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F-box/WD repeat-containing protein 7 (Archipelago homolog) (hAgo) (F-box and WD-40 domain-containing protein 7) (F-box protein FBX30) (SEL-10) (hCdc4)

 FBXW7_HUMAN             Reviewed;         707 AA.
Q969H0; B7ZLP9; Q68DR0; Q96A16; Q96LE0; Q96RI2; Q9NUX6;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
10-OCT-2018, entry version 170.
RecName: Full=F-box/WD repeat-containing protein 7 {ECO:0000305};
AltName: Full=Archipelago homolog {ECO:0000303|PubMed:11565033};
Short=hAgo {ECO:0000303|PubMed:11565033};
AltName: Full=F-box and WD-40 domain-containing protein 7 {ECO:0000305};
AltName: Full=F-box protein FBX30 {ECO:0000305|PubMed:10531037};
AltName: Full=SEL-10 {ECO:0000303|PubMed:12354302};
AltName: Full=hCdc4 {ECO:0000303|PubMed:11565034};
Name=FBXW7 {ECO:0000312|HGNC:HGNC:16712};
Synonyms=FBW7 {ECO:0000312|EMBL:AAK57547.1},
FBX30 {ECO:0000312|EMBL:AAK60269.1},
SEL10 {ECO:0000312|EMBL:AAL07271.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=10531037; DOI=10.1016/S0960-9822(00)80021-4;
Winston J.T., Koepp D.M., Zhu C., Elledge S.J., Harper J.W.;
"A family of mammalian F-box proteins.";
Curr. Biol. 9:1180-1182(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS CYS-465
AND LEU-505.
PubMed=11565033; DOI=10.1038/35095068;
Moberg K.H., Bell D.W., Wahrer D.C.R., Haber D.A., Hariharan I.K.;
"Archipelago regulates cyclin E levels in Drosophila and is mutated in
human cancer cell lines.";
Nature 413:311-316(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN
SCF COMPLEX, AND INTERACTION WITH CYCLIN E.
PubMed=11565034; DOI=10.1038/35095076;
Strohmaier H., Spruck C.H., Kaiser P., Won K.-A., Sangfelt O.,
Reed S.I.;
"Human F-box protein hCdc4 targets cyclin E for proteolysis and is
mutated in a breast cancer cell line.";
Nature 413:316-322(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY,
AND INTERACTION WITH PSEN1.
PubMed=12354302; DOI=10.1046/j.1471-4159.2002.01105.x;
Li J., Pauley A.M., Myers R.L., Shuang R., Brashler J.R., Yan R.,
Buhl A.E., Ruble C., Gurney M.E.;
"SEL-10 interacts with presenilin 1, facilitates its ubiquitination,
and alters A-beta peptide production.";
J. Neurochem. 82:1540-1548(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Salivary gland;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND PARTIAL
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
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).
[7]
PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
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).
[8]
FUNCTION, AND INTERACTION WITH NOTCH1; NOTCH4 AND SKP1.
PubMed=11585921; DOI=10.1128/MCB.21.21.7403-7415.2001;
Wu G., Lyapina S., Das I., Li J., Gurney M., Pauley A., Chui I.,
Deshaies R.J., Kitajewski J.;
"SEL-10 is an inhibitor of notch signaling that targets notch for
ubiquitin-mediated protein degradation.";
Mol. Cell. Biol. 21:7403-7415(2001).
[9]
FUNCTION, COMPONENT OF THE SCF(FBXW7) COMPLEX, AND INTERACTION WITH
MYC.
PubMed=15103331; DOI=10.1038/sj.emboj.7600217;
Yada M., Hatakeyama S., Kamura T., Nishiyama M., Tsunematsu R.,
Imaki H., Ishida N., Okumura F., Nakayama K., Nakayama K.I.;
"Phosphorylation-dependent degradation of c-Myc is mediated by the F-
box protein Fbw7.";
EMBO J. 23:2116-2125(2004).
[10]
FUNCTION, AND INTERACTION WITH JUN.
PubMed=14739463; DOI=10.1126/science.1092880;
Nateri A.S., Riera-Sans L., Da Costa C., Behrens A.;
"The ubiquitin ligase SCFFbw7 antagonizes apoptotic JNK signaling.";
Science 303:1374-1378(2004).
[11]
INTERACTION WITH SV40 LARGE T ANTIGEN (MICROBIAL INFECTION).
PubMed=15611062; DOI=10.1074/jbc.M413377200;
Welcker M., Clurman B.E.;
"The SV40 large T antigen contains a decoy phosphodegron that mediates
its interactions with Fbw7/hCdc4.";
J. Biol. Chem. 280:7654-7658(2005).
[12]
FUNCTION, AND INTERACTION WITH MYC AND USP28.
PubMed=17873522; DOI=10.4161/cc.6.19.4804;
Popov N., Herold S., Llamazares M., Schulein C., Eilers M.;
"Fbw7 and Usp28 regulate myc protein stability in response to DNA
damage.";
Cell Cycle 6:2327-2331(2007).
[13]
FUNCTION, INTERACTION WITH MYC AND USP28, AND SUBCELLULAR LOCATION.
PubMed=17558397; DOI=10.1038/ncb1601;
Popov N., Wanzel M., Madiredjo M., Zhang D., Beijersbergen R.,
Bernards R., Moll R., Elledge S.J., Eilers M.;
"The ubiquitin-specific protease USP28 is required for MYC
stability.";
Nat. Cell Biol. 9:765-774(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[15]
PHOSPHORYLATION AT SER-227 BY SGK1, AND INTERACTION WITH SGK1 AND
NOTCH1.
PubMed=21147854; DOI=10.1242/jcs.073924;
Mo J.S., Ann E.J., Yoon J.H., Jung J., Choi Y.H., Kim H.Y., Ahn J.S.,
Kim S.M., Kim M.Y., Hong J.A., Seo M.S., Lang F., Choi E.J.,
Park H.S.;
"Serum- and glucocorticoid-inducible kinase 1 (SGK1) controls Notch1
signaling by downregulation of protein stability through Fbw7
ubiquitin ligase.";
J. Cell Sci. 124:100-112(2011).
[16]
FUNCTION, HOMODIMERIZATION, INTERACTION WITH JUN AND PIN1,
PHOSPHORYLATION AT THR-205, UBIQUITINATION, AND MUTAGENESIS OF
SER-159; THR-205; SER-349 AND SER-372.
PubMed=22608923; DOI=10.1016/j.molcel.2012.04.012;
Min S.H., Lau A.W., Lee T.H., Inuzuka H., Wei S., Huang P., Shaik S.,
Lee D.Y., Finn G., Balastik M., Chen C.H., Luo M., Tron A.E.,
Decaprio J.A., Zhou X.Z., Wei W., Lu K.P.;
"Negative regulation of the stability and tumor suppressor function of
Fbw7 by the Pin1 prolyl isomerase.";
Mol. Cell 46:771-783(2012).
[17]
FUNCTION, AND SUBUNIT.
PubMed=22748924; DOI=10.1016/j.molcel.2012.05.044;
Duda D.M., Olszewski J.L., Tron A.E., Hammel M., Lambert L.J.,
Waddell M.B., Mittag T., DeCaprio J.A., Schulman B.A.;
"Structure of a glomulin-RBX1-CUL1 complex: inhibition of a RING E3
ligase through masking of its E2-binding surface.";
Mol. Cell 47:371-382(2012).
[18]
INTERACTION WITH STOML1.
PubMed=23082202; DOI=10.1371/journal.pone.0047736;
Zhang W., MacDonald E.M., Koepp D.M.;
"The stomatin-like protein SLP-1 and Cdk2 interact with the F-Box
protein Fbw7-gamma.";
PLoS ONE 7:E47736-E47736(2012).
[19]
INTERACTION WITH UBE2QL1.
PubMed=24000165; DOI=10.1002/humu.22433;
Wake N.C., Ricketts C.J., Morris M.R., Prigmore E., Gribble S.M.,
Skytte A.B., Brown M., Clarke N., Banks R.E., Hodgson S.,
Turnell A.S., Maher E.R., Woodward E.R.;
"UBE2QL1 is disrupted by a constitutional translocation associated
with renal tumor predisposition and is a novel candidate renal tumor
suppressor gene.";
Hum. Mutat. 34:1650-1661(2013).
[20]
INTERACTION WITH FAM83D.
PubMed=24344117;
Wang Z., Liu Y., Zhang P., Zhang W., Wang W., Curr K., Wei G.,
Mao J.H.;
"FAM83D promotes cell proliferation and motility by downregulating
tumor suppressor gene FBXW7.";
Oncotarget 4:2476-2486(2013).
[21]
FUNCTION (ISOFORM 3), INTERACTION WITH MYC AND USP28 (ISOFORM 3), AND
SUBCELLULAR LOCATION (ISOFORM 3).
PubMed=25775507; DOI=10.1073/pnas.1411713112;
Sun X.X., He X., Yin L., Komada M., Sears R.C., Dai M.S.;
"The nucleolar ubiquitin-specific protease USP36 deubiquitinates and
stabilizes c-Myc.";
Proc. Natl. Acad. Sci. U.S.A. 112:3734-3739(2015).
[22]
IDENTIFICATION IN COMPLEX WITH JUN AND PRR7, AND INTERACTION WITH JUN
AND PRR7.
PubMed=27458189; DOI=10.15252/embj.201593070;
Kravchick D.O., Karpova A., Hrdinka M., Lopez-Rojas J., Iacobas S.,
Carbonell A.U., Iacobas D.A., Kreutz M.R., Jordan B.A.;
"Synaptonuclear messenger PRR7 inhibits c-Jun ubiquitination and
regulates NMDA-mediated excitotoxicity.";
EMBO J. 35:1923-1934(2016).
[23]
INTERACTION WITH MYCN.
PubMed=27837025; DOI=10.1073/PNAS.1610626113;
Richards M.W., Burgess S.G., Poon E., Carstensen A., Eilers M.,
Chesler L., Bayliss R.;
"Structural basis of N-Myc binding by Aurora-A and its destabilization
by kinase inhibitors.";
Proc. Natl. Acad. Sci. U.S.A. 113:13726-13731(2016).
[24]
FUNCTION, INTERACTION WITH STYX, IDENTIFICATION IN THE SCF(FBXW7)
COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
SPECTROMETRY, AND CHARACTERIZATION OF VARIANT CYS-465.
PubMed=28007894; DOI=10.15252/embj.201694795;
Reiterer V., Figueras-Puig C., Le Guerroue F., Confalonieri S.,
Vecchi M., Jalapothu D., Kanse S.M., Deshaies R.J., Di Fiore P.P.,
Behrends C., Farhan H.;
"The pseudophosphatase STYX targets the F-box of FBXW7 and inhibits
SCFFBXW7 function.";
EMBO J. 36:260-273(2017).
[25]
FUNCTION, AND INTERACTION WITH NOTCH2.
PubMed=29149593; DOI=10.1016/j.molcel.2017.10.018;
Fukushima H., Shimizu K., Watahiki A., Hoshikawa S., Kosho T., Oba D.,
Sakano S., Arakaki M., Yamada A., Nagashima K., Okabe K., Fukumoto S.,
Jimi E., Bigas A., Nakayama K.I., Nakayama K., Aoki Y., Wei W.,
Inuzuka H.;
"NOTCH2 Hajdu-Cheney mutations escape SCFFBW7-dependent proteolysis to
promote osteoporosis.";
Mol. Cell 68:645-658(2017).
[26]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 263-707 IN COMPLEX WITH SKP1
AND CCNE1 PHOSPHORYLATED PEPTIDE, FUNCTION, DOMAIN, SUBUNIT, AND
MUTAGENESIS OF 252-ALA--ILE-257.
PubMed=17434132; DOI=10.1016/j.molcel.2007.02.022;
Hao B., Oehlmann S., Sowa M.E., Harper J.W., Pavletich N.P.;
"Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated
substrate recognition by SCF ubiquitin ligases.";
Mol. Cell 26:131-143(2007).
[27] {ECO:0000244|PDB:5IBK}
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 263-323 IN COMPLEX WITH
SKIP1 AND UBIQUITIN, FUNCTION, AND SUBUNIT.
PubMed=26976582; DOI=10.1073/pnas.1519389113;
Gorelik M., Orlicky S., Sartori M.A., Tang X., Marcon E., Kurinov I.,
Greenblatt J.F., Tyers M., Moffat J., Sicheri F., Sidhu S.S.;
"Inhibition of SCF ubiquitin ligases by engineered ubiquitin variants
that target the Cul1 binding site on the Skp1-F-box interface.";
Proc. Natl. Acad. Sci. U.S.A. 113:3527-3532(2016).
[28] {ECO:0000244|PDB:5V4B}
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 263-706 IN COMPLEX WITH
SKIP1 AND DISC1 PEPTIDE, AND FUNCTION.
PubMed=28727686; DOI=10.1038/mp.2017.138;
Yalla K., Elliott C., Day J.P., Findlay J., Barratt S., Hughes Z.A.,
Wilson L., Whiteley E., Popiolek M., Li Y., Dunlop J., Killick R.,
Adams D.R., Brandon N.J., Houslay M.D., Hao B., Baillie G.S.;
"FBXW7 regulates DISC1 stability via the ubiquitin-proteosome
system.";
Mol. Psychiatry 23:1278-1286(2018).
[29]
VARIANTS [LARGE SCALE ANALYSIS] HIS-465; LEU-505 AND LEU-582.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[30]
VARIANT LYS-117.
PubMed=17224074; DOI=10.1186/bcr1637;
Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A.,
Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S.,
Kristensen V., Perou C.M., Boerresen-Dale A.-L.;
"Somatic sequence alterations in twenty-one genes selected by
expression profile analysis of breast carcinomas.";
Breast Cancer Res. 9:R5-R5(2007).
-!- 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 and binds phosphorylated
sites/phosphodegrons within target proteins and thereafter bring
them to the SCF complex for ubiquitination (PubMed:22748924,
PubMed:17434132, PubMed:26976582, PubMed:28727686). Identified
substrates include cyclin-E (CCNE1 or CCNE2), DISC1, JUN, MYC,
NOTCH1 released notch intracellular domain (NICD), NOTCH2, MCL1,
and probably PSEN1 (PubMed:11565034, PubMed:12354302,
PubMed:11585921, PubMed:15103331, PubMed:14739463,
PubMed:17558397, PubMed:17873522, PubMed:22608923,
PubMed:22748924, PubMed:29149593, PubMed:25775507,
PubMed:28007894, PubMed:26976582, PubMed:28727686). Acts as a
negative regulator of JNK signaling by binding to phosphorylated
JUN and promoting its ubiquitination and subsequent degradation
(PubMed:14739463). SCF(FBXW7) complex mediates the ubiquitination
and subsequent degradation of NFE2L1 (By similarity). Involved in
bone homeostasis and negative regulation of osteoclast
differentiation (PubMed:29149593). {ECO:0000250|UniProtKB:Q8VBV4,
ECO:0000269|PubMed:11565034, ECO:0000269|PubMed:11585921,
ECO:0000269|PubMed:14739463, ECO:0000269|PubMed:15103331,
ECO:0000269|PubMed:17434132, ECO:0000269|PubMed:17558397,
ECO:0000269|PubMed:17873522, ECO:0000269|PubMed:22608923,
ECO:0000269|PubMed:22748924, ECO:0000269|PubMed:25775507,
ECO:0000269|PubMed:26976582, ECO:0000269|PubMed:28007894,
ECO:0000269|PubMed:28727686, ECO:0000269|PubMed:29149593,
ECO:0000305|PubMed:12354302}.
-!- SUBUNIT: Homodimer; homodimerization plays a role in substrate
binding and/or ubiquitination and degradation (PubMed:22608923,
PubMed:17434132, PubMed:28007894). Component of the SCF(FBXW7)
complex consisting of CUL1, RBX1, SKP1 and FBXW7 (PubMed:11565034,
PubMed:15103331, PubMed:22748924, PubMed:28007894,
PubMed:26976582, PubMed:28727686). Interacts (via F-box domain)
with SKP1 (PubMed:11585921, PubMed:17434132, PubMed:28007894,
PubMed:26976582, PubMed:28727686). Interacts (via F-box domain)
with pseudophosphatase STYX; the interaction is direct and
prevents FBXW7 interaction with SKP1 (PubMed:28007894). Interacts
with cyclin-E (CCNE1 or CCNE2) (PubMed:11565034, PubMed:17434132).
Interacts with PSEN1 (PubMed:12354302). Forms a trimeric complex
with NOTCH1 and SGK1 (PubMed:21147854). Interacts with NOTCH1
intracellular domain/NICD and NOTCH4 intracellular domain/NICD
(PubMed:11585921). Interacts with NOTCH2 intracellular domain
(N2ICD) (PubMed:29149593). Interacts with MYC (when
phosphorylated) (PubMed:17873522, PubMed:25775507,
PubMed:28007894). Interacts with USP28, leading to counteract
ubiquitination of MYC (PubMed:17873522). Interacts with JUN
(PubMed:14739463, PubMed:22608923). Found in a complex with JUN
and PRR7 (PubMed:27458189). Interacts with JUN and PRR7; the
interaction inhibits ubiquitination-mediated JUN degradation
promoting its phosphorylation and transcriptional activity
(PubMed:27458189). Interacts (when phosphorylated at Thr-205) with
PIN1, leading to disrupt FBXW7 dimerization and promoting FBXW7
autoubiquitination and degradation (PubMed:22608923). Interacts
with UBE2QL1 (PubMed:24000165). Interacts with FAM83D; promotes
FBXW7 degradation (PubMed:24344117). Interacts with MYCN; FBXW7
competes with AURKA for binding to unphosphorylated MYCN but not
for binding to phosphorylated MYCN (PubMed:27837025). Interacts
with STOML1 (PubMed:23082202). Interacts with NFE2L1 (By
similarity). Interacts with USP36, leading to counteract
ubiquitination of MYC (PubMed:25775507).
{ECO:0000250|UniProtKB:Q8VBV4, ECO:0000269|PubMed:11565034,
ECO:0000269|PubMed:11585921, ECO:0000269|PubMed:12354302,
ECO:0000269|PubMed:14739463, ECO:0000269|PubMed:15103331,
ECO:0000269|PubMed:15611062, ECO:0000269|PubMed:17434132,
ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:17873522,
ECO:0000269|PubMed:21147854, ECO:0000269|PubMed:22608923,
ECO:0000269|PubMed:23082202, ECO:0000269|PubMed:24000165,
ECO:0000269|PubMed:24344117, ECO:0000269|PubMed:27458189,
ECO:0000269|PubMed:27837025, ECO:0000269|PubMed:28007894,
ECO:0000269|PubMed:29149593}.
-!- SUBUNIT: (Microbial infection) Interacts (via WD repeats) with
SV40 large T antigen (via CPD region).
{ECO:0000269|PubMed:15611062}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-359574, EBI-359574;
Q91LX9:- (xeno); NbExp=5; IntAct=EBI-359574, EBI-15662601;
Q16204:CCDC6; NbExp=9; IntAct=EBI-359574, EBI-1045350;
P24941:CDK2; NbExp=2; IntAct=EBI-6502391, EBI-375096;
Q9Z0Z7:Klf5 (xeno); NbExp=2; IntAct=EBI-359574, EBI-647919;
P01106:MYC; NbExp=4; IntAct=EBI-359574, EBI-447544;
P46531:NOTCH1; NbExp=10; IntAct=EBI-359574, EBI-636374;
P63208:SKP1; NbExp=5; IntAct=EBI-359574, EBI-307486;
P63208-1:SKP1; NbExp=2; IntAct=EBI-359574, EBI-307497;
Q9UBI4:STOML1; NbExp=3; IntAct=EBI-6502391, EBI-2681162;
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus, nucleoplasm
{ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:25775507,
ECO:0000269|PubMed:28007894}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:28007894}.
-!- SUBCELLULAR LOCATION: Isoform 3: Nucleus, nucleolus
{ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:25775507,
ECO:0000269|PubMed:28007894}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Archipelago alpha, FBW7alpha
{ECO:0000303|PubMed:17873522, ECO:0000303|PubMed:25775507}, 110K,
common;
IsoId=Q969H0-1; Sequence=Displayed;
Name=2; Synonyms=Archipelago beta, FBW7beta
{ECO:0000303|PubMed:17873522}, 69K;
IsoId=Q969H0-2; Sequence=VSP_009483, VSP_009484;
Note=Ref.6 (AAH37320) sequence is in conflict in position:
7:G->V. Ref.7 (BAA91986) sequence is in conflict in position:
50:L->I.;
Name=3; Synonyms=Archipelago gamma, FBW7gamma
{ECO:0000303|PubMed:17873522, ECO:0000303|PubMed:25775507},
Hippocampal;
IsoId=Q969H0-4; Sequence=VSP_009482, VSP_009485;
-!- TISSUE SPECIFICITY: Isoform 1 is widely expressed. Isoform 3 is
expressed in brain. {ECO:0000269|PubMed:12354302}.
-!- DOMAIN: The WD repeats mediate interaction with substrates of the
SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex.
{ECO:0000269|PubMed:17434132}.
-!- DOMAIN: The F-box domain mediates interaction with SKP1.
{ECO:0000269|PubMed:17434132, ECO:0000269|PubMed:28007894}.
-!- PTM: Phosphorylation at Thr-205 promotes interaction with PIN1,
leading to disrupt FBXW7 dimerization and promoting FBXW7
autoubiquitination and degradation (PubMed:22608923).
{ECO:0000269|PubMed:22608923}.
-!- PTM: Ubiquitinated: autoubiquitinates following phosphorylation at
Thr-205 and subsequent interaction with PIN1. Ubiquitination leads
to its proteasomal degradation (PubMed:22608923).
{ECO:0000269|PubMed:22608923}.
-!- SEQUENCE CAUTION:
Sequence=BAA91986.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY033553; AAK57547.1; -; mRNA.
EMBL; AF383178; AAK60269.1; -; mRNA.
EMBL; AF411971; AAL06290.1; -; mRNA.
EMBL; AF411972; AAL06291.1; -; mRNA.
EMBL; AY049984; AAL07271.1; -; mRNA.
EMBL; AY008274; AAG16640.1; -; mRNA.
EMBL; CR749305; CAH18160.1; -; mRNA.
EMBL; BC037320; AAH37320.1; -; mRNA.
EMBL; BC117244; AAI17245.1; -; mRNA.
EMBL; BC117246; AAI17247.1; -; mRNA.
EMBL; BC143944; AAI43945.1; -; mRNA.
EMBL; AK001933; BAA91986.1; ALT_INIT; mRNA.
CCDS; CCDS34078.1; -. [Q969H0-4]
CCDS; CCDS3777.1; -. [Q969H0-1]
CCDS; CCDS3778.1; -. [Q969H0-2]
RefSeq; NP_001013433.1; NM_001013415.1. [Q969H0-4]
RefSeq; NP_060785.2; NM_018315.4. [Q969H0-2]
RefSeq; NP_361014.1; NM_033632.3. [Q969H0-1]
RefSeq; XP_011530385.1; XM_011532083.1.
RefSeq; XP_011530386.1; XM_011532084.1. [Q969H0-1]
RefSeq; XP_011530387.1; XM_011532085.1. [Q969H0-1]
RefSeq; XP_016863851.1; XM_017008362.1.
UniGene; Hs.561245; -.
UniGene; Hs.717081; -.
PDB; 2OVP; X-ray; 2.90 A; B=263-707.
PDB; 2OVQ; X-ray; 2.60 A; B=263-707.
PDB; 2OVR; X-ray; 2.50 A; B=263-707.
PDB; 5IBK; X-ray; 2.50 A; B/E=263-323.
PDB; 5V4B; X-ray; 2.60 A; B=263-706.
PDBsum; 2OVP; -.
PDBsum; 2OVQ; -.
PDBsum; 2OVR; -.
PDBsum; 5IBK; -.
PDBsum; 5V4B; -.
ProteinModelPortal; Q969H0; -.
SMR; Q969H0; -.
BioGrid; 120581; 321.
CORUM; Q969H0; -.
DIP; DIP-27613N; -.
ELM; Q969H0; -.
IntAct; Q969H0; 49.
MINT; Q969H0; -.
STRING; 9606.ENSP00000281708; -.
iPTMnet; Q969H0; -.
PhosphoSitePlus; Q969H0; -.
BioMuta; FBXW7; -.
DMDM; 44887885; -.
EPD; Q969H0; -.
MaxQB; Q969H0; -.
PaxDb; Q969H0; -.
PeptideAtlas; Q969H0; -.
PRIDE; Q969H0; -.
ProteomicsDB; 75759; -.
ProteomicsDB; 75760; -. [Q969H0-2]
ProteomicsDB; 75762; -. [Q969H0-4]
DNASU; 55294; -.
Ensembl; ENST00000263981; ENSP00000263981; ENSG00000109670. [Q969H0-2]
Ensembl; ENST00000281708; ENSP00000281708; ENSG00000109670. [Q969H0-1]
Ensembl; ENST00000296555; ENSP00000296555; ENSG00000109670. [Q969H0-4]
Ensembl; ENST00000393956; ENSP00000377528; ENSG00000109670. [Q969H0-2]
Ensembl; ENST00000603548; ENSP00000474725; ENSG00000109670. [Q969H0-1]
Ensembl; ENST00000603841; ENSP00000474971; ENSG00000109670. [Q969H0-1]
GeneID; 55294; -.
KEGG; hsa:55294; -.
UCSC; uc003imq.4; human. [Q969H0-1]
CTD; 55294; -.
DisGeNET; 55294; -.
EuPathDB; HostDB:ENSG00000109670.13; -.
GeneCards; FBXW7; -.
HGNC; HGNC:16712; FBXW7.
HPA; CAB013793; -.
HPA; CAB029987; -.
MIM; 606278; gene.
neXtProt; NX_Q969H0; -.
OpenTargets; ENSG00000109670; -.
PharmGKB; PA28054; -.
eggNOG; KOG0274; Eukaryota.
eggNOG; ENOG410XRWX; LUCA.
GeneTree; ENSGT00760000119106; -.
HOVERGEN; HBG051596; -.
InParanoid; Q969H0; -.
KO; K10260; -.
OMA; VWRVAFE; -.
OrthoDB; EOG091G04EW; -.
PhylomeDB; Q969H0; -.
TreeFam; TF101074; -.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2644607; Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q969H0; -.
SIGNOR; Q969H0; -.
ChiTaRS; FBXW7; human.
EvolutionaryTrace; Q969H0; -.
GeneWiki; FBXW7; -.
GenomeRNAi; 55294; -.
PRO; PR:Q969H0; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000109670; Expressed in 239 organ(s), highest expression level in corpus callosum.
CleanEx; HS_FBXW7; -.
ExpressionAtlas; Q969H0; baseline and differential.
Genevisible; Q969H0; HS.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:1990452; C:Parkin-FBXW7-Cul1 ubiquitin ligase complex; IPI:ParkinsonsUK-UCL.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0030332; F:cyclin binding; IDA:ParkinsonsUK-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0050816; F:phosphothreonine residue binding; IDA:UniProtKB.
GO; GO:0030674; F:protein binding, bridging; IDA:ParkinsonsUK-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IDA:ParkinsonsUK-UCL.
GO; GO:0004842; F:ubiquitin-protein transferase activity; EXP:Reactome.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
GO; GO:0055088; P:lipid homeostasis; ISS:BHF-UCL.
GO; GO:0032876; P:negative regulation of DNA endoreduplication; IMP:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
GO; GO:2000346; P:negative regulation of hepatocyte proliferation; ISS:BHF-UCL.
GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:BHF-UCL.
GO; GO:2001205; P:negative regulation of osteoclast development; IMP:UniProtKB.
GO; GO:2000639; P:negative regulation of SREBP signaling pathway; ISS:BHF-UCL.
GO; GO:0010868; P:negative regulation of triglyceride biosynthetic process; ISS:BHF-UCL.
GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; IDA:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
GO; GO:1903378; P:positive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IDA:ParkinsonsUK-UCL.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:ARUK-UCL.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; TAS:ParkinsonsUK-UCL.
GO; GO:0010883; P:regulation of lipid storage; ISS:BHF-UCL.
GO; GO:0032880; P:regulation of protein localization; ISS:BHF-UCL.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0007062; P:sister chromatid cohesion; IMP:BHF-UCL.
GO; GO:0001944; P:vasculature development; TAS:BHF-UCL.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR036047; F-box-like_dom_sf.
InterPro; IPR001810; F-box_dom.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF12937; F-box-like; 1.
Pfam; PF00400; WD40; 7.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00256; FBOX; 1.
SMART; SM00320; WD40; 8.
SUPFAM; SSF50978; SSF50978; 1.
SUPFAM; SSF81383; SSF81383; 1.
PROSITE; PS50181; FBOX; 1.
PROSITE; PS00678; WD_REPEATS_1; 5.
PROSITE; PS50082; WD_REPEATS_2; 7.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Host-virus interaction; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway;
WD repeat.
CHAIN 1 707 F-box/WD repeat-containing protein 7.
/FTId=PRO_0000050994.
DOMAIN 278 324 F-box. {ECO:0000255|PROSITE-
ProRule:PRU00080}.
REPEAT 378 418 WD 1.
REPEAT 420 456 WD 2.
REPEAT 459 498 WD 3.
REPEAT 500 536 WD 4.
REPEAT 539 578 WD 5.
REPEAT 580 618 WD 6.
REPEAT 622 659 WD 7.
MOD_RES 205 205 Phosphothreonine.
{ECO:0000269|PubMed:22608923}.
MOD_RES 227 227 Phosphoserine; by SGK1.
{ECO:0000269|PubMed:21147854}.
VAR_SEQ 1 118 Missing (in isoform 3).
{ECO:0000303|PubMed:12354302}.
/FTId=VSP_009482.
VAR_SEQ 1 80 Missing (in isoform 2).
{ECO:0000303|PubMed:10531037,
ECO:0000303|PubMed:11565033}.
/FTId=VSP_009483.
VAR_SEQ 81 166 NNRFISVDEDSSGNQEEQEEDEEHAGEQDEEDEEEEEMDQE
SDDFDQSDDSSREDEHTHTNSVTNSSSIVDLPVHQLSSPFY
TKTT -> MCVPRSGLILSCICLYCGVLLPVLLPNLPFLTC
LSMSTLESVTYLPEKGLYCQRLPSSRTHGGTESLKGKNTEN
MGFYGTLKMIFY (in isoform 2).
{ECO:0000303|PubMed:10531037,
ECO:0000303|PubMed:11565033}.
/FTId=VSP_009484.
VAR_SEQ 119 167 DQESDDFDQSDDSSREDEHTHTNSVTNSSSIVDLPVHQLSS
PFYTKTTK -> MSKPGKPTLNHGLVPVDLKSAKEPLPHQT
VMKIFSISIIAQGLPFCRRR (in isoform 3).
{ECO:0000303|PubMed:12354302}.
/FTId=VSP_009485.
VARIANT 115 115 E -> K (in dbSNP:rs6816935).
/FTId=VAR_017812.
VARIANT 117 117 E -> K (in a breast cancer sample;
somatic mutation; dbSNP:rs991177157).
{ECO:0000269|PubMed:17224074}.
/FTId=VAR_033030.
VARIANT 133 133 R -> G (in dbSNP:rs6842544).
/FTId=VAR_017813.
VARIANT 144 144 T -> R (in dbSNP:rs7660281).
/FTId=VAR_017814.
VARIANT 465 465 R -> C (in an acute lymphoblastic
leukemia cell line; loss of interaction
with substrate; does not affect
interaction with SKP1 or STYX;
dbSNP:rs867384286).
{ECO:0000269|PubMed:11565033,
ECO:0000269|PubMed:28007894}.
/FTId=VAR_017815.
VARIANT 465 465 R -> H (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035880.
VARIANT 505 505 R -> L (in an ovarian cancer cell line;
dbSNP:rs1057519896).
{ECO:0000269|PubMed:11565033,
ECO:0000269|PubMed:16959974}.
/FTId=VAR_017816.
VARIANT 582 582 S -> L (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035881.
VARIANT 668 668 S -> G (in dbSNP:rs7679116).
/FTId=VAR_017817.
MUTAGEN 159 159 S->A: Does not affect interaction with
PIN1. {ECO:0000269|PubMed:22608923}.
MUTAGEN 205 205 T->A: Impaired interaction with PIN1.
{ECO:0000269|PubMed:22608923}.
MUTAGEN 252 257 ALDELI->DDDEDD: Prevents
homodimerization.
{ECO:0000269|PubMed:17434132}.
MUTAGEN 349 349 S->A: Does not affect interaction with
PIN1. {ECO:0000269|PubMed:22608923}.
MUTAGEN 372 372 S->A: Does not affect interaction with
PIN1. {ECO:0000269|PubMed:22608923}.
CONFLICT 344 344 P -> L (in Ref. 6; AAH37320).
{ECO:0000305}.
CONFLICT 377 377 K -> N (in Ref. 6; AAH37320).
{ECO:0000305}.
CONFLICT 508 508 Q -> R (in Ref. 6; AAH37320).
{ECO:0000305}.
HELIX 265 272 {ECO:0000244|PDB:2OVR}.
TURN 280 282 {ECO:0000244|PDB:2OVR}.
HELIX 286 293 {ECO:0000244|PDB:2OVR}.
HELIX 298 304 {ECO:0000244|PDB:2OVR}.
HELIX 309 315 {ECO:0000244|PDB:2OVR}.
HELIX 319 325 {ECO:0000244|PDB:2OVR}.
TURN 326 329 {ECO:0000244|PDB:2OVR}.
HELIX 350 367 {ECO:0000244|PDB:2OVR}.
STRAND 374 377 {ECO:0000244|PDB:2OVR}.
STRAND 384 390 {ECO:0000244|PDB:2OVR}.
STRAND 393 398 {ECO:0000244|PDB:2OVR}.
STRAND 403 407 {ECO:0000244|PDB:2OVR}.
TURN 408 410 {ECO:0000244|PDB:2OVR}.
STRAND 413 416 {ECO:0000244|PDB:2OVR}.
STRAND 424 430 {ECO:0000244|PDB:2OVR}.
STRAND 433 438 {ECO:0000244|PDB:2OVR}.
STRAND 443 447 {ECO:0000244|PDB:2OVR}.
TURN 448 451 {ECO:0000244|PDB:2OVR}.
STRAND 452 457 {ECO:0000244|PDB:2OVR}.
STRAND 464 470 {ECO:0000244|PDB:2OVR}.
STRAND 473 478 {ECO:0000244|PDB:2OVR}.
STRAND 481 490 {ECO:0000244|PDB:2OVR}.
STRAND 493 498 {ECO:0000244|PDB:2OVR}.
STRAND 504 509 {ECO:0000244|PDB:2OVR}.
STRAND 514 518 {ECO:0000244|PDB:2OVR}.
STRAND 523 527 {ECO:0000244|PDB:2OVR}.
HELIX 528 530 {ECO:0000244|PDB:2OVR}.
STRAND 532 537 {ECO:0000244|PDB:2OVR}.
STRAND 544 549 {ECO:0000244|PDB:2OVR}.
STRAND 551 558 {ECO:0000244|PDB:2OVR}.
STRAND 563 567 {ECO:0000244|PDB:2OVR}.
TURN 568 570 {ECO:0000244|PDB:2OVR}.
STRAND 573 577 {ECO:0000244|PDB:2OVR}.
STRAND 584 590 {ECO:0000244|PDB:2OVR}.
STRAND 593 598 {ECO:0000244|PDB:2OVR}.
STRAND 603 607 {ECO:0000244|PDB:2OVR}.
TURN 608 610 {ECO:0000244|PDB:2OVR}.
STRAND 613 617 {ECO:0000244|PDB:2OVR}.
STRAND 627 632 {ECO:0000244|PDB:2OVR}.
STRAND 634 641 {ECO:0000244|PDB:2OVR}.
STRAND 644 650 {ECO:0000244|PDB:2OVR}.
TURN 651 653 {ECO:0000244|PDB:2OVR}.
STRAND 656 662 {ECO:0000244|PDB:2OVR}.
HELIX 666 668 {ECO:0000244|PDB:2OVR}.
STRAND 671 677 {ECO:0000244|PDB:2OVR}.
STRAND 679 687 {ECO:0000244|PDB:2OVR}.
STRAND 689 693 {ECO:0000244|PDB:2OVR}.
STRAND 696 701 {ECO:0000244|PDB:2OVR}.
SEQUENCE 707 AA; 79663 MW; E4A357F76DFD8203 CRC64;
MNQELLSVGS KRRRTGGSLR GNPSSSQVDE EQMNRVVEEE QQQQLRQQEE EHTARNGEVV
GVEPRPGGQN DSQQGQLEEN NNRFISVDED SSGNQEEQEE DEEHAGEQDE EDEEEEEMDQ
ESDDFDQSDD SSREDEHTHT NSVTNSSSIV DLPVHQLSSP FYTKTTKMKR KLDHGSEVRS
FSLGKKPCKV SEYTSTTGLV PCSATPTTFG DLRAANGQGQ QRRRITSVQP PTGLQEWLKM
FQSWSGPEKL LALDELIDSC EPTQVKHMMQ VIEPQFQRDF ISLLPKELAL YVLSFLEPKD
LLQAAQTCRY WRILAEDNLL WREKCKEEGI DEPLHIKRRK VIKPGFIHSP WKSAYIRQHR
IDTNWRRGEL KSPKVLKGHD DHVITCLQFC GNRIVSGSDD NTLKVWSAVT GKCLRTLVGH
TGGVWSSQMR DNIIISGSTD RTLKVWNAET GECIHTLYGH TSTVRCMHLH EKRVVSGSRD
ATLRVWDIET GQCLHVLMGH VAAVRCVQYD GRRVVSGAYD FMVKVWDPET ETCLHTLQGH
TNRVYSLQFD GIHVVSGSLD TSIRVWDVET GNCIHTLTGH QSLTSGMELK DNILVSGNAD
STVKIWDIKT GQCLQTLQGP NKHQSAVTCL QFNKNFVITS SDDGTVKLWD LKTGEFIRNL
VTLESGGSGG VVWRIRASNT KLVCAVGSRN GTEETKLLVL DFDVDMK


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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
EIAAB34424 Constitutive photomorphogenesis protein 1 homolog,COP1,E3 ubiquitin-protein ligase RFWD2,hCOP1,Homo sapiens,Human,RFWD2,RING finger and WD repeat domain protein 2,RING finger protein 200,RNF200
EIAAB38308 Homo sapiens,Human,KIAA0862,Leucine-rich repeat protein SHOC-2,Protein soc-2 homolog,Protein sur-8 homolog,SHOC2
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
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
EIAAB38306 Leucine-rich repeat protein SHOC-2,Mouse,Mus musculus,Protein soc-2 homolog,Protein sur-8 homolog,Shoc2
EIAAB38310 Leucine-rich repeat protein SHOC-2,Protein soc-2 homolog,Protein sur-8 homolog,Rat,Rattus norvegicus,Shoc2
EIAAB38307 Bos taurus,Bovine,Leucine-rich repeat protein SHOC-2,Protein soc-2 homolog,Protein sur-8 homolog,SHOC2
EIAAB46338 Kiaa1971,Mouse,Mus musculus,WAS protein homology region 2 domain-containing protein 1,WASP homolog-associated protein with actin, membranes and microtubules,WH2 domain-containing protein 1,Whamm,Whdc1
EIAAB46339 Homo sapiens,Human,KIAA1971,WAS protein homology region 2 domain-containing protein 1,WASP homolog-associated protein with actin, membranes and microtubules,WH2 domain-containing protein 1,WHAMM,WHDC1
EIAAB38884 Brain-enriched WD repeat-containing protein,Bwd,Rat,Rattus norvegicus,Smu1,Smu-1 suppressor of mec-8 and unc-52 protein homolog,WD40 repeat-containing protein SMU1
EIAAB13053 CAG repeat protein 32,CAGH32,Domino homolog,E1A-binding protein p400,EP400,hDomino,Homo sapiens,Human,KIAA1498,KIAA1818,p400 kDa SWI2_SNF2-related protein,TNRC12,Trinucleotide repeat-containing gene 1


 

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