CEP20_MOUSE
ID CEP20_MOUSE Reviewed; 174 AA.
AC Q9CZS3; Q3UIK2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Centrosomal protein 20 {ECO:0000305};
DE AltName: Full=FGFR1OP N-terminal-like protein;
DE AltName: Full=FOP-related protein of 20 kDa;
DE AltName: Full=LisH domain-containing protein FOPNL;
GN Name=Cep20 {ECO:0000312|MGI:MGI:1913336};
GN Synonyms=Fopnl {ECO:0000312|MGI:MGI:1913336},
GN For20 {ECO:0000303|PubMed:20551181};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Stomach, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP SUBCELLULAR LOCATION.
RX PubMed=20551181; DOI=10.1242/jcs.065045;
RA Sedjai F., Acquaviva C., Chevrier V., Chauvin J.P., Coppin E., Aouane A.,
RA Coulier F., Tolun A., Pierres M., Birnbaum D., Rosnet O.;
RT "Control of ciliogenesis by FOR20, a novel centrosome and pericentriolar
RT satellite protein.";
RL J. Cell Sci. 123:2391-2401(2010).
RN [4]
RP INTERACTION WITH KIAA0753 AND OFD1.
RX PubMed=26643951; DOI=10.1093/hmg/ddv488;
RA Chevrier V., Bruel A.L., Van Dam T.J., Franco B., Lo Scalzo M., Lembo F.,
RA Audebert S., Baudelet E., Isnardon D., Bole A., Borg J.P., Kuentz P.,
RA Thevenon J., Burglen L., Faivre L., Riviere J.B., Huynen M.A., Birnbaum D.,
RA Rosnet O., Thauvin-Robinet C.;
RT "OFIP/KIAA0753 forms a complex with OFD1 and FOR20 at pericentriolar
RT satellites and centrosomes and is mutated in one individual with oral-
RT facial-digital syndrome.";
RL Hum. Mol. Genet. 25:497-513(2016).
CC -!- FUNCTION: Involved in the biogenesis of cilia (By similarity). Required
CC for the recruitment of PLK1 to centrosomes and S phase progression (By
CC similarity). {ECO:0000250|UniProtKB:Q96NB1}.
CC -!- SUBUNIT: Homooligomer; probably required for localization to
CC centrosomes (By similarity). Forms a complex with KIAA0753/OFIP and
CC OFD1; within this complex may stabilize the interaction between OFD1
CC and KIAA0753/OFIP (PubMed:26643951). Interacts with PCM1; this
CC interaction may be mediated by KIAA0753/OFIP (PubMed:26643951).
CC {ECO:0000250|UniProtKB:Q96NB1, ECO:0000269|PubMed:26643951}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:Q96NB1}. Cell
CC projection, cilium {ECO:0000269|PubMed:20551181}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:20551181}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250}. Cytoplasmic granule {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriolar
CC satellite {ECO:0000250|UniProtKB:Q96NB1}. Note=Localization to
CC centrioles and pericentriolar satellites may be mediated by
CC KIAA0753/OFIP. {ECO:0000250|UniProtKB:Q96NB1}.
CC -!- SIMILARITY: Belongs to the CEP43 family. {ECO:0000305}.
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DR EMBL; AK012206; BAB28098.1; -; mRNA.
DR EMBL; AK146884; BAE27504.1; -; mRNA.
DR EMBL; AK153894; BAE32240.1; -; mRNA.
DR EMBL; BC011300; AAH11300.1; -; mRNA.
DR CCDS; CCDS27973.1; -.
DR RefSeq; NP_079621.1; NM_025345.2.
DR AlphaFoldDB; Q9CZS3; -.
DR SMR; Q9CZS3; -.
DR BioGRID; 211204; 1.
DR STRING; 10090.ENSMUSP00000023357; -.
DR iPTMnet; Q9CZS3; -.
DR PhosphoSitePlus; Q9CZS3; -.
DR EPD; Q9CZS3; -.
DR MaxQB; Q9CZS3; -.
DR PaxDb; Q9CZS3; -.
DR PeptideAtlas; Q9CZS3; -.
DR PRIDE; Q9CZS3; -.
DR ProteomicsDB; 267392; -.
DR Antibodypedia; 51607; 49 antibodies from 10 providers.
DR DNASU; 66086; -.
DR Ensembl; ENSMUST00000023357; ENSMUSP00000023357; ENSMUSG00000022677.
DR GeneID; 66086; -.
DR KEGG; mmu:66086; -.
DR UCSC; uc007yhh.1; mouse.
DR CTD; 123811; -.
DR MGI; MGI:1913336; Cep20.
DR VEuPathDB; HostDB:ENSMUSG00000022677; -.
DR eggNOG; ENOG502S0C1; Eukaryota.
DR GeneTree; ENSGT00390000007773; -.
DR HOGENOM; CLU_119108_1_0_1; -.
DR InParanoid; Q9CZS3; -.
DR OMA; EYLVFNR; -.
DR OrthoDB; 1472201at2759; -.
DR PhylomeDB; Q9CZS3; -.
DR TreeFam; TF328861; -.
DR BioGRID-ORCS; 66086; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9CZS3; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9CZS3; protein.
DR Bgee; ENSMUSG00000022677; Expressed in interventricular septum and 250 other tissues.
DR ExpressionAtlas; Q9CZS3; baseline and differential.
DR Genevisible; Q9CZS3; MM.
DR GO; GO:0034451; C:centriolar satellite; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0034453; P:microtubule anchoring; IEA:InterPro.
DR InterPro; IPR018993; FOP_dimerisation-dom_N.
DR InterPro; IPR006594; LisH.
DR Pfam; PF09398; FOP_dimer; 1.
DR SMART; SM00667; LisH; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..174
FT /note="Centrosomal protein 20"
FT /id="PRO_0000264466"
FT DOMAIN 49..81
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REGION 1..104
FT /note="Necessary and sufficient for homooligomerization and
FT localization to centrosomes and pericentriolar satellites"
FT /evidence="ECO:0000250"
FT REGION 136..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96NB1"
FT CONFLICT 87
FT /note="Q -> R (in Ref. 1; BAE27504)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 174 AA; 19642 MW; 046850BD48712570 CRC64;
MATVTELKAV LKDTLEKRGV LGHLKARIRA EVFNALDDDR EPRPSLSHEN LLINELIREY
LEFNKYKYTA SVLIAESGQP VVPLDRQFLI RELNAFEESK DNSIPLLYGI LAHFLRGPPD
GAQNVLLTES TLHPATKHLS WKPSRRPDDD HVRKDTGPRT TTEELPAAAQ AVSR
