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Centrosomal protein of 290 kDa (Cep290) (Bardet-Biedl syndrome 14 protein homolog) (Nephrocystin-6)

 CE290_MOUSE             Reviewed;        2472 AA.
Q6A078; Q8BIB8;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
31-OCT-2006, sequence version 2.
30-AUG-2017, entry version 120.
RecName: Full=Centrosomal protein of 290 kDa;
Short=Cep290;
AltName: Full=Bardet-Biedl syndrome 14 protein homolog;
AltName: Full=Nephrocystin-6;
Name=Cep290 {ECO:0000312|MGI:MGI:2384917};
Synonyms=Kiaa0373 {ECO:0000312|EMBL:BAD32218.1},
Nphp6 {ECO:0000250|UniProtKB:O15078};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:BAC26700.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26700.1};
TISSUE=Testis {ECO:0000312|EMBL:BAC26700.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3] {ECO:0000305, ECO:0000312|EMBL:BAD32218.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1103-2472 (ISOFORM 1).
TISSUE=Fetal brain {ECO:0000312|EMBL:BAD32218.1};
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 11:205-218(2004).
[4] {ECO:0000305}
INVOLVEMENT IN EARLY-ONSET RETINAL DEGENERATION, FUNCTION, INTERACTION
WITH RPGR, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=16632484; DOI=10.1093/hmg/ddl107;
Chang B., Khanna H., Hawes N., Jimeno D., He S., Lillo C.,
Parapuram S.K., Cheng H., Scott A., Hurd R.E., Sayer J.A., Otto E.A.,
Attanasio M., O'Toole J.F., Jin G., Shou C., Hildebrandt F.,
Williams D.S., Heckenlively J.R., Swaroop A.;
"In-frame deletion in a novel centrosomal/ciliary protein CEP290/NPHP6
perturbs its interaction with RPGR and results in early-onset retinal
degeneration in the rd16 mouse.";
Hum. Mol. Genet. 15:1847-1857(2006).
[5] {ECO:0000305}
MUTAGENESIS OF TRP-7, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
TISSUE SPECIFICITY.
PubMed=16682970; DOI=10.1038/ng1805;
International Joubert syndrome related disorders (JSRD) study group;
Valente E.M., Silhavy J.L., Brancati F., Barrano G.,
Krishnaswami S.R., Castori M., Lancaster M.A., Boltshauser E.,
Boccone L., Al-Gazali L., Fazzi E., Signorini S., Louie C.M.,
Bellacchio E., Bertini E., Dallapiccola B., Gleeson J.G.;
"Mutations in CEP290, which encodes a centrosomal protein, cause
pleiotropic forms of Joubert syndrome.";
Nat. Genet. 38:623-625(2006).
[6] {ECO:0000305}
SUBCELLULAR LOCATION.
PubMed=16682973; DOI=10.1038/ng1786;
Sayer J.A., Otto E.A., O'toole J.F., Nurnberg G., Kennedy M.A.,
Becker C., Hennies H.C., Helou J., Attanasio M., Fausett B.V.,
Utsch B., Khanna H., Liu Y., Drummond I., Kawakami I., Kusakabe T.,
Tsuda M., Ma L., Lee H., Larson R.G., Allen S.J., Wilkinson C.J.,
Nigg E.A., Shou C., Lillo C., Williams D.S., Hoppe B., Kemper M.J.,
Neuhaus T., Parisi M.A., Glass I.A., Petry M., Kispert A., Gloy J.,
Ganner A., Walz G., Zhu X., Goldman D., Nurnberg P., Swaroop A.,
Leroux M.R., Hildebrandt F.;
"The centrosomal protein nephrocystin-6 is mutated in Joubert syndrome
and activates transcription factor ATF4.";
Nat. Genet. 38:674-681(2006).
[7]
INTERACTION WITH PCM1.
PubMed=17705300; DOI=10.1002/humu.20614;
Frank V., den Hollander A.I., Bruechle N.O., Zonneveld M.N.,
Nuernberg G., Becker C., Du Bois G., Kendziorra H., Roosing S.,
Senderek J., Nuernberg P., Cremers F.P., Zerres K., Bergmann C.;
"Mutations of the CEP290 gene encoding a centrosomal protein cause
Meckel-Gruber syndrome.";
Hum. Mutat. 29:45-52(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, AND INTERACTION WITH IQCB1.
PubMed=21565611; DOI=10.1016/j.cell.2011.04.019;
Sang L., Miller J.J., Corbit K.C., Giles R.H., Brauer M.J., Otto E.A.,
Baye L.M., Wen X., Scales S.J., Kwong M., Huntzicker E.G.,
Sfakianos M.K., Sandoval W., Bazan J.F., Kulkarni P.,
Garcia-Gonzalo F.R., Seol A.D., O'Toole J.F., Held S., Reutter H.M.,
Lane W.S., Rafiq M.A., Noor A., Ansar M., Devi A.R., Sheffield V.C.,
Slusarski D.C., Vincent J.B., Doherty D.A., Hildebrandt F.,
Reiter J.F., Jackson P.K.;
"Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease
genes and pathways.";
Cell 145:513-528(2011).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE
TECTONIC-LIKE COMPLEX.
PubMed=21725307; DOI=10.1038/ng.891;
Garcia-Gonzalo F.R., Corbit K.C., Sirerol-Piquer M.S., Ramaswami G.,
Otto E.A., Noriega T.R., Seol A.D., Robinson J.F., Bennett C.L.,
Josifova D.J., Garcia-Verdugo J.M., Katsanis N., Hildebrandt F.,
Reiter J.F.;
"A transition zone complex regulates mammalian ciliogenesis and
ciliary membrane composition.";
Nat. Genet. 43:776-784(2011).
[11]
SUBCELLULAR LOCATION.
PubMed=23807208; DOI=10.1007/s00018-013-1401-6;
Kypri E., Christodoulou A., Maimaris G., Lethan M., Markaki M.,
Lysandrou C., Lederer C.W., Tavernarakis N., Geimer S., Pedersen L.B.,
Santama N.;
"The nucleotide-binding proteins Nubp1 and Nubp2 are negative
regulators of ciliogenesis.";
Cell. Mol. Life Sci. 71:517-538(2014).
[12]
SUBCELLULAR LOCATION.
PubMed=23943788; DOI=10.1093/hmg/ddt394;
Zhang Y., Seo S., Bhattarai S., Bugge K., Searby C.C., Zhang Q.,
Drack A.V., Stone E.M., Sheffield V.C.;
"BBS mutations modify phenotypic expression of CEP290-related
ciliopathies.";
Hum. Mol. Genet. 23:40-51(2014).
-!- FUNCTION: Involved in early and late steps in cilia formation
(PubMed:21565611). Its association with CCP110 is required for
inhibition of primary cilia formation by CCP110 (By similarity).
May play a role in early ciliogenesis in the disappearance of
centriolar satellites and in the transition of primary ciliar
vesicles (PCVs) to capped ciliary vesicles (CCVs). Required for
the centrosomal recruitment of RAB8A and for the targeting of
centriole satellite proteins to centrosomes such as of PCM1 (By
similarity). Required for the correct localization of ciliary and
phototransduction proteins in retinal photoreceptor cells; may
play a role in ciliary transport processes (PubMed:16632484).
Required for efficient recruitment of RAB8A to primary cilium (By
similarity). In the ciliary transition zone is part of the
tectonic-like complex (also named B9 complex) which is required
for tissue-specific ciliogenesis and may regulate ciliary membrane
composition (PubMed:21725307). Involved in regulation of the
BBSome complex integrity, specifically for presence of BBS2, BBS5
and BBS8/TTC8 in the complex, and in ciliary targeting of selected
BBSome cargos. May play a role in controlling entry of the BBSome
complex to cilia possibly implicating IQCB1/NPHP5 (By similarity).
Activates ATF4-mediated transcription (By similarity).
{ECO:0000250|UniProtKB:O15078, ECO:0000269|PubMed:16632484,
ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:21725307}.
-!- SUBUNIT: Part of the tectonic-like complex (also named B9 complex)
(PubMed:21725307). Interacts with ATF4 via its N-terminal region
(By similarity). Associates with the BBSome complex, interacting
(via N-terminus) with BBS4 (By similarity). Interacts with
IQCB1/NPHP5; IQCB1 and CEP290/NPHP6 are proposed to form a
functional NPHP5-6 module localized to the centrosome. Interacts
with NPHP4; the interaction likely requires additional interactors
(PubMed:21565611). Interacts with ZNF423, FAM161A, CEP162, CEP162,
CEP131, TALPID3, CCDC13, CC2D2A, RPGRIP1 (By similarity). Can
self-associate (homo- or heteromeric) (By similarity). Interacts
with CCP110; required for suppressing cilia formation (By
similarity). Interacts with RPGR (PubMed:16632484). Associates
(via C-terminus) with microtubules; association to microtubule is
reduced in response to cellular stress, such as ultraviolet light
(UV) radiation or heat shock, in a process that requires p38 MAP
kinase signaling (By similarity). Interacts with FAM161A (By
similarity). Interacts with PCM1 (PubMed:17705300).
{ECO:0000250|UniProtKB:O15078, ECO:0000250|UniProtKB:Q9TU23,
ECO:0000269|PubMed:16632484, ECO:0000269|PubMed:17705300,
ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:21725307}.
-!- INTERACTION:
Q7TSH4:Ccp110; NbExp=3; IntAct=EBI-1811999, EBI-646843;
O08788:Dctn1; NbExp=2; IntAct=EBI-1811999, EBI-776180;
Q8BP00:Iqcb1; NbExp=6; IntAct=EBI-1811999, EBI-4282243;
P28741:Kif3a; NbExp=2; IntAct=EBI-1811999, EBI-6169413;
Q9R0L6:Pcm1; NbExp=4; IntAct=EBI-1811999, EBI-4284371;
P48725:Pcnt; NbExp=2; IntAct=EBI-1811999, EBI-2290976;
Q9CU62:Smc1a; NbExp=2; IntAct=EBI-1811999, EBI-2550016;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:16632484,
ECO:0000269|PubMed:16682970, ECO:0000269|PubMed:16682973}.
Cytoplasm {ECO:0000269|PubMed:16682973}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome, centriolar satellite
{ECO:0000269|PubMed:21725307}. Nucleus
{ECO:0000269|PubMed:16632484, ECO:0000269|PubMed:16682973}.
Cytoplasm, cytoskeleton, microtubule organizing center,
centrosome, centriole {ECO:0000269|PubMed:16632484,
ECO:0000269|PubMed:16682970, ECO:0000269|PubMed:23807208}. Cell
projection, cilium {ECO:0000269|PubMed:16632484,
ECO:0000269|PubMed:16682970, ECO:0000269|PubMed:23943788}.
Cytoplasm, cytoskeleton, cilium basal body
{ECO:0000269|PubMed:23807208}. Cytoplasmic vesicle
{ECO:0000250|UniProtKB:O15078}. Note=Displaced from centriolar
satellites in response to cellular stress, such as ultraviolet
light (UV) radiation or heat shock (By similarity). Found in the
connecting cilium of photoreceptor cells (PubMed:16632484,
PubMed:23943788), base of cilium in kidney intramedullary
collecting duct cells (PubMed:16682970). Localizes at the
transition zone, a region between the basal body and the ciliary
axoneme (PubMed:21725307). Localization at the ciliary transition
zone as well as at centriolar satellites is BBsome-dependent (By
similarity). {ECO:0000250|UniProtKB:O15078,
ECO:0000269|PubMed:16632484, ECO:0000269|PubMed:16682970,
ECO:0000269|PubMed:21725307, ECO:0000269|PubMed:23943788}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:15368895};
IsoId=Q6A078-1; Sequence=Displayed;
Note=No experimental confirmation available. {ECO:0000305};
Name=2 {ECO:0000269|PubMed:16141072};
IsoId=Q6A078-2; Sequence=VSP_052188, VSP_052189;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in multiple organs during early
postnatal development, with highest levels in hindbrain.
{ECO:0000269|PubMed:16682970}.
-!- DEVELOPMENTAL STAGE: Similar levels from E7 to E17 in whole embryo
and brain. In the cerebellum, expressed most strongly in dividing
cells of the external granule layer.
{ECO:0000269|PubMed:16682970}.
-!- PTM: Ubiquitinated. May undergo monoubiquitination;
monoubiquitination is inhibited in response to cellular stress,
such as ultraviolet light (UV) radiation or heat shock, but does
not cause it displacement from centriolar satellites (By
similarity). {ECO:0000250}.
-!- DISEASE: Note=Defects in Cep290 are a cause of early-onset retinal
degeneration with autosomal recessive inheritance. The rd16 mutant
carries a deletion of residues 1599-1897 in the Cep290 protein.
Homozygous rd16 mice are characterized by the appearance of white
retinal vessels at 1 month of age and large pigment patches at 2
months. Retinal degeneration is apparent as early as postnatal day
19 and progresses with age. The rd16 retina exhibits altered
disitribution of Rpgr and phototransduction proteins within the
photoreceptor cells.
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EMBL; AK029960; BAC26700.1; -; mRNA.
EMBL; AC153501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK172940; BAD32218.1; -; mRNA.
RefSeq; NP_666121.2; NM_146009.2.
RefSeq; XP_006513591.1; XM_006513528.2. [Q6A078-1]
UniGene; Mm.229114; -.
SMR; Q6A078; -.
BioGrid; 229729; 44.
DIP; DIP-46317N; -.
IntAct; Q6A078; 40.
STRING; 10090.ENSMUSP00000130899; -.
iPTMnet; Q6A078; -.
PhosphoSitePlus; Q6A078; -.
PaxDb; Q6A078; -.
PRIDE; Q6A078; -.
Ensembl; ENSMUST00000219765; ENSMUSP00000151712; ENSMUSG00000019971. [Q6A078-1]
GeneID; 216274; -.
KEGG; mmu:216274; -.
UCSC; uc007gxw.2; mouse. [Q6A078-2]
CTD; 80184; -.
MGI; MGI:2384917; Cep290.
eggNOG; ENOG410IIIW; Eukaryota.
eggNOG; ENOG410XRSC; LUCA.
GeneTree; ENSGT00730000111039; -.
HOGENOM; HOG000111526; -.
HOVERGEN; HBG081077; -.
InParanoid; Q6A078; -.
KO; K16533; -.
PhylomeDB; Q6A078; -.
ChiTaRS; Cep290; mouse.
PRO; PR:Q6A078; -.
Proteomes; UP000000589; Chromosome 10.
CleanEx; MM_CEP290; -.
ExpressionAtlas; Q6A078; baseline and differential.
GO; GO:0034451; C:centriolar satellite; IDA:MGI.
GO; GO:0005814; C:centriole; ISO:MGI.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0035869; C:ciliary transition zone; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; ISS:HGNC.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0036038; C:MKS complex; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:HGNC.
GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
GO; GO:0042462; P:eye photoreceptor cell development; ISS:HGNC.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0030902; P:hindbrain development; ISS:HGNC.
GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
GO; GO:0030916; P:otic vesicle formation; ISS:HGNC.
GO; GO:0045494; P:photoreceptor cell maintenance; IMP:MGI.
GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:HGNC.
GO; GO:0048793; P:pronephros development; ISS:HGNC.
GO; GO:0015031; P:protein transport; IMP:UniProtKB.
GO; GO:0030814; P:regulation of cAMP metabolic process; IMP:MGI.
GO; GO:0070201; P:regulation of establishment of protein localization; ISO:MGI.
GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR032321; Cep209_CC5.
InterPro; IPR026201; Cep290.
PANTHER; PTHR18879; PTHR18879; 1.
Pfam; PF16574; CEP209_CC5; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Cell projection; Cilium;
Cilium biogenesis/degradation; Coiled coil; Complete proteome;
Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Nucleus;
Protein transport; Reference proteome; Transcription;
Transcription regulation; Transport; Ubl conjugation.
CHAIN 1 2472 Centrosomal protein of 290 kDa.
/FTId=PRO_0000258013.
REGION 1 689 Self-association (with itself or C-
terminus).
{ECO:0000250|UniProtKB:O15078}.
REGION 690 890 Interaction with IQCB1.
{ECO:0000250|UniProtKB:O15078}.
REGION 1960 2472 Self-association (with itself or N-
terminus).
{ECO:0000250|UniProtKB:O15078}.
COILED 59 747 {ECO:0000255}.
COILED 1129 1392 {ECO:0000255}.
COILED 1459 1492 {ECO:0000255}.
VAR_SEQ 1 1664 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_052188.
VAR_SEQ 1665 1665 R -> M (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_052189.
MUTAGEN 7 7 W->C: Centrosomal localization retained.
{ECO:0000269|PubMed:16682970}.
CONFLICT 1425 1425 A -> P (in Ref. 3; BAD32218).
{ECO:0000305}.
CONFLICT 1470 1470 S -> A (in Ref. 3; BAD32218).
{ECO:0000305}.
CONFLICT 1533 1533 H -> Q (in Ref. 3; BAD32218).
{ECO:0000305}.
CONFLICT 1544 1544 N -> T (in Ref. 3; BAD32218).
{ECO:0000305}.
CONFLICT 1559 1559 K -> R (in Ref. 3; BAD32218).
{ECO:0000305}.
CONFLICT 1686 1686 H -> N (in Ref. 3; BAD32218).
{ECO:0000305}.
CONFLICT 2037 2037 Q -> E (in Ref. 3; BAD32218).
{ECO:0000305}.
CONFLICT 2134 2134 V -> L (in Ref. 3; BAD32218).
{ECO:0000305}.
CONFLICT 2158 2158 A -> G (in Ref. 3; BAD32218).
{ECO:0000305}.
CONFLICT 2345 2345 M -> L (in Ref. 3; BAD32218).
{ECO:0000305}.
CONFLICT 2389 2389 L -> S (in Ref. 3; BAD32218).
{ECO:0000305}.
SEQUENCE 2472 AA; 289077 MW; D6ABC2C8A86340A0 CRC64;
MPPNIKWKEL IKVDPDDLPR QEELADKLLI SLSKVEVNEL KNEDQENMIH LFRITQSLMK
MKAQEVELAL EEVEKAGEEQ AKFENQLKTK VMKLENELEM AQQSAGGRDT RFLRDEIRQL
EKQLEQKDRE LEDMEKELDK EKKVNEQLAL RNEEAENENS KLRRENEQLR QDIIDYQKQI
DSQKESLLSR RGEDSDYRSQ LSKKNYELVQ YLDEIQTLTE ANEKIEVQNQ EMRKNLEESV
QEMEKMTDEY NRMKALVHQS DAVMDQIKKE NEHYRLQVRE LTDLLKAKDE EDDPVMMAVN
AKVEEWKLIL SSKDDEIIEY QQMLQSLRGK LKNAQLDADK SNIMALKQGI QERDSQIKML
TEQVEQYTKE MEKNTFIIED LKNELQKDKG TSNFYQQTHY MKIHSKVQIL EEKTKEAERI
AELAEADARE KDKELVEALK RLKDYESGVY GLEDAVIEIK NCKAQIKIRD GEMEVLTKEI
NKLEMKINDI LDENEALRER AGLEPKTMID LTEFRNSKRL KQQQYRAENQ VLLKEIESLE
EERLDLKRKI RQMAQERGKR NAASGLTIDD LNLSETFSHE NKIEGRKLNF MSLNNMNETQ
SKNEFLSREL AEKEKDLERS RTVIAKFQSK LKELVEENKQ LEEGMKEILQ AIKDMPKDSD
VKGGETSLII PSLERLVNAM ESKNAEGIFD ASLHLKAQVD QLTGRNEELR QELRQSRKEA
VNYSQQLVKA NLKIDHLEKE TDLLRQSAGS NVVYKGIDLP DGIAPSSAYI INSQNEYLIH
LLQELDNKEK KLKHLEDSLE DYNRKFAVIR HQQSLLYKEY LSEKDIWKTD SEMIREEKRK
LEDQAEQDAV KVKEYNNLLS ALQMDSNEMK KMLSENSRKI TVLQVNEKSL IRQYTTLVEM
ERHLRKENGK HRNDVIAMEA EVTEKLGSLQ RFKEMAIFKI AALQKVIDNS VSLSELELAN
KQYNELTTKY RDILQKDNML VQRTSNLEHL ECENASLKEQ MEAISKELEI TKEKLHTIEQ
AWEQETKLGN DSNMDKAKKS MTNSDIVSIS KKITVLEMKE LNERQRAEHC QKMYEHLRTS
LKQMEERNFE LETKFTELTK INLDAQKVEQ MLRDELADSV TKAVSDADRQ RILELEKSEV
ELKVEVSKLR EISDIAKRQV DFLNSQQQSR EKEVESLRTQ LLDFQAQSDE KALIAKLHQH
VVSLQISEAT ALGKLESVTS KLQKMEAYNL RLEQKLDEKE QALYYARLEG RNRAKHLRQT
IQSLRRQFSG ALPLAQQEKF SKTMIQLQND KLKIMQEMKN SQQEHRNMEN KTLELELKLK
GLEELISTLK DARGAQKVIN WHVKIEELRL QELKLNRELV KGKEEIKYLN NIISEYEHTI
NSLEEEIVQQ SKFHEERQMA WDQREVELER QLDIFDHQQN EILSAAQKFE DSTGSMPDPS
LPLPNQLEIA LRKIKENIQV ILKTQATCKS LEEKLKEKES ALRLAEQNIL SRDKVINELR
LRLPATADRE KLIAELERKE LEPKSHHTMK IAHQTIANMQ ARLNHKEEVL KKYQHLLEKA
REEQREIVKK HEEDLHVLHH KLEQQADNSL NKFRQTAQDL LKQSPAPVPT NKHFIRLAEM
EQTVAEQDDS LSSLLTKLKK VSKDLEKQKE ITELKVREFE NTKLRLQETH ASEVKKVKAE
VEDLRHALAQ AHKDSQSLKS ELQAQKEANS RAPTTTMRNL VDRLKSQLAL KEKQQKALSR
ALLELRSEMT AAAEERIIAV TSQKEANLNV QQVVERHTRE LKSQIEDLNE NLLKLKEALK
TSKNKENSLA DDLNELNNEL QKKQKAYNKI LREKDGIDQE NDELRRQIKR LSSGLQSKTL
IDNKQSLIDE LQKKVKKLES QLERKVDDVD IKPVKEKSSK EELIRWEEGK KWQTKVEGLR
NRLKEKEGEA HGLAKQLNTL KELFAKADKE KLTLQKKLKT TGMTVDQVLG VRALESEKEL
EELKKKNLDL ENDILYMRTQ QALPRDSVVE DLHLQNKYLQ EKLHTLEKKL SKEKYSQSLT
SEIESDDHCQ KEQELQKENL KLSSENIELK FQLEQANKDL PRLKNQVKDL KEMCEFLKKG
KLELERKLGQ VRGAGRSGKT IPELEKTIGL MKKVVEKVQR ENEQLKKASG ILTSEKMATI
EEENRNLKAE LEKLKAHFGR QLSMQFESKN KGTEKIVAEN ERLRKELKKE IEASEKLRIA
KNNLELVNDK MAAQLEETGK RLQFAESRAP QLEGADSKSW KSIVVSRVYE TKMKELESDI
AKKNQSITDL KQLVREATER EQKAKKYTED LEQQIEILKN VPEGAETEQE LIRELQLLRL
ANNQMDKERA ELIHQIEINK DQTRADSSIP DSDQLKEKIN DLETQLRKLE LEKQHSKEEV
KKLKKELENF DPSFFEEIED LKYNYKEEVK KNILLEEKLK KLSEQFGFEL PSPLAASEHS
EDGESPHSFP IY


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