CEP20_HUMAN
ID CEP20_HUMAN Reviewed; 174 AA.
AC Q96NB1; B3KPU9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
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|HGNC:HGNC:26435};
GN Synonyms=C16orf63, FOPNL, FOR20, PHSECRG2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Du J., Nie Z., Lin G., Lu G.;
RT "The cloning and functional analysis of PHSECRG2 gene.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [5]
RP FUNCTION, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-49
RP AND GLU-76, AND TISSUE SPECIFICITY.
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 [6]
RP FUNCTION, INTERACTION WITH PLK1, AND SUBCELLULAR LOCATION.
RX PubMed=24018379; DOI=10.1038/cr.2013.127;
RA Shen M., Cai Y., Yang Y., Yan X., Liu X., Zhou T.;
RT "Centrosomal protein FOR20 is essential for S-phase progression by
RT recruiting Plk1 to centrosomes.";
RL Cell Res. 23:1284-1295(2013).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP INTERACTION WITH KIAA0753 AND OFD1, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF GLU-49; ILE-53; GLU-76 AND LEU-106.
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 (PubMed:20551181).
CC Required for the recruitment of PLK1 to centrosomes and S phase
CC progression (PubMed:24018379). {ECO:0000269|PubMed:20551181,
CC ECO:0000269|PubMed:24018379}.
CC -!- SUBUNIT: Homooligomer; probably required for localization to
CC centrosomes (PubMed:20551181). 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 Interacts with PLK1 in later G1, S, G2 and M phases of the cell cycle;
CC this interaction recruits PLK1 to centrosomes (PubMed:24018379).
CC {ECO:0000269|PubMed:20551181, ECO:0000269|PubMed:24018379,
CC ECO:0000269|PubMed:26643951}.
CC -!- INTERACTION:
CC Q96NB1; Q8IYX3: CCDC116; NbExp=3; IntAct=EBI-2872654, EBI-744311;
CC Q96NB1; Q96NB1: CEP20; NbExp=13; IntAct=EBI-2872654, EBI-2872654;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:26643951}. Cell
CC projection, cilium {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:20551181,
CC ECO:0000269|PubMed:24018379}. Cytoplasmic granule
CC {ECO:0000269|PubMed:20551181}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000269|PubMed:20551181, ECO:0000269|PubMed:26643951}.
CC Note=Localizes to the centrosome throughout cell cycle progression
CC (PubMed:24018379). Localization to centrioles and pericentriolar
CC satellites may be mediated by KIAA0753/OFIP (PubMed:26643951).
CC {ECO:0000269|PubMed:24018379, ECO:0000269|PubMed:26643951}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96NB1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96NB1-2; Sequence=VSP_056998;
CC -!- TISSUE SPECIFICITY: Widely expressed. Detected in brain, heart, kidney,
CC liver, lung, skeletal muscle, placenta and intestine.
CC {ECO:0000269|PubMed:20551181}.
CC -!- SIMILARITY: Belongs to the CEP43 family. {ECO:0000305}.
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DR EMBL; AY507846; AAR98812.1; -; mRNA.
DR EMBL; AK055715; BAB70994.1; -; mRNA.
DR EMBL; AK056798; BAG51811.1; -; mRNA.
DR EMBL; AC130651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022321; AAH22321.1; -; mRNA.
DR CCDS; CCDS10567.1; -. [Q96NB1-1]
DR CCDS; CCDS76830.1; -. [Q96NB1-2]
DR RefSeq; NP_001291426.1; NM_001304497.1. [Q96NB1-2]
DR RefSeq; NP_653201.1; NM_144600.3. [Q96NB1-1]
DR AlphaFoldDB; Q96NB1; -.
DR SMR; Q96NB1; -.
DR BioGRID; 125836; 48.
DR CORUM; Q96NB1; -.
DR IntAct; Q96NB1; 43.
DR STRING; 9606.ENSP00000255759; -.
DR iPTMnet; Q96NB1; -.
DR PhosphoSitePlus; Q96NB1; -.
DR BioMuta; FOPNL; -.
DR DMDM; 74732531; -.
DR EPD; Q96NB1; -.
DR jPOST; Q96NB1; -.
DR MassIVE; Q96NB1; -.
DR MaxQB; Q96NB1; -.
DR PaxDb; Q96NB1; -.
DR PeptideAtlas; Q96NB1; -.
DR PRIDE; Q96NB1; -.
DR ProteomicsDB; 3537; -.
DR ProteomicsDB; 77497; -. [Q96NB1-1]
DR Antibodypedia; 51607; 49 antibodies from 10 providers.
DR DNASU; 123811; -.
DR Ensembl; ENST00000255759.11; ENSP00000255759.6; ENSG00000133393.13. [Q96NB1-1]
DR Ensembl; ENST00000573968.5; ENSP00000460312.1; ENSG00000133393.13. [Q96NB1-2]
DR Ensembl; ENST00000622266.2; ENSP00000481290.1; ENSG00000276914.2. [Q96NB1-1]
DR Ensembl; ENST00000631974.1; ENSP00000488488.1; ENSG00000276914.2. [Q96NB1-2]
DR GeneID; 123811; -.
DR KEGG; hsa:123811; -.
DR MANE-Select; ENST00000255759.11; ENSP00000255759.6; NM_144600.4; NP_653201.1.
DR UCSC; uc002dec.2; human. [Q96NB1-1]
DR CTD; 123811; -.
DR DisGeNET; 123811; -.
DR GeneCards; CEP20; -.
DR HGNC; HGNC:26435; CEP20.
DR HPA; ENSG00000133393; Low tissue specificity.
DR MIM; 617149; gene.
DR neXtProt; NX_Q96NB1; -.
DR OpenTargets; ENSG00000133393; -.
DR VEuPathDB; HostDB:ENSG00000133393; -.
DR eggNOG; ENOG502S0C1; Eukaryota.
DR GeneTree; ENSGT00390000007773; -.
DR InParanoid; Q96NB1; -.
DR PhylomeDB; Q96NB1; -.
DR TreeFam; TF328861; -.
DR PathwayCommons; Q96NB1; -.
DR SignaLink; Q96NB1; -.
DR BioGRID-ORCS; 123811; 14 hits in 1080 CRISPR screens.
DR ChiTaRS; FOPNL; human.
DR GenomeRNAi; 123811; -.
DR Pharos; Q96NB1; Tbio.
DR PRO; PR:Q96NB1; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96NB1; protein.
DR Bgee; ENSG00000133393; Expressed in islet of Langerhans and 103 other tissues.
DR ExpressionAtlas; Q96NB1; baseline and differential.
DR Genevisible; Q96NB1; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0060271; P:cilium assembly; IMP: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 Alternative splicing; Cell projection; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..174
FT /note="Centrosomal protein 20"
FT /id="PRO_0000264465"
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 REGION 129..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 76..149
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056998"
FT MUTAGEN 49
FT /note="E->A: Loss of homooligomerization and loss of
FT localization to centrosomes and pericentriolar satellites;
FT when associated with A-76."
FT /evidence="ECO:0000269|PubMed:20551181"
FT MUTAGEN 49
FT /note="E->A: Strongly decreased interaction with KIAA0753;
FT when associated with A-76."
FT /evidence="ECO:0000269|PubMed:26643951"
FT MUTAGEN 53
FT /note="I->Q: Loss of interaction with KIAA0753; when
FT associated with A-76."
FT /evidence="ECO:0000269|PubMed:26643951"
FT MUTAGEN 76
FT /note="E->A: Loss of homooligomerization and loss of
FT localization to centrosomes and pericentriolar satellites;
FT when associated with A-49."
FT /evidence="ECO:0000269|PubMed:20551181"
FT MUTAGEN 76
FT /note="E->A: Strongly decreased interaction with KIAA0753;
FT when associated with A-49. Loss of interaction with
FT KIAA0753; when associated with Q-53."
FT /evidence="ECO:0000269|PubMed:26643951"
FT MUTAGEN 106
FT /note="L->R: No effect on interaction with KIAA0753."
FT /evidence="ECO:0000269|PubMed:26643951"
SQ SEQUENCE 174 AA; 19778 MW; 2362137C1024038F CRC64;
MATVAELKAV LKDTLEKKGV LGHLKARIRA EVFNALDDDR EPRPSLSHEN LLINELIREY
LEFNKYKYTA SVLIAESGQP VVPLDRQFLI HELNAFEESK DNTIPLLYGI LAHFLRGTKD
GIQNAFLKGP SLQPSDPSLG RQPSRRKPMD DHLRKEEQKS TNIEDLHVSQ AVNR
