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F-box/WD repeat-containing protein 8 (F-box and WD-40 domain-containing protein 8) (F-box only protein 29)

 FBXW8_HUMAN             Reviewed;         598 AA.
Q8N3Y1; Q9UK95;
03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
20-JUN-2018, entry version 154.
RecName: Full=F-box/WD repeat-containing protein 8;
AltName: Full=F-box and WD-40 domain-containing protein 8;
AltName: Full=F-box only protein 29;
Name=FBXW8; Synonyms=FBW6, FBW8, FBX29, FBXO29, FBXW6;
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), AND VARIANT GLN-192.
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 [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLN-192.
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).
[4]
IDENTIFICATION IN SCF-LIKE COMPLEX.
PubMed=12481031; DOI=10.1073/pnas.252646399;
Dias D.C., Dolios G., Wang R., Pan Z.Q.;
"CUL7: a DOC domain-containing cullin selectively binds Skp1.Fbx29 to
form an SCF-like complex.";
Proc. Natl. Acad. Sci. U.S.A. 99:16601-16606(2002).
[5]
IDENTIFICATION IN A COMPLEX WITH CUL7; SKP1; RBX1 AND GLMN.
PubMed=12904573; DOI=10.1073/pnas.1733908100;
Arai T., Kasper J.S., Skaar J.R., Ali S.H., Takahashi C.,
DeCaprio J.A.;
"Targeted disruption of p185/Cul7 gene results in abnormal vascular
morphogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 100:9855-9860(2003).
[6]
INTERACTION WITH CUL7.
PubMed=17332328; DOI=10.1158/0008-5472.CAN-06-3241;
Skaar J.R., Florens L., Tsutsumi T., Arai T., Tron A., Swanson S.K.,
Washburn M.P., DeCaprio J.A.;
"PARC and CUL7 form atypical cullin RING ligase complexes.";
Cancer Res. 67:2006-2014(2007).
[7]
FUNCTION, AND INTERACTION WITH IRS1.
PubMed=18498745; DOI=10.1016/j.molcel.2008.03.009;
Xu X., Sarikas A., Dias-Santagata D.C., Dolios G., Lafontant P.J.,
Tsai S.C., Zhu W., Nakajima H., Nakajima H.O., Field L.J., Wang R.,
Pan Z.Q.;
"The CUL7 E3 ubiquitin ligase targets insulin receptor substrate 1 for
ubiquitin-dependent degradation.";
Mol. Cell 30:403-414(2008).
[8]
FUNCTION, INTERACTION WITH OBSL1; CUL1; CUL2; CUL7; SKP1; CCT6B;
PFDN5; CCT2; CCT3; CCT6A; CCT7; VBP1; CCDC8; ARF1; TRIP13; PDCD5 AND
GORASP1, AND SUBCELLULAR LOCATION.
PubMed=21572988; DOI=10.1371/journal.pbio.1001060;
Litterman N., Ikeuchi Y., Gallardo G., O'Connell B.C., Sowa M.E.,
Gygi S.P., Harper J.W., Bonni A.;
"An OBSL1-Cul7Fbxw8 ubiquitin ligase signaling mechanism regulates
Golgi morphology and dendrite patterning.";
PLoS Biol. 9:E1001060-E1001060(2011).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[10]
FUNCTION, AND INTERACTION WITH CUL7 AND MAP4K1.
PubMed=24362026; DOI=10.1074/jbc.M113.520106;
Wang H., Chen Y., Lin P., Li L., Zhou G., Liu G., Logsdon C., Jin J.,
Abbruzzese J.L., Tan T.H., Wang H.;
"The CUL7/F-box and WD repeat domain containing 8 (CUL7/Fbxw8)
ubiquitin ligase promotes degradation of hematopoietic progenitor
kinase 1.";
J. Biol. Chem. 289:4009-4017(2014).
[11]
FUNCTION.
PubMed=24793695; DOI=10.1016/j.molcel.2014.03.047;
Yan J., Yan F., Li Z., Sinnott B., Cappell K.M., Yu Y., Mo J.,
Duncan J.A., Chen X., Cormier-Daire V., Whitehurst A.W., Xiong Y.;
"The 3M complex maintains microtubule and genome integrity.";
Mol. Cell 54:791-804(2014).
-!- FUNCTION: Substrate-recognition component of a Cul7-RING
ubiquitin-protein ligase complex, which mediates the
ubiquitination and subsequent proteasomal degradation of target
proteins. The Cul7-RING(FBXW8) complex mediates ubiquitination and
consequent degradation of GORASP1, acting as a component of the
ubiquitin ligase pathway that regulates Golgi morphogenesis and
dendrite patterning in brain (PubMed:21572988). Mediates
ubiquitination and degradation of IRS1 in a mTOR-dependent manner:
the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously
phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2)
(PubMed:18498745). The Cul7-RING(FBXW8) complex also mediates
ubiquitination of MAP4K1/HPK1: recognizes and binds
autophosphorylated MAP4K1/HPK1, leading to its degradation,
thereby affecting cell proliferation and differentiation
(PubMed:24362026). Associated component of the 3M complex,
suggesting that it mediates some of 3M complex functions
(PubMed:24793695). {ECO:0000269|PubMed:18498745,
ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24362026,
ECO:0000269|PubMed:24793695}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Part of a Cul7-RING ubiquitin-protein ligase complex,
consisting of CUL7, RBX1, SKP1 and FBXW8. Interacts with GLMN
isoform 1. Interacts with CUL7. Interacts with OBSL1, CUL1, CUL2,
SKP1, CCT6B, PFDN5, CCT2, CCT3, CCT6A, CCT7, VBP1, CCDC8, ARF1,
TRIP13, PDCD5 and GORASP1. Interacts with IRS1 (when
phosphorylated). Interacts with MAP4K1/HPK1 (when
autophosphorylated). Associated component of the 3M complex.
Interacts with POUF51 (when phosphorylated on 'Ser-355') (By
similarity). {ECO:0000250|UniProtKB:Q8BIA4,
ECO:0000269|PubMed:12481031, ECO:0000269|PubMed:12904573,
ECO:0000269|PubMed:17332328, ECO:0000269|PubMed:18498745,
ECO:0000269|PubMed:21572988, ECO:0000269|PubMed:24362026}.
-!- INTERACTION:
B1WBR1:Gorasp1 (xeno); NbExp=2; IntAct=EBI-15927105, EBI-15927064;
P01106:MYC; NbExp=3; IntAct=EBI-914770, EBI-447544;
P63208:SKP1; NbExp=2; IntAct=EBI-914770, EBI-307486;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
{ECO:0000269|PubMed:21572988}. Golgi apparatus
{ECO:0000269|PubMed:21572988}. Note=Colocalizes with CUL7 at the
Golgi apparatus in neurons. {ECO:0000250|UniProtKB:P0DL28}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8N3Y1-1; Sequence=Displayed;
Name=2;
IsoId=Q8N3Y1-2; Sequence=VSP_008501;
-!- SEQUENCE CAUTION:
Sequence=AAF03129.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAF03129.1; Type=Frameshift; Positions=282, 295; Evidence={ECO:0000305};
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EMBL; AF176707; AAF03129.1; ALT_SEQ; mRNA.
EMBL; AC026368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC083806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC127164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC037296; AAH37296.1; -; mRNA.
CCDS; CCDS44988.1; -. [Q8N3Y1-2]
CCDS; CCDS9182.1; -. [Q8N3Y1-1]
RefSeq; NP_036306.1; NM_012174.1. [Q8N3Y1-2]
RefSeq; NP_699179.2; NM_153348.2. [Q8N3Y1-1]
UniGene; Hs.624537; -.
UniGene; Hs.696428; -.
ProteinModelPortal; Q8N3Y1; -.
BioGrid; 117645; 52.
CORUM; Q8N3Y1; -.
DIP; DIP-37970N; -.
IntAct; Q8N3Y1; 20.
MINT; Q8N3Y1; -.
STRING; 9606.ENSP00000310686; -.
iPTMnet; Q8N3Y1; -.
PhosphoSitePlus; Q8N3Y1; -.
BioMuta; FBXW8; -.
DMDM; 296434513; -.
EPD; Q8N3Y1; -.
MaxQB; Q8N3Y1; -.
PaxDb; Q8N3Y1; -.
PeptideAtlas; Q8N3Y1; -.
PRIDE; Q8N3Y1; -.
ProteomicsDB; 71847; -.
ProteomicsDB; 71848; -. [Q8N3Y1-2]
Ensembl; ENST00000309909; ENSP00000310686; ENSG00000174989. [Q8N3Y1-1]
Ensembl; ENST00000455858; ENSP00000389144; ENSG00000174989. [Q8N3Y1-2]
GeneID; 26259; -.
KEGG; hsa:26259; -.
UCSC; uc001twf.2; human. [Q8N3Y1-1]
CTD; 26259; -.
DisGeNET; 26259; -.
EuPathDB; HostDB:ENSG00000174989.12; -.
GeneCards; FBXW8; -.
H-InvDB; HIX0026457; -.
H-InvDB; HIX0037115; -.
HGNC; HGNC:13597; FBXW8.
HPA; HPA038850; -.
HPA; HPA038851; -.
MIM; 609073; gene.
neXtProt; NX_Q8N3Y1; -.
OpenTargets; ENSG00000174989; -.
PharmGKB; PA28039; -.
eggNOG; ENOG410IQD1; Eukaryota.
eggNOG; ENOG4110ZIH; LUCA.
GeneTree; ENSGT00390000017221; -.
HOGENOM; HOG000112555; -.
HOVERGEN; HBG051597; -.
InParanoid; Q8N3Y1; -.
KO; K10264; -.
OMA; FEHDARI; -.
OrthoDB; EOG091G0KZ9; -.
PhylomeDB; Q8N3Y1; -.
TreeFam; TF332593; -.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q8N3Y1; -.
UniPathway; UPA00143; -.
ChiTaRS; FBXW8; human.
GeneWiki; FBXW8; -.
GenomeRNAi; 26259; -.
PRO; PR:Q8N3Y1; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000174989; -.
CleanEx; HS_FBXW8; -.
Genevisible; Q8N3Y1; HS.
GO; GO:0031467; C:Cul7-RING ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IEA:Ensembl.
GO; GO:0004842; F:ubiquitin-protein transferase activity; EXP:Reactome.
GO; GO:0008283; P:cell proliferation; IDA:UniProtKB.
GO; GO:0007030; P:Golgi organization; IGI:UniProtKB.
GO; GO:0060716; P:labyrinthine layer blood vessel development; IEA:Ensembl.
GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IDA:UniProtKB.
GO; GO:1901485; P:positive regulation of transcription factor catabolic process; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0060712; P:spongiotrophoblast layer development; IEA:Ensembl.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR036047; F-box-like_dom_sf.
InterPro; IPR001810; F-box_dom.
InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
Pfam; PF12937; F-box-like; 1.
SMART; SM00256; FBOX; 1.
SMART; SM00320; WD40; 5.
SUPFAM; SSF50998; SSF50998; 2.
SUPFAM; SSF81383; SSF81383; 1.
PROSITE; PS50181; FBOX; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 1.
PROSITE; PS50294; WD_REPEATS_REGION; 2.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Golgi apparatus; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Ubl conjugation pathway; WD repeat.
CHAIN 1 598 F-box/WD repeat-containing protein 8.
/FTId=PRO_0000050997.
DOMAIN 113 159 F-box. {ECO:0000255|PROSITE-
ProRule:PRU00080}.
REPEAT 197 245 WD 1.
REPEAT 254 294 WD 2.
REPEAT 297 336 WD 3.
REPEAT 430 470 WD 4.
REPEAT 473 510 WD 5.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIA4}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BIA4}.
VAR_SEQ 41 106 Missing (in isoform 2).
{ECO:0000303|PubMed:10531037}.
/FTId=VSP_008501.
VARIANT 192 192 R -> Q (in dbSNP:rs4076700).
{ECO:0000269|PubMed:10531037,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_060326.
VARIANT 211 211 T -> A (in dbSNP:rs36021180).
/FTId=VAR_057597.
VARIANT 536 536 T -> M (in dbSNP:rs3741466).
/FTId=VAR_057598.
VARIANT 563 563 V -> M (in dbSNP:rs56350562).
/FTId=VAR_062096.
CONFLICT 46 46 G -> S (in Ref. 3; AAH37296).
{ECO:0000305}.
CONFLICT 58 58 R -> G (in Ref. 3; AAH37296).
{ECO:0000305}.
CONFLICT 380 380 L -> I (in Ref. 3; AAH37296).
{ECO:0000305}.
CONFLICT 510 510 E -> K (in Ref. 1; AAF03129).
{ECO:0000305}.
SEQUENCE 598 AA; 67394 MW; 03B3C283BA46DB6B CRC64;
MDDYSLDEFR RRWQEELAQA QAPKKRRRPE AAERRARRPE VGSGRGEQAS GDPALAQRLL
EGAGRPPAAR ATRAEGQDVA SRSRSPLARE GAGGGEQLVD QLIRDLNEMN DVPFFDIQLP
YELAINIFQY LDRKELGRCA QVSKTWKVIA EDEVLWYRLC QQEGHLPDSS ISDYSCWKLI
FQECRAKEHM LRTNWKNRKG AVSELEHVPD TVLCDVHSHD GVVIAGYTSG DVRVWDTRTW
DYVAPFLESE DEEDEPGMQP NVSFVRINSS LAVAAYEDGF LNIWDLRTGK YPVHRFEHDA
RIQALALSQD DATVATASAF DVVMLSPNEE GYWQIAAEFE VPKLVQYLEI VPETRRYPVA
VAAAGDLMYL LKAEDSARTL LYAHGPPVTC LDVSANQVAF GVQGLGWVYE GSKILVYSLE
AGRRLLKLGN VLRDFTCVNL SDSPPNLMVS GNMDGRVRIH DLRSGNIALS LSAHQLRVSA
VQMDDWKIVS GGEEGLVSVW DYRMNQKLWE VYSGHPVQHI SFSSHSLITA NVPYQTVMRN
ADLDSFTTHR RHRGLIRAYE FAVDQLAFQS PLPVCRSSCD AMATHYYDLA LAFPYNHV


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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
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
EIAAB37934 Homo sapiens,Human,Huntingtin-interacting protein-like protein,Protein Solo,SEC14 domain and spectrin repeat-containing protein 1,SESTD1,SOLO
EIAAB14634 F-box and WD-40 domain-containing protein 4,F-box_WD repeat-containing protein 4,Fbw4,Fbxw4,Mouse,Mus musculus,Protein hagoromo
27-617 ZC3H7B is a protein that contains a tetratricopeptide repeat domain. The encoded protein also interacts with the rotavirus non-structural protein NSP3. 0.1 mg
EIAAB37933 Huntingtin-interacting protein-like protein,Mouse,Mus musculus,SEC14 domain and spectrin repeat-containing protein 1,Sestd1
EIAAB14632 F-box and WD-40 domain-containing protein 2,F-box_WD repeat-containing protein 2,FBW2,FBXW2,FWD2,Homo sapiens,Human,Protein MD6
EIAAB14631 F-box and WD-40 domain-containing protein 2,F-box_WD repeat-containing protein 2,Fbxw2,Mouse,Mus musculus,Protein MD6
EIAAB14633 F-box and WD-40 domain-containing protein 2,F-box_WD repeat-containing protein 2,Fbxw2,Protein MD6,Rat,Rattus norvegicus


 

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