Entry sw: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   30-NOV-2016, entry version 86.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
RP   NUCLEOTIDE 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, INTERACTION WITH TACC2 AND TACC3, SUBCELLULAR LOCATION,
RP   TISSUE 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
RT   neural 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
RT   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.,
RA   Sykora M.M., Augsburg M., Hudecz O., Buschhorn B.A., Bulkescher J.,
RA   Conrad C., Comartin D., Schleiffer A., Sarov M., Pozniakovsky A.,
RA   Slabicki M.M., Schloissnig S., Steinmacher I., Leuschner M.,
RA   Ssykor A., Lawo S., Pelletier L., Stark H., Nasmyth K., Ellenberg J.,
RA   Durbin R., Buchholz F., 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
RT   progenitors.";
RL   PLoS ONE 9:E107943-E107943(2014).
CC   -!- FUNCTION: Plays a role in the microtubule-dependent coupling of
CC       the nucleus and the centrosome. Involved in the processes that
CC       regulate centrosome-mediated interkinetic nuclear migration (INM)
CC       of neural progenitors and for proper positioning of neurons during
CC       brain development. Also implicated in the migration and
CC       selfrenewal of neural progenitors. Required for centriole
CC       duplication and maturation during mitosis and subsequent
CC       ciliogenesis. {ECO:0000269|PubMed:17920017,
CC       ECO:0000269|PubMed:20360068, 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       E9PV87:Talpid3; NbExp=3; IntAct=EBI-2553947, EBI-11692182;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000269|PubMed:17920017}.
CC       Note=Regulates the localization of TACC3 to the centrosome in
CC       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         Note=No experimental confirmation available.;
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
CC       and kidney and weakly expressed in heart, liver, small intestine
CC       and limb (at protein level). Expressed in brain.
CC       {ECO:0000269|PubMed:17920017}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryonic brain from 10.5 to
CC       17.5 dpc. Expressed in neocortical neural progenitors at the
CC       ventrical surface at 12.5 dpc (at protein level). Expressed in
CC       brain, heart, lung, liver, kidney, small intestine and limb at
CC       16.5 dpc. {ECO:0000269|PubMed:17920017}.
CC   -!- SIMILARITY: Belongs to the CEP120 family. {ECO:0000305}.
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   UniGene; Mm.193678; -.
DR   ProteinModelPortal; Q7TSG1; -.
DR   SMR; Q7TSG1; -.
DR   BioGrid; 230403; 37.
DR   IntAct; Q7TSG1; 39.
DR   STRING; 10090.ENSMUSP00000062433; -.
DR   iPTMnet; Q7TSG1; -.
DR   PhosphoSitePlus; Q7TSG1; -.
DR   PaxDb; Q7TSG1; -.
DR   PeptideAtlas; Q7TSG1; -.
DR   PRIDE; Q7TSG1; -.
DR   Ensembl; ENSMUST00000049811; ENSMUSP00000062433; ENSMUSG00000048799. [Q7TSG1-1]
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   eggNOG; ENOG410IDYJ; Eukaryota.
DR   eggNOG; ENOG410XNN2; LUCA.
DR   GeneTree; ENSGT00390000009378; -.
DR   HOVERGEN; HBG107643; -.
DR   InParanoid; Q7TSG1; -.
DR   KO; K16459; -.
DR   OMA; LKTQNEH; -.
DR   OrthoDB; EOG091G074C; -.
DR   PhylomeDB; Q7TSG1; -.
DR   TreeFam; TF329430; -.
DR   PRO; PR:Q7TSG1; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   Bgee; ENSMUSG00000048799; -.
DR   Genevisible; Q7TSG1; MM.
DR   GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR   GO; GO:0005813; C:centrosome; IDA:MGI.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:MGI.
DR   GO; GO:0030953; P:astral microtubule organization; IDA:MGI.
DR   GO; GO:0008283; P:cell proliferation; IMP:MGI.
DR   GO; GO:0051297; P:centrosome organization; 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:0010825; P:positive regulation of centrosome duplication; IMP:UniProtKB.
DR   GO; GO:0045724; P:positive regulation of cilium assembly; IMP: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   Gene3D; 2.60.40.150; -; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR022136; DUF3668.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF12416; DUF3668; 1.
DR   SUPFAM; SSF49562; SSF49562; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW   Cytoskeleton; Phosphoprotein; Reference proteome.
FT   CHAIN         1    988       Centrosomal protein of 120 kDa.
FT                                /FTId=PRO_0000348263.
FT   COILED      706    929       {ECO:0000255}.
FT   MOD_RES     934    934       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     938    938       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   VAR_SEQ       1    901       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_035126.
FT   VAR_SEQ     347    365       SLIELKTQNGHEAEHSQKR -> AGGDSAFTCQFSHARDDK
FT                                R (in isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_035127.
FT   VAR_SEQ     366    988       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_035128.
FT   VAR_SEQ     902    911       ELLDIRNELN -> MNLLRRSLHP (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_035129.
FT   VAR_SEQ     913    988       LRQQEQNQYQDCKEIASGKLGSPRGSGLEEGLDDYLTRLIE
FT                                ERDTLMRTGVYNHEDRIISELDRQIREVLTKNSAS -> YC
FT                                PYNHSFSHQHRSDSQ (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_035130.
FT   CONFLICT    614    614       R -> G (in Ref. 1; BAC33092).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       532    564       ipfam:C2 [T]
FT   MYHIT       118    340       ipfam:DUF3668 [T]
FT   MYHIT        11    114       ipfam:C2 [T]
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
//