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F-box/WD repeat-containing protein 2 (F-box and WD-40 domain-containing protein 2) (Protein MD6)

 FBXW2_HUMAN             Reviewed;         454 AA.
Q9UKT8; B3KRL8; Q4VXH2; Q7Z4V6; Q8WV51; Q9HA09; Q9UKA3;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAR-2005, sequence version 2.
18-JUL-2018, entry version 177.
RecName: Full=F-box/WD repeat-containing protein 2;
AltName: Full=F-box and WD-40 domain-containing protein 2;
AltName: Full=Protein MD6;
Name=FBXW2; Synonyms=FBW2, FWD2;
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 1).
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).
Zhou Y., Yu L., Zhao S.Y.;
"Cloning and characterization of human MD6 protein.";
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Mammary gland;
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).
[4]
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Uterus;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-422 (ISOFORM 1), AND INTERACTION WITH
SKP1 AND CUL1.
PubMed=10531035; DOI=10.1016/S0960-9822(00)80020-2;
Cenciarelli C., Chiaur D.S., Guardavaccaro D., Parks W., Vidal M.,
Pagano M.;
"Identification of a family of human F-box proteins.";
Curr. Biol. 9:1177-1179(1999).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-298, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
-!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-
box protein)-type E3 ubiquitin ligase complex.
-!- SUBUNIT: Directly interacts with SKP1 and CUL1.
{ECO:0000269|PubMed:10531035}.
-!- INTERACTION:
Q16543:CDC37; NbExp=2; IntAct=EBI-914727, EBI-295634;
Q13616:CUL1; NbExp=2; IntAct=EBI-914727, EBI-359390;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-914727, EBI-352572;
Q9Y266:NUDC; NbExp=2; IntAct=EBI-914727, EBI-357298;
P63208:SKP1; NbExp=4; IntAct=EBI-914727, EBI-307486;
P63209:SKP1 (xeno); NbExp=2; IntAct=EBI-914727, EBI-7114014;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UKT8-1; Sequence=Displayed;
Name=2; Synonyms=MD6b;
IsoId=Q9UKT8-2; Sequence=VSP_012983;
-!- SEQUENCE CAUTION:
Sequence=AAF04465.1; Type=Frameshift; Positions=420; Evidence={ECO:0000305};
Sequence=AAF13226.1; Type=Frameshift; Positions=420; Evidence={ECO:0000305};
Sequence=AAP97276.1; Type=Frameshift; Positions=420; Evidence={ECO:0000305};
Sequence=AAP97280.1; Type=Frameshift; Positions=420; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF176698; AAF13226.1; ALT_FRAME; mRNA.
EMBL; AF145024; AAP97276.1; ALT_FRAME; mRNA.
EMBL; AF193594; AAP97280.1; ALT_FRAME; mRNA.
EMBL; AK022484; BAB14051.1; -; mRNA.
EMBL; AK091860; BAG52430.1; -; mRNA.
EMBL; AL161911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC018738; AAH18738.1; -; mRNA.
EMBL; BC110334; AAI10335.1; -; mRNA.
EMBL; AF129531; AAF04465.1; ALT_FRAME; mRNA.
CCDS; CCDS43872.1; -. [Q9UKT8-1]
RefSeq; NP_036296.2; NM_012164.3. [Q9UKT8-1]
RefSeq; XP_005251967.1; XM_005251910.3. [Q9UKT8-1]
RefSeq; XP_016870104.1; XM_017014615.1. [Q9UKT8-2]
UniGene; Hs.494985; -.
ProteinModelPortal; Q9UKT8; -.
BioGrid; 117603; 22.
CORUM; Q9UKT8; -.
DIP; DIP-37972N; -.
IntAct; Q9UKT8; 16.
MINT; Q9UKT8; -.
STRING; 9606.ENSP00000363036; -.
iPTMnet; Q9UKT8; -.
PhosphoSitePlus; Q9UKT8; -.
BioMuta; FBXW2; -.
DMDM; 60416443; -.
EPD; Q9UKT8; -.
PaxDb; Q9UKT8; -.
PeptideAtlas; Q9UKT8; -.
PRIDE; Q9UKT8; -.
ProteomicsDB; 84853; -.
ProteomicsDB; 84854; -. [Q9UKT8-2]
DNASU; 26190; -.
Ensembl; ENST00000608872; ENSP00000476369; ENSG00000119402. [Q9UKT8-1]
GeneID; 26190; -.
KEGG; hsa:26190; -.
UCSC; uc004bkm.2; human. [Q9UKT8-1]
CTD; 26190; -.
EuPathDB; HostDB:ENSG00000119402.16; -.
GeneCards; FBXW2; -.
HGNC; HGNC:13608; FBXW2.
HPA; HPA067878; -.
MIM; 609071; gene.
neXtProt; NX_Q9UKT8; -.
OpenTargets; ENSG00000119402; -.
PharmGKB; PA28052; -.
eggNOG; ENOG410IQD2; Eukaryota.
eggNOG; ENOG410XP3H; LUCA.
GeneTree; ENSGT00760000119106; -.
HOVERGEN; HBG051593; -.
InParanoid; Q9UKT8; -.
KO; K10261; -.
OMA; QTHTCAT; -.
OrthoDB; EOG091G060Z; -.
PhylomeDB; Q9UKT8; -.
TreeFam; TF333134; -.
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; Q9UKT8; -.
ChiTaRS; FBXW2; human.
GeneWiki; FBXW2; -.
GenomeRNAi; 26190; -.
PRO; PR:Q9UKT8; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000119402; -.
CleanEx; HS_FBXW2; -.
ExpressionAtlas; Q9UKT8; baseline and differential.
Genevisible; Q9UKT8; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0004842; F:ubiquitin-protein transferase activity; EXP:Reactome.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
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; 3.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00256; FBOX; 1.
SMART; SM00320; WD40; 5.
SUPFAM; SSF50978; SSF50978; 1.
SUPFAM; SSF81383; SSF81383; 1.
PROSITE; PS50181; FBOX; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 2.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome;
Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
CHAIN 1 454 F-box/WD repeat-containing protein 2.
/FTId=PRO_0000050988.
DOMAIN 54 101 F-box. {ECO:0000255|PROSITE-
ProRule:PRU00080}.
REPEAT 139 175 WD 1.
REPEAT 179 213 WD 2.
REPEAT 217 255 WD 3.
REPEAT 259 306 WD 4.
REPEAT 313 352 WD 5.
REPEAT 364 403 WD 6.
REPEAT 410 452 WD 7.
MOD_RES 298 298 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 164 228 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_012983.
CONFLICT 405 405 E -> G (in Ref. 3; BAB14051).
{ECO:0000305}.
CONFLICT 408 408 K -> E (in Ref. 1; AAF04465).
{ECO:0000305}.
SEQUENCE 454 AA; 51512 MW; F182998504BF2734 CRC64;
MERKDFETWL DNISVTFLSL TDLQKNETLD HLISLSGAVQ LRHLSNNLET LLKRDFLKLL
PLELSFYLLK WLDPQTLLTC CLVSKQWNKV ISACTEVWQT ACKNLGWQID DSVQDALHWK
KVYLKAILRM KQLEDHEAFE TSSLIGHSAR VYALYYKDGL LCTGSDDLSA KLWDVSTGQC
VYGIQTHTCA AVKFDEQKLV TGSFDNTVAC WEWSSGARTQ HFRGHTGAVF SVDYNDELDI
LVSGSADFTV KVWALSAGTC LNTLTGHTEW VTKVVLQKCK VKSLLHSPGD YILLSADKYE
IKIWPIGREI NCKCLKTLSV SEDRSICLQP RLHFDGKYIV CSSALGLYQW DFASYDILRV
IKTPEIANLA LLGFGDIFAL LFDNRYLYIM DLRTESLISR WPLPEYRKSK RGSSFLAGEA
SWLNGLDGHN DTGLVFATSM PDHSIHLVLW KEHG


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