CE120_MOUSE
ID CE120_MOUSE Reviewed; 988 AA.
AC Q7TSG1; Q80Y93; Q80ZQ2; Q8BG01; Q8C580; Q8C8B6; Q8CAF2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Centrosomal protein of 120 kDa;
DE Short=Cep120;
DE AltName: Full=Coiled-coil domain-containing protein 100;
GN Name=Cep120; Synonyms=Ccdc100;
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] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-701 (ISOFORM 1/2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, and Hypothalamus;
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] (ISOFORMS 1 AND 4).
RC TISSUE=Embryo, Eye, and Testis;
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 FUNCTION, INTERACTION WITH TACC2 AND TACC3, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17920017; DOI=10.1016/j.neuron.2007.08.026;
RA Xie Z., Moy L.Y., Sanada K., Zhou Y., Buchman J.J., Tsai L.-H.;
RT "Cep120 and TACCs control interkinetic nuclear migration and the neural
RT progenitor pool.";
RL Neuron 56:79-93(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-934 AND SER-938, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, AND INTERACTION WITH CCDC52.
RX PubMed=20360068; DOI=10.1126/science.1181348;
RA Hutchins J.R., Toyoda Y., Hegemann B., Poser I., Heriche J.K., Sykora M.M.,
RA Augsburg M., Hudecz O., Buschhorn B.A., Bulkescher J., Conrad C.,
RA Comartin D., Schleiffer A., Sarov M., Pozniakovsky A., Slabicki M.M.,
RA Schloissnig S., Steinmacher I., Leuschner M., Ssykor A., Lawo S.,
RA Pelletier L., Stark H., Nasmyth K., Ellenberg J., Durbin R., Buchholz F.,
RA Mechtler K., Hyman A.A., Peters J.M.;
RT "Systematic analysis of human protein complexes identifies chromosome
RT segregation proteins.";
RL Science 328:593-599(2010).
RN [6]
RP FUNCTION, AND INTERACTION WITH TALPID3.
RX PubMed=25251415; DOI=10.1371/journal.pone.0107943;
RA Wu C., Yang M., Li J., Wang C., Cao T., Tao K., Wang B.;
RT "Talpid3-binding centrosomal protein Cep120 is required for centriole
RT duplication and proliferation of cerebellar granule neuron progenitors.";
RL PLoS ONE 9:E107943-E107943(2014).
CC -!- FUNCTION: Plays a role in the microtubule-dependent coupling of the
CC nucleus and the centrosome. Involved in the processes that regulate
CC centrosome-mediated interkinetic nuclear migration (INM) of neural
CC progenitors and for proper positioning of neurons during brain
CC development. Also implicated in the migration and selfrenewal of neural
CC progenitors. Required for centriole duplication and maturation during
CC mitosis and subsequent ciliogenesis. Required for the recruitment of
CC CEP295 to the proximal end of new-born centrioles at the centriolar
CC microtubule wall during early S phase in a PLK4-dependent manner (By
CC similarity). {ECO:0000250|UniProtKB:Q8N960,
CC ECO:0000269|PubMed:17920017, ECO:0000269|PubMed:20360068,
CC ECO:0000269|PubMed:25251415}.
CC -!- SUBUNIT: Interacts with TACC2, TACC3, CCDC52, TALPID3.
CC {ECO:0000269|PubMed:17920017, ECO:0000269|PubMed:20360068,
CC ECO:0000269|PubMed:25251415}.
CC -!- INTERACTION:
CC Q7TSG1; E9PV87: Talpid3; NbExp=3; IntAct=EBI-2553947, EBI-11692182;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:17920017}. Note=Regulates the
CC localization of TACC3 to the centrosome in neural progenitors in vivo.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q7TSG1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TSG1-2; Sequence=VSP_035130;
CC Name=3;
CC IsoId=Q7TSG1-3; Sequence=VSP_035127, VSP_035128;
CC Name=4;
CC IsoId=Q7TSG1-4; Sequence=VSP_035126, VSP_035129;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain, lung and
CC kidney and weakly expressed in heart, liver, small intestine and limb
CC (at protein level). Expressed in brain. {ECO:0000269|PubMed:17920017}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic brain from 10.5 to 17.5
CC dpc. Expressed in neocortical neural progenitors at the ventrical
CC surface at 12.5 dpc (at protein level). Expressed in brain, heart,
CC lung, liver, kidney, small intestine and limb at 16.5 dpc.
CC {ECO:0000269|PubMed:17920017}.
CC -!- SIMILARITY: Belongs to the CEP120 family. {ECO:0000305}.
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DR EMBL; AK038916; BAC30167.1; -; mRNA.
DR EMBL; AK044808; BAC32100.1; -; mRNA.
DR EMBL; AK044952; BAC32156.1; -; mRNA.
DR EMBL; AK047594; BAC33092.1; -; mRNA.
DR EMBL; AK079319; BAC37606.1; -; mRNA.
DR EMBL; BC046493; AAH46493.1; -; mRNA.
DR EMBL; BC048590; AAH48590.1; -; mRNA.
DR EMBL; BC053439; AAH53439.1; -; mRNA.
DR CCDS; CCDS37822.1; -. [Q7TSG1-1]
DR RefSeq; NP_848801.2; NM_178686.3. [Q7TSG1-1]
DR PDB; 6EWP; X-ray; 1.85 A; A/B/C=436-634.
DR PDBsum; 6EWP; -.
DR AlphaFoldDB; Q7TSG1; -.
DR SMR; Q7TSG1; -.
DR BioGRID; 230403; 39.
DR IntAct; Q7TSG1; 38.
DR STRING; 10090.ENSMUSP00000062433; -.
DR iPTMnet; Q7TSG1; -.
DR PhosphoSitePlus; Q7TSG1; -.
DR EPD; Q7TSG1; -.
DR jPOST; Q7TSG1; -.
DR MaxQB; Q7TSG1; -.
DR PaxDb; Q7TSG1; -.
DR PeptideAtlas; Q7TSG1; -.
DR PRIDE; Q7TSG1; -.
DR ProteomicsDB; 281156; -. [Q7TSG1-1]
DR ProteomicsDB; 281157; -. [Q7TSG1-2]
DR ProteomicsDB; 281158; -. [Q7TSG1-3]
DR ProteomicsDB; 281159; -. [Q7TSG1-4]
DR Antibodypedia; 25668; 79 antibodies from 17 providers.
DR DNASU; 225523; -.
DR Ensembl; ENSMUST00000049811; ENSMUSP00000062433; ENSMUSG00000048799. [Q7TSG1-1]
DR Ensembl; ENSMUST00000237062; ENSMUSP00000158481; ENSMUSG00000048799. [Q7TSG1-2]
DR GeneID; 225523; -.
DR KEGG; mmu:225523; -.
DR UCSC; uc008exy.1; mouse. [Q7TSG1-1]
DR UCSC; uc008exz.1; mouse. [Q7TSG1-2]
DR CTD; 153241; -.
DR MGI; MGI:2147298; Cep120.
DR VEuPathDB; HostDB:ENSMUSG00000048799; -.
DR eggNOG; ENOG502QPT0; Eukaryota.
DR GeneTree; ENSGT00390000009378; -.
DR HOGENOM; CLU_012372_0_0_1; -.
DR InParanoid; Q7TSG1; -.
DR OMA; DELETWK; -.
DR OrthoDB; 277001at2759; -.
DR PhylomeDB; Q7TSG1; -.
DR TreeFam; TF329430; -.
DR BioGRID-ORCS; 225523; 10 hits in 74 CRISPR screens.
DR ChiTaRS; Cep120; mouse.
DR PRO; PR:Q7TSG1; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q7TSG1; protein.
DR Bgee; ENSMUSG00000048799; Expressed in superior cervical ganglion and 233 other tissues.
DR Genevisible; Q7TSG1; MM.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:MGI.
DR GO; GO:0030953; P:astral microtubule organization; IDA:MGI.
DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0022027; P:interkinetic nuclear migration; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR GO; GO:1903724; P:positive regulation of centriole elongation; ISS:UniProtKB.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; IMP:UniProtKB.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:1904951; P:positive regulation of establishment of protein localization; ISS:UniProtKB.
DR GO; GO:0032886; P:regulation of microtubule-based process; IMP:MGI.
DR GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR039893; CEP120-like.
DR InterPro; IPR022136; DUF3668.
DR PANTHER; PTHR21574; PTHR21574; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF12416; DUF3668; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..988
FT /note="Centrosomal protein of 120 kDa"
FT /id="PRO_0000348263"
FT DOMAIN 1..112
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 435..569
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 354..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 706..929
FT /evidence="ECO:0000255"
FT COMPBIAS 354..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..396
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 934
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..901
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035126"
FT VAR_SEQ 347..365
FT /note="SLIELKTQNGHEAEHSQKR -> AGGDSAFTCQFSHARDDKR (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035127"
FT VAR_SEQ 366..988
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035128"
FT VAR_SEQ 902..911
FT /note="ELLDIRNELN -> MNLLRRSLHP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035129"
FT VAR_SEQ 913..988
FT /note="LRQQEQNQYQDCKEIASGKLGSPRGSGLEEGLDDYLTRLIEERDTLMRTGVY
FT NHEDRIISELDRQIREVLTKNSAS -> YCPYNHSFSHQHRSDSQ (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035130"
FT CONFLICT 614
FT /note="R -> G (in Ref. 1; BAC33092)"
FT /evidence="ECO:0000305"
FT STRAND 455..467
FT /evidence="ECO:0007829|PDB:6EWP"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:6EWP"
FT STRAND 475..481
FT /evidence="ECO:0007829|PDB:6EWP"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:6EWP"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:6EWP"
FT STRAND 512..519
FT /evidence="ECO:0007829|PDB:6EWP"
FT HELIX 521..530
FT /evidence="ECO:0007829|PDB:6EWP"
FT STRAND 533..539
FT /evidence="ECO:0007829|PDB:6EWP"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:6EWP"
FT STRAND 547..554
FT /evidence="ECO:0007829|PDB:6EWP"
FT HELIX 556..561
FT /evidence="ECO:0007829|PDB:6EWP"
FT STRAND 565..568
FT /evidence="ECO:0007829|PDB:6EWP"
FT STRAND 574..593
FT /evidence="ECO:0007829|PDB:6EWP"
FT STRAND 595..610
FT /evidence="ECO:0007829|PDB:6EWP"
SQ SEQUENCE 988 AA; 112579 MW; AF9A80D682A93953 CRC64;
MVPKSDQLLI VVSILEGRHF PKRPKHLLVV EAKFDGEQLA TDPVDHTDQP EFATELAWEI
DRKVLHQHRL QRTPIKLQCF ALDPQTSAKE TVGYIVLDLR TAQETKQAPK WYQLLSNKYT
KFKAEVQISL TLETDTKAQV DSYKAKAAPP RDGKVLASLA GVDPKDIVAV LNEEGGYHQI
GPAEHCTDPF ILSVTIAFAT QLEQLIPCTM KLPERQPEFF FYYSLLGNDV TNEPFSDLIN
PNFEPERASV RIRSSVEILR VYLALHSKLQ IHLCCGDQSL GSTEIPLNGL LKKGSTEINQ
HPVTVEGAFT LDPPNRAKQK LAPVPLDLAP TVGVSVALQR EGIDSQSLIE LKTQNGHEAE
HSQKRVLTPI KEKTLTGPKS PRESPAPPPP PNQTPPTKDD ATESEVESLQ YDKDPKPTVK
GIGSVPASLA QPEATCGASE VVTSGQKIAV PAASHHFCFS VDLRSVHDLE LSFPVNCILR
YSYPFFGSAA PIMTNPPVEV RKNMEVFLPQ SYCAFDFATM PHQLQDTFLR IPLLVELWHK
DKMSKDLLLG VARIQLSNIL SSEKTRFLGA NGEQCWRQTY SESVPVIAAQ GSNNRILDLS
YTMTLEDYGL VKMREIFVSE SSQGVPAVDQ KPSSPPPAPC PSEIQMEPRE TLEYKAALEL
EMWKEMQEDI FESQLKQKEL AHMQALAEEW KKRDRERESL VKKKVAEYSI LEGKLQKALT
ELETREQQLA SAEAELQRER KELQLERERN LQELQDSVRR ARDDCVYQVE LERLKLKQLE
EDKQRLQQQL NDAGNKYKTL EKEFQQFKDQ QNNKPEIRLQ SEINLLTLEK VELERKLESA
TKSKLHYKQQ WGRALKELAR LKQREQESQM ARLKKQQEEL EQMRLRYLAA EEKETVRTEQ
QELLDIRNEL NRLRQQEQNQ YQDCKEIASG KLGSPRGSGL EEGLDDYLTR LIEERDTLMR
TGVYNHEDRI ISELDRQIRE VLTKNSAS
