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Q9Y3I1 (FBX7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
F-box only protein 7
Gene names
Name:FBXO7
Synonyms:FBX7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length522 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.11 Ref.13

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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

Subcellular location

Cytoplasm. Nucleus. Mitochondrion. Cytoplasmcytosol. Note: Predominantly cytoplasmic. A minor proportion is detected in the nucleus. Relocates from the cytosol to depolarized mitochondria. Ref.10 Ref.12 Ref.13

Domain

The ubiquitin-like region mediates interaction with PARK2.

The proline-rich region is important for protein-protein interactions.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.15

Sequence similarities

Contains 1 F-box domain.

Sequence caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SKP1P632082EBI-1161222,EBI-307486

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y3I1-1)

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.
Isoform 2 (identifier: Q9Y3I1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.
     80-91: DDIPAPNIPSST → MARPPGGSGPLL
Isoform 3 (identifier: Q9Y3I1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-114: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 522522F-box only protein 7
PRO_0000119885

Regions

Domain329 – 37547F-box
Region1 – 8888Ubiquitin-like
Region92 – 12938Important for interaction with PINK1
Region129 – 16941Important for interaction with CDK6
Region180 – 324145Important for dimerization and interaction with PSMF1
Region381 – 522142Important for interaction with CDK6
Motif481 – 4844RFDP motif
Compositional bias423 – 51492Pro-rich

Natural variations

Alternative sequence1 – 114114Missing in isoform 3.
VSP_044723
Alternative sequence1 – 7979Missing in isoform 2.
VSP_041073
Alternative sequence80 – 9112DDIPA…IPSST → MARPPGGSGPLL in isoform 2.
VSP_041074
Natural variant1151M → I. Ref.4 Ref.6 Ref.7 Ref.15
Corresponds to variant rs11107 [ dbSNP | Ensembl ].
VAR_021408
Natural variant3781R → G in PARK15; no effect on interaction with PARK2. Ref.13 Ref.15
Corresponds to variant rs71799110 [ dbSNP | Ensembl ].
VAR_047938
Natural variant4811R → C Found in two patients with Kufor-Rakeb syndrome also carrying R-877 in ATP13A2. Ref.16
VAR_066022

Experimental info

Mutagenesis221T → M: Impairs interaction with PARK2. Ref.13
Mutagenesis2531V → E: Abolishes interaction with PSMF1. Ref.12
Sequence conflict791Q → H in AAF04471. Ref.7
Sequence conflict841A → P in AAF04471. Ref.7
Sequence conflict1541N → S in BAG63187. Ref.4
Sequence conflict1691M → L in AAF04471. Ref.7
Sequence conflict2241M → L in AAF04471. Ref.7
Sequence conflict2411P → H in AAF04471. Ref.7
Sequence conflict3281D → N in AAF04471. Ref.7
Sequence conflict4131M → L in AAF04471. Ref.7
Sequence conflict4751F → L in AAF04471. Ref.7

Secondary structure

............................... 522
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: C4E5E70A0747287A

FASTA52258,503
        10         20         30         40         50         60 
MRLRVRLLKR TWPLEVPETE PTLGHLRSHL RQSLLCTWGY SSNTRFTITL NYKDPLTGDE 

        70         80         90        100        110        120 
ETLASYGIVS GDLICLILQD DIPAPNIPSS TDSEHSSLQN NEQPSLATSS NQTSMQDEQP 

       130        140        150        160        170        180 
SDSFQGQAAQ SGVWNDDSML GPSQNFEAES IQDNAHMAEG TGFYPSEPML CSESVEGQVP 

       190        200        210        220        230        240 
HSLETLYQSA DCSDANDALI VLIHLLMLES GYIPQGTEAK ALSMPEKWKL SGVYKLQYMH 

       250        260        270        280        290        300 
PLCEGSSATL TCVPLGNLIV VNATLKINNE IRSVKRLQLL PESFICKEKL GENVANIYKD 

       310        320        330        340        350        360 
LQKLSRLFKD QLVYPLLAFT RQALNLPDVF GLVVLPLELK LRIFRLLDVR SVLSLSAVCR 

       370        380        390        400        410        420 
DLFTASNDPL LWRFLYLRDF RDNTVRVQDT DWKELYRKRH IQRKESPKGR FVMLLPSSTH 

       430        440        450        460        470        480 
TIPFYPNPLH PRPFPSSRLP PGIIGGEYDQ RPTLPYVGDP ISSLIPGPGE TPSQFPPLRP 

       490        500        510        520 
RFDPVGPLPG PNPILPGRGG PNDRFPFRPS RGRPTDGRLS FM 

« Hide

Isoform 2 [UniParc].

Checksum: 263A319CE0096FFB
Show »

FASTA44349,358
Isoform 3 [UniParc].

Checksum: FE4FE5ECFEAC37C5
Show »

FASTA40845,781

References

« Hide 'large scale' references
[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]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"Identification of a family of human F-box proteins."
Cenciarelli C., Chiaur D.S., Guardavaccaro D., Parks W., Vidal M., Pagano M.
Curr. Biol. 9:1177-1179(1999) [PubMed] [Europe PMC] [Abstract]
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]"The Parkinson's disease-linked proteins Fbxo7 and Parkin interact to mediate mitophagy."
Burchell V.S., Nelson D.E., Sanchez-Martinez A., Delgado-Camprubi M., Ivatt R.M., Pogson J.H., Randle S.J., Wray S., Lewis P.A., Houlden H., Abramov A.Y., Hardy J., Wood N.W., Whitworth A.J., Laman H., Plun-Favreau H.
Nat. Neurosci. 16:1257-1265(2013) [PubMed] [Europe PMC] [Abstract]
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]"Novel ATP13A2 (PARK9) homozygous mutation in a family with marked phenotype variability."
Santoro L., Breedveld G.J., Manganelli F., Iodice R., Pisciotta C., Nolano M., Punzo F., Quarantelli M., Pappata S., Di Fonzo A., Oostra B.A., Bonifati V.
Neurogenetics 12:33-39(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-481.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001028196.1. NM_001033024.1.
NP_001244919.1. NM_001257990.1.
NP_036311.3. NM_012179.3.
UniGeneHs.5912.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4L9CX-ray2.10A/B180-335[»]
4L9HX-ray2.00A180-335[»]
ProteinModelPortalQ9Y3I1.
SMRQ9Y3I1. Positions 1-81, 181-316, 333-372.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117326. 19 interactions.
DIPDIP-36125N.
IntActQ9Y3I1. 6 interactions.
MINTMINT-108554.
STRING9606.ENSP00000266087.

PTM databases

PhosphoSiteQ9Y3I1.

Polymorphism databases

DMDM13124249.

Proteomic databases

PaxDbQ9Y3I1.
PRIDEQ9Y3I1.

Protocols and materials databases

DNASU25793.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266087; ENSP00000266087; ENSG00000100225. [Q9Y3I1-1]
ENST00000382058; ENSP00000371490; ENSG00000100225. [Q9Y3I1-2]
ENST00000397426; ENSP00000380571; ENSG00000100225. [Q9Y3I1-3]
GeneID25793.
KEGGhsa:25793.
UCSCuc003amq.3. human. [Q9Y3I1-1]
uc003amt.3. human. [Q9Y3I1-2]

Organism-specific databases

CTD25793.
GeneCardsGC22P032870.
HGNCHGNC:13586. FBXO7.
HPACAB034296.
HPA032114.
MIM260300. phenotype.
605648. gene.
neXtProtNX_Q9Y3I1.
Orphanet171695. Parkinsonian-pyramidal syndrome.
PharmGKBPA28047.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG78399.
HOGENOMHOG000112551.
HOVERGENHBG005648.
KOK10293.
OMAPLCEGGS.
OrthoDBEOG7S7SDG.
PhylomeDBQ9Y3I1.
TreeFamTF329830.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9Y3I1.
BgeeQ9Y3I1.
CleanExHS_FBXO7.
GenevestigatorQ9Y3I1.

Family and domain databases

InterProIPR001810. F-box_dom.
IPR021625. FP_dom.
[Graphical view]
PfamPF00646. F-box. 1 hit.
PF11566. PI31_Prot_N. 1 hit.
[Graphical view]
SMARTSM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMSSF81383. SSF81383. 1 hit.
PROSITEPS50181. FBOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFBXO7. human.
GeneWikiFBXO7.
GenomeRNAi25793.
NextBio46969.
PROQ9Y3I1.
SOURCESearch...

Entry information

Entry nameFBX7_HUMAN
AccessionPrimary (citable) accession number: Q9Y3I1
Secondary accession number(s): B4DNB3 expand/collapse secondary AC list , B4DWX5, Q5TGC4, Q5TI86, Q96HM6, Q9UF21, Q9UKT2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM