FBX11_HUMAN
ID FBX11_HUMAN Reviewed; 927 AA.
AC Q86XK2; A1L491; Q52ZP1; Q53EP7; Q53RT5; Q8IXG3; Q96E90; Q9H6V8; Q9H9L1;
AC Q9NR14; Q9UFK1; Q9UHI1; Q9UKC2;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=F-box only protein 11;
DE AltName: Full=Protein arginine N-methyltransferase 9;
DE AltName: Full=Vitiligo-associated protein 1;
DE Short=VIT-1;
GN Name=FBXO11; Synonyms=FBX11, PRMT9, VIT1; ORFNames=UG063H01;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH TP53, AND IDENTIFICATION IN A COMPLEX WITH SKP1; CUL1 AND
RP RBX1.
RX PubMed=17098746; DOI=10.1074/jbc.m609001200;
RA Abida W.M., Nikolaev A., Zhao W., Zhang W., Gu W.;
RT "FBXO11 promotes the neddylation of p53 and inhibits its transcriptional
RT activity.";
RL J. Biol. Chem. 282:1797-1804(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Fetal brain;
RA Mao Y.-M., Xie Y.;
RT "Isolation of full-length cDNA clones from human fetal brain cDNA
RT library.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Kidney;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 6), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 646-927 (ISOFORM 1).
RC TISSUE=Hepatoma, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 15-927 (ISOFORM 1).
RC TISSUE=Brain, Ovary, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-212.
RX PubMed=10531035; DOI=10.1016/s0960-9822(00)80020-2;
RA Cenciarelli C., Chiaur D.S., Guardavaccaro D., Parks W., Vidal M.,
RA Pagano M.;
RT "Identification of a family of human F-box proteins.";
RL Curr. Biol. 9:1177-1179(1999).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-927 (ISOFORM 4).
RX PubMed=10531037; DOI=10.1016/s0960-9822(00)80021-4;
RA Winston J.T., Koepp D.M., Zhu C., Elledge S.J., Harper J.W.;
RT "A family of mammalian F-box proteins.";
RL Curr. Biol. 9:1180-1182(1999).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 720-927.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 744-927 (ISOFORM 5), AND TISSUE SPECIFICITY.
RX PubMed=11775060; DOI=10.1034/j.1600-0749.2001.140608.x;
RA Le Poole I.C., Sarangarajan R., Zhao Y., Stennett L.S., Brown T.L.,
RA Sheth P., Miki T., Boissy R.E.;
RT "'VIT1', a novel gene associated with vitiligo.";
RL Pigment Cell Res. 14:475-484(2001).
RN [12]
RP ALTERNATIVE SPLICING, AND CAUTION (ISOFORM 2).
RX PubMed=16487488; DOI=10.1016/j.bbrc.2006.01.167;
RA Cook J.R., Lee J.H., Yang Z.H., Krause C.D., Herth N., Hoffmann R.,
RA Pestka S.;
RT "FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically
RT dimethylates arginine residues.";
RL Biochem. Biophys. Res. Commun. 342:472-481(2006).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=23892434; DOI=10.4161/cc.25314;
RA Abbas T., Keaton M., Dutta A.;
RT "Regulation of TGF-beta signaling, exit from the cell cycle, and cellular
RT migration through cullin cross-regulation: SCF-FBXO11 turns off CRL4-
RT Cdt2.";
RL Cell Cycle 12:2175-2182(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP FUNCTION IN UBIQUITINATION OF DTL, AND INTERACTION WITH DTL.
RX PubMed=23478445; DOI=10.1016/j.molcel.2013.02.003;
RA Abbas T., Mueller A.C., Shibata E., Keaton M., Rossi M., Dutta A.;
RT "CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-
RT Set7/Set8-mediated cellular migration.";
RL Mol. Cell 49:1147-1158(2013).
RN [16]
RP FUNCTION IN UBIQUITINATION OF DTL, AND INTERACTION WITH DTL.
RX PubMed=23478441; DOI=10.1016/j.molcel.2013.02.004;
RA Rossi M., Duan S., Jeong Y.T., Horn M., Saraf A., Florens L.,
RA Washburn M.P., Antebi A., Pagano M.;
RT "Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the
RT SCF(Fbxo11) ubiquitin ligase.";
RL Mol. Cell 49:1159-1166(2013).
RN [17]
RP FUNCTION IN UBIQUITINATION OF PRDM1, INTERACTION WITH PRDM1, AND
RP MUTAGENESIS OF GLN-575.
RX PubMed=24613396; DOI=10.1016/j.devcel.2014.01.028;
RA Horn M., Geisen C., Cermak L., Becker B., Nakamura S., Klein C., Pagano M.,
RA Antebi A.;
RT "DRE-1/FBXO11-dependent degradation of BLMP-1/BLIMP-1 governs C. elegans
RT developmental timing and maturation.";
RL Dev. Cell 28:697-710(2014).
RN [18]
RP INTERACTION WITH PRDM1.
RX PubMed=24968003; DOI=10.1371/journal.pgen.1004428;
RA Huang T.F., Cho C.Y., Cheng Y.T., Huang J.W., Wu Y.Z., Yeh A.Y.,
RA Nishiwaki K., Chang S.C., Wu Y.C.;
RT "BLMP-1/Blimp-1 regulates the spatiotemporal cell migration pattern in C.
RT elegans.";
RL PLoS Genet. 10:E1004428-E1004428(2014).
RN [19]
RP VARIANTS CYS-206; CYS-644; GLU-684; ASN-715 AND GLN-715, CHARACTERIZATION
RP OF VARIANTS CYS-644; GLU-684; ASN-715 AND GLN-715, FUNCTION IN
RP UBIQUITINATION OF BCL6, INTERACTION WITH BCL6, IDENTIFICATION IN THE
RP SCF(FBXO11) COMPLEX, SUBCELLULAR LOCATION, AND INVOLVEMENT IN LYMPHOMA.
RX PubMed=22113614; DOI=10.1038/nature10688;
RA Duan S., Cermak L., Pagan J.K., Rossi M., Martinengo C., di Celle P.F.,
RA Chapuy B., Shipp M., Chiarle R., Pagano M.;
RT "FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-
RT cell lymphomas.";
RL Nature 481:90-93(2012).
RN [20]
RP INVOLVEMENT IN IDDFBA, AND VARIANT IDDFBA 913-TYR--ASN-927 DEL.
RX PubMed=27620904; DOI=10.1136/jmedgenet-2016-103964;
RA Martinez F., Caro-Llopis A., Rosello M., Oltra S., Mayo S., Monfort S.,
RA Orellana C.;
RT "High diagnostic yield of syndromic intellectual disability by targeted
RT next-generation sequencing.";
RL J. Med. Genet. 54:87-92(2017).
RN [21]
RP INVOLVEMENT IN IDDFBA, AND VARIANTS IDDFBA SER-138; ARG-156; VAL-538;
RP 609-GLU--ASN-927 DEL; ARG-623; 697-GLY--ASN-927 DEL; PRO-840; ASP-892;
RP 904-GLU--ASN-927 DEL; ARG-905 AND GLY-910.
RX PubMed=30057029; DOI=10.1016/j.ajhg.2018.07.003;
RG University of Washington Center for Mendelian Genomics;
RG DDD Study;
RA Gregor A., Sadleir L.G., Asadollahi R., Azzarello-Burri S., Battaglia A.,
RA Ousager L.B., Boonsawat P., Bruel A.L., Buchert R., Calpena E., Cogne B.,
RA Dallapiccola B., Distelmaier F., Elmslie F., Faivre L., Haack T.B.,
RA Harrison V., Henderson A., Hunt D., Isidor B., Joset P., Kumada S.,
RA Lachmeijer A.M.A., Lees M., Lynch S.A., Martinez F., Matsumoto N.,
RA McDougall C., Mefford H.C., Miyake N., Myers C.T., Moutton S., Nesbitt A.,
RA Novelli A., Orellana C., Rauch A., Rosello M., Saida K., Santani A.B.,
RA Sarkar A., Scheffer I.E., Shinawi M., Steindl K., Symonds J.D.,
RA Zackai E.H., Reis A., Sticht H., Zweier C.;
RT "De Novo Variants in the F-Box Protein FBXO11 in 20 Individuals with a
RT Variable Neurodevelopmental Disorder.";
RL Am. J. Hum. Genet. 103:305-316(2018).
RN [22]
RP INVOLVEMENT IN IDDFBA, AND VARIANT IDDFBA 913-TYR--ASN-927 DEL.
RX PubMed=29796876; DOI=10.1007/s00439-018-1892-1;
RA Fritzen D., Kuechler A., Grimmel M., Becker J., Peters S., Sturm M.,
RA Hundertmark H., Schmidt A., Kreiss M., Strom T.M., Wieczorek D.,
RA Haack T.B., Beck-Woedl S., Cremer K., Engels H.;
RT "De novo FBXO11 mutations are associated with intellectual disability and
RT behavioural anomalies.";
RL Hum. Genet. 137:401-411(2018).
RN [23]
RP VARIANT MET-866.
RX PubMed=28097321; DOI=10.1001/jamapsychiatry.2016.3798;
RA Reuter M.S., Tawamie H., Buchert R., Hosny Gebril O., Froukh T., Thiel C.,
RA Uebe S., Ekici A.B., Krumbiegel M., Zweier C., Hoyer J., Eberlein K.,
RA Bauer J., Scheller U., Strom T.M., Hoffjan S., Abdelraouf E.R.,
RA Meguid N.A., Abboud A., Al Khateeb M.A., Fakher M., Hamdan S., Ismael A.,
RA Muhammad S., Abdallah E., Sticht H., Wieczorek D., Reis A., Abou Jamra R.;
RT "Diagnostic yield and novel candidate genes by exome sequencing in 152
RT consanguineous families with neurodevelopmental disorders.";
RL JAMA Psychiatry 74:293-299(2017).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins, such as DTL/CDT2, BCL6 and PRDM1/BLIMP1. The SCF(FBXO11)
CC complex mediates ubiquitination and degradation of BCL6, thereby
CC playing a role in the germinal center B-cells terminal differentiation
CC toward memory B-cells and plasma cells. The SCF(FBXO11) complex also
CC mediates ubiquitination and degradation of DTL, an important step for
CC the regulation of TGF-beta signaling, cell migration and the timing of
CC the cell-cycle progression and exit. Binds to and neddylates
CC phosphorylated p53/TP53, inhibiting its transcriptional activity.
CC SCF(FBXO11) does not seem to direct ubiquitination of p53/TP53.
CC {ECO:0000269|PubMed:17098746, ECO:0000269|PubMed:22113614,
CC ECO:0000269|PubMed:23478441, ECO:0000269|PubMed:23478445,
CC ECO:0000269|PubMed:23892434, ECO:0000269|PubMed:24613396}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the SCF(FBXO11) complex consisting of CUL1, RBX1,
CC SKP1 and FBXO11. Interacts with p53/TP53, BCL6 and DTL (when not
CC phosphorylated). Interacts with PRMD1. {ECO:0000269|PubMed:17098746,
CC ECO:0000269|PubMed:22113614, ECO:0000269|PubMed:23478441,
CC ECO:0000269|PubMed:23478445, ECO:0000269|PubMed:24613396,
CC ECO:0000269|PubMed:24968003}.
CC -!- INTERACTION:
CC Q86XK2; P41182: BCL6; NbExp=9; IntAct=EBI-1047804, EBI-765407;
CC Q86XK2; P63208: SKP1; NbExp=8; IntAct=EBI-1047804, EBI-307486;
CC Q86XK2; P63208-1: SKP1; NbExp=5; IntAct=EBI-1047804, EBI-307497;
CC Q86XK2; O95863: SNAI1; NbExp=6; IntAct=EBI-1047804, EBI-1045459;
CC Q86XK2; P04637: TP53; NbExp=4; IntAct=EBI-1047804, EBI-366083;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q86XK2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86XK2-2; Sequence=VSP_022574, VSP_008863, VSP_008864;
CC Name=6;
CC IsoId=Q86XK2-6; Sequence=VSP_022573;
CC Name=3;
CC IsoId=Q86XK2-3; Sequence=VSP_022573, VSP_008862;
CC Name=4;
CC IsoId=Q86XK2-4; Sequence=VSP_008860, VSP_008861;
CC Name=5;
CC IsoId=Q86XK2-5; Sequence=VSP_008865;
CC -!- TISSUE SPECIFICITY: Isoform 5 is expressed in keratinocytes,
CC fibroblasts and melanocytes. {ECO:0000269|PubMed:11775060}.
CC -!- DEVELOPMENTAL STAGE: Protein levels increase during G1 and S phases to
CC decline as cells progress through G2 to enter in G1 phase of the next
CC cell cycle. {ECO:0000269|PubMed:23892434}.
CC -!- DISEASE: Intellectual developmental disorder with dysmorphic facies and
CC behavioral abnormalities (IDDFBA) [MIM:618089]: An autosomal dominant
CC developmental disorder with variable manifestations and onset in
CC infancy or first years of life. Clinical features include intellectual
CC disability, speech delay, hyperkinetic disorder, hyperactivity,
CC seizures, pre- and postnatal growth retardation, microcephaly, and
CC facial dysmorphism. {ECO:0000269|PubMed:27620904,
CC ECO:0000269|PubMed:29796876, ECO:0000269|PubMed:30057029}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Note=Defects in FBXO11 may be a cause of diffuse large B-cell
CC lymphoma by allowing the accumulation of BCL6, an oncoprotein that has
CC a critical role in lymphomas. {ECO:0000269|PubMed:22113614}.
CC -!- CAUTION: [Isoform 2]: Has been initially named PRMT9 and reported to
CC act as an arginine methyltransferase that can catalyze the formation of
CC omega-N monomethylarginine (MMA) as well as symmetrical and
CC asymmetrical dimethylarginine (sDMA and aDMA), however no further works
CC support these observations (PubMed:16487488). It should not be confused
CC with official PRMT9 (AC Q6P2P2). {ECO:0000305|PubMed:16487488}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF76888.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAN76518.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAY24083.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB15143.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY827075; AAV87312.1; -; mRNA.
DR EMBL; AF351618; AAN76518.1; ALT_SEQ; mRNA.
DR EMBL; AK223592; BAD97312.1; -; mRNA.
DR EMBL; AK022735; BAB14214.1; -; mRNA.
DR EMBL; AK025477; BAB15143.1; ALT_INIT; mRNA.
DR EMBL; AK292877; BAF85566.1; -; mRNA.
DR EMBL; AC006509; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079807; AAY24083.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471053; EAX00205.1; -; Genomic_DNA.
DR EMBL; BC012728; AAH12728.2; -; mRNA.
DR EMBL; BC043258; AAH43258.2; -; mRNA.
DR EMBL; BC130445; AAI30446.1; -; mRNA.
DR EMBL; BC136480; AAI36481.1; -; mRNA.
DR EMBL; AF174599; AAF04520.1; -; mRNA.
DR EMBL; AF176706; AAF17611.1; -; mRNA.
DR EMBL; AL117620; CAB56019.1; -; mRNA.
DR EMBL; AF264714; AAF76888.1; ALT_SEQ; mRNA.
DR CCDS; CCDS1837.1; -. [Q86XK2-6]
DR CCDS; CCDS54357.1; -. [Q86XK2-1]
DR PIR; T17329; T17329.
DR RefSeq; NP_001177203.1; NM_001190274.1. [Q86XK2-1]
DR RefSeq; NP_079409.3; NM_025133.4. [Q86XK2-6]
DR RefSeq; XP_005264629.1; XM_005264572.4. [Q86XK2-5]
DR RefSeq; XP_016860506.1; XM_017005017.1.
DR PDB; 5VMD; X-ray; 2.20 A; A/B/C/D=833-904.
DR PDBsum; 5VMD; -.
DR AlphaFoldDB; Q86XK2; -.
DR SMR; Q86XK2; -.
DR BioGRID; 123173; 125.
DR CORUM; Q86XK2; -.
DR DIP; DIP-35680N; -.
DR IntAct; Q86XK2; 51.
DR MINT; Q86XK2; -.
DR STRING; 9606.ENSP00000384823; -.
DR iPTMnet; Q86XK2; -.
DR PhosphoSitePlus; Q86XK2; -.
DR BioMuta; FBXO11; -.
DR DMDM; 124012093; -.
DR EPD; Q86XK2; -.
DR jPOST; Q86XK2; -.
DR MassIVE; Q86XK2; -.
DR MaxQB; Q86XK2; -.
DR PaxDb; Q86XK2; -.
DR PeptideAtlas; Q86XK2; -.
DR PRIDE; Q86XK2; -.
DR ProteomicsDB; 149; -.
DR ProteomicsDB; 70286; -. [Q86XK2-1]
DR ProteomicsDB; 70287; -. [Q86XK2-2]
DR ProteomicsDB; 70288; -. [Q86XK2-3]
DR ProteomicsDB; 70289; -. [Q86XK2-4]
DR ProteomicsDB; 70290; -. [Q86XK2-5]
DR Antibodypedia; 15211; 358 antibodies from 29 providers.
DR DNASU; 80204; -.
DR Ensembl; ENST00000402508.5; ENSP00000385398.1; ENSG00000138081.22. [Q86XK2-6]
DR Ensembl; ENST00000403359.8; ENSP00000384823.4; ENSG00000138081.22. [Q86XK2-1]
DR GeneID; 80204; -.
DR KEGG; hsa:80204; -.
DR MANE-Select; ENST00000403359.8; ENSP00000384823.4; NM_001190274.2; NP_001177203.1.
DR UCSC; uc002rwe.3; human. [Q86XK2-1]
DR CTD; 80204; -.
DR DisGeNET; 80204; -.
DR GeneCards; FBXO11; -.
DR HGNC; HGNC:13590; FBXO11.
DR HPA; ENSG00000138081; Low tissue specificity.
DR MalaCards; FBXO11; -.
DR MIM; 607871; gene.
DR MIM; 618089; phenotype.
DR neXtProt; NX_Q86XK2; -.
DR OpenTargets; ENSG00000138081; -.
DR PharmGKB; PA28031; -.
DR VEuPathDB; HostDB:ENSG00000138081; -.
DR eggNOG; KOG1777; Eukaryota.
DR GeneTree; ENSGT00530000063425; -.
DR HOGENOM; CLU_005078_1_0_1; -.
DR InParanoid; Q86XK2; -.
DR OMA; LGYFEAN; -.
DR OrthoDB; 355502at2759; -.
DR PhylomeDB; Q86XK2; -.
DR TreeFam; TF313602; -.
DR PathwayCommons; Q86XK2; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q86XK2; -.
DR SIGNOR; Q86XK2; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 80204; 115 hits in 1133 CRISPR screens.
DR ChiTaRS; FBXO11; human.
DR GeneWiki; FBXO11; -.
DR GenomeRNAi; 80204; -.
DR Pharos; Q86XK2; Tbio.
DR PRO; PR:Q86XK2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q86XK2; protein.
DR Bgee; ENSG00000138081; Expressed in cortical plate and 204 other tissues.
DR ExpressionAtlas; Q86XK2; baseline and differential.
DR Genevisible; Q86XK2; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0000151; C:ubiquitin ligase complex; NAS:UniProtKB.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IDA:HGNC-UCL.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 2.160.20.10; -; 3.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR029799; FBX11/DRE-1.
DR InterPro; IPR007742; NosD_dom.
DR InterPro; IPR022441; Para_beta_helix_rpt-2.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR22990:SF20; PTHR22990:SF20; 1.
DR Pfam; PF13229; Beta_helix; 2.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF05048; NosD; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00722; CASH; 3.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00710; PbH1; 19.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF51126; SSF51126; 3.
DR SUPFAM; SSF81383; SSF81383; 1.
DR TIGRFAMs; TIGR03804; para_beta_helix; 4.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; Disease variant;
KW Intellectual disability; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..927
FT /note="F-box only protein 11"
FT /id="PRO_0000273574"
FT DOMAIN 153..199
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 395..417
FT /note="PbH1 1"
FT REPEAT 418..440
FT /note="PbH1 2"
FT REPEAT 441..463
FT /note="PbH1 3"
FT REPEAT 464..486
FT /note="PbH1 4"
FT REPEAT 487..509
FT /note="PbH1 5"
FT REPEAT 510..532
FT /note="PbH1 6"
FT REPEAT 533..555
FT /note="PbH1 7"
FT REPEAT 556..578
FT /note="PbH1 8"
FT REPEAT 579..601
FT /note="PbH1 9"
FT REPEAT 602..624
FT /note="PbH1 10"
FT REPEAT 625..647
FT /note="PbH1 11"
FT REPEAT 648..670
FT /note="PbH1 12"
FT REPEAT 671..693
FT /note="PbH1 13"
FT REPEAT 694..716
FT /note="PbH1 14"
FT REPEAT 717..739
FT /note="PbH1 15"
FT REPEAT 740..762
FT /note="PbH1 16"
FT REPEAT 763..785
FT /note="PbH1 17"
FT REPEAT 786..808
FT /note="PbH1 18"
FT REPEAT 809..830
FT /note="PbH1 19"
FT ZN_FING 833..904
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..70
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..209
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022574"
FT VAR_SEQ 1..84
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.3"
FT /id="VSP_022573"
FT VAR_SEQ 197..211
FT /note="KRLYMEVFEYTRPMM -> LGEVAHAYNPSTLGG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10531037"
FT /id="VSP_008860"
FT VAR_SEQ 212..927
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10531037"
FT /id="VSP_008861"
FT VAR_SEQ 670..927
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_008862"
FT VAR_SEQ 744..770
FT /note="LLEENDIFRNAQAGVLISTNSHPILRK -> IVVNFALVKNPVFHYSSISLM
FT INDIAN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008863"
FT VAR_SEQ 771..927
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008864"
FT VAR_SEQ 885
FT /note="R -> RYVAHLLDILPNYFPPHFSNIWVSFCFR (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11775060"
FT /id="VSP_008865"
FT VARIANT 126
FT /note="T -> S (in dbSNP:rs17036993)"
FT /id="VAR_024441"
FT VARIANT 138
FT /note="R -> S (in IDDFBA; dbSNP:rs1553342109)"
FT /evidence="ECO:0000269|PubMed:30057029"
FT /id="VAR_081341"
FT VARIANT 156
FT /note="Q -> R (in IDDFBA)"
FT /evidence="ECO:0000269|PubMed:30057029"
FT /id="VAR_081342"
FT VARIANT 206
FT /note="Y -> C (found in a patient with lymphoma)"
FT /evidence="ECO:0000269|PubMed:22113614"
FT /id="VAR_070073"
FT VARIANT 538
FT /note="I -> V (in IDDFBA; dbSNP:rs1553338592)"
FT /evidence="ECO:0000269|PubMed:30057029"
FT /id="VAR_081343"
FT VARIANT 609..927
FT /note="Missing (in IDDFBA)"
FT /evidence="ECO:0000269|PubMed:30057029"
FT /id="VAR_081344"
FT VARIANT 623
FT /note="T -> R (in IDDFBA)"
FT /evidence="ECO:0000269|PubMed:30057029"
FT /id="VAR_081345"
FT VARIANT 644
FT /note="Y -> C (found in a lymphoma cell line; diminishes
FT ubiquitin-mediated degradation of BCL6)"
FT /evidence="ECO:0000269|PubMed:22113614"
FT /id="VAR_070074"
FT VARIANT 684
FT /note="G -> E (found in a patient with lymphoma; strongly
FT diminishes ubiquitin-mediated degradation of BCL6)"
FT /evidence="ECO:0000269|PubMed:22113614"
FT /id="VAR_070075"
FT VARIANT 697..927
FT /note="Missing (in IDDFBA)"
FT /evidence="ECO:0000269|PubMed:30057029"
FT /id="VAR_081346"
FT VARIANT 715
FT /note="K -> N (found in a patient with lymphoma; strongly
FT diminishes ubiquitin-mediated degradation of BCL6;
FT dbSNP:rs1572764737)"
FT /evidence="ECO:0000269|PubMed:22113614"
FT /id="VAR_070076"
FT VARIANT 715
FT /note="K -> Q (found in a patient with lymphoma; almost
FT abolishes ubiquitin-mediated degradation of BCL6)"
FT /evidence="ECO:0000269|PubMed:22113614"
FT /id="VAR_070077"
FT VARIANT 840
FT /note="S -> P (in IDDFBA; dbSNP:rs1553335247)"
FT /evidence="ECO:0000269|PubMed:30057029"
FT /id="VAR_081347"
FT VARIANT 866
FT /note="V -> M (found in a patient with severe intellectual
FT disability and muscular hypotonia; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28097321"
FT /id="VAR_081348"
FT VARIANT 892
FT /note="A -> D (in IDDFBA)"
FT /evidence="ECO:0000269|PubMed:30057029"
FT /id="VAR_081349"
FT VARIANT 904..927
FT /note="Missing (in IDDFBA)"
FT /evidence="ECO:0000269|PubMed:30057029"
FT /id="VAR_081350"
FT VARIANT 905
FT /note="P -> R (in IDDFBA)"
FT /evidence="ECO:0000269|PubMed:30057029"
FT /id="VAR_081351"
FT VARIANT 910
FT /note="D -> G (in IDDFBA)"
FT /evidence="ECO:0000269|PubMed:30057029"
FT /id="VAR_081352"
FT VARIANT 913..927
FT /note="Missing (in IDDFBA)"
FT /evidence="ECO:0000269|PubMed:27620904,
FT ECO:0000269|PubMed:29796876"
FT /id="VAR_081353"
FT MUTAGEN 575
FT /note="Q->L: Greatly reduced ability to bind PRDM1 and
FT reduced proteolysis of PRDM1."
FT /evidence="ECO:0000269|PubMed:24613396"
FT CONFLICT 239
FT /note="L -> S (in Ref. 4; BAB14214)"
FT /evidence="ECO:0000305"
FT CONFLICT 577
FT /note="R -> G (in Ref. 2; AAN76518)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="R -> G (in Ref. 3; BAD97312)"
FT /evidence="ECO:0000305"
FT CONFLICT 903
FT /note="G -> S (in Ref. 1; AAV87312 and 7; AAH43258)"
FT /evidence="ECO:0000305"
FT HELIX 839..844
FT /evidence="ECO:0007829|PDB:5VMD"
FT STRAND 845..856
FT /evidence="ECO:0007829|PDB:5VMD"
FT HELIX 866..872
FT /evidence="ECO:0007829|PDB:5VMD"
FT STRAND 878..884
FT /evidence="ECO:0007829|PDB:5VMD"
FT TURN 889..893
FT /evidence="ECO:0007829|PDB:5VMD"
FT STRAND 895..897
FT /evidence="ECO:0007829|PDB:5VMD"
SQ SEQUENCE 927 AA; 103585 MW; CADBD23A6B892A78 CRC64;
MNSVRAANRR PRRVSRPRPV QQQQQQPPQQ PPPQPPQQQP PQQQPPPPPQ QQQQQQPPPP
PPPPPPLPQE RNNVGERDDD VPADMVAEES GPGAQNSPYQ LRRKTLLPKR TACPTKNSME
GASTSTTENF GHRAKRARVS GKSQDLSAAP AEQYLQEKLP DEVVLKIFSY LLEQDLCRAA
CVCKRFSELA NDPILWKRLY MEVFEYTRPM MHPEPGKFYQ INPEEYEHPN PWKESFQQLY
KGAHVKPGFA EHFYSNPARY KGRENMLYYD TIEDALGGVQ EAHFDGLIFV HSGIYTDEWI
YIESPITMIG AAPGKVADKV IIENTRDSTF VFMEGSEDAY VGYMTIRFNP DDKSAQHHNA
HHCLEITVNC SPIIDHCIIR STCTVGSAVC VSGQGACPTI KHCNISDCEN VGLYITDHAQ
GIYEDNEISN NALAGIWVKN HGNPIIRRNH IHHGRDVGVF TFDHGMGYFE SCNIHRNRIA
GFEVKAYANP TVVRCEIHHG QTGGIYVHEK GRGQFIENKI YANNFAGVWI TSNSDPTIRG
NSIFNGNQGG VYIFGDGRGL IEGNDIYGNA LAGIQIRTNS CPIVRHNKIH DGQHGGIYVH
EKGQGVIEEN EVYSNTLAGV WVTTGSTPVL RRNRIHSGKQ VGVYFYDNGH GVLEDNDIYN
HMYSGVQIRT GSNPKIRRNK IWGGQNGGIL VYNSGLGCIE DNEIFDNAMA GVWIKTDSNP
TLRRNKIHDG RDGGICIFNG GRGLLEENDI FRNAQAGVLI STNSHPILRK NRIFDGFAAG
IEITNHATAT LEGNQIFNNR FGGLFLASGV NVTMKDNKIM NNQDAIEKAV SRGQCLYKIS
SYTSYPMHDF YRCHTCNTTD RNAICVNCIK KCHQGHDVEF IRHDRFFCDC GAGTLSNPCT
LAGEPTHDTD TLYDSAPPIE SNTLQHN
