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Q9UKT4

- FBX5_HUMAN

UniProt

Q9UKT4 - FBX5_HUMAN

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Protein

F-box only protein 5

Gene

FBXO5

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

Functioni

Regulates progression through early mitosis by inhibiting the anaphase promoting complex/cyclosome (APC). Binds to the APC activators CDC20 and FZR1/CDH1 to prevent APC activation. Can also bind directly to the APC to inhibit substrate-binding.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri357 – 41963IBR-typeAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein kinase binding Source: UniProtKB

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. G1/S transition of mitotic cell cycle Source: Reactome
  3. inhibition of mitotic anaphase-promoting complex activity Source: UniProtKB
  4. metaphase/anaphase transition of mitotic cell cycle Source: Reactome
  5. microtubule polymerization Source: Ensembl
  6. mitotic cell cycle Source: Reactome
  7. negative regulation of meiosis Source: Ensembl
  8. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: UniProtKB
  9. oocyte maturation Source: Ensembl
  10. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  11. regulation of mitotic cell cycle Source: UniProtKB
  12. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Reactome
  13. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  14. spindle assembly involved in female meiosis I Source: Ensembl
  15. vesicle organization Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1016. Mitotic Metaphase/Anaphase Transition.
REACT_471. E2F mediated regulation of DNA replication.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_683. G1/S-Specific Transcription.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6875. Phosphorylation of Emi1.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box only protein 5
Alternative name(s):
Early mitotic inhibitor 1
Gene namesi
Name:FBXO5
Synonyms:EMI1, FBX5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:13584. FBXO5.

Subcellular locationi

Nucleus. Cytoplasm. Cytoplasmcytoskeletonspindle
Note: In interphase, localizes in a punctate manner in the nucleus and cytoplasm with some perinuclear concentration. In mitotic cells, localizes throughout the cell, particularly at the spindle.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. spindle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi143 – 1431E → A: Delays degradation. 1 Publication
Mutagenesisi145 – 1451S → E: Degraded in similar manner to wild-type. 3 Publications
Mutagenesisi145 – 1451S → N: Not mitotically degraded. Shows impaired interaction with BTRC and reduced phosphate incorporation; when associated with N-149. 3 Publications
Mutagenesisi148 – 1481S → A: Degraded in similar manner to wild-type. 1 Publication
Mutagenesisi149 – 1491S → E: Degraded in similar manner to wild-type. 3 Publications
Mutagenesisi149 – 1491S → N: Not mitotically degraded. Shows impaired interaction with BTRC and reduced phosphate incorporation; when associated with N-145. 3 Publications
Mutagenesisi182 – 1821S → A: Shows impaired interaction with BTRC. 1 Publication
Mutagenesisi210 – 2167KRNPKVD → AAAAAAA: Loss of interaction with EVI5. 1 Publication
Mutagenesisi401 – 4011C → S: Reduced inhibition of APC. 1 Publication

Organism-specific databases

PharmGKBiPA28045.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447F-box only protein 5PRO_0000119881Add
BLAST

Post-translational modificationi

Phosphorylation by CDK2 and subsequently by PLK1 triggers degradation during early mitosis through ubiquitin-mediated proteolysis by the SCF ubiquitin ligase complex containing the F-box protein BTRC. This degradation is necessary for the activation of APC in late mitosis and subsequent mitotic progression.
Ubiquitinated by the by the SCF(BTRC) complex following phosphorylation by PLK1.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9UKT4.
PaxDbiQ9UKT4.
PRIDEiQ9UKT4.

PTM databases

PhosphoSiteiQ9UKT4.

Expressioni

Developmental stagei

Accumulates in late G1 phase, levels rise during S phase and drop in early mitosis.1 Publication

Gene expression databases

BgeeiQ9UKT4.
CleanExiHS_FBXO5.
GenevestigatoriQ9UKT4.

Organism-specific databases

HPAiCAB008106.
HPA029048.

Interactioni

Subunit structurei

Part of a SCF (SKP1-cullin-F-box) protein ligase complex (By similarity). Interacts with BTRC, FZR1/CDH1 and the N-terminal substrate-binding domain of CDC20. Also interacts with EVI5 which blocks its phosphorylation by PLK1 and prevents its subsequent binding to BTRC and degradation.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC27P302602EBI-852298,EBI-994813
EVI5O604476EBI-852298,EBI-852291

Protein-protein interaction databases

BioGridi117655. 32 interactions.
DIPiDIP-38023N.
IntActiQ9UKT4. 10 interactions.
MINTiMINT-4789777.
STRINGi9606.ENSP00000229758.

Structurei

Secondary structure

1
447
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni379 – 3813Combined sources
Beta strandi384 – 3885Combined sources
Turni389 – 3924Combined sources
Beta strandi393 – 3964Combined sources
Beta strandi404 – 4063Combined sources
Turni407 – 4093Combined sources
Beta strandi410 – 4123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M6NNMR-A364-447[»]
ProteinModelPortaliQ9UKT4.
SMRiQ9UKT4. Positions 374-419.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini250 – 29647F-boxAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni135 – 244110Interaction with EVI5Add
BLAST

Domaini

The C-terminal region is required for inhibition of APC activity.

Sequence similaritiesi

Contains 1 F-box domain.Curated
Contains 1 IBR-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri357 – 41963IBR-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG45978.
GeneTreeiENSGT00530000063692.
HOGENOMiHOG000035122.
HOVERGENiHBG010089.
InParanoidiQ9UKT4.
KOiK10292.
OMAiSTTWKKI.
OrthoDBiEOG783MXX.
PhylomeDBiQ9UKT4.
TreeFamiTF101170.

Family and domain databases

InterProiIPR001810. F-box_dom.
[Graphical view]
PfamiPF00646. F-box. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UKT4-1) [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
MSRRPCSCAL RPPRCSCSAS PSAVTAAGRP RPSDSCKEES STLSVKMKCD
60 70 80 90 100
FNCNHVHSGL KLVKPDDIGR LVSYTPAYLE GSCKDCIKDY ERLSCIGSPI
110 120 130 140 150
VSPRIVQLET ESKRLHNKEN QHVQQTLNST NEIEALETSR LYEDSGYSSF
160 170 180 190 200
SLQSGLSEHE EGSLLEENFG DSLQSCLLQI QSPDQYPNKN LLPVLHFEKV
210 220 230 240 250
VCSTLKKNAK RNPKVDREML KEIIARGNFR LQNIIGRKMG LECVDILSEL
260 270 280 290 300
FRRGLRHVLA TILAQLSDMD LINVSKVSTT WKKILEDDKG AFQLYSKAIQ
310 320 330 340 350
RVTENNNKFS PHASTREYVM FRTPLASVQK SAAQTSLKKD AQTKLSNQGD
360 370 380 390 400
QKGSTYSRHN EFSEVAKTLK KNESLKACIR CNSPAKYDCY LQRATCKREG
410 420 430 440
CGFDYCTKCL CNYHTTKDCS DGKLLKASCK IGPLPGTKKS KKNLRRL
Length:447
Mass (Da):50,146
Last modified:May 1, 2000 - v1
Checksum:i196FBC2578F92120
GO
Isoform 2 (identifier: Q9UKT4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: Missing.

Show »
Length:401
Mass (Da):45,353
Checksum:i8E9E775625E62A4F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti212 – 2121N → D in BAG51487. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071Q → E.2 Publications
Corresponds to variant rs2073260 [ dbSNP | Ensembl ].
VAR_024440
Natural varianti164 – 1641L → F.
Corresponds to variant rs7763565 [ dbSNP | Ensembl ].
VAR_049038

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4646Missing in isoform 2. 1 PublicationVSP_041362Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF129535 mRNA. Translation: AAF04469.1.
AY079515 mRNA. Translation: AAL86610.1.
AK055221 mRNA. Translation: BAG51487.1.
AL080276 Genomic DNA. Translation: CAI18894.1.
AL080276 Genomic DNA. Translation: CAI18895.1.
CH471051 Genomic DNA. Translation: EAW47719.1.
BC018905 mRNA. Translation: AAH18905.1.
CCDSiCCDS47501.1. [Q9UKT4-2]
CCDS5242.1. [Q9UKT4-1]
RefSeqiNP_001135994.1. NM_001142522.1. [Q9UKT4-2]
NP_036309.1. NM_012177.3. [Q9UKT4-1]
UniGeneiHs.520506.

Genome annotation databases

EnsembliENST00000229758; ENSP00000229758; ENSG00000112029. [Q9UKT4-1]
ENST00000367241; ENSP00000356210; ENSG00000112029. [Q9UKT4-2]
GeneIDi26271.
KEGGihsa:26271.
UCSCiuc003qpg.3. human. [Q9UKT4-1]

Polymorphism databases

DMDMi24636847.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF129535 mRNA. Translation: AAF04469.1 .
AY079515 mRNA. Translation: AAL86610.1 .
AK055221 mRNA. Translation: BAG51487.1 .
AL080276 Genomic DNA. Translation: CAI18894.1 .
AL080276 Genomic DNA. Translation: CAI18895.1 .
CH471051 Genomic DNA. Translation: EAW47719.1 .
BC018905 mRNA. Translation: AAH18905.1 .
CCDSi CCDS47501.1. [Q9UKT4-2 ]
CCDS5242.1. [Q9UKT4-1 ]
RefSeqi NP_001135994.1. NM_001142522.1. [Q9UKT4-2 ]
NP_036309.1. NM_012177.3. [Q9UKT4-1 ]
UniGenei Hs.520506.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2M6N NMR - A 364-447 [» ]
ProteinModelPortali Q9UKT4.
SMRi Q9UKT4. Positions 374-419.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117655. 32 interactions.
DIPi DIP-38023N.
IntActi Q9UKT4. 10 interactions.
MINTi MINT-4789777.
STRINGi 9606.ENSP00000229758.

PTM databases

PhosphoSitei Q9UKT4.

Polymorphism databases

DMDMi 24636847.

Proteomic databases

MaxQBi Q9UKT4.
PaxDbi Q9UKT4.
PRIDEi Q9UKT4.

Protocols and materials databases

DNASUi 26271.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000229758 ; ENSP00000229758 ; ENSG00000112029 . [Q9UKT4-1 ]
ENST00000367241 ; ENSP00000356210 ; ENSG00000112029 . [Q9UKT4-2 ]
GeneIDi 26271.
KEGGi hsa:26271.
UCSCi uc003qpg.3. human. [Q9UKT4-1 ]

Organism-specific databases

CTDi 26271.
GeneCardsi GC06M153291.
HGNCi HGNC:13584. FBXO5.
HPAi CAB008106.
HPA029048.
MIMi 606013. gene.
neXtProti NX_Q9UKT4.
PharmGKBi PA28045.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG45978.
GeneTreei ENSGT00530000063692.
HOGENOMi HOG000035122.
HOVERGENi HBG010089.
InParanoidi Q9UKT4.
KOi K10292.
OMAi STTWKKI.
OrthoDBi EOG783MXX.
PhylomeDBi Q9UKT4.
TreeFami TF101170.

Enzyme and pathway databases

Reactomei REACT_1016. Mitotic Metaphase/Anaphase Transition.
REACT_471. E2F mediated regulation of DNA replication.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_683. G1/S-Specific Transcription.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6875. Phosphorylation of Emi1.

Miscellaneous databases

GeneWikii FBXO5.
GenomeRNAii 26271.
NextBioi 48561.
PROi Q9UKT4.
SOURCEi Search...

Gene expression databases

Bgeei Q9UKT4.
CleanExi HS_FBXO5.
Genevestigatori Q9UKT4.

Family and domain databases

InterProi IPR001810. F-box_dom.
[Graphical view ]
Pfami PF00646. F-box. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "E2F-dependent accumulation of hEmi1 regulates S phase entry by inhibiting APC(Cdh1)."
    Hsu J.Y., Reimann J.D.R., Sorensen C.S., Lukas J., Jackson P.K.
    Nat. Cell Biol. 4:358-366(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH FZR1, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  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] (ISOFORM 2), VARIANT GLU-107.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [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] (ISOFORM 1), VARIANT GLU-107.
    Tissue: Placenta.
  7. "Prophase destruction of Emi1 by the SCF(betaTrCP/Slimb) ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase."
    Margottin-Goguet F., Hsu J.Y., Loktev A., Hsieh H.-M., Reimann J.D.R., Jackson P.K.
    Dev. Cell 4:813-826(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BTRC; PHOSPHORYLATION, DEGRADATION, MUTAGENESIS OF SER-145; SER-149 AND SER-182.
  8. "Plk1 regulates activation of the anaphase promoting complex by phosphorylating and triggering SCFbetaTrCP-dependent destruction of the APC inhibitor Emi1."
    Hansen D.V., Loktev A.V., Ban K.H., Jackson P.K.
    Mol. Biol. Cell 15:5623-5634(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, UBIQUITINATION, MUTAGENESIS OF GLU-143; SER-145; SER-148 AND SER-149.
  9. "Role of Polo-like kinase in the degradation of early mitotic inhibitor 1, a regulator of the anaphase promoting complex/cyclosome."
    Moshe Y., Boulaire J., Pagano M., Hershko A.
    Proc. Natl. Acad. Sci. U.S.A. 101:7937-7942(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, UBIQUITINATION, MUTAGENESIS OF SER-145 AND SER-149.
  10. "The evi5 oncogene regulates cyclin accumulation by stabilizing the anaphase-promoting complex inhibitor emi1."
    Eldridge A.G., Loktev A.V., Hansen D.V., Verschuren E.W., Reimann J.D.R., Jackson P.K.
    Cell 124:367-380(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EVI5, MUTAGENESIS OF 210-LYS--ASP-216.
  11. "Emi1 stably binds and inhibits the anaphase-promoting complex/cyclosome as a pseudosubstrate inhibitor."
    Miller J.J., Summers M.K., Hansen D.V., Nachury M.V., Lehman N.L., Loktev A., Jackson P.K.
    Genes Dev. 20:2410-2420(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-401.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiFBX5_HUMAN
AccessioniPrimary (citable) accession number: Q9UKT4
Secondary accession number(s): B3KNX5
, Q5TF47, Q8WV29, Q9UGC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 119 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 6
    Human chromosome 6: 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