Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

F-box/WD repeat-containing protein 5 (F-box and WD-40 domain-containing protein 5)

 FBXW5_HUMAN             Reviewed;         566 AA.
Q969U6; B2RDZ6; Q59ET5; Q5SPZ8; Q5SPZ9; Q5SQ00; Q5SQ02; Q5SQ03;
Q5SQ04; Q8WY79; Q96GJ6; Q9BSU8; Q9H6A8; Q9HBQ6; Q9NSZ3;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
12-SEP-2018, entry version 157.
RecName: Full=F-box/WD repeat-containing protein 5;
AltName: Full=F-box and WD-40 domain-containing protein 5;
Name=FBXW5; Synonyms=FBW5; ORFNames=PP3971;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix, Colon, Ovary, Placenta, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-566 (ISOFORM 1).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
"Homo sapiens protein coding cDNA.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 186-566 (ISOFORM 2).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 219-566 (ISOFORM 1).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[8]
FUNCTION, INTERACTION WITH TSC1 AND TSC2, AND IDENTIFICATION IN A DCX
PROTEIN LIGASE COMPLEX.
PubMed=18381890; DOI=10.1101/gad.1624008;
Hu J., Zacharek S., He Y.J., Lee H., Shumway S., Duronio R.J.,
Xiong Y.;
"WD40 protein FBW5 promotes ubiquitination of tumor suppressor TSC2 by
DDB1-CUL4-ROC1 ligase.";
Genes Dev. 22:866-871(2008).
[9]
FUNCTION.
PubMed=19232515; DOI=10.1016/j.bbrc.2009.02.052;
Minoda Y., Sakurai H., Kobayashi T., Yoshimura A., Takaesu G.;
"An F-box protein, FBXW5, negatively regulates TAK1 MAP3K in the IL-
1beta signaling pathway.";
Biochem. Biophys. Res. Commun. 381:412-417(2009).
[10]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SASS6 AND CDC20,
IDENTIFICATION IN A SCF PROTEIN LIGASE COMPLEX, DEVELOPMENTAL STAGE,
UBIQUITINATION, PHOSPHORYLATION AT SER-151, AND MUTAGENESIS OF
SER-151.
PubMed=21725316; DOI=10.1038/ncb2282;
Puklowski A., Homsi Y., Keller D., May M., Chauhan S., Kossatz U.,
Grunwald V., Kubicka S., Pich A., Manns M.P., Hoffmann I., Gonczy P.,
Malek N.P.;
"The SCF-FBXW5 E3-ubiquitin ligase is regulated by PLK4 and targets
HsSAS-6 to control centrosome duplication.";
Nat. Cell Biol. 13:1004-1009(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Substrate recognition component of both SCF (SKP1-CUL1-
F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein
ligase complexes. Substrate recognition component of the
SCF(FBXW5) E3 ubiquitin-protein ligase complex which mediates the
ubiquitination and subsequent proteasomal degradation of SASS6
during S phase, leading to prevent centriole reduplication. The
SCF(FBXW5) complex also mediates ubiquitination and degradation of
actin-regulator EPS8 during G2 phase, leading to the transient
degradation of EPS8 and subsequent cell shape changes required to
allow mitotic progression. Substrate-specific adapter of the
DCX(FBXW5) E3 ubiquitin-protein ligase complex which mediates the
polyubiquitination and subsequent degradation of TSC2. May also
act as a negative regulator of MAP3K7/TAK1 signaling in the
interleukin-1B (IL1B) signaling pathway.
{ECO:0000269|PubMed:18381890, ECO:0000269|PubMed:19232515,
ECO:0000269|PubMed:21725316}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein
ligase complex SCF(FBXW5) composed of CUL1, SKP1, RBX1 and FBXW5.
Component of the DCX(FBXW5) E3 ubiquitin ligase complex, at least
composed of (CUL4A or CUL4B), DDB1, FBXW5 and RBX1. Interacts with
CDC20, EPS8, TSC1, TSC2 and SASS6. Interacts with TNFAIP8L1;
TNFAIP8L1 competes with TSC2 to bind FBXW5 increasing TSC2
stability by preventing its ubiquitination.
{ECO:0000250|UniProtKB:Q9QXW2, ECO:0000269|PubMed:18381890,
ECO:0000269|PubMed:21725316}.
-!- INTERACTION:
Q6UY14-3:ADAMTSL4; NbExp=5; IntAct=EBI-741068, EBI-10173507;
Q16531:DDB1; NbExp=3; IntAct=EBI-16031873, EBI-350322;
Q12929:EPS8; NbExp=3; IntAct=EBI-16031873, EBI-375576;
Q15323:KRT31; NbExp=5; IntAct=EBI-741068, EBI-948001;
Q6A162:KRT40; NbExp=3; IntAct=EBI-741068, EBI-10171697;
P60410:KRTAP10-8; NbExp=5; IntAct=EBI-741068, EBI-10171774;
Q9BYQ2:KRTAP9-4; NbExp=3; IntAct=EBI-741068, EBI-10185730;
Q7Z3S9:NOTCH2NL; NbExp=5; IntAct=EBI-741068, EBI-945833;
P63208:SKP1; NbExp=4; IntAct=EBI-741068, EBI-307486;
P63208-1:SKP1; NbExp=3; IntAct=EBI-16031873, EBI-307497;
P14373:TRIM27; NbExp=5; IntAct=EBI-741068, EBI-719493;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21725316}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q969U6-1; Sequence=Displayed;
Name=2;
IsoId=Q969U6-2; Sequence=VSP_009479, VSP_009480;
-!- DEVELOPMENTAL STAGE: Degraded by the APC/C complex during G1 phase
and reaccumulates at the G1/S phase transition.
{ECO:0000269|PubMed:21725316}.
-!- DOMAIN: The F-box domain mediates interaction with components of
SCF (SKP1-CUL1-F-box protein) complexes, while WD repeats mediate
interaction with components of DCX (DDB1-CUL4-X-box) complexes.
{ECO:0000305}.
-!- DOMAIN: The D-box (destruction box) mediate the interaction with
APC proteins, and acts as a recognition signal for degradation via
the ubiquitin-proteasome pathway. {ECO:0000250}.
-!- PTM: Phosphorylated at Ser-151 by PLK4 during the G1/S transition,
leading to inhibit its ability to ubiquitinate SASS6.
{ECO:0000269|PubMed:21725316}.
-!- PTM: Ubiquitinated and degraded by the APC/C complex during
mitosis and G1 phase. {ECO:0000269|PubMed:21725316}.
-!- SIMILARITY: Belongs to the FBXW5 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG17240.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=AAG23772.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=AAH00850.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AK026081; BAB15354.1; -; mRNA.
EMBL; AK315738; BAG38093.1; -; mRNA.
EMBL; CH471090; EAW88307.1; -; Genomic_DNA.
EMBL; BC000850; AAH00850.1; ALT_INIT; mRNA.
EMBL; BC004541; AAH04541.2; -; mRNA.
EMBL; BC009429; AAH09429.1; -; mRNA.
EMBL; BC014297; AAH14297.1; -; mRNA.
EMBL; AL807752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC014130; AAH14130.1; -; mRNA.
EMBL; AB209726; BAD92963.1; -; mRNA.
EMBL; AL137631; CAB70851.1; -; mRNA.
EMBL; AF217998; AAG17240.1; ALT_FRAME; mRNA.
EMBL; AF258569; AAG23772.1; ALT_FRAME; mRNA.
CCDS; CCDS7014.1; -. [Q969U6-1]
PIR; T46483; T46483.
RefSeq; NP_061871.1; NM_018998.3. [Q969U6-1]
UniGene; Hs.522507; -.
ProteinModelPortal; Q969U6; -.
BioGrid; 119967; 46.
DIP; DIP-37971N; -.
IntAct; Q969U6; 39.
MINT; Q969U6; -.
STRING; 9606.ENSP00000313034; -.
iPTMnet; Q969U6; -.
PhosphoSitePlus; Q969U6; -.
BioMuta; FBXW5; -.
DMDM; 44887886; -.
EPD; Q969U6; -.
MaxQB; Q969U6; -.
PaxDb; Q969U6; -.
PeptideAtlas; Q969U6; -.
PRIDE; Q969U6; -.
ProteomicsDB; 75846; -.
ProteomicsDB; 75847; -. [Q969U6-2]
DNASU; 54461; -.
Ensembl; ENST00000325285; ENSP00000313034; ENSG00000159069. [Q969U6-1]
GeneID; 54461; -.
KEGG; hsa:54461; -.
UCSC; uc004cjx.4; human. [Q969U6-1]
CTD; 54461; -.
DisGeNET; 54461; -.
EuPathDB; HostDB:ENSG00000159069.13; -.
GeneCards; FBXW5; -.
HGNC; HGNC:13613; FBXW5.
HPA; HPA046615; -.
MIM; 609072; gene.
neXtProt; NX_Q969U6; -.
OpenTargets; ENSG00000159069; -.
PharmGKB; PA134928070; -.
eggNOG; ENOG410IEAX; Eukaryota.
eggNOG; ENOG410XTK0; LUCA.
GeneTree; ENSGT00730000111276; -.
HOVERGEN; HBG051595; -.
InParanoid; Q969U6; -.
KO; K10263; -.
OMA; PHQIGFK; -.
OrthoDB; EOG091G04E0; -.
PhylomeDB; Q969U6; -.
TreeFam; TF324320; -.
Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q969U6; -.
UniPathway; UPA00143; -.
ChiTaRS; FBXW5; human.
GeneWiki; FBXW5; -.
GenomeRNAi; 54461; -.
PRO; PR:Q969U6; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000159069; Expressed in 168 organ(s), highest expression level in right testis.
ExpressionAtlas; Q969U6; baseline and differential.
Genevisible; Q969U6; HS.
GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; EXP:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB.
GO; GO:0007088; P:regulation of mitotic nuclear division; IEA:Ensembl.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR036047; F-box-like_dom_sf.
InterPro; IPR001810; F-box_dom.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF12937; F-box-like; 1.
Pfam; PF00400; WD40; 1.
SMART; SM00256; FBOX; 1.
SMART; SM00320; WD40; 3.
SUPFAM; SSF50978; SSF50978; 2.
SUPFAM; SSF81383; SSF81383; 2.
PROSITE; PS50181; FBOX; 1.
PROSITE; PS50082; WD_REPEATS_2; 2.
PROSITE; PS50294; WD_REPEATS_REGION; 2.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Ubl conjugation;
Ubl conjugation pathway; WD repeat.
CHAIN 1 566 F-box/WD repeat-containing protein 5.
/FTId=PRO_0000050992.
DOMAIN 3 49 F-box. {ECO:0000255|PROSITE-
ProRule:PRU00080}.
REPEAT 83 125 WD 1.
REPEAT 126 178 WD 2.
REPEAT 179 238 WD 3.
REPEAT 239 281 WD 4.
REPEAT 394 447 WD 5.
REPEAT 458 501 WD 6.
REPEAT 502 539 WD 7.
MOTIF 303 311 D-box.
MOD_RES 151 151 Phosphoserine; by PLK4.
{ECO:0000269|PubMed:21725316}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 367 377 IKQILPHQMTT -> TPLPPCCPPRS (in isoform
2). {ECO:0000303|PubMed:17974005}.
/FTId=VSP_009479.
VAR_SEQ 378 566 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_009480.
VARIANT 340 340 E -> K (in dbSNP:rs7850438).
/FTId=VAR_053393.
MUTAGEN 151 151 S->A: Impairs phosphorylation by PLK4 and
enhances ubiquitination of SASS6.
{ECO:0000269|PubMed:21725316}.
CONFLICT 490 490 D -> G (in Ref. 1; BAB15354).
{ECO:0000305}.
CONFLICT 508 508 R -> Q (in Ref. 5; BAD92963).
{ECO:0000305}.
SEQUENCE 566 AA; 63922 MW; 7D389AB6F50193B1 CRC64;
MDEGGTPLLP DSLVYQIFLS LGPADVLAAG LVCRQWQAVS RDEFLWREQF YRYYQVARDV
PRHPAAMSWY EEFQRLYDTV PCVEVQTLRE HTDQVLHLSF SHSGYQFASC SKDCTVKIWS
NDLTISLLHS ADMRPYNWSY TQFSQFNKDD SLLLASGVFL GPHNSSSGEI AVISLDSFAL
LSRVRNKPYD VFGCWLTETS LISGNLHRIG DITSCSVLWL NNAFQDVESE NVNVVKRLFK
IQNLNASTVR TVMVADCSRF DSPDLLLEAG DPATSPCRIF DLGSDNEEVV AGPAPAHAKE
GLRHFLDRVL EGRAQPQLSE RMLETKVAEL LAQGHTKPPE RSATGAKSKY LIFTTGCLTY
SPHQIGIKQI LPHQMTTAGP VLGEGRGSDA FFDALDHVID IHGHIIGMGL SPDNRYLYVN
SRAWPNGAVV ADPMQPPPIA EEIDLLVFDL KTMREVRRAL RAHRAYTPND ECFFIFLDVS
RDFVASGAED RHGYIWDRHY NICLARLRHE DVVNSVVFSP QEQELLLTAS DDATIKAWRS
PRTMRVLQAP RPRPRTFFSW LASQRR


Related products :

Catalog number Product name Quantity
EIAAB46368 DXImx38e,Mouse,Mus musculus,WD repeat domain phosphoinositide-interacting protein 4,WD repeat domain X-linked 1,WD repeat-containing protein 45,Wdr45,Wdrx1,Wipi4,WIPI-4
EIAAB08269 CNPY3,CTG repeat protein 4a,CTG4A,ERDA5,Expanded repeat-domain protein CAG_CTG 5,Homo sapiens,HSPC084,Human,PRAT4A,Protein associated with TLR4,Protein canopy homolog 3,TNRC5,Trinucleotide repeat-cont
EIAAB46365 Homo sapiens,Human,WD repeat domain phosphoinositide-interacting protein 3,WD repeat-containing protein 45-like,WDR45L,WDR45-like protein,WIPI3,WIPI-3,WIPI49-like protein
AS11 1793 Antibody: Protein kinase protein with tetratricopeptide repeat domain , Immunogen: recombinant part ofArabidopsis thalianaProtein kinase protein with tetratricopeptide repeat domain Q9M324, Host: rabb 100
EIAAB46125 Beach domain, WD repeat and FYVE domain-containing protein 1,BWF1,Mouse,Mus musculus,WD repeat and FYVE domain-containing protein 3,Wdfy3
EIAAB46364 Mouse,Mus musculus,WD repeat domain phosphoinositide-interacting protein 3,WD repeat-containing protein 45-like,Wdr45l,WDR45-like protein,Wipi3,WIPI-3
EIAAB30470 Papin,PDZ domain-containing protein 2,PDZ domain-containing protein 3,Pdzd2,Pdzk3,Pin1,Plakophilin-related armadillo repeat protein-interacting PDZ protein,Rat,Rattus norvegicus
18-003-43413 JmjC domain-containing histone demethylation protein 1A - EC 1.14.11.27; [Histone-H3]-lysine-36 demethylase 1A; F-box_LRR-repeat protein 11; F-box and leucine-rich repeat protein 11; F-box protein FBL 0.05 mg Aff Pur
EIAAB14640 F-box and WD-40 domain-containing protein 7,F-box protein FBW7,F-box protein Fbxw6,F-box_WD repeat-containing protein 7,F-box-WD40 repeat protein 6,Fbw7,Fbwd6,Fbxw6,Fbxw7,Mouse,Mus musculus,SEL-10
EIAAB46363 Chicken,Gallus gallus,RCJMB04_8d21,WD repeat domain phosphoinositide-interacting protein 3,WD repeat protein 45-like,WDR45L,WDR45-like protein,WIPI3,WIPI-3
EIAAB06739 BRUNOL1,Bruno-like protein 1,CAG repeat protein 4,CAGH4,CELF3,CELF-3,CUG-BP- and ETR-3-like factor 3,CUGBP Elav-like family member 3,ELAV-type RNA-binding protein 1,ERDA4,ETR-1,Expanded repeat domain
EIAAB46366 Rat,Rattus norvegicus,WD repeat domain phosphoinositide-interacting protein 4,WD repeat-containing protein 45,Wdr45,Wipi4,WIPI-4
EIAAB46367 Homo sapiens,Human,JM5,WD repeat domain phosphoinositide-interacting protein 4,WD repeat-containing protein 45,WDR45,WDRX1,WDRXI4,WIPI4,WIPI-4
EIAAB46124 Homo sapiens,Human,WD repeat and FYVE domain-containing protein 2,WD40- and FYVE domain-containing protein 2,WDF2,WDFY2,ZFYVE22,Zinc finger FYVE domain-containing protein 22
EIAAB46358 Atg18 protein homolog,Homo sapiens,Human,WD repeat domain phosphoinositide-interacting protein 1,WD40 repeat protein interacting with phosphoinositides of 49 kDa,WIPI 49 kDa,WIPI1,WIPI-1,WIPI49
EIAAB14615 Afh,Fbl3a,F-box and leucine-rich repeat protein 3A,F-box_LRR-repeat protein 3,F-box_LRR-repeat protein 3A,Fbxl3,Fbxl3a,Mouse,Mus musculus,Ovtm,Protein after-hours,Protein overtime
EIAAB30918 Homo sapiens,Human,KIAA0931,PH domain leucine-rich repeat-containing protein phosphatase 2,PH domain leucine-rich repeat-containing protein phosphatase-like,PHLPP2,PHLPPL,PHLPP-like
25-030 ZC3H7B is a protein that contains a tetratricopeptide repeat domain. The encoded protein also interacts with the rotavirus non-structural protein NSP3. This gene encodes a protein that contains a tetr 0.05 mg
EIAAB44425 DCRR1,E3 ubiquitin-protein ligase TTC3,Homo sapiens,Human,Protein DCRR1,RING finger protein 105,RNF105,Tetratricopeptide repeat protein 3,TPR repeat protein 3,TPR repeat protein D,TPRD,TTC3
EIAAB41359 Homo sapiens,Human,KIAA1728,Protein TANC1,TANC1,Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1
EIAAB41360 Homo sapiens,Human,KIAA1148,KIAA1636,Protein TANC2,TANC2,Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 2
EIAAB41361 Kiaa1148,Mouse,Mus musculus,Protein TANC2,Tanc2,Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 2
EIAAB41358 Mouse,Mus musculus,Protein TANC1,Tanc1,Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1
EIAAB30919 Mouse,Mus musculus,PH domain leucine-rich repeat-containing protein phosphatase 2,PH domain leucine-rich repeat-containing protein phosphatase-like,Phlpp2,Phlppl,PHLPP-like
EIAAB46122 FENS-1,Homo sapiens,Human,KIAA1435,Phosphoinositide-binding protein 1,WD repeat and FYVE domain-containing protein 1,WD40- and FYVE domain-containing protein 1,WDF1,WDFY1,ZFYVE17,Zinc finger FYVE doma


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur