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Q9UK22

- FBX2_HUMAN

UniProt

Q9UK22 - FBX2_HUMAN

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Protein

F-box only protein 2

Gene

FBXO2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 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 that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Involved in the endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranslocated into the cytosol and promoting their ubiquitination and subsequent degradation. Prevents formation of cytosolic aggregates of unfolded glycoproteins that have been retrotranslocated into the cytosol. Able to recognize and bind denatured glycoproteins, preferentially those of the high-mannose type (By similarity).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei173 – 1731Important for carbohydrate bindingBy similarity

GO - Molecular functioni

  1. beta-amyloid binding Source: Ensembl
  2. carbohydrate binding Source: UniProtKB-KW
  3. ubiquitin-protein transferase activity Source: ProtInc

GO - Biological processi

  1. cellular protein modification process Source: ProtInc
  2. ER-associated ubiquitin-dependent protein catabolic process Source: Ensembl
  3. glycoprotein catabolic process Source: UniProtKB
  4. negative regulation of cell proliferation Source: Ensembl
  5. protein ubiquitination Source: UniProtKB
  6. proteolysis Source: ProtInc
  7. regulation of protein ubiquitination Source: Ensembl
  8. SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Lectin

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box only protein 2
Gene namesi
Name:FBXO2
Synonyms:FBX2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:13581. FBXO2.

Subcellular locationi

Cytoplasm By similarity. Microsome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. dendritic spine Source: Ensembl
  3. endoplasmic reticulum Source: UniProtKB-KW
  4. extracellular vesicular exosome Source: UniProt
  5. membrane Source: UniProtKB-KW
  6. SCF ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31895.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296F-box only protein 2PRO_0000119875Add
BLAST

Proteomic databases

MaxQBiQ9UK22.
PaxDbiQ9UK22.
PeptideAtlasiQ9UK22.
PRIDEiQ9UK22.

PTM databases

PhosphoSiteiQ9UK22.

Expressioni

Gene expression databases

BgeeiQ9UK22.
CleanExiHS_FBXO2.
ExpressionAtlasiQ9UK22. baseline and differential.
GenevestigatoriQ9UK22.

Interactioni

Subunit structurei

Component of the SCF(FBXO2) complex consisting of CUL1, RBX1, SKP1 and FBXO2. Predominantly detected as heterodimer with SKP1; the heterodimer with SKP1 is not part of the SCF(FBXO2) complex (By similarity).By similarity

Protein-protein interaction databases

BioGridi117623. 28 interactions.
IntActiQ9UK22. 1 interaction.
MINTiMINT-5001615.
STRINGi9606.ENSP00000346240.

Structurei

3D structure databases

ProteinModelPortaliQ9UK22.
SMRiQ9UK22. Positions 57-296.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 9148F-boxPROSITE-ProRule annotationAdd
BLAST
Domaini113 – 296184FBAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni210 – 2123Carbohydrate bindingBy similarity
Regioni278 – 2792Carbohydrate bindingBy similarity

Sequence similaritiesi

Contains 1 F-box domain.PROSITE-ProRule annotation
Contains 1 FBA (F-box associated) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG85061.
GeneTreeiENSGT00390000003865.
HOGENOMiHOG000231084.
HOVERGENiHBG003593.
InParanoidiQ9UK22.
KOiK10099.
OMAiEFNSGQV.
OrthoDBiEOG7DRJ3R.
PhylomeDBiQ9UK22.
TreeFamiTF320527.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR007397. F-box-assoc_dom.
IPR001810. F-box_dom.
IPR008979. Galactose-bd-like.
[Graphical view]
PfamiPF12937. F-box-like. 1 hit.
PF04300. FBA. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEiPS51114. FBA. 1 hit.
PS50181. FBOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UK22-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDGDGDPESV GQPEEASPEE QPEEASAEEE RPEDQQEEEA AAAAAYLDEL
60 70 80 90 100
PEPLLLRVLA ALPAAELVQA CRLVCLRWKE LVDGAPLWLL KCQQEGLVPE
110 120 130 140 150
GGVEEERDHW QQFYFLSKRR RNLLRNPCGE EDLEGWCDVE HGGDGWRVEE
160 170 180 190 200
LPGDSGVEFT HDESVKKYFA SSFEWCRKAQ VIDLQAEGYW EELLDTTQPA
210 220 230 240 250
IVVKDWYSGR SDAGCLYELT VKLLSEHENV LAEFSSGQVA VPQDSDGGGW
260 270 280 290
MEISHTFTDY GPGVRFVRFE HGGQDSVYWK GWFGARVTNS SVWVEP
Length:296
Mass (Da):33,328
Last modified:August 16, 2004 - v2
Checksum:i5226F19E27D884AF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451Missing in AAF01822. (PubMed:10531037)Curated
Sequence conflicti125 – 1251R → C in CAG46907. 1 PublicationCurated
Sequence conflicti163 – 1631E → D in CAG46907. 1 PublicationCurated
Sequence conflicti275 – 2751D → G in AAF04515. (PubMed:10531035)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti118 – 1181K → T.1 Publication
Corresponds to variant rs9614 [ dbSNP | Ensembl ].
VAR_049036

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF187318 mRNA. Translation: AAF01822.1.
CR542110 mRNA. Translation: CAG46907.1.
AK313019 mRNA. Translation: BAG35854.1.
AL031731 Genomic DNA. Translation: CAI20209.1.
CH471130 Genomic DNA. Translation: EAW71689.1.
BC025233 mRNA. Translation: AAH25233.1.
BC096747 mRNA. Translation: AAH96747.1.
AF174594 mRNA. Translation: AAF04515.1.
CCDSiCCDS130.1.
RefSeqiNP_036300.2. NM_012168.5.
UniGeneiHs.132753.
Hs.556006.

Genome annotation databases

EnsembliENST00000354287; ENSP00000346240; ENSG00000116661.
GeneIDi26232.
KEGGihsa:26232.
UCSCiuc001asj.3. human.

Polymorphism databases

DMDMi51338836.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF187318 mRNA. Translation: AAF01822.1 .
CR542110 mRNA. Translation: CAG46907.1 .
AK313019 mRNA. Translation: BAG35854.1 .
AL031731 Genomic DNA. Translation: CAI20209.1 .
CH471130 Genomic DNA. Translation: EAW71689.1 .
BC025233 mRNA. Translation: AAH25233.1 .
BC096747 mRNA. Translation: AAH96747.1 .
AF174594 mRNA. Translation: AAF04515.1 .
CCDSi CCDS130.1.
RefSeqi NP_036300.2. NM_012168.5.
UniGenei Hs.132753.
Hs.556006.

3D structure databases

ProteinModelPortali Q9UK22.
SMRi Q9UK22. Positions 57-296.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117623. 28 interactions.
IntActi Q9UK22. 1 interaction.
MINTi MINT-5001615.
STRINGi 9606.ENSP00000346240.

PTM databases

PhosphoSitei Q9UK22.

Polymorphism databases

DMDMi 51338836.

Proteomic databases

MaxQBi Q9UK22.
PaxDbi Q9UK22.
PeptideAtlasi Q9UK22.
PRIDEi Q9UK22.

Protocols and materials databases

DNASUi 26232.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000354287 ; ENSP00000346240 ; ENSG00000116661 .
GeneIDi 26232.
KEGGi hsa:26232.
UCSCi uc001asj.3. human.

Organism-specific databases

CTDi 26232.
GeneCardsi GC01M011708.
HGNCi HGNC:13581. FBXO2.
MIMi 607112. gene.
neXtProti NX_Q9UK22.
PharmGKBi PA31895.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG85061.
GeneTreei ENSGT00390000003865.
HOGENOMi HOG000231084.
HOVERGENi HBG003593.
InParanoidi Q9UK22.
KOi K10099.
OMAi EFNSGQV.
OrthoDBi EOG7DRJ3R.
PhylomeDBi Q9UK22.
TreeFami TF320527.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSi FBXO2. human.
GeneWikii FBXO2.
GenomeRNAii 26232.
NextBioi 48407.
PROi Q9UK22.
SOURCEi Search...

Gene expression databases

Bgeei Q9UK22.
CleanExi HS_FBXO2.
ExpressionAtlasi Q9UK22. baseline and differential.
Genevestigatori Q9UK22.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
InterProi IPR007397. F-box-assoc_dom.
IPR001810. F-box_dom.
IPR008979. Galactose-bd-like.
[Graphical view ]
Pfami PF12937. F-box-like. 1 hit.
PF04300. FBA. 1 hit.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEi PS51114. FBA. 1 hit.
PS50181. FBOX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-118.
  3. "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].
    Tissue: Cerebellum.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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].
    Tissue: Brain and Pancreas.
  7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 40-296.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFBX2_HUMAN
AccessioniPrimary (citable) accession number: Q9UK22
Secondary accession number(s): B2R7K7
, Q5TGY0, Q6FGJ7, Q8TB29, Q9UKC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: August 16, 2004
Last modified: October 29, 2014
This is version 125 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3