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Q9Y3I1

- FBX7_HUMAN

UniProt

Q9Y3I1 - FBX7_HUMAN

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Protein

F-box only protein 7

Gene

FBXO7

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

Functioni

Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes BIRC2 and DLGAP5. Plays a role downstream of PINK1 in the clearance of damaged mitochondria via selective autophagy (mitophagy) by targeting PARK2 to dysfunctional depolarized mitochondria. Promotes MFN1 ubiquitination.3 Publications

Pathwayi

GO - Molecular functioni

  1. ubiquitin-protein transferase activity Source: ProtInc

GO - Biological processi

  1. cell death Source: UniProtKB-KW
  2. mitochondrion degradation Source: UniProtKB
  3. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: Ensembl
  4. negative regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  5. negative regulation of lymphocyte differentiation Source: Ensembl
  6. protein targeting to mitochondrion Source: UniProtKB
  7. protein ubiquitination Source: UniProtKB
  8. regulation of protein stability Source: UniProtKB
  9. ubiquitin-dependent protein catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box only protein 7
Gene namesi
Name:FBXO7
Synonyms:FBX7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:13586. FBXO7.

Subcellular locationi

Cytoplasm. Nucleus. Mitochondrion. Cytoplasmcytosol
Note: Predominantly cytoplasmic. A minor proportion is detected in the nucleus. Relocates from the cytosol to depolarized mitochondria.

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. mitochondrion Source: UniProtKB
  3. nucleus Source: UniProtKB
  4. protein complex Source: LIFEdb
  5. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Parkinson disease 15 (PARK15) [MIM:260300]: A neurodegenerative disorder characterized by parkinsonian and pyramidal signs. Clinical manifestations include tremor, bradykinesia, rigidity, postural instability, spasticity, mainly in the lower limbs, and hyperreflexia.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti378 – 3781R → G in PARK15; no effect on interaction with PARK2. 1 Publication
Corresponds to variant rs71799110 [ dbSNP | Ensembl ].
VAR_047938

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221T → M: Impairs interaction with PARK2. 1 Publication
Mutagenesisi253 – 2531V → E: Abolishes interaction with PSMF1. 1 Publication

Keywords - Diseasei

Disease mutation, Neurodegeneration, Parkinsonism

Organism-specific databases

MIMi260300. phenotype.
Orphaneti171695. Parkinsonian-pyramidal syndrome.
PharmGKBiPA28047.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522F-box only protein 7PRO_0000119885Add
BLAST

Proteomic databases

MaxQBiQ9Y3I1.
PaxDbiQ9Y3I1.
PRIDEiQ9Y3I1.

PTM databases

PhosphoSiteiQ9Y3I1.

Expressioni

Gene expression databases

BgeeiQ9Y3I1.
CleanExiHS_FBXO7.
ExpressionAtlasiQ9Y3I1. baseline and differential.
GenevestigatoriQ9Y3I1.

Organism-specific databases

HPAiCAB034296.
HPA032114.

Interactioni

Subunit structurei

Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXO7) formed of CUL1, SKP1, RBX1 and FBXO7. Interacts via its C-terminal proline-rich region with DLGAP5. Interacts with BIRC2. Interacts with CDK6 and promotes its interaction with D-type cyclin. Isoform 1 interacts (via the N-terminal Ubl domain) with PARK2. Isoforms that lack the ubiquitin-like domain do not interact with PARK2. Isoform 1 and isoform 2 interact (via N-terminal region) with PINK1. Isoform 3 does not interact with PINK1. Interacts with PSMF1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PARK2O6026010EBI-1161222,EBI-716346
PINK1Q9BXM78EBI-1161222,EBI-2846068
SKP1P632082EBI-1161222,EBI-307486

Protein-protein interaction databases

BioGridi117326. 29 interactions.
DIPiDIP-36125N.
IntActiQ9Y3I1. 8 interactions.
MINTiMINT-108554.
STRINGi9606.ENSP00000266087.

Structurei

Secondary structure

1
522
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi181 – 19010
Helixi195 – 20915
Beta strandi213 – 2164
Turni220 – 2223
Beta strandi228 – 2303
Beta strandi233 – 2397
Helixi241 – 2433
Beta strandi247 – 2559
Beta strandi258 – 26710
Beta strandi270 – 27910
Helixi281 – 2833
Helixi287 – 2893
Helixi294 – 2974
Helixi301 – 31111
Helixi313 – 32311

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4L9CX-ray2.10A/B180-335[»]
4L9HX-ray2.00A180-335[»]
ProteinModelPortaliQ9Y3I1.
SMRiQ9Y3I1. Positions 180-330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini329 – 37547F-boxPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8888Ubiquitin-likeAdd
BLAST
Regioni92 – 12938Important for interaction with PINK1Add
BLAST
Regioni129 – 16941Important for interaction with CDK6Add
BLAST
Regioni180 – 324145Important for dimerization and interaction with PSMF1Add
BLAST
Regioni381 – 522142Important for interaction with CDK6Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi481 – 4844RFDP motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi423 – 51492Pro-richAdd
BLAST

Domaini

The ubiquitin-like region mediates interaction with PARK2.
The proline-rich region is important for protein-protein interactions.

Sequence similaritiesi

Contains 1 F-box domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG78399.
GeneTreeiENSGT00390000006670.
HOGENOMiHOG000112551.
HOVERGENiHBG005648.
InParanoidiQ9Y3I1.
KOiK10293.
OMAiPLCEGGS.
OrthoDBiEOG7S7SDG.
PhylomeDBiQ9Y3I1.
TreeFamiTF329830.

Family and domain databases

InterProiIPR001810. F-box_dom.
IPR021625. FP_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00646. F-box. 1 hit.
PF11566. PI31_Prot_N. 1 hit.
[Graphical view]
SMARTiSM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y3I1-1) [UniParc]FASTAAdd to Basket

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
MRLRVRLLKR TWPLEVPETE PTLGHLRSHL RQSLLCTWGY SSNTRFTITL
60 70 80 90 100
NYKDPLTGDE ETLASYGIVS GDLICLILQD DIPAPNIPSS TDSEHSSLQN
110 120 130 140 150
NEQPSLATSS NQTSMQDEQP SDSFQGQAAQ SGVWNDDSML GPSQNFEAES
160 170 180 190 200
IQDNAHMAEG TGFYPSEPML CSESVEGQVP HSLETLYQSA DCSDANDALI
210 220 230 240 250
VLIHLLMLES GYIPQGTEAK ALSMPEKWKL SGVYKLQYMH PLCEGSSATL
260 270 280 290 300
TCVPLGNLIV VNATLKINNE IRSVKRLQLL PESFICKEKL GENVANIYKD
310 320 330 340 350
LQKLSRLFKD QLVYPLLAFT RQALNLPDVF GLVVLPLELK LRIFRLLDVR
360 370 380 390 400
SVLSLSAVCR DLFTASNDPL LWRFLYLRDF RDNTVRVQDT DWKELYRKRH
410 420 430 440 450
IQRKESPKGR FVMLLPSSTH TIPFYPNPLH PRPFPSSRLP PGIIGGEYDQ
460 470 480 490 500
RPTLPYVGDP ISSLIPGPGE TPSQFPPLRP RFDPVGPLPG PNPILPGRGG
510 520
PNDRFPFRPS RGRPTDGRLS FM
Length:522
Mass (Da):58,503
Last modified:November 1, 1999 - v1
Checksum:iC4E5E70A0747287A
GO
Isoform 2 (identifier: Q9Y3I1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.
     80-91: DDIPAPNIPSST → MARPPGGSGPLL

Show »
Length:443
Mass (Da):49,358
Checksum:i263A319CE0096FFB
GO
Isoform 3 (identifier: Q9Y3I1-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-114: Missing.

Note: No experimental confirmation available.

Show »
Length:408
Mass (Da):45,781
Checksum:iFE4FE5ECFEAC37C5
GO

Sequence cautioni

The sequence AAF04471.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791Q → H in AAF04471. (PubMed:10531035)Curated
Sequence conflicti84 – 841A → P in AAF04471. (PubMed:10531035)Curated
Sequence conflicti154 – 1541N → S in BAG63187. (PubMed:14702039)Curated
Sequence conflicti169 – 1691M → L in AAF04471. (PubMed:10531035)Curated
Sequence conflicti224 – 2241M → L in AAF04471. (PubMed:10531035)Curated
Sequence conflicti241 – 2411P → H in AAF04471. (PubMed:10531035)Curated
Sequence conflicti328 – 3281D → N in AAF04471. (PubMed:10531035)Curated
Sequence conflicti413 – 4131M → L in AAF04471. (PubMed:10531035)Curated
Sequence conflicti475 – 4751F → L in AAF04471. (PubMed:10531035)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti115 – 1151M → I.4 Publications
Corresponds to variant rs11107 [ dbSNP | Ensembl ].
VAR_021408
Natural varianti378 – 3781R → G in PARK15; no effect on interaction with PARK2. 1 Publication
Corresponds to variant rs71799110 [ dbSNP | Ensembl ].
VAR_047938
Natural varianti481 – 4811R → C Found in two patients with Kufor-Rakeb syndrome also carrying R-877 in ATP13A2. 1 Publication
VAR_066022

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 114114Missing in isoform 3. 1 PublicationVSP_044723Add
BLAST
Alternative sequencei1 – 7979Missing in isoform 2. 1 PublicationVSP_041073Add
BLAST
Alternative sequencei80 – 9112DDIPA…IPSST → MARPPGGSGPLL in isoform 2. 1 PublicationVSP_041074Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF233225 mRNA. Translation: AAF67155.1.
AL050254 mRNA. Translation: CAB43356.1.
CR456491 mRNA. Translation: CAG30377.1.
AK297841 mRNA. Translation: BAG60175.1.
AK301716 mRNA. Translation: BAG63187.1.
AL021937, AL035068, Z71183 Genomic DNA. Translation: CAI19587.1.
AL021937, AL035068, Z71183 Genomic DNA. Translation: CAI19588.2.
AL035068, AL021937, Z71183 Genomic DNA. Translation: CAI19333.1.
AL035068, AL021937, Z71183 Genomic DNA. Translation: CAI19334.2.
Z71183, AL021937, AL035068 Genomic DNA. Translation: CAI18782.1.
Z71183, AL021937, AL035068 Genomic DNA. Translation: CAI18783.2.
BC008361 mRNA. Translation: AAH08361.1.
AF129537 mRNA. Translation: AAF04471.1. Different initiation.
CCDSiCCDS13907.1. [Q9Y3I1-1]
CCDS58806.1. [Q9Y3I1-3]
RefSeqiNP_001028196.1. NM_001033024.1. [Q9Y3I1-2]
NP_001244919.1. NM_001257990.1. [Q9Y3I1-3]
NP_036311.3. NM_012179.3. [Q9Y3I1-1]
UniGeneiHs.5912.

Genome annotation databases

EnsembliENST00000266087; ENSP00000266087; ENSG00000100225. [Q9Y3I1-1]
ENST00000397426; ENSP00000380571; ENSG00000100225. [Q9Y3I1-3]
GeneIDi25793.
KEGGihsa:25793.
UCSCiuc003amq.3. human. [Q9Y3I1-1]
uc003amt.3. human. [Q9Y3I1-2]

Polymorphism databases

DMDMi13124249.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF233225 mRNA. Translation: AAF67155.1 .
AL050254 mRNA. Translation: CAB43356.1 .
CR456491 mRNA. Translation: CAG30377.1 .
AK297841 mRNA. Translation: BAG60175.1 .
AK301716 mRNA. Translation: BAG63187.1 .
AL021937 , AL035068 , Z71183 Genomic DNA. Translation: CAI19587.1 .
AL021937 , AL035068 , Z71183 Genomic DNA. Translation: CAI19588.2 .
AL035068 , AL021937 , Z71183 Genomic DNA. Translation: CAI19333.1 .
AL035068 , AL021937 , Z71183 Genomic DNA. Translation: CAI19334.2 .
Z71183 , AL021937 , AL035068 Genomic DNA. Translation: CAI18782.1 .
Z71183 , AL021937 , AL035068 Genomic DNA. Translation: CAI18783.2 .
BC008361 mRNA. Translation: AAH08361.1 .
AF129537 mRNA. Translation: AAF04471.1 . Different initiation.
CCDSi CCDS13907.1. [Q9Y3I1-1 ]
CCDS58806.1. [Q9Y3I1-3 ]
RefSeqi NP_001028196.1. NM_001033024.1. [Q9Y3I1-2 ]
NP_001244919.1. NM_001257990.1. [Q9Y3I1-3 ]
NP_036311.3. NM_012179.3. [Q9Y3I1-1 ]
UniGenei Hs.5912.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4L9C X-ray 2.10 A/B 180-335 [» ]
4L9H X-ray 2.00 A 180-335 [» ]
ProteinModelPortali Q9Y3I1.
SMRi Q9Y3I1. Positions 180-330.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117326. 29 interactions.
DIPi DIP-36125N.
IntActi Q9Y3I1. 8 interactions.
MINTi MINT-108554.
STRINGi 9606.ENSP00000266087.

PTM databases

PhosphoSitei Q9Y3I1.

Polymorphism databases

DMDMi 13124249.

Proteomic databases

MaxQBi Q9Y3I1.
PaxDbi Q9Y3I1.
PRIDEi Q9Y3I1.

Protocols and materials databases

DNASUi 25793.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000266087 ; ENSP00000266087 ; ENSG00000100225 . [Q9Y3I1-1 ]
ENST00000397426 ; ENSP00000380571 ; ENSG00000100225 . [Q9Y3I1-3 ]
GeneIDi 25793.
KEGGi hsa:25793.
UCSCi uc003amq.3. human. [Q9Y3I1-1 ]
uc003amt.3. human. [Q9Y3I1-2 ]

Organism-specific databases

CTDi 25793.
GeneCardsi GC22P032870.
GeneReviewsi FBXO7.
HGNCi HGNC:13586. FBXO7.
HPAi CAB034296.
HPA032114.
MIMi 260300. phenotype.
605648. gene.
neXtProti NX_Q9Y3I1.
Orphaneti 171695. Parkinsonian-pyramidal syndrome.
PharmGKBi PA28047.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG78399.
GeneTreei ENSGT00390000006670.
HOGENOMi HOG000112551.
HOVERGENi HBG005648.
InParanoidi Q9Y3I1.
KOi K10293.
OMAi PLCEGGS.
OrthoDBi EOG7S7SDG.
PhylomeDBi Q9Y3I1.
TreeFami TF329830.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

ChiTaRSi FBXO7. human.
GeneWikii FBXO7.
GenomeRNAii 25793.
NextBioi 46969.
PROi Q9Y3I1.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y3I1.
CleanExi HS_FBXO7.
ExpressionAtlasi Q9Y3I1. baseline and differential.
Genevestigatori Q9Y3I1.

Family and domain databases

InterProi IPR001810. F-box_dom.
IPR021625. FP_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF00646. F-box. 1 hit.
PF11566. PI31_Prot_N. 1 hit.
[Graphical view ]
SMARTi SM00256. FBOX. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEi PS50181. FBOX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and expression analysis of new members of the mammalian F-box protein family."
    Ilyin G.P., Rialland M., Pigeon C., Guguen-Guillouzo C.
    Genomics 67:40-47(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
    Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
    Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), VARIANT ILE-115.
    Tissue: Heart and Testis.
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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), VARIANT ILE-115.
    Tissue: Pancreas.
  7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-522 (ISOFORM 1), VARIANT ILE-115.
  8. "Identification of a novel cell cycle regulated gene, HURP, overexpressed in human hepatocellular carcinoma."
    Tsou A.-P., Yang C.-W., Huang C.-Y.F., Yu R.C.-T., Lee Y.-C.G., Chang C.-W., Chen B.-R., Chung Y.-F., Fann M.-J., Chi C.-W., Chiu J.-H., Chou C.-K.
    Oncogene 22:298-307(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DLGAP5, IDENTIFICATION IN SCF COMPLEX.
  9. "Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a proline-rich region."
    Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F.
    J. Biol. Chem. 279:32592-32602(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DLGAP5; CUL1 AND SKP1, FUNCTION IN UBIQUITINATION OF DLGAP5.
  10. "Transforming activity of Fbxo7 is mediated specifically through regulation of cyclin D/cdk6."
    Laman H., Funes J.M., Ye H., Henderson S., Galinanes-Garcia L., Hara E., Knowles P., McDonald N., Boshoff C.
    EMBO J. 24:3104-3116(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDK6, SUBCELLULAR LOCATION.
  11. "The F-box protein Fbxo7 interacts with human inhibitor of apoptosis protein cIAP1 and promotes cIAP1 ubiquitination."
    Chang Y.F., Cheng C.M., Chang L.K., Jong Y.J., Yuo C.Y.
    Biochem. Biophys. Res. Commun. 342:1022-1026(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BIRC2, FUNCTION IN UBIQUITINATION OF BIRC2.
  12. "Structure of a conserved dimerization domain within the F-box protein Fbxo7 and the PI31 proteasome inhibitor."
    Kirk R., Laman H., Knowles P.P., Murray-Rust J., Lomonosov M., Meziane E.K., McDonald N.Q.
    J. Biol. Chem. 283:22325-22335(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SKP1; PSMF1 AND CDK6, SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH SKP1 AND CUL1, MUTAGENESIS OF VAL-253.
  13. Cited for: FUNCTION, INTERACTION WITH PARK2 AND PINK1, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-22, CHARACTERIZATION OF VARIANT PARK15 GLY-378.
  14. "Structure of the FP domain of Fbxo7 reveals a novel mode of protein-protein interaction."
    Shang J., Wang G., Yang Y., Huang X., Du Z.
    Acta Crystallogr. D 70:155-164(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 180-335.
  15. "Genome-wide linkage analysis of a Parkinsonian-pyramidal syndrome pedigree by 500 K SNP arrays."
    Shojaee S., Sina F., Banihosseini S.S., Kazemi M.H., Kalhor R., Shahidi G.-A., Fakhrai-Rad H., Ronaghi M., Elahi E.
    Am. J. Hum. Genet. 82:1375-1384(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PARK15 GLY-378, VARIANT ILE-115.
  16. Cited for: VARIANT CYS-481.

Entry informationi

Entry nameiFBX7_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3I1
Secondary accession number(s): B4DNB3
, B4DWX5, Q5TGC4, Q5TI86, Q96HM6, Q9UF21, Q9UKT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 133 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 22
    Human chromosome 22: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3