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Q6A078 (CE290_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centrosomal protein of 290 kDa

Short name=Cep290
Alternative name(s):
Bardet-Biedl syndrome 14 protein homolog
Nephrocystin-6
Gene names
Name:Cep290
Synonyms:Kiaa0373, Nphp6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2472 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition. Activates ATF4-mediated transcription By similarity. Required for the correct localization of ciliary and phototransduction proteins in retinal photoreceptor cells; may play a role in ciliary transport processes. Ref.4 Ref.7 Ref.8

Subunit structure

Part of the tectonic-like complex (also named B9 complex). Interacts with ATF4 via its N-terminal region By similarity. Part of selected centrosomal and microtubule-associated protein complexes. Interacts with IQCB1 By similarity. Interacts with ZNF423 By similarity. Interacts with FAM161A. Interacts with CEP162 By similarity. Interacts with CEP131. Associates with microtubule; 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 RPGR. Ref.4 Ref.8

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriolar satellite By similarity. Nucleus By similarity. Cell projectioncilium. Cytoplasmcytoskeletoncilium basal body. Note: Displaced from centriolar satellites in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock By similarity. Connecting cilium of photoreceptor cells, base of cilium in kidney intramedullary collecting duct cells. Localizes at the transition zone, a region between the basal body and the ciliary axoneme. Ref.4 Ref.5 Ref.6 Ref.8

Tissue specificity

Expressed in multiple organs during early postnatal development, with highest levels in hindbrain. Ref.5

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. Ref.5

Post-translational modification

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.

Involvement in disease

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.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
Protein transport
Transcription
Transcription regulation
Transport
   Cellular componentCell projection
Cilium
Cytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   Molecular functionActivator
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcilium assembly

Inferred from mutant phenotype Ref.7. Source: UniProtKB

cilium morphogenesis

Inferred from mutant phenotype Ref.8. Source: UniProtKB

establishment or maintenance of cell polarity

Inferred from mutant phenotype PubMed 22832925. Source: MGI

eye photoreceptor cell development

Inferred from sequence or structural similarity. Source: HGNC

hindbrain development

Inferred from sequence or structural similarity. Source: HGNC

otic vesicle formation

Inferred from sequence or structural similarity. Source: HGNC

positive regulation of intracellular protein transport

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: HGNC

pronephros development

Inferred from sequence or structural similarity. Source: HGNC

protein transport

Inferred from mutant phenotype Ref.4. Source: UniProtKB

regulation of cAMP metabolic process

Inferred from mutant phenotype PubMed 22832925. Source: MGI

retina development in camera-type eye

Inferred from mutant phenotype PubMed 21052544. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentTCTN-B9D complex

Inferred from direct assay Ref.8. Source: UniProtKB

centriolar satellite

Inferred from sequence or structural similarity. Source: UniProtKB

centrosome

Inferred from direct assay Ref.4. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: HGNC

gamma-tubulin complex

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from sequence or structural similarity. Source: HGNC

photoreceptor connecting cilium

Inferred from direct assay Ref.4Ref.6. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.4. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Iqcb1Q8BP006EBI-1811999,EBI-4282243

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.3 (identifier: Q6A078-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available.
Isoform 2 Ref.1 (identifier: Q6A078-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1664: Missing.
     1665-1665: R → M
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24722472Centrosomal protein of 290 kDa
PRO_0000258013

Regions

Coiled coil59 – 747689 Potential
Coiled coil1129 – 1392264 Potential
Coiled coil1459 – 149234 Potential

Natural variations

Alternative sequence1 – 16641664Missing in isoform 2. Ref.1
VSP_052188
Alternative sequence16651R → M in isoform 2. Ref.1
VSP_052189

Experimental info

Mutagenesis71W → C: Centrosomal localization retained. Ref.5
Sequence conflict14251A → P in BAD32218. Ref.3
Sequence conflict14701S → A in BAD32218. Ref.3
Sequence conflict15331H → Q in BAD32218. Ref.3
Sequence conflict15441N → T in BAD32218. Ref.3
Sequence conflict15591K → R in BAD32218. Ref.3
Sequence conflict16861H → N in BAD32218. Ref.3
Sequence conflict20371Q → E in BAD32218. Ref.3
Sequence conflict21341V → L in BAD32218. Ref.3
Sequence conflict21581A → G in BAD32218. Ref.3
Sequence conflict23451M → L in BAD32218. Ref.3
Sequence conflict23891L → S in BAD32218. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: D6ABC2C8A86340A0

FASTA2,472289,077
        10         20         30         40         50         60 
MPPNIKWKEL IKVDPDDLPR QEELADKLLI SLSKVEVNEL KNEDQENMIH LFRITQSLMK 

        70         80         90        100        110        120 
MKAQEVELAL EEVEKAGEEQ AKFENQLKTK VMKLENELEM AQQSAGGRDT RFLRDEIRQL 

       130        140        150        160        170        180 
EKQLEQKDRE LEDMEKELDK EKKVNEQLAL RNEEAENENS KLRRENEQLR QDIIDYQKQI 

       190        200        210        220        230        240 
DSQKESLLSR RGEDSDYRSQ LSKKNYELVQ YLDEIQTLTE ANEKIEVQNQ EMRKNLEESV 

       250        260        270        280        290        300 
QEMEKMTDEY NRMKALVHQS DAVMDQIKKE NEHYRLQVRE LTDLLKAKDE EDDPVMMAVN 

       310        320        330        340        350        360 
AKVEEWKLIL SSKDDEIIEY QQMLQSLRGK LKNAQLDADK SNIMALKQGI QERDSQIKML 

       370        380        390        400        410        420 
TEQVEQYTKE MEKNTFIIED LKNELQKDKG TSNFYQQTHY MKIHSKVQIL EEKTKEAERI 

       430        440        450        460        470        480 
AELAEADARE KDKELVEALK RLKDYESGVY GLEDAVIEIK NCKAQIKIRD GEMEVLTKEI 

       490        500        510        520        530        540 
NKLEMKINDI LDENEALRER AGLEPKTMID LTEFRNSKRL KQQQYRAENQ VLLKEIESLE 

       550        560        570        580        590        600 
EERLDLKRKI RQMAQERGKR NAASGLTIDD LNLSETFSHE NKIEGRKLNF MSLNNMNETQ 

       610        620        630        640        650        660 
SKNEFLSREL AEKEKDLERS RTVIAKFQSK LKELVEENKQ LEEGMKEILQ AIKDMPKDSD 

       670        680        690        700        710        720 
VKGGETSLII PSLERLVNAM ESKNAEGIFD ASLHLKAQVD QLTGRNEELR QELRQSRKEA 

       730        740        750        760        770        780 
VNYSQQLVKA NLKIDHLEKE TDLLRQSAGS NVVYKGIDLP DGIAPSSAYI INSQNEYLIH 

       790        800        810        820        830        840 
LLQELDNKEK KLKHLEDSLE DYNRKFAVIR HQQSLLYKEY LSEKDIWKTD SEMIREEKRK 

       850        860        870        880        890        900 
LEDQAEQDAV KVKEYNNLLS ALQMDSNEMK KMLSENSRKI TVLQVNEKSL IRQYTTLVEM 

       910        920        930        940        950        960 
ERHLRKENGK HRNDVIAMEA EVTEKLGSLQ RFKEMAIFKI AALQKVIDNS VSLSELELAN 

       970        980        990       1000       1010       1020 
KQYNELTTKY RDILQKDNML VQRTSNLEHL ECENASLKEQ MEAISKELEI TKEKLHTIEQ 

      1030       1040       1050       1060       1070       1080 
AWEQETKLGN DSNMDKAKKS MTNSDIVSIS KKITVLEMKE LNERQRAEHC QKMYEHLRTS 

      1090       1100       1110       1120       1130       1140 
LKQMEERNFE LETKFTELTK INLDAQKVEQ MLRDELADSV TKAVSDADRQ RILELEKSEV 

      1150       1160       1170       1180       1190       1200 
ELKVEVSKLR EISDIAKRQV DFLNSQQQSR EKEVESLRTQ LLDFQAQSDE KALIAKLHQH 

      1210       1220       1230       1240       1250       1260 
VVSLQISEAT ALGKLESVTS KLQKMEAYNL RLEQKLDEKE QALYYARLEG RNRAKHLRQT 

      1270       1280       1290       1300       1310       1320 
IQSLRRQFSG ALPLAQQEKF SKTMIQLQND KLKIMQEMKN SQQEHRNMEN KTLELELKLK 

      1330       1340       1350       1360       1370       1380 
GLEELISTLK DARGAQKVIN WHVKIEELRL QELKLNRELV KGKEEIKYLN NIISEYEHTI 

      1390       1400       1410       1420       1430       1440 
NSLEEEIVQQ SKFHEERQMA WDQREVELER QLDIFDHQQN EILSAAQKFE DSTGSMPDPS 

      1450       1460       1470       1480       1490       1500 
LPLPNQLEIA LRKIKENIQV ILKTQATCKS LEEKLKEKES ALRLAEQNIL SRDKVINELR 

      1510       1520       1530       1540       1550       1560 
LRLPATADRE KLIAELERKE LEPKSHHTMK IAHQTIANMQ ARLNHKEEVL KKYQHLLEKA 

      1570       1580       1590       1600       1610       1620 
REEQREIVKK HEEDLHVLHH KLEQQADNSL NKFRQTAQDL LKQSPAPVPT NKHFIRLAEM 

      1630       1640       1650       1660       1670       1680 
EQTVAEQDDS LSSLLTKLKK VSKDLEKQKE ITELKVREFE NTKLRLQETH ASEVKKVKAE 

      1690       1700       1710       1720       1730       1740 
VEDLRHALAQ AHKDSQSLKS ELQAQKEANS RAPTTTMRNL VDRLKSQLAL KEKQQKALSR 

      1750       1760       1770       1780       1790       1800 
ALLELRSEMT AAAEERIIAV TSQKEANLNV QQVVERHTRE LKSQIEDLNE NLLKLKEALK 

      1810       1820       1830       1840       1850       1860 
TSKNKENSLA DDLNELNNEL QKKQKAYNKI LREKDGIDQE NDELRRQIKR LSSGLQSKTL 

      1870       1880       1890       1900       1910       1920 
IDNKQSLIDE LQKKVKKLES QLERKVDDVD IKPVKEKSSK EELIRWEEGK KWQTKVEGLR 

      1930       1940       1950       1960       1970       1980 
NRLKEKEGEA HGLAKQLNTL KELFAKADKE KLTLQKKLKT TGMTVDQVLG VRALESEKEL 

      1990       2000       2010       2020       2030       2040 
EELKKKNLDL ENDILYMRTQ QALPRDSVVE DLHLQNKYLQ EKLHTLEKKL SKEKYSQSLT 

      2050       2060       2070       2080       2090       2100 
SEIESDDHCQ KEQELQKENL KLSSENIELK FQLEQANKDL PRLKNQVKDL KEMCEFLKKG 

      2110       2120       2130       2140       2150       2160 
KLELERKLGQ VRGAGRSGKT IPELEKTIGL MKKVVEKVQR ENEQLKKASG ILTSEKMATI 

      2170       2180       2190       2200       2210       2220 
EEENRNLKAE LEKLKAHFGR QLSMQFESKN KGTEKIVAEN ERLRKELKKE IEASEKLRIA 

      2230       2240       2250       2260       2270       2280 
KNNLELVNDK MAAQLEETGK RLQFAESRAP QLEGADSKSW KSIVVSRVYE TKMKELESDI 

      2290       2300       2310       2320       2330       2340 
AKKNQSITDL KQLVREATER EQKAKKYTED LEQQIEILKN VPEGAETEQE LIRELQLLRL 

      2350       2360       2370       2380       2390       2400 
ANNQMDKERA ELIHQIEINK DQTRADSSIP DSDQLKEKIN DLETQLRKLE LEKQHSKEEV 

      2410       2420       2430       2440       2450       2460 
KKLKKELENF DPSFFEEIED LKYNYKEEVK KNILLEEKLK KLSEQFGFEL PSPLAASEHS 

      2470 
EDGESPHSFP IY 

« Hide

Isoform 2 [UniParc].

Checksum: B3AE0E431A7E365F
Show »

FASTA80893,782

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Testis.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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."
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.
DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1103-2472 (ISOFORM 1).
Tissue: Fetal brain.
[4]"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."
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.
Hum. Mol. Genet. 15:1847-1857(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN EARLY-ONSET RETINAL DEGENERATION, FUNCTION, INTERACTION WITH RPGR, SUBUNIT, SUBCELLULAR LOCATION.
[5]"Mutations in CEP290, which encodes a centrosomal protein, cause pleiotropic forms of Joubert syndrome."
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.
Nat. Genet. 38:623-625(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TRP-7, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
[6]"The centrosomal protein nephrocystin-6 is mutated in Joubert syndrome and activates transcription factor ATF4."
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. expand/collapse author list , 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.
Nat. Genet. 38:674-681(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes and pathways."
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. expand/collapse author list , 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.
Cell 145:513-528(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"A transition zone complex regulates mammalian ciliogenesis and ciliary membrane composition."
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.
Nat. Genet. 43:776-784(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE TECTONIC-LIKE COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK029960 mRNA. Translation: BAC26700.1.
AC153501 Genomic DNA. No translation available.
AK172940 mRNA. Translation: BAD32218.1.
RefSeqNP_666121.2. NM_146009.2.
XP_006513591.1. XM_006513528.1. [Q6A078-1]
UniGeneMm.229114.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid229729. 36 interactions.
DIPDIP-46317N.
IntActQ6A078. 28 interactions.

PTM databases

PhosphoSiteQ6A078.

Proteomic databases

PaxDbQ6A078.
PRIDEQ6A078.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID216274.
KEGGmmu:216274.
UCSCuc007gxw.2. mouse. [Q6A078-2]

Organism-specific databases

CTD80184.
MGIMGI:2384917. Cep290.
RougeSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000111526.
HOVERGENHBG081077.
InParanoidQ6A078.
KOK16533.
PhylomeDBQ6A078.

Gene expression databases

BgeeQ6A078.
CleanExMM_CEP290.
GenevestigatorQ6A078.

Family and domain databases

InterProIPR026201. Cep290.
[Graphical view]
PANTHERPTHR18879. PTHR18879. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCEP290. mouse.
NextBio375097.
PROQ6A078.
SOURCESearch...

Entry information

Entry nameCE290_MOUSE
AccessionPrimary (citable) accession number: Q6A078
Secondary accession number(s): Q8BIB8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: July 9, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot