CEP43_HUMAN
ID CEP43_HUMAN Reviewed; 399 AA.
AC O95684; A8K1D1; B2R705; Q49AI0; Q5R3F6; Q96EW1;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Centrosomal protein 43 {ECO:0000305};
DE AltName: Full=FGFR1 oncogene partner;
GN Name=CEP43 {ECO:0000312|HGNC:HGNC:17012}; Synonyms=FGFR1OP, FOP;
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), CHROMOSOMAL TRANSLOCATION WITH
RP FGFR1, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=9949182;
RA Popovici C., Zhang B., Gregoire M.-J., Jonveaux P., Lafage-Pochitaloff M.,
RA Birnbaum D., Pebusque M.-J.;
RT "The t(6;8)(q27;p11) translocation in a stem cell myeloproliferative
RT disorder fuses a novel gene, FOP, to fibroblast growth factor receptor 1.";
RL Blood 93:1381-1389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP ASN-271.
RC TISSUE=Brain, and Muscle;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-160, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAPRE1 AND CEP350.
RX PubMed=16314388; DOI=10.1091/mbc.e05-08-0810;
RA Yan X., Habedanck R., Nigg E.A.;
RT "A complex of two centrosomal proteins, CAP350 and FOP, cooperates with EB1
RT in microtubule anchoring.";
RL Mol. Biol. Cell 17:634-644(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-160 AND SER-202, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-160, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-156; SER-160;
RP THR-170; SER-202; THR-234; SER-301 AND SER-326, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-143 AND SER-160, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP FUNCTION, INTERACTION WITH CEP19 AND CEP350, SUBCELLULAR LOCATION, AND
RP PHYLOGENETIC ANALYSIS.
RX PubMed=28625565; DOI=10.1016/j.devcel.2017.05.016;
RA Kanie T., Abbott K.L., Mooney N.A., Plowey E.D., Demeter J., Jackson P.K.;
RT "The CEP19-RABL2 GTPase complex binds IFT-B to initiate intraflagellar
RT transport at the ciliary base.";
RL Dev. Cell 42:1-15(2017).
RN [18]
RP INTERACTION WITH CEP19 AND CEP350, AND SUBCELLULAR LOCATION.
RX PubMed=28428259; DOI=10.1091/mbc.e17-01-0017;
RA Nishijima Y., Hagiya Y., Kubo T., Takei R., Katoh Y., Nakayama K.;
RT "RABL2 interacts with the intraflagellar transport-B complex and CEP19 and
RT participates in ciliary assembly.";
RL Mol. Biol. Cell 28:1652-1666(2017).
RN [19]
RP FUNCTION, INTERACTION WITH CEP19, AND SUBCELLULAR LOCATION.
RX PubMed=28659385; DOI=10.1098/rsob.170114;
RA Mojarad B.A., Gupta G.D., Hasegan M., Goudiam O., Basto R., Gingras A.C.,
RA Pelletier L.;
RT "CEP19 cooperates with FOP and CEP350 to drive early steps in the
RT ciliogenesis programme.";
RL Open Biol. 7:0-0(2017).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 54-134, MUTAGENESIS OF VAL-74,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=16690081; DOI=10.1016/j.jmb.2006.03.070;
RA Mikolajka A., Yan X., Popowicz G.M., Smialowski P., Nigg E.A., Holak T.A.;
RT "Structure of the N-terminal domain of the FOP (FGFR1OP) protein and
RT implications for its dimerization and centrosomal localization.";
RL J. Mol. Biol. 359:863-875(2006).
CC -!- FUNCTION: Required for anchoring microtubules to the centrosomes
CC (PubMed:16314388, PubMed:28659385). Required for ciliation
CC (PubMed:28625565, PubMed:28659385). {ECO:0000269|PubMed:16314388,
CC ECO:0000269|PubMed:28625565, ECO:0000269|PubMed:28659385}.
CC -!- SUBUNIT: Homodimer (PubMed:16690081). Part of a ternary complex that
CC contains CEP350, CEP43 and MAPRE1. Interacts directly with CEP350 and
CC MAPRE1 (PubMed:16314388). Interacts with CEP19 (PubMed:28625565,
CC PubMed:28428259, PubMed:28659385). Interacts (via N-terminus) with
CC CEP350 (via C-terminus) (PubMed:28625565, PubMed:28428259).
CC {ECO:0000269|PubMed:16314388, ECO:0000269|PubMed:16690081,
CC ECO:0000269|PubMed:28428259, ECO:0000269|PubMed:28625565,
CC ECO:0000269|PubMed:28659385}.
CC -!- INTERACTION:
CC O95684; Q96LK0: CEP19; NbExp=6; IntAct=EBI-1266334, EBI-741885;
CC O95684; P06703: S100A6; NbExp=2; IntAct=EBI-1266334, EBI-352877;
CC O95684; P50552: VASP; NbExp=3; IntAct=EBI-1266334, EBI-748201;
CC O95684-2; Q96LK0: CEP19; NbExp=7; IntAct=EBI-1266347, EBI-741885;
CC O95684-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1266347, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:16314388, ECO:0000269|PubMed:16690081,
CC ECO:0000269|PubMed:28659385}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:28428259,
CC ECO:0000269|PubMed:28625565, ECO:0000269|PubMed:28659385}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:28659385}.
CC Note=Associated with gamma-tubulin (PubMed:16314388). Localizes on both
CC mother and daughter centrioles (PubMed:28625565, PubMed:28428259).
CC Localizes to an axial position on the mother centriole
CC (PubMed:28625565). Localizes to the distal end of the centriole partly
CC on the subdistal appendage region (PubMed:28659385).
CC {ECO:0000269|PubMed:16314388, ECO:0000269|PubMed:28428259,
CC ECO:0000269|PubMed:28625565, ECO:0000269|PubMed:28659385}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95684-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=O95684-2; Sequence=VSP_018120;
CC Name=3;
CC IsoId=O95684-3; Sequence=VSP_018119, VSP_018121;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, liver,
CC muscle, kidney, intestine, colon, adrenal gland, prostate, testis, and
CC pancreas. {ECO:0000269|PubMed:9949182}.
CC -!- DISEASE: Note=A chromosomal aberration involving CEP43 may be a cause
CC of stem cell myeloproliferative disorder (MPD). Translocation
CC t(6;8)(q27;p11) with FGFR1. MPD is characterized by myeloid
CC hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma.
CC In general it progresses to acute myeloid leukemia. The fusion proteins
CC CEP43-FGFR1 or FGFR1-CEP43 may exhibit constitutive kinase activity and
CC be responsible for the transforming activity (PubMed:9949182).
CC {ECO:0000269|PubMed:9949182}.
CC -!- SIMILARITY: Belongs to the CEP43 family. {ECO:0000305}.
CC -!- CAUTION: Interacting region of CEP19 is conflicting: According to a
CC report, interacts via N-terminus (PubMed:28428259). According to
CC another report, interacts via C-terminus (PubMed:28659385).
CC {ECO:0000269|PubMed:28428259, ECO:0000269|PubMed:28659385}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FOPID140.html";
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DR EMBL; Y18046; CAA77020.1; -; mRNA.
DR EMBL; AK289846; BAF82535.1; -; mRNA.
DR EMBL; AK312791; BAG35652.1; -; mRNA.
DR EMBL; Z94721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47509.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47510.1; -; Genomic_DNA.
DR EMBL; BC011902; AAH11902.1; -; mRNA.
DR EMBL; BC037785; AAH37785.1; -; mRNA.
DR CCDS; CCDS5296.1; -. [O95684-1]
DR CCDS; CCDS5297.1; -. [O95684-2]
DR RefSeq; NP_008976.1; NM_007045.3. [O95684-1]
DR RefSeq; NP_919410.1; NM_194429.2. [O95684-2]
DR PDB; 2D68; X-ray; 1.60 A; A/B=54-134.
DR PDBsum; 2D68; -.
DR AlphaFoldDB; O95684; -.
DR SMR; O95684; -.
DR BioGRID; 116291; 198.
DR IntAct; O95684; 162.
DR MINT; O95684; -.
DR STRING; 9606.ENSP00000355812; -.
DR GlyGen; O95684; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95684; -.
DR PhosphoSitePlus; O95684; -.
DR BioMuta; FGFR1OP; -.
DR EPD; O95684; -.
DR jPOST; O95684; -.
DR MassIVE; O95684; -.
DR MaxQB; O95684; -.
DR PaxDb; O95684; -.
DR PeptideAtlas; O95684; -.
DR PRIDE; O95684; -.
DR ProteomicsDB; 50996; -. [O95684-1]
DR ProteomicsDB; 50997; -. [O95684-2]
DR ProteomicsDB; 50998; -. [O95684-3]
DR Antibodypedia; 33532; 296 antibodies from 32 providers.
DR DNASU; 11116; -.
DR Ensembl; ENST00000349556.4; ENSP00000230248.6; ENSG00000213066.13. [O95684-2]
DR Ensembl; ENST00000366847.9; ENSP00000355812.3; ENSG00000213066.13. [O95684-1]
DR GeneID; 11116; -.
DR KEGG; hsa:11116; -.
DR MANE-Select; ENST00000366847.9; ENSP00000355812.3; NM_007045.4; NP_008976.1.
DR UCSC; uc003qvj.5; human. [O95684-1]
DR CTD; 11116; -.
DR DisGeNET; 11116; -.
DR GeneCards; CEP43; -.
DR HGNC; HGNC:17012; CEP43.
DR HPA; ENSG00000213066; Tissue enhanced (testis).
DR MIM; 605392; gene.
DR neXtProt; NX_O95684; -.
DR OpenTargets; ENSG00000213066; -.
DR PharmGKB; PA134941638; -.
DR VEuPathDB; HostDB:ENSG00000213066; -.
DR eggNOG; ENOG502QR70; Eukaryota.
DR GeneTree; ENSGT00390000007441; -.
DR HOGENOM; CLU_039837_2_0_1; -.
DR InParanoid; O95684; -.
DR OMA; DITQDHT; -.
DR OrthoDB; 1316797at2759; -.
DR PhylomeDB; O95684; -.
DR TreeFam; TF331893; -.
DR PathwayCommons; O95684; -.
DR Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; O95684; -.
DR SIGNOR; O95684; -.
DR BioGRID-ORCS; 11116; 351 hits in 1098 CRISPR screens.
DR ChiTaRS; FGFR1OP; human.
DR EvolutionaryTrace; O95684; -.
DR GeneWiki; FGFR1OP; -.
DR GenomeRNAi; 11116; -.
DR Pharos; O95684; Tbio.
DR PRO; PR:O95684; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O95684; protein.
DR Bgee; ENSG00000213066; Expressed in sperm and 194 other tissues.
DR ExpressionAtlas; O95684; baseline and differential.
DR Genevisible; O95684; HS.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005814; C:centriole; IDA:CACAO.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0030292; F:protein tyrosine kinase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0034453; P:microtubule anchoring; IEA:InterPro.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR InterPro; IPR018993; FOP_dimerisation-dom_N.
DR InterPro; IPR006594; LisH.
DR Pfam; PF09398; FOP_dimer; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection;
KW Chromosomal rearrangement; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..399
FT /note="Centrosomal protein 43"
FT /id="PRO_0000233293"
FT DOMAIN 70..102
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REGION 139..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 173..174
FT /note="Breakpoint for translocation to form CEP43-FGFR1 or
FT FGFR1-CEP43 fusion proteins"
FT MOD_RES 143
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 337
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q66JX5"
FT VAR_SEQ 1..249
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018119"
FT VAR_SEQ 174..193
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_018120"
FT VAR_SEQ 376..399
FT /note="LDDLTQDLTVSQLSDVADYLEDVA -> TITQLECLLSIGALHFKNTADIF
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018121"
FT VARIANT 190
FT /note="A -> G (in dbSNP:rs34617108)"
FT /id="VAR_061651"
FT VARIANT 271
FT /note="K -> N (in dbSNP:rs17856382)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_051000"
FT MUTAGEN 74
FT /note="V->F: Abolishes homodimerization and leads to
FT aggregation."
FT /evidence="ECO:0000269|PubMed:16690081"
FT CONFLICT 63
FT /note="K -> R (in Ref. 5; AAH11902)"
FT /evidence="ECO:0000305"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:2D68"
FT HELIX 69..84
FT /evidence="ECO:0007829|PDB:2D68"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:2D68"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:2D68"
FT TURN 120..124
FT /evidence="ECO:0007829|PDB:2D68"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:2D68"
SQ SEQUENCE 399 AA; 43065 MW; 7A4B65F627B9D272 CRC64;
MAATAAAVVA EEDTELRDLL VQTLENSGVL NRIKAELRAA VFLALEEQEK VENKTPLVNE
SLKKFLNTKD GRLVASLVAE FLQFFNLDFT LAVFQPETST LQGLEGRENL ARDLGIIEAE
GTVGGPLLLE VIRRCQQKEK GPTTGEGALD LSDVHSPPKS PEGKTSAQTT PSKIPRYKGQ
GKKKTSGQKA GDKKANDEAN QSDTSVSLSE PKSKSSLHLL SHETKIGSFL SNRTLDGKDK
AGLCPDEDDM EGDSFFDDPI PKPEKTYGLR KEPRKQAGSL ASLSDAPPLK SGLSSLAGAP
SLKDSESKRG NTVLKDLKLI SDKIGSLGLG TGEDDDYVDD FNSTSHRSEK SEISIGEEIE
EDLSVEIDDI NTSDKLDDLT QDLTVSQLSD VADYLEDVA
