCL
  • Notch signaling pathway Source: Reactome
  • positive regulation of epidermal growth factor-activated receptor activity Source: BHF-UCL
  • positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • positive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  • positive regulation of proteasomal protein catabolic process Source: ParkinsonsUK-UCL
  • positive regulation of protein ubiquitination Source: ParkinsonsUK-UCL
  • positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCL
  • positive regulation of ubiquitin-protein transferase activity Source: ParkinsonsUK-UCL
  • protein stabilization Source: BHF-UCL
  • protein ubiquitination Source: UniProtKB
  • regulation of cell cycle G1/S phase transition Source: ParkinsonsUK-UCL
  • regulation of lipid storage Source: BHF-UCL
  • regulation of protein localization Source: BHF-UCL
  • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  • sister chromatid cohesion Source: BHF-UCL
  • vasculature development Source: BHF-UCL
  • vasculogenesis Source: Ensembl
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_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_16907. Association of TriC/CCT with target proteins during biosynthesis.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ969H0.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box/WD repeat-containing protein 7Curated
Alternative name(s):
Archipelago homolog1 Publication
Short name:
hAgo1 Publication
F-box and WD-40 domain-containing protein 7Curated
F-box protein FBX301 Publication
SEL-101 Publication
hCdc41 Publication
Gene namesi
Name:FBXW7Imported
Synonyms:FBW7Imported, FBX30Imported, SEL10Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:16712. FBXW7.

Subcellular locationi

Isoform 1 :
Isoform 2 :
Isoform 3 :

GO - Cellular componenti

  • cytoplasm Source: ParkinsonsUK-UCL
  • endoplasmic reticulum Source: Ensembl
  • Golgi apparatus Source: Ensembl
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • Parkin-FBXW7-Cul1 ubiquitin ligase complex Source: ParkinsonsUK-UCL
  • protein complex Source: UniProtKB
  • SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi159 – 1591S → A: Does not affect interaction with PIN1. 1 Publication
Mutagenesisi205 – 2051T → A: Impaired interaction with PIN1. 1 Publication
Mutagenesisi252 – 2576ALDELI → DDDEDD: Prevents homodimerization. 1 Publication
Mutagenesisi349 – 3491S → A: Does not affect interaction with PIN1. 1 Publication
Mutagenesisi372 – 3721S → A: Does not affect interaction with PIN1. 1 Publication

Organism-specific databases

PharmGKBiPA28054.

Polymorphism and mutation databases

BioMutaiFBXW7.
DMDMi44887885.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 707707F-box/WD repeat-containing protein 7PRO_0000050994Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei205 – 2051Phosphothreonine1 Publication
Modified residuei227 – 2271Phosphoserine; by SGK11 Publication

Post-translational modificationi

Phosphorylation at Thr-205 promotes interaction with PIN1, leading to disrupt FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation (PubMed:22608923).1 Publication
Ubiquitinated: autoubiquitinates following phosphorylation at Thr-205 and subsequent interaction with PIN1. Ubiquitination leads to its degradation (PubMed:22608923).1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ969H0.
PaxDbiQ969H0.
PRIDEiQ969H0.

PTM databases

PhosphoSiteiQ969H0.

Expressioni

Tissue specificityi

Isoform 1 is widely expressed. Isoform 3 is expressed in brain.1 Publication

Gene expression databases

BgeeiQ969H0.
CleanExiHS_FBXW7.
ExpressionAtlasiQ969H0. baseline and differential.
GenevestigatoriQ969H0.

Organism-specific databases

HPAiCAB013793.
CAB029987.
HPA045958.

Interactioni

Subunit structurei

Homodimer; homodimerization plays a role in substrate binding and/or ubiquitination and degradation (PubMed:22608923, PubMed:17434132). Component of the SCF(FBXW7) complex consisting of CUL1, RBX1, SKP1 and FBXW7. Interacts with PSEN1, cyclin-E (CCNE1 or CCNE2), NOTCH1 intracellular domain/NICD, NOTCH4 intracellular domain/NICD and SKP1. Interacts with MYC (when phosphorylated). Isoform 1 interacts with USP28, leading to counteract ubiquitination of MYC. Isoform 3 interacts (via WD repeats) with SV40 large T antigen (via CPD region). Forms a trimeric complex with NOTCH1 and SGK1. Interacts with JUN (PubMed:14739463, PubMed:22608923). Interacts (when phosphorylated at Thr-205) with PIN1, leading to disrupt FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation (PubMed:22608923).11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-359574,EBI-359574
CCDC6Q162049EBI-359574,EBI-1045350
CDK2P249412EBI-6502391,EBI-375096
MYCP011064EBI-359574,EBI-447544
SKP1P632085EBI-359574,EBI-307486
STOML1Q9UBI43EBI-6502391,EBI-2681162

Protein-protein interaction databases

BioGridi120581. 97 interactions.
DIPiDIP-27613N.
IntActiQ969H0. 45 interactions.
MINTiMINT-276696.
STRINGi9606.ENSP00000281708.

Structurei

Secondary structure

1
707
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi265 – 2728Combined sources
Turni280 – 2823Combined sources
Helixi286 – 2938Combined sources
Helixi298 – 3047Combined sources
Helixi309 – 3157Combined sources
Helixi319 – 3257Combined sources
Turni326 – 3294Combined sources
Helixi350 – 36718Combined sources
Beta strandi374 – 3774Combined sources
Beta strandi384 – 3907Combined sources
Beta strandi393 – 3986Combined sources
Beta strandi403 – 4075Combined sources
Turni408 – 4103Combined sources
Beta strandi413 – 4164Combined sources
Beta strandi424 – 4307Combined sources
Beta strandi433 – 4386Combined sources
Beta strandi443 – 4475Combined sources
Turni448 – 4514Combined sources
Beta strandi452 – 4576Combined sources
Beta strandi464 – 4707Combined sources
Beta strandi473 – 4786Combined sources
Beta strandi481 – 49010Combined sources
Beta strandi493 – 4986Combined sources
Beta strandi504 – 5096Combined sources
Beta strandi514 – 5185Combined sources
Beta strandi523 – 5275Combined sources
Helixi528 – 5303Combined sources
Beta strandi532 – 5376Combined sources
Beta strandi544 – 5496Combined sources
Beta strandi551 – 5588Combined sources
Beta strandi563 – 5675Combined sources
Turni568 – 5703Combined sources
Beta strandi573 – 5775Combined sources
Beta strandi584 – 5907Combined sources
Beta strandi593 – 5986Combined sources
Beta strandi603 – 6075Combined sources
Turni608 – 6103Combined sources
Beta strandi613 – 6175Combined sources
Beta strandi627 – 6326Combined sources
Beta strandi634 – 6418Combined sources
Beta strandi644 – 6507Combined sources
Turni651 – 6533Combined sources
Beta strandi656 – 6627Combined sources
Helixi666 – 6683Combined sources
Beta strandi671 – 6777Combined sources
Beta strandi679 – 6879Combined sources
Beta strandi689 – 6935Combined sources
Beta strandi696 – 7016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OVPX-ray2.90B263-707[»]
2OVQX-ray2.60B263-707[»]
2OVRX-ray2.50B263-707[»]
ProteinModelPortaliQ969H0.
SMRiQ969H0. Positions 263-706.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ969H0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini278 – 32447F-boxPROSITE-ProRule annotationAdd
BLAST
Repeati378 – 41841WD 1Add
BLAST
Repeati420 – 45637WD 2Add
BLAST
Repeati459 – 49840WD 3Add
BLAST
Repeati500 – 53637WD 4Add
BLAST
Repeati539 – 57840WD 5Add
BLAST
Repeati580 – 61839WD 6Add
BLAST
Repeati622 – 65938WD 7Add
BLAST

Domaini

The WD repeats mediate interaction with substrates of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex.1 Publication
The F-box domain mediates interaction with SKP1.1 Publication

Sequence similaritiesi

Contains 1 F-box domain.PROSITE-ProRule annotation
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000119106.
HOVERGENiHBG051596.
InParanoidiQ969H0.
KOiK10260.
OMAiREDEHAN.
OrthoDBiEOG7VX8VF.
PhylomeDBiQ969H0.
TreeFamiTF101074.

Family and domain databases

Gene3Di2.130.10.10. 3 hits.
InterProiIPR001810. F-box_dom.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12937. F-box-like. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00256. FBOX. 1 hit.
SM00320. WD40. 8 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
PS00678. WD_REPEATS_1. 5 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q969H0-1) [UniParc]FASTAAdd to basket

Also known as: Archipelago alpha, FBW7alpha, 110K, common

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNQELLSVGS KRRRTGGSLR GNPSSSQVDE EQMNRVVEEE QQQQLRQQEE
60 70 80 90 100
EHTARNGEVV GVEPRPGGQN DSQQGQLEEN NNRFISVDED SSGNQEEQEE
110 120 130 140 150
DEEHAGEQDE EDEEEEEMDQ ESDDFDQSDD SSREDEHTHT NSVTNSSSIV
160 170 180 190 200
DLPVHQLSSP FYTKTTKMKR KLDHGSEVRS FSLGKKPCKV SEYTSTTGLV
210 220 230 240 250
PCSATPTTFG DLRAANGQGQ QRRRITSVQP PTGLQEWLKM FQSWSGPEKL
260 270 280 290 300
LALDELIDSC EPTQVKHMMQ VIEPQFQRDF ISLLPKELAL YVLSFLEPKD
310 320 330 340 350
LLQAAQTCRY WRILAEDNLL WREKCKEEGI DEPLHIKRRK VIKPGFIHSP
360 370 380 390 400
WKSAYIRQHR IDTNWRRGEL KSPKVLKGHD DHVITCLQFC GNRIVSGSDD
410 420 430 440 450
NTLKVWSAVT GKCLRTLVGH TGGVWSSQMR DNIIISGSTD RTLKVWNAET
460 470 480 490 500
GECIHTLYGH TSTVRCMHLH EKRVVSGSRD ATLRVWDIET GQCLHVLMGH
510 520 530 540 550
VAAVRCVQYD GRRVVSGAYD FMVKVWDPET ETCLHTLQGH TNRVYSLQFD
560 570 580 590 600
GIHVVSGSLD TSIRVWDVET GNCIHTLTGH QSLTSGMELK DNILVSGNAD
610 620 630 640 650
STVKIWDIKT GQCLQTLQGP NKHQSAVTCL QFNKNFVITS SDDGTVKLWD
660 670 680 690 700
LKTGEFIRNL VTLESGGSGG VVWRIRASNT KLVCAVGSRN GTEETKLLVL

DFDVDMK
Length:707
Mass (Da):79,663
Last modified:December 1, 2001 - v1
Checksum:iE4A357F76DFD8203
GO
Isoform 2 (identifier: Q969H0-2) [UniParc]FASTAAdd to basket

Also known as: Archipelago beta, FBW7beta, 69K

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: Missing.
     81-166: NNRFISVDED...LSSPFYTKTT → MCVPRSGLIL...FYGTLKMIFY

Show »
Length:627
Mass (Da):70,324
Checksum:i3D4107C053381BED
GO
Isoform 3 (identifier: Q969H0-4) [UniParc]FASTAAdd to basket

Also known as: Archipelago gamma, FBW7gamma, Hippocampal

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.
     119-167: DQESDDFDQS...SSPFYTKTTK → MSKPGKPTLN...AQGLPFCRRR

Show »
Length:589
Mass (Da):66,120
Checksum:i2AFB6E8A36E6E8DE
GO

Sequence cautioni

The sequence BAA91986.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti344 – 3441P → L in AAH37320 (PubMed:15489334).Curated
Sequence conflicti377 – 3771K → N in AAH37320 (PubMed:15489334).Curated
Sequence conflicti508 – 5081Q → R in AAH37320 (PubMed:15489334).Curated
Isoform 2 (identifier: Q969H0-2)
Sequence conflicti7 – 71G → V in AAH37320 (PubMed:15489334).Curated
Sequence conflicti50 – 501L → I in BAA91986 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti115 – 1151E → K.
Corresponds to variant rs6816935 [ dbSNP | Ensembl ].
VAR_017812
Natural varianti117 – 1171E → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_033030
Natural varianti133 – 1331R → G.
Corresponds to variant rs6842544 [ dbSNP | Ensembl ].
VAR_017813
Natural varianti144 – 1441T → R.
Corresponds to variant rs7660281 [ dbSNP | Ensembl ].
VAR_017814
Natural varianti465 – 4651R → C in a acute lymphoblastic leukemia cell line. 1 Publication
VAR_017815
Natural varianti465 – 4651R → H in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035880
Natural varianti505 – 5051R → L in an ovarian cancer cell line. 2 Publications
VAR_017816
Natural varianti582 – 5821S → L in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035881
Natural varianti668 – 6681S → G.
Corresponds to variant rs7679116 [ dbSNP | Ensembl ].
VAR_017817

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 118118Missing in isoform 3. 1 PublicationVSP_009482Add
BLAST
Alternative sequencei1 – 8080Missing in isoform 2. 2 PublicationsVSP_009483Add
BLAST
Alternative sequencei81 – 16686NNRFI…YTKTT → MCVPRSGLILSCICLYCGVL LPVLLPNLPFLTCLSMSTLE SVTYLPEKGLYCQRLPSSRT HGGTESLKGKNTENMGFYGT LKMIFY in isoform 2. 2 PublicationsVSP_009484Add
BLAST
Alternative sequencei119 – 16749DQESD…TKTTK → MSKPGKPTLNHGLVPVDLKS AKEPLPHQTVMKIFSISIIA QGLPFCRRR in isoform 3. 1 PublicationVSP_009485Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY033553 mRNA. Translation: AAK57547.1.
AF383178 mRNA. Translation: AAK60269.1.
AF411971 mRNA. Translation: AAL06290.1.
AF411972 mRNA. Translation: AAL06291.1.
AY049984 mRNA. Translation: AAL07271.1.
AY008274 mRNA. Translation: AAG16640.1.
CR749305 mRNA. Translation: CAH18160.1.
BC037320 mRNA. Translation: AAH37320.1.
BC117244 mRNA. Translation: AAI17245.1.
BC117246 mRNA. Translation: AAI17247.1.
BC143944 mRNA. Translation: AAI43945.1.
AK001933 mRNA. Translation: BAA91986.1. Different initiation.
CCDSiCCDS34078.1. [Q969H0-4]
CCDS3777.1. [Q969H0-1]
CCDS3778.1. [Q969H0-2]
RefSeqiNP_001013433.1. NM_001013415.1. [Q969H0-4]
NP_060785.2. NM_018315.4. [Q969H0-2]
NP_361014.1. NM_033632.3. [Q969H0-1]
UniGeneiHs.561245.
Hs.717081.

Genome annotation databases

EnsembliENST00000263981; ENSP00000263981; ENSG00000109670. [Q969H0-2]
ENST00000281708; ENSP00000281708; ENSG00000109670. [Q969H0-1]
ENST00000296555; ENSP00000296555; ENSG00000109670. [Q969H0-4]
ENST00000603548; ENSP00000474725; ENSG00000109670. [Q969H0-1]
ENST00000603841; ENSP00000474971; ENSG00000109670. [Q969H0-1]
GeneIDi55294.
KEGGihsa:55294.
UCSCiuc003imq.3. human. [Q969H0-2]
uc003imr.3. human. [Q969H0-4]
uc003ims.3. human. [Q969H0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY033553 mRNA. Translation: AAK57547.1.
AF383178 mRNA. Translation: AAK60269.1.
AF411971 mRNA. Translation: AAL06290.1.
AF411972 mRNA. Translation: AAL06291.1.
AY049984 mRNA. Translation: AAL07271.1.
AY008274 mRNA. Translation: AAG16640.1.
CR749305 mRNA. Translation: CAH18160.1.
BC037320 mRNA. Translation: AAH37320.1.
BC117244 mRNA. Translation: AAI17245.1.
BC117246 mRNA. Translation: AAI17247.1.
BC143944 mRNA. Translation: AAI43945.1.
AK001933 mRNA. Translation: BAA91986.1. Different initiation.
CCDSiCCDS34078.1. [Q969H0-4]
CCDS3777.1. [Q969H0-1]
CCDS3778.1. [Q969H0-2]
RefSeqiNP_001013433.1. NM_001013415.1. [Q969H0-4]
NP_060785.2. NM_018315.4. [Q969H0-2]
NP_361014.1. NM_033632.3. [Q969H0-1]
UniGeneiHs.561245.
Hs.717081.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OVPX-ray2.90B263-707[»]
2OVQX-ray2.60B263-707[»]
2OVRX-ray2.50B263-707[»]
ProteinModelPortaliQ969H0.
SMRiQ969H0. Positions 263-706.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120581. 97 interactions.
DIPiDIP-27613N.
IntActiQ969H0. 45 interactions.
MINTiMINT-276696.
STRINGi9606.ENSP00000281708.

PTM databases

PhosphoSiteiQ969H0.

Polymorphism and mutation databases

BioMutaiFBXW7.
DMDMi44887885.

Proteomic databases

MaxQBiQ969H0.
PaxDbiQ969H0.
PRIDEiQ969H0.

Protocols and materials databases

DNASUi55294.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263981; ENSP00000263981; ENSG00000109670. [Q969H0-2]
ENST00000281708; ENSP00000281708; ENSG00000109670. [Q969H0-1]
ENST00000296555; ENSP00000296555; ENSG00000109670. [Q969H0-4]
ENST00000603548; ENSP00000474725; ENSG00000109670. [Q969H0-1]
ENST00000603841; ENSP00000474971; ENSG00000109670. [Q969H0-1]
GeneIDi55294.
KEGGihsa:55294.
UCSCiuc003imq.3. human. [Q969H0-2]
uc003imr.3. human. [Q969H0-4]
uc003ims.3. human. [Q969H0-1]

Organism-specific databases

CTDi55294.
GeneCardsiGC04M153242.
HGNCiHGNC:16712. FBXW7.
HPAiCAB013793.
CAB029987.
HPA045958.
MIMi606278. gene.
neXtProtiNX_Q969H0.
PharmGKBiPA28054.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000119106.
HOVERGENiHBG051596.
InParanoidiQ969H0.
KOiK10260.
OMAiREDEHAN.
OrthoDBiEOG7VX8VF.
PhylomeDBiQ969H0.
TreeFamiTF101074.

Enzyme and pathway databases

ReactomeiREACT_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_16907. Association of TriC/CCT with target proteins during biosynthesis.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ969H0.

Miscellaneous databases

ChiTaRSiFBXW7. human.
EvolutionaryTraceiQ969H0.
GeneWikiiFBXW7.
GenomeRNAii55294.
NextBioi59488.
PROiQ969H0.
SOURCEiSearch...

Gene expression databases

BgeeiQ969H0.
CleanExiHS_FBXW7.
ExpressionAtlasiQ969H0. baseline and differential.
GenevestigatoriQ969H0.

Family and domain databases

Gene3Di2.130.10.10. 3 hits.
InterProiIPR001810. F-box_dom.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF12937. F-box-like. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00256. FBOX. 1 hit.
SM00320. WD40. 8 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
PS00678. WD_REPEATS_1. 5 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Archipelago regulates cyclin E levels in Drosophila and is mutated in human cancer cell lines."
    Moberg K.H., Bell D.W., Wahrer D.C.R., Haber D.A., Hariharan I.K.
    Nature 413:311-316(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS CYS-465 AND LEU-505.
  3. "Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line."
    Strohmaier H., Spruck C.H., Kaiser P., Won K.-A., Sangfelt O., Reed S.I.
    Nature 413:316-322(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN SCF COMPLEX, INTERACTION WITH CYCLIN E.
  4. "SEL-10 interacts with presenilin 1, facilitates its ubiquitination, and alters A-beta peptide production."
    Li J., Pauley A.M., Myers R.L., Shuang R., Brashler J.R., Yan R., Buhl A.E., Ruble C., Gurney M.E.
    J. Neurochem. 82:1540-1548(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PSEN1.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Salivary gland.
  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] (ISOFORM 1), PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  8. "SEL-10 is an inhibitor of notch signaling that targets notch for ubiquitin-mediated protein degradation."
    Wu G., Lyapina S., Das I., Li J., Gurney M., Pauley A., Chui I., Deshaies R.J., Kitajewski J.
    Mol. Cell. Biol. 21:7403-7415(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NOTCH1; NOTCH4 AND SKP1.
  9. "Phosphorylation-dependent degradation of c-Myc is mediated by the F-box protein Fbw7."
    Yada M., Hatakeyama S., Kamura T., Nishiyama M., Tsunematsu R., Imaki H., Ishida N., Okumura F., Nakayama K., Nakayama K.I.
    EMBO J. 23:2116-2125(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COMPONENT OF THE SCF(FBXW7) COMPLEX, INTERACTION WITH MYC.
  10. "The ubiquitin ligase SCFFbw7 antagonizes apoptotic JNK signaling."
    Nateri A.S., Riera-Sans L., Da Costa C., Behrens A.
    Science 303:1374-1378(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH JUN.
  11. "The SV40 large T antigen contains a decoy phosphodegron that mediates its interactions with Fbw7/hCdc4."
    Welcker M., Clurman B.E.
    J. Biol. Chem. 280:7654-7658(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SV40 LARGE T ANTIGEN.
  12. "Fbw7 and Usp28 regulate myc protein stability in response to DNA damage."
    Popov N., Herold S., Llamazares M., Schulein C., Eilers M.
    Cell Cycle 6:2327-2331(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MYC AND USP28.
  13. Cited for: FUNCTION, INTERACTION WITH MYC AND USP28, SUBCELLULAR LOCATION.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  15. "Serum- and glucocorticoid-inducible kinase 1 (SGK1) controls Notch1 signaling by downregulation of protein stability through Fbw7 ubiquitin ligase."
    Mo J.S., Ann E.J., Yoon J.H., Jung J., Choi Y.H., Kim H.Y., Ahn J.S., Kim S.M., Kim M.Y., Hong J.A., Seo M.S., Lang F., Choi E.J., Park H.S.
    J. Cell Sci. 124:100-112(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-227 BY SGK1, INTERACTION WITH SGK1 AND NOTCH1.
  16. "Negative regulation of the stability and tumor suppressor function of Fbw7 by the Pin1 prolyl isomerase."
    Min S.H., Lau A.W., Lee T.H., Inuzuka H., Wei S., Huang P., Shaik S., Lee D.Y., Finn G., Balastik M., Chen C.H., Luo M., Tron A.E., Decaprio J.A., Zhou X.Z., Wei W., Lu K.P.
    Mol. Cell 46:771-783(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMODIMERIZATION, INTERACTION WITH JUN AND PIN1, PHOSPHORYLATION AT THR-205, UBIQUITINATION, MUTAGENESIS OF SER-159; THR-205; SER-349 AND SER-372.
  17. Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-465; LEU-505 AND LEU-582.
  18. "Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas."
    Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A., Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S., Kristensen V., Perou C.M., Boerresen-Dale A.-L.
    Breast Cancer Res. 9:R5-R5(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LYS-117.
  19. "Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases."
    Hao B., Oehlmann S., Sowa M.E., Harper J.W., Pavletich N.P.
    Mol. Cell 26:131-143(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 263-707 IN COMPLEX WITH SKP1 AND CCNE1 PHOSPHORYLATED PEPTIDE, FUNCTION, DOMAIN, SUBUNIT, MUTAGENESIS OF 252-ALA--ILE-257.

Entry informationi

Entry nameiFBXW7_HUMAN
AccessioniPrimary (citable) accession number: Q969H0
Secondary accession number(s): B7ZLP9
, Q68DR0, Q96A16, Q96LE0, Q96RI2, Q9NUX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: December 1, 2001
Last modified: April 29, 2015
This is version 136 of the entry and version 1 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 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.