CE290_HUMAN
ID CE290_HUMAN Reviewed; 2479 AA.
AC O15078; Q1PSK5; Q66GS8; Q9H2G6; Q9H6Q7; Q9H8I0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Centrosomal protein of 290 kDa;
DE Short=Cep290;
DE AltName: Full=Bardet-Biedl syndrome 14 protein;
DE AltName: Full=Cancer/testis antigen 87;
DE Short=CT87;
DE AltName: Full=Nephrocystin-6;
DE AltName: Full=Tumor antigen se2-2;
GN Name=CEP290; Synonyms=BBS14, KIAA0373, NPHP6;
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], FUNCTION, INTERACTION WITH ATF4, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INVOLVEMENT IN JBTS5 AND SLSN6.
RX PubMed=16682973; DOI=10.1038/ng1786;
RA Sayer J.A., Otto E.A., O'toole J.F., Nurnberg G., Kennedy M.A., Becker C.,
RA Hennies H.C., Helou J., Attanasio M., Fausett B.V., Utsch B., Khanna H.,
RA Liu Y., Drummond I., Kawakami I., Kusakabe T., Tsuda M., Ma L., Lee H.,
RA Larson R.G., Allen S.J., Wilkinson C.J., Nigg E.A., Shou C., Lillo C.,
RA Williams D.S., Hoppe B., Kemper M.J., Neuhaus T., Parisi M.A., Glass I.A.,
RA Petry M., Kispert A., Gloy J., Ganner A., Walz G., Zhu X., Goldman D.,
RA Nurnberg P., Swaroop A., Leroux M.R., Hildebrandt F.;
RT "The centrosomal protein nephrocystin-6 is mutated in Joubert syndrome and
RT activates transcription factor ATF4.";
RL Nat. Genet. 38:674-681(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1058.
RC TISSUE=Hepatoma, and Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 940-2479.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1616-2382, TISSUE SPECIFICITY, AND DISEASE.
RC TISSUE=Testis;
RX PubMed=11149944; DOI=10.1073/pnas.98.2.629;
RA Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., Schadendorf D.;
RT "Serological detection of cutaneous T-cell lymphoma-associated antigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001).
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 INVOLVEMENT IN LCA10.
RX PubMed=16909394; DOI=10.1086/507318;
RA den Hollander A.I., Koenekoop R.K., Yzer S., Lopez I., Arends M.L.,
RA Voesenek K.E.J., Zonneveld M.N., Strom T.M., Meitinger T., Brunner H.G.,
RA Hoyng C.B., van den Born L.I., Rohrschneider K., Cremers F.P.M.;
RT "Mutations in the CEP290 (NPHP6) gene are a frequent cause of Leber
RT congenital amaurosis.";
RL Am. J. Hum. Genet. 79:556-561(2006).
RN [8]
RP INTERACTION WITH CC2D2A.
RX PubMed=18950740; DOI=10.1016/j.ajhg.2008.10.002;
RA Gorden N.T., Arts H.H., Parisi M.A., Coene K.L.M., Letteboer S.J.F.,
RA van Beersum S.E.C., Mans D.A., Hikida A., Eckert M., Knutzen D.,
RA Alswaid A.F., Oezyurek H., Dibooglu S., Otto E.A., Liu Y., Davis E.E.,
RA Hutter C.M., Bammler T.K., Farin F.M., Dorschner M., Topcu M., Zackai E.H.,
RA Rosenthal P., Owens K.N., Katsanis N., Vincent J.B., Hildebrandt F.,
RA Rubel E.W., Raible D.W., Knoers N.V.A.M., Chance P.F., Roepman R.,
RA Moens C.B., Glass I.A., Doherty D.;
RT "CC2D2A is mutated in Joubert syndrome and interacts with the ciliopathy-
RT associated basal body protein CEP290.";
RL Am. J. Hum. Genet. 83:559-571(2008).
RN [9]
RP FUNCTION, AND INTERACTION WITH CCP110.
RX PubMed=18694559; DOI=10.1016/j.devcel.2008.07.004;
RA Tsang W.Y., Bossard C., Khanna H., Peraenen J., Swaroop A., Malhotra V.,
RA Dynlacht B.D.;
RT "CP110 suppresses primary cilia formation through its interaction with
RT CEP290, a protein deficient in human ciliary disease.";
RL Dev. Cell 15:187-197(2008).
RN [10]
RP INTERACTION WITH IQCB1, AND SELF-ASSOCIATION.
RX PubMed=18723859; DOI=10.1093/hmg/ddn260;
RA Schaefer T., Puetz M., Lienkamp S., Ganner A., Bergbreiter A.,
RA Ramachandran H., Gieloff V., Gerner M., Mattonet C., Czarnecki P.G.,
RA Sayer J.A., Otto E.A., Hildebrandt F., Kramer-Zucker A., Walz G.;
RT "Genetic and physical interaction between the NPHP5 and NPHP6 gene
RT products.";
RL Hum. Mol. Genet. 17:3655-3662(2008).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17705300; DOI=10.1002/humu.20614;
RA Frank V., den Hollander A.I., Bruechle N.O., Zonneveld M.N., Nuernberg G.,
RA Becker C., Du Bois G., Kendziorra H., Roosing S., Senderek J.,
RA Nuernberg P., Cremers F.P., Zerres K., Bergmann C.;
RT "Mutations of the CEP290 gene encoding a centrosomal protein cause Meckel-
RT Gruber syndrome.";
RL Hum. Mutat. 29:45-52(2008).
RN [12]
RP INVOLVEMENT IN BBS14.
RX PubMed=18327255; DOI=10.1038/ng.97;
RA Leitch C.C., Zaghloul N.A., Davis E.E., Stoetzel C., Diaz-Font A., Rix S.,
RA Alfadhel M., Lewis R.A., Eyaid W., Banin E., Dollfus H., Beales P.L.,
RA Badano J.L., Katsanis N.;
RT "Hypomorphic mutations in syndromic encephalocele genes are associated with
RT Bardet-Biedl syndrome.";
RL Nat. Genet. 40:443-448(2008).
RN [13]
RP INTERACTION WITH RPGRIP1.
RX PubMed=20200501; DOI=10.1038/ki.2010.27;
RA Gerner M., Haribaskar R., Puetz M., Czerwitzki J., Walz G., Schaefer T.;
RT "The retinitis pigmentosa GTPase regulator interacting protein 1 (RPGRIP1)
RT links RPGR to the nephronophthisis protein network.";
RL Kidney Int. 77:891-896(2010).
RN [14]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH IQCB1.
RX PubMed=21565611; DOI=10.1016/j.cell.2011.04.019;
RA Sang L., Miller J.J., Corbit K.C., Giles R.H., Brauer M.J., Otto E.A.,
RA Baye L.M., Wen X., Scales S.J., Kwong M., Huntzicker E.G., Sfakianos M.K.,
RA Sandoval W., Bazan J.F., Kulkarni P., Garcia-Gonzalo F.R., Seol A.D.,
RA O'Toole J.F., Held S., Reutter H.M., Lane W.S., Rafiq M.A., Noor A.,
RA Ansar M., Devi A.R., Sheffield V.C., Slusarski D.C., Vincent J.B.,
RA Doherty D.A., Hildebrandt F., Reiter J.F., Jackson P.K.;
RT "Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes
RT and pathways.";
RL Cell 145:513-528(2011).
RN [15]
RP INTERACTION WITH ZNF423.
RX PubMed=22863007; DOI=10.1016/j.cell.2012.06.028;
RA Chaki M., Airik R., Ghosh A.K., Giles R.H., Chen R., Slaats G.G., Wang H.,
RA Hurd T.W., Zhou W., Cluckey A., Gee H.Y., Ramaswami G., Hong C.J.,
RA Hamilton B.A., Cervenka I., Ganji R.S., Bryja V., Arts H.H.,
RA van Reeuwijk J., Oud M.M., Letteboer S.J., Roepman R., Husson H.,
RA Ibraghimov-Beskrovnaya O., Yasunaga T., Walz G., Eley L., Sayer J.A.,
RA Schermer B., Liebau M.C., Benzing T., Le Corre S., Drummond I., Janssen S.,
RA Allen S.J., Natarajan S., O'Toole J.F., Attanasio M., Saunier S.,
RA Antignac C., Koenekoop R.K., Ren H., Lopez I., Nayir A., Stoetzel C.,
RA Dollfus H., Massoudi R., Gleeson J.G., Andreoli S.P., Doherty D.G.,
RA Lindstrad A., Golzio C., Katsanis N., Pape L., Abboud E.B., Al-Rajhi A.A.,
RA Lewis R.A., Omran H., Lee E.Y., Wang S., Sekiguchi J.M., Saunders R.,
RA Johnson C.A., Garner E., Vanselow K., Andersen J.S., Shlomai J.,
RA Nurnberg G., Nurnberg P., Levy S., Smogorzewska A., Otto E.A.,
RA Hildebrandt F.;
RT "Exome capture reveals ZNF423 and CEP164 mutations, linking renal
RT ciliopathies to DNA damage response signaling.";
RL Cell 150:533-548(2012).
RN [16]
RP INTERACTION WITH FAM161A.
RX PubMed=22940612; DOI=10.1093/hmg/dds368;
RA Di Gioia S.A., Letteboer S.J., Kostic C., Bandah-Rozenfeld D.,
RA Hetterschijt L., Sharon D., Arsenijevic Y., Roepman R., Rivolta C.;
RT "FAM161A, associated with retinitis pigmentosa, is a component of the
RT cilia-basal body complex and interacts with proteins involved in
RT ciliopathies.";
RL Hum. Mol. Genet. 21:5174-5184(2012).
RN [17]
RP INTERACTION WITH CEP131, AND SUBCELLULAR LOCATION.
RX PubMed=22797915; DOI=10.1242/jcs.104059;
RA Staples C.J., Myers K.N., Beveridge R.D., Patil A.A., Lee A.J., Swanton C.,
RA Howell M., Boulton S.J., Collis S.J.;
RT "The centriolar satellite protein Cep131 is important for genome
RT stability.";
RL J. Cell Sci. 125:4770-4779(2012).
RN [18]
RP UBIQUITINATION, ASSOCIATION WITH MICROTUBULE, AND SUBCELLULAR LOCATION.
RX PubMed=24121310; DOI=10.1038/emboj.2013.223;
RA Villumsen B.H., Danielsen J.R., Povlsen L., Sylvestersen K.B., Merdes A.,
RA Beli P., Yang Y.G., Choudhary C., Nielsen M.L., Mailand N.,
RA Bekker-Jensen S.;
RT "A new cellular stress response that triggers centriolar satellite
RT reorganization and ciliogenesis.";
RL EMBO J. 32:3029-3040(2013).
RN [19]
RP INTERACTION WITH IQCB1.
RX PubMed=23446637; DOI=10.1093/hmg/ddt100;
RA Barbelanne M., Song J., Ahmadzai M., Tsang W.Y.;
RT "Pathogenic NPHP5 mutations impair protein interaction with Cep290, a
RT prerequisite for ciliogenesis.";
RL Hum. Mol. Genet. 22:2482-2494(2013).
RN [20]
RP SUBCELLULAR LOCATION, AND ASSOCIATION WITH MICROTUBULES.
RX PubMed=24051377; DOI=10.1172/jci69448;
RA Drivas T.G., Holzbaur E.L., Bennett J.;
RT "Disruption of CEP290 microtubule/membrane-binding domains causes retinal
RT degeneration.";
RL J. Clin. Invest. 123:4525-4539(2013).
RN [21]
RP INTERACTION WITH CEP162.
RX PubMed=23644468; DOI=10.1038/ncb2739;
RA Wang W.J., Tay H.G., Soni R., Perumal G.S., Goll M.G., Macaluso F.P.,
RA Asara J.M., Amack J.D., Bryan Tsou M.F.;
RT "CEP162 is an axoneme-recognition protein promoting ciliary transition zone
RT assembly at the cilia base.";
RL Nat. Cell Biol. 15:591-601(2013).
RN [22]
RP INTERACTION WITH BBS4, AND SUBCELLULAR LOCATION.
RX PubMed=23943788; DOI=10.1093/hmg/ddt394;
RA Zhang Y., Seo S., Bhattarai S., Bugge K., Searby C.C., Zhang Q.,
RA Drack A.V., Stone E.M., Sheffield V.C.;
RT "BBS mutations modify phenotypic expression of CEP290-related
RT ciliopathies.";
RL Hum. Mol. Genet. 23:40-51(2014).
RN [23]
RP FUNCTION, AND INTERACTION WITH TALPID3.
RX PubMed=24421332; DOI=10.1083/jcb.201304153;
RA Kobayashi T., Kim S., Lin Y.C., Inoue T., Dynlacht B.D.;
RT "The CP110-interacting proteins Talpid3 and Cep290 play overlapping and
RT distinct roles in cilia assembly.";
RL J. Cell Biol. 204:215-229(2014).
RN [24]
RP FUNCTION, AND INVOLVEMENT IN JBTS5.
RX PubMed=26166481; DOI=10.1016/j.ajhg.2015.06.003;
RA Alby C., Piquand K., Huber C., Megarbane A., Ichkou A., Legendre M.,
RA Pelluard F., Encha-Ravazi F., Abi-Tayeh G., Bessieres B.,
RA El Chehadeh-Djebbar S., Laurent N., Faivre L., Sztriha L., Zombor M.,
RA Szabo H., Failler M., Garfa-Traore M., Bole C., Nitschke P., Nizon M.,
RA Elkhartoufi N., Clerget-Darpoux F., Munnich A., Lyonnet S., Vekemans M.,
RA Saunier S., Cormier-Daire V., Attie-Bitach T., Thomas S.;
RT "Mutations in KIAA0586 cause lethal ciliopathies ranging from a
RT hydrolethalus phenotype to short-rib polydactyly syndrome.";
RL Am. J. Hum. Genet. 97:311-318(2015).
RN [25]
RP FUNCTION, AND INTERACTION WITH THE BBSOME COMPLEX AND IQCB1.
RX PubMed=25552655; DOI=10.1093/hmg/ddu738;
RA Barbelanne M., Hossain D., Chan D.P., Peraenen J., Tsang W.Y.;
RT "Nephrocystin proteins NPHP5 and Cep290 regulate BBSome integrity, ciliary
RT trafficking and cargo delivery.";
RL Hum. Mol. Genet. 24:2185-2200(2015).
RN [26]
RP VARIANT JBTS5 CYS-7.
RX PubMed=16682970; DOI=10.1038/ng1805;
RG International Joubert syndrome related disorders (JSRD) study group;
RA Valente E.M., Silhavy J.L., Brancati F., Barrano G., Krishnaswami S.R.,
RA Castori M., Lancaster M.A., Boltshauser E., Boccone L., Al-Gazali L.,
RA Fazzi E., Signorini S., Louie C.M., Bellacchio E., Bertini E.,
RA Dallapiccola B., Gleeson J.G.;
RT "Mutations in CEP290, which encodes a centrosomal protein, cause
RT pleiotropic forms of Joubert syndrome.";
RL Nat. Genet. 38:623-625(2006).
RN [27]
RP INVOLVEMENT IN MKS4.
RX PubMed=17564974; DOI=10.1086/519494;
RA Baala L., Audollent S., Martinovic J., Ozilou C., Babron M.-C.,
RA Sivanandamoorthy S., Saunier S., Salomon R., Gonzales M., Rattenberry E.,
RA Esculpavit C., Toutain A., Moraine C., Parent P., Marcorelles P.,
RA Dauge M.-C., Roume J., Le Merrer M., Meiner V., Meir K., Menez F.,
RA Beaufrere A.-M., Francannet C., Tantau J., Sinico M., Dumez Y.,
RA MacDonald F., Munnich A., Lyonnet S., Gubler M.-C., Genin E., Johnson C.A.,
RA Vekemans M., Encha-Razavi F., Attie-Bitach T.;
RT "Pleiotropic effects of CEP290 (NPHP6) mutations extend to Meckel
RT syndrome.";
RL Am. J. Hum. Genet. 81:170-179(2007).
RN [28]
RP INTERACTION WITH CCDC13.
RX PubMed=24816561; DOI=10.1242/jcs.147785;
RA Staples C.J., Myers K.N., Beveridge R.D., Patil A.A., Howard A.E.,
RA Barone G., Lee A.J., Swanton C., Howell M., Maslen S., Skehel J.M.,
RA Boulton S.J., Collis S.J.;
RT "Ccdc13 is a novel human centriolar satellite protein required for
RT ciliogenesis and genome stability.";
RL J. Cell Sci. 127:2910-2919(2014).
RN [29]
RP INTERACTION WITH CCDC66.
RX PubMed=28235840; DOI=10.1242/jcs.196832;
RA Conkar D., Culfa E., Odabasi E., Rauniyar N., Yates J.R. III,
RA Firat-Karalar E.N.;
RT "The centriolar satellite protein CCDC66 interacts with CEP290 and
RT functions in cilium formation and trafficking.";
RL J. Cell Sci. 130:1450-1462(2017).
RN [30]
RP INTERACTION WITH ARMC9 AND CSPP1.
RX PubMed=32453716; DOI=10.1172/jci131656;
RG University of Washington Center for Mendelian Genomics;
RG Genomics England Research Consortium;
RA Latour B.L., Van De Weghe J.C., Rusterholz T.D., Letteboer S.J., Gomez A.,
RA Shaheen R., Gesemann M., Karamzade A., Asadollahi M., Barroso-Gil M.,
RA Chitre M., Grout M.E., van Reeuwijk J., van Beersum S.E., Miller C.V.,
RA Dempsey J.C., Morsy H., Bamshad M.J., Nickerson D.A., Neuhauss S.C.,
RA Boldt K., Ueffing M., Keramatipour M., Sayer J.A., Alkuraya F.S.,
RA Bachmann-Gagescu R., Roepman R., Doherty D.;
RT "Dysfunction of the ciliary ARMC9/TOGARAM1 protein module causes Joubert
RT syndrome.";
RL J. Clin. Invest. 130:4423-4439(2020).
RN [31]
RP VARIANTS GLN-277; GLY-664; GLU-838; TRP-906 AND LYS-2228.
RX PubMed=17564967; DOI=10.1086/519026;
RA Brancati F., Barrano G., Silhavy J.L., Marsh S.E., Travaglini L.,
RA Bielas S.L., Amorini M., Zablocka D., Kayserili H., Al-Gazali L.,
RA Bertini E., Boltshauser E., D'Hooghe M., Fazzi E., Fenerci E.Y.,
RA Hennekam R.C., Kiss A., Lees M.M., Marco E., Phadke S.R., Rigoli L.,
RA Romano S., Salpietro C.D., Sherr E.H., Signorini S., Stromme P., Stuart B.,
RA Sztriha L., Viskochil D.H., Yuksel A., Dallapiccola B., Valente E.M.,
RA Gleeson J.G.;
RT "CEP290 mutations are frequently identified in the oculo-renal form of
RT Joubert syndrome-related disorders.";
RL Am. J. Hum. Genet. 81:104-113(2007).
RN [32]
RP VARIANT GLY-664.
RX PubMed=17617513; DOI=10.1136/jmg.2007.052027;
RA Helou J., Otto E.A., Attanasio M., Allen S.J., Parisi M.A., Glass I.,
RA Utsch B., Hashmi S., Fazzi E., Omran H., O'Toole J.F., Sayer J.A.,
RA Hildebrandt F.;
RT "Mutation analysis of NPHP6/CEP290 in patients with Joubert syndrome and
RT Senior-Loken syndrome.";
RL J. Med. Genet. 44:657-663(2007).
RN [33]
RP VARIANTS PRO-1566 AND PRO-1694, AND VARIANT SLSN6 CYS-7.
RX PubMed=20683928; DOI=10.1002/humu.21336;
RA Coppieters F., Casteels I., Meire F., De Jaegere S., Hooghe S.,
RA van Regemorter N., Van Esch H., Matuleviciene A., Nunes L., Meersschaut V.,
RA Walraedt S., Standaert L., Coucke P., Hoeben H., Kroes H.Y.,
RA Vande Walle J., de Ravel T., Leroy B.P., De Baere E.;
RT "Genetic screening of LCA in Belgium: predominance of CEP290 and
RT identification of potential modifier alleles in AHI1 of CEP290-related
RT phenotypes.";
RL Hum. Mutat. 31:E1709-E1766(2010).
RN [34]
RP VARIANT CYS-2210, AND SUBCELLULAR LOCATION.
RX PubMed=21493627; DOI=10.1093/hmg/ddr151;
RA Hopp K., Heyer C.M., Hommerding C.J., Henke S.A., Sundsbak J.L., Patel S.,
RA Patel P., Consugar M.B., Czarnecki P.G., Gliem T.J., Torres V.E.,
RA Rossetti S., Harris P.C.;
RT "B9D1 is revealed as a novel Meckel syndrome (MKS) gene by targeted exon-
RT enriched next-generation sequencing and deletion analysis.";
RL Hum. Mol. Genet. 20:2524-2534(2011).
RN [35]
RP VARIANT GLY-2263.
RX PubMed=21602930; DOI=10.1371/journal.pone.0019458;
RA Li L., Xiao X., Li S., Jia X., Wang P., Guo X., Jiao X., Zhang Q.,
RA Hejtmancik J.F.;
RT "Detection of variants in 15 genes in 87 unrelated Chinese patients with
RT Leber congenital amaurosis.";
RL PLoS ONE 6:E19458-E19458(2011).
RN [36]
RP VARIANT JBTS5 LYS-534.
RX PubMed=22425360; DOI=10.1016/j.ajhg.2012.02.011;
RA Srour M., Schwartzentruber J., Hamdan F.F., Ospina L.H., Patry L.,
RA Labuda D., Massicotte C., Dobrzeniecka S., Capo-Chichi J.M.,
RA Papillon-Cavanagh S., Samuels M.E., Boycott K.M., Shevell M.I.,
RA Laframboise R., Desilets V., Maranda B., Rouleau G.A., Majewski J.,
RA Michaud J.L.;
RT "Mutations in C5ORF42 cause Joubert syndrome in the French Canadian
RT population.";
RL Am. J. Hum. Genet. 90:693-700(2012).
RN [37]
RP VARIANT JBTS5 THR-2134.
RX PubMed=26477546; DOI=10.1016/j.ajhg.2015.09.009;
RG Care4Rare Canada Consortium;
RA Srour M., Hamdan F.F., McKnight D., Davis E., Mandel H.,
RA Schwartzentruber J., Martin B., Patry L., Nassif C., Dionne-Laporte A.,
RA Ospina L.H., Lemyre E., Massicotte C., Laframboise R., Maranda B.,
RA Labuda D., Decarie J.C., Rypens F., Goldsher D., Fallet-Bianco C.,
RA Soucy J.F., Laberge A.M., Maftei C., Boycott K., Brais B., Boucher R.M.,
RA Rouleau G.A., Katsanis N., Majewski J., Elpeleg O., Kukolich M.K.,
RA Shalev S., Michaud J.L.;
RT "Joubert Syndrome in French Canadians and Identification of Mutations in
RT CEP104.";
RL Am. J. Hum. Genet. 97:744-753(2015).
CC -!- FUNCTION: Involved in early and late steps in cilia formation. Its
CC association with CCP110 is required for inhibition of primary cilia
CC formation by CCP110 (PubMed:18694559). May play a role in early
CC ciliogenesis in the disappearance of centriolar satellites and in the
CC transition of primary ciliar vesicles (PCVs) to capped ciliary vesicles
CC (CCVs). Required for the centrosomal recruitment of RAB8A and for the
CC targeting of centriole satellite proteins to centrosomes such as of
CC PCM1 (PubMed:24421332). Required for the correct localization of
CC ciliary and phototransduction proteins in retinal photoreceptor cells;
CC may play a role in ciliary transport processes (By similarity).
CC Required for efficient recruitment of RAB8A to primary cilium
CC (PubMed:17705300). In the ciliary transition zone is part of the
CC tectonic-like complex which is required for tissue-specific
CC ciliogenesis and may regulate ciliary membrane composition (By
CC similarity). Involved in regulation of the BBSome complex integrity,
CC specifically for presence of BBS2, BBS5 and BBS8/TTC8 in the complex,
CC and in ciliary targeting of selected BBSome cargos. May play a role in
CC controlling entry of the BBSome complex to cilia possibly implicating
CC IQCB1/NPHP5 (PubMed:25552655). Activates ATF4-mediated transcription
CC (PubMed:16682973). {ECO:0000250|UniProtKB:Q6A078,
CC ECO:0000269|PubMed:16682973, ECO:0000269|PubMed:17705300,
CC ECO:0000269|PubMed:18694559, ECO:0000269|PubMed:24421332,
CC ECO:0000269|PubMed:25552655}.
CC -!- SUBUNIT: Part of the tectonic-like complex (also named B9 complex) (By
CC similarity). Interacts with ATF4 via its N-terminal region
CC (PubMed:16682973). Associates with the BBSome complex (PubMed:25552655,
CC PubMed:23943788), interacting (via N-terminus) with BBS4
CC (PubMed:23943788). Interacts with IQCB1/NPHP5; IQCB1 and CEP290/NPHP6
CC are proposed to form a functional NPHP5-6 module localized to the
CC centrosome. Interacts with NPHP4; the interaction likely requires
CC additional interactors. Interacts with ZNF423, FAM161A, CEP162, CEP162,
CC CEP131, TALPID3, CCDC13, CC2D2A, RPGRIP1 (PubMed:18950740,
CC PubMed:18723859, PubMed:21565611, PubMed:22863007, PubMed:22940612,
CC PubMed:22797915, PubMed:23446637, PubMed:23644468, PubMed:24421332,
CC PubMed:24816561, PubMed:20200501). Can self-associate (homo- or
CC heteromeric) (PubMed:18723859). Interacts with CCP110; required for
CC suppressing cilia formation (PubMed:18694559). Interacts with RPGR (By
CC similarity). Associates (via C-terminus) with microtubules
CC (PubMed:24121310, PubMed:24051377); association to microtubule is
CC reduced in response to cellular stress, such as ultraviolet light (UV)
CC radiation or heat shock, in a process that requires p38 MAP kinase
CC signaling (PubMed:24121310). Interacts with FAM161A (By similarity).
CC Interacts with PCM1 (By similarity). Interacts with CCDC66
CC (PubMed:28235840). Interacts with ARMC9 and CSPP1 (PubMed:32453716).
CC {ECO:0000250|UniProtKB:Q6A078, ECO:0000250|UniProtKB:Q9TU23,
CC ECO:0000269|PubMed:16682973, ECO:0000269|PubMed:18694559,
CC ECO:0000269|PubMed:18723859, ECO:0000269|PubMed:18950740,
CC ECO:0000269|PubMed:20200501, ECO:0000269|PubMed:21565611,
CC ECO:0000269|PubMed:22797915, ECO:0000269|PubMed:22863007,
CC ECO:0000269|PubMed:22940612, ECO:0000269|PubMed:23446637,
CC ECO:0000269|PubMed:23644468, ECO:0000269|PubMed:23943788,
CC ECO:0000269|PubMed:24051377, ECO:0000269|PubMed:24121310,
CC ECO:0000269|PubMed:24421332, ECO:0000269|PubMed:24816561,
CC ECO:0000269|PubMed:25552655, ECO:0000269|PubMed:28235840,
CC ECO:0000269|PubMed:32453716, ECO:0000305}.
CC -!- INTERACTION:
CC O15078; Q9BUW7: BBLN; NbExp=6; IntAct=EBI-1811944, EBI-752084;
CC O15078; P62158: CALM3; NbExp=5; IntAct=EBI-1811944, EBI-397435;
CC O15078; O43303: CCP110; NbExp=18; IntAct=EBI-1811944, EBI-1566217;
CC O15078; Q9UPN4: CEP131; NbExp=9; IntAct=EBI-1811944, EBI-2558372;
CC O15078; Q5TB80: CEP162; NbExp=7; IntAct=EBI-1811944, EBI-1059012;
CC O15078; O15078: CEP290; NbExp=2; IntAct=EBI-1811944, EBI-1811944;
CC O15078; Q15051: IQCB1; NbExp=24; IntAct=EBI-1811944, EBI-2805823;
CC O15078; Q86T90: KIAA1328; NbExp=3; IntAct=EBI-1811944, EBI-3437878;
CC O15078; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-1811944, EBI-79165;
CC O15078; Q2M1K9: ZNF423; NbExp=3; IntAct=EBI-1811944, EBI-950016;
CC O15078; P62161: Calm3; Xeno; NbExp=2; IntAct=EBI-1811944, EBI-397530;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:16682973, ECO:0000269|PubMed:21493627,
CC ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:22797915}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriolar
CC satellite {ECO:0000269|PubMed:17705300, ECO:0000269|PubMed:21493627,
CC ECO:0000269|PubMed:22797915, ECO:0000269|PubMed:23943788,
CC ECO:0000269|PubMed:24121310}. Nucleus {ECO:0000250|UniProtKB:Q6A078}.
CC Cell projection, cilium {ECO:0000269|PubMed:23943788}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q6A078}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000269|PubMed:22797915}. Cytoplasmic vesicle
CC {ECO:0000303|PubMed:24051377}. Note=Displaced from centriolar
CC satellites in response to cellular stress, such as ultraviolet light
CC (UV) radiation or heat shock (PubMed:24121310). Found in the connecting
CC cilium of photoreceptor cells, base of cilium in kidney intramedullary
CC collecting duct cells (By similarity). Localizes at the transition
CC zone, a region between the basal body and the ciliary axoneme
CC (PubMed:23943788). Localization at the ciliary transition zone as well
CC as at centriolar satellites is BBsome-dependent (PubMed:23943788).
CC {ECO:0000250|UniProtKB:Q6A078, ECO:0000269|PubMed:23943788,
CC ECO:0000269|PubMed:24121310}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed strongly in placenta and
CC weakly in brain. {ECO:0000269|PubMed:11149944,
CC ECO:0000269|PubMed:16682973}.
CC -!- PTM: Ubiquitinated. May undergo monoubiquitination; monoubiquitination
CC is inhibited in response to cellular stress, such as ultraviolet light
CC (UV) radiation or heat shock, but does not cause it displacement from
CC centriolar satellites. {ECO:0000269|PubMed:24121310}.
CC -!- DISEASE: Joubert syndrome 5 (JBTS5) [MIM:610188]: A disorder presenting
CC with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal
CC breathing abnormalities and psychomotor delay. Neuroradiologically, it
CC is characterized by cerebellar vermian hypoplasia/aplasia, thickened
CC and reoriented superior cerebellar peduncles, and an abnormally large
CC interpeduncular fossa, giving the appearance of a molar tooth on
CC transaxial slices (molar tooth sign). Additional variable features
CC include retinal dystrophy and renal disease. Joubert syndrome type 5
CC shares the neurologic and neuroradiologic features of Joubert syndrome
CC together with severe retinal dystrophy and/or progressive renal failure
CC characterized by nephronophthisis. {ECO:0000269|PubMed:16682970,
CC ECO:0000269|PubMed:16682973, ECO:0000269|PubMed:22425360,
CC ECO:0000269|PubMed:26166481, ECO:0000269|PubMed:26477546}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Senior-Loken syndrome 6 (SLSN6) [MIM:610189]: A renal-retinal
CC disorder characterized by progressive wasting of the filtering unit of
CC the kidney (nephronophthisis), with or without medullary cystic renal
CC disease, and progressive eye disease. Typically this disorder becomes
CC apparent during the first year of life. {ECO:0000269|PubMed:20683928}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Leber congenital amaurosis 10 (LCA10) [MIM:611755]: A severe
CC dystrophy of the retina, typically becoming evident in the first years
CC of life. Visual function is usually poor and often accompanied by
CC nystagmus, sluggish or near-absent pupillary responses, photophobia,
CC high hyperopia and keratoconus. {ECO:0000269|PubMed:16909394}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Meckel syndrome 4 (MKS4) [MIM:611134]: A disorder
CC characterized by a combination of renal cysts and variably associated
CC features including developmental anomalies of the central nervous
CC system (typically encephalocele), hepatic ductal dysplasia and cysts,
CC and polydactyly. {ECO:0000269|PubMed:17564974}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Note=Antibodies against CEP290 are present in sera from
CC patients with cutaneous T-cell lymphomas, but not in the healthy
CC control population. {ECO:0000269|PubMed:11149944}.
CC -!- DISEASE: Bardet-Biedl syndrome 14 (BBS14) [MIM:615991]: A syndrome
CC characterized by usually severe pigmentary retinopathy, early-onset
CC obesity, polydactyly, hypogenitalism, renal malformation and
CC intellectual disability. Secondary features include diabetes mellitus,
CC hypertension and congenital heart disease. Bardet-Biedl syndrome
CC inheritance is autosomal recessive, but three mutated alleles (two at
CC one locus, and a third at a second locus) may be required for clinical
CC manifestation of some forms of the disease.
CC {ECO:0000269|PubMed:18327255}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG34904.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AK023677; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB15196.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=CEP290 Mutation Database;
CC URL="https://cep290base.cmgg.be/";
CC ---------------------------------------------------------------------------
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DR EMBL; DQ109808; AAZ83370.1; -; mRNA.
DR EMBL; AC091516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB002371; BAA20828.2; -; mRNA.
DR EMBL; AK023677; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK025632; BAB15196.1; ALT_SEQ; mRNA.
DR EMBL; AF273044; AAG34904.1; ALT_SEQ; mRNA.
DR EMBL; BK005587; DAA05591.1; -; mRNA.
DR CCDS; CCDS55858.1; -.
DR RefSeq; NP_079390.3; NM_025114.3.
DR AlphaFoldDB; O15078; -.
DR SMR; O15078; -.
DR BioGRID; 123163; 145.
DR CORUM; O15078; -.
DR DIP; DIP-46541N; -.
DR IntAct; O15078; 132.
DR MINT; O15078; -.
DR STRING; 9606.ENSP00000448012; -.
DR iPTMnet; O15078; -.
DR PhosphoSitePlus; O15078; -.
DR BioMuta; CEP290; -.
DR EPD; O15078; -.
DR jPOST; O15078; -.
DR MassIVE; O15078; -.
DR MaxQB; O15078; -.
DR PaxDb; O15078; -.
DR PeptideAtlas; O15078; -.
DR PRIDE; O15078; -.
DR Antibodypedia; 29900; 262 antibodies from 35 providers.
DR DNASU; 80184; -.
DR Ensembl; ENST00000552810.6; ENSP00000448012.1; ENSG00000198707.17.
DR GeneID; 80184; -.
DR KEGG; hsa:80184; -.
DR MANE-Select; ENST00000552810.6; ENSP00000448012.1; NM_025114.4; NP_079390.3.
DR UCSC; uc001taq.4; human.
DR CTD; 80184; -.
DR DisGeNET; 80184; -.
DR GeneCards; CEP290; -.
DR GeneReviews; CEP290; -.
DR HGNC; HGNC:29021; CEP290.
DR HPA; ENSG00000198707; Low tissue specificity.
DR MalaCards; CEP290; -.
DR MIM; 610142; gene.
DR MIM; 610188; phenotype.
DR MIM; 610189; phenotype.
DR MIM; 611134; phenotype.
DR MIM; 611755; phenotype.
DR MIM; 615991; phenotype.
DR neXtProt; NX_O15078; -.
DR OpenTargets; ENSG00000198707; -.
DR Orphanet; 110; Bardet-Biedl syndrome.
DR Orphanet; 2318; Joubert syndrome with oculorenal defect.
DR Orphanet; 65; Leber congenital amaurosis.
DR Orphanet; 564; Meckel syndrome.
DR Orphanet; 3156; Senior-Loken syndrome.
DR PharmGKB; PA143485433; -.
DR VEuPathDB; HostDB:ENSG00000198707; -.
DR eggNOG; ENOG502QPTZ; Eukaryota.
DR GeneTree; ENSGT00730000111039; -.
DR HOGENOM; CLU_246874_0_0_1; -.
DR InParanoid; O15078; -.
DR OrthoDB; 27774at2759; -.
DR PhylomeDB; O15078; -.
DR TreeFam; TF326911; -.
DR PathwayCommons; O15078; -.
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-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; O15078; -.
DR SIGNOR; O15078; -.
DR BioGRID-ORCS; 80184; 48 hits in 1082 CRISPR screens.
DR ChiTaRS; CEP290; human.
DR GeneWiki; CEP290; -.
DR GenomeRNAi; 80184; -.
DR Pharos; O15078; Tbio.
DR PRO; PR:O15078; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O15078; protein.
DR Bgee; ENSG00000198707; Expressed in right uterine tube and 186 other tissues.
DR ExpressionAtlas; O15078; baseline and differential.
DR Genevisible; O15078; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0035869; C:ciliary transition zone; IDA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HGNC-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0036038; C:MKS complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0032391; C:photoreceptor connecting cilium; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043010; P:camera-type eye development; IBA:GO_Central.
DR GO; GO:0097711; P:ciliary basal body-plasma membrane docking; IBA:GO_Central.
DR GO; GO:1905349; P:ciliary transition zone assembly; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IDA:UniProtKB.
DR GO; GO:0042462; P:eye photoreceptor cell development; ISS:HGNC-UCL.
DR GO; GO:0030902; P:hindbrain development; ISS:HGNC-UCL.
DR GO; GO:0001822; P:kidney development; IBA:GO_Central.
DR GO; GO:1905515; P:non-motile cilium assembly; IBA:GO_Central.
DR GO; GO:0030916; P:otic vesicle formation; ISS:HGNC-UCL.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:HGNC-UCL.
DR GO; GO:0048793; P:pronephros development; ISS:HGNC-UCL.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR GO; GO:0070201; P:regulation of establishment of protein localization; IMP:MGI.
DR InterPro; IPR032321; Cep209_CC5.
DR InterPro; IPR026201; Cep290.
DR PANTHER; PTHR18879; PTHR18879; 3.
DR Pfam; PF16574; CEP209_CC5; 1.
PE 1: Evidence at protein level;
KW Activator; Bardet-Biedl syndrome; Cell projection; Ciliopathy; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Disease variant; Intellectual disability; Joubert syndrome;
KW Leber congenital amaurosis; Meckel syndrome; Nephronophthisis; Nucleus;
KW Obesity; Protein transport; Reference proteome; Senior-Loken syndrome;
KW Transport; Ubl conjugation.
FT CHAIN 1..2479
FT /note="Centrosomal protein of 290 kDa"
FT /id="PRO_0000089464"
FT REGION 1..695
FT /note="Self-association (with itself or C-terminus)"
FT /evidence="ECO:0000269|PubMed:18723859"
FT REGION 149..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..896
FT /note="Interaction with IQCB1"
FT /evidence="ECO:0000269|PubMed:18723859"
FT REGION 1966..2479
FT /note="Self-association (with itself or N-terminus)"
FT /evidence="ECO:0000269|PubMed:18723859"
FT REGION 2458..2479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 59..565
FT /evidence="ECO:0000255"
FT COILED 598..664
FT /evidence="ECO:0000255"
FT COILED 697..931
FT /evidence="ECO:0000255"
FT COILED 958..1027
FT /evidence="ECO:0000255"
FT COILED 1071..1498
FT /evidence="ECO:0000255"
FT COILED 1533..1584
FT /evidence="ECO:0000255"
FT COILED 1635..2452
FT /evidence="ECO:0000255"
FT VARIANT 7
FT /note="W -> C (in JBTS5 and SLSN6; dbSNP:rs62635288)"
FT /evidence="ECO:0000269|PubMed:16682970,
FT ECO:0000269|PubMed:20683928"
FT /id="VAR_028356"
FT VARIANT 277
FT /note="E -> Q (in dbSNP:rs45502896)"
FT /evidence="ECO:0000269|PubMed:17564967"
FT /id="VAR_064397"
FT VARIANT 534
FT /note="E -> K (in JBTS5; dbSNP:rs895126773)"
FT /evidence="ECO:0000269|PubMed:22425360"
FT /id="VAR_068168"
FT VARIANT 664
FT /note="D -> G (in dbSNP:rs79705698)"
FT /evidence="ECO:0000269|PubMed:17564967,
FT ECO:0000269|PubMed:17617513"
FT /id="VAR_064398"
FT VARIANT 838
FT /note="K -> E (in dbSNP:rs11104738)"
FT /evidence="ECO:0000269|PubMed:17564967"
FT /id="VAR_031058"
FT VARIANT 906
FT /note="L -> W (in dbSNP:rs7970228)"
FT /evidence="ECO:0000269|PubMed:17564967"
FT /id="VAR_031059"
FT VARIANT 1237
FT /note="R -> H (in dbSNP:rs7307793)"
FT /id="VAR_031060"
FT VARIANT 1566
FT /note="A -> P"
FT /evidence="ECO:0000269|PubMed:20683928"
FT /id="VAR_064399"
FT VARIANT 1694
FT /note="L -> P"
FT /evidence="ECO:0000269|PubMed:20683928"
FT /id="VAR_064400"
FT VARIANT 1836
FT /note="I -> V (in dbSNP:rs11104729)"
FT /id="VAR_031061"
FT VARIANT 2134
FT /note="I -> T (in JBTS5; benign variant;
FT dbSNP:rs117852025)"
FT /evidence="ECO:0000269|PubMed:26477546"
FT /id="VAR_075696"
FT VARIANT 2210
FT /note="R -> C (in dbSNP:rs374852145)"
FT /evidence="ECO:0000269|PubMed:21493627"
FT /id="VAR_066997"
FT VARIANT 2228
FT /note="N -> K (in dbSNP:rs373711746)"
FT /evidence="ECO:0000269|PubMed:17564967"
FT /id="VAR_064401"
FT VARIANT 2263
FT /note="S -> G (found in a patient with LCA10; unknown
FT pathological significance; dbSNP:rs77778467)"
FT /evidence="ECO:0000269|PubMed:21602930"
FT /id="VAR_067192"
FT CONFLICT 544
FT /note="S -> C (in Ref. 3; AK023677)"
FT /evidence="ECO:0000305"
FT CONFLICT 718
FT /note="E -> G (in Ref. 3; AK023677)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2479 AA; 290386 MW; 7CA87D53FAF036FC CRC64;
MPPNINWKEI MKVDPDDLPR QEELADNLLI SLSKVEVNEL KSEKQENVIH LFRITQSLMK
MKAQEVELAL EEVEKAGEEQ AKFENQLKTK VMKLENELEM AQQSAGGRDT RFLRNEICQL
EKQLEQKDRE LEDMEKELEK EKKVNEQLAL RNEEAENENS KLRRENKRLK KKNEQLCQDI
IDYQKQIDSQ KETLLSRRGE DSDYRSQLSK KNYELIQYLD EIQTLTEANE KIEVQNQEMR
KNLEESVQEM EKMTDEYNRM KAIVHQTDNV IDQLKKENDH YQLQVQELTD LLKSKNEEDD
PIMVAVNAKV EEWKLILSSK DDEIIEYQQM LHNLREKLKN AQLDADKSNV MALQQGIQER
DSQIKMLTEQ VEQYTKEMEK NTCIIEDLKN ELQRNKGAST LSQQTHMKIQ STLDILKEKT
KEAERTAELA EADAREKDKE LVEALKRLKD YESGVYGLED AVVEIKNCKN QIKIRDREIE
ILTKEINKLE LKISDFLDEN EALRERVGLE PKTMIDLTEF RNSKHLKQQQ YRAENQILLK
EIESLEEERL DLKKKIRQMA QERGKRSATS GLTTEDLNLT ENISQGDRIS ERKLDLLSLK
NMSEAQSKNE FLSRELIEKE RDLERSRTVI AKFQNKLKEL VEENKQLEEG MKEILQAIKE
MQKDPDVKGG ETSLIIPSLE RLVNAIESKN AEGIFDASLH LKAQVDQLTG RNEELRQELR
ESRKEAINYS QQLAKANLKI DHLEKETSLL RQSEGSNVVF KGIDLPDGIA PSSASIINSQ
NEYLIHLLQE LENKEKKLKN LEDSLEDYNR KFAVIRHQQS LLYKEYLSEK ETWKTESKTI
KEEKRKLEDQ VQQDAIKVKE YNNLLNALQM DSDEMKKILA ENSRKITVLQ VNEKSLIRQY
TTLVELERQL RKENEKQKNE LLSMEAEVCE KIGCLQRFKE MAIFKIAALQ KVVDNSVSLS
ELELANKQYN ELTAKYRDIL QKDNMLVQRT SNLEHLECEN ISLKEQVESI NKELEITKEK
LHTIEQAWEQ ETKLGNESSM DKAKKSITNS DIVSISKKIT MLEMKELNER QRAEHCQKMY
EHLRTSLKQM EERNFELETK FAELTKINLD AQKVEQMLRD ELADSVSKAV SDADRQRILE
LEKNEMELKV EVSKLREISD IARRQVEILN AQQQSRDKEV ESLRMQLLDY QAQSDEKSLI
AKLHQHNVSL QLSEATALGK LESITSKLQK MEAYNLRLEQ KLDEKEQALY YARLEGRNRA
KHLRQTIQSL RRQFSGALPL AQQEKFSKTM IQLQNDKLKI MQEMKNSQQE HRNMENKTLE
MELKLKGLEE LISTLKDTKG AQKVINWHMK IEELRLQELK LNRELVKDKE EIKYLNNIIS
EYERTISSLE EEIVQQNKFH EERQMAWDQR EVDLERQLDI FDRQQNEILN AAQKFEEATG
SIPDPSLPLP NQLEIALRKI KENIRIILET RATCKSLEEK LKEKESALRL AEQNILSRDK
VINELRLRLP ATAEREKLIA ELGRKEMEPK SHHTLKIAHQ TIANMQARLN QKEEVLKKYQ
RLLEKAREEQ REIVKKHEED LHILHHRLEL QADSSLNKFK QTAWDLMKQS PTPVPTNKHF
IRLAEMEQTV AEQDDSLSSL LVKLKKVSQD LERQREITEL KVKEFENIKL QLQENHEDEV
KKVKAEVEDL KYLLDQSQKE SQCLKSELQA QKEANSRAPT TTMRNLVERL KSQLALKEKQ
QKALSRALLE LRAEMTAAAE ERIISATSQK EAHLNVQQIV DRHTRELKTQ VEDLNENLLK
LKEALKTSKN RENSLTDNLN DLNNELQKKQ KAYNKILREK EEIDQENDEL KRQIKRLTSG
LQGKPLTDNK QSLIEELQRK VKKLENQLEG KVEEVDLKPM KEKNAKEELI RWEEGKKWQA
KIEGIRNKLK EKEGEVFTLT KQLNTLKDLF AKADKEKLTL QRKLKTTGMT VDQVLGIRAL
ESEKELEELK KRNLDLENDI LYMRAHQALP RDSVVEDLHL QNRYLQEKLH ALEKQFSKDT
YSKPSISGIE SDDHCQREQE LQKENLKLSS ENIELKFQLE QANKDLPRLK NQVRDLKEMC
EFLKKEKAEV QRKLGHVRGS GRSGKTIPEL EKTIGLMKKV VEKVQRENEQ LKKASGILTS
EKMANIEQEN EKLKAELEKL KAHLGHQLSM HYESKTKGTE KIIAENERLR KELKKETDAA
EKLRIAKNNL EILNEKMTVQ LEETGKRLQF AESRGPQLEG ADSKSWKSIV VTRMYETKLK
ELETDIAKKN QSITDLKQLV KEATEREQKV NKYNEDLEQQ IKILKHVPEG AETEQGLKRE
LQVLRLANHQ LDKEKAELIH QIEANKDQSG AESTIPDADQ LKEKIKDLET QLKMSDLEKQ
HLKEEIKKLK KELENFDPSF FEEIEDLKYN YKEEVKKNIL LEEKVKKLSE QLGVELTSPV
AASEEFEDEE ESPVNFPIY
