CEP70_MOUSE
ID CEP70_MOUSE Reviewed; 616 AA.
AC Q6IQY5; Q3V0L8; Q9CRL9; Q9CTS4; Q9JIC1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Centrosomal protein of 70 kDa;
DE Short=Cep70;
GN Name=Cep70;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RA Zimmermann S., Kemler R., Orsulic S.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE GENOMIC DNA] OF 1-170 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Testis, Urinary bladder, and Wolffian duct;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Embryo, and Limb;
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).
CC -!- FUNCTION: Plays a role in the organization of both preexisting and
CC nascent microtubules in interphase cells. During mitosis, required for
CC the organization and orientation of the mitotic spindle (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Directly interacts with tubulin-gamma; this interaction
CC determines centrosomal localization. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6IQY5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6IQY5-2; Sequence=VSP_042142, VSP_042143;
CC -!- DOMAIN: The coiled-coil domains may be important for tubulin-gamma-
CC binding and hence for centrosomal localization. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF97768.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF242319; AAF97768.1; ALT_FRAME; mRNA.
DR EMBL; AK020174; BAB32020.1; -; mRNA.
DR EMBL; AK020622; BAB32153.1; -; mRNA.
DR EMBL; AK133048; BAE21486.1; -; mRNA.
DR EMBL; BC050819; AAH50819.1; -; mRNA.
DR EMBL; BC071260; AAH71260.1; -; mRNA.
DR CCDS; CCDS40738.1; -. [Q6IQY5-1]
DR RefSeq; NP_076362.2; NM_023873.3. [Q6IQY5-1]
DR RefSeq; XP_006511449.1; XM_006511386.3.
DR RefSeq; XP_011241104.1; XM_011242802.2.
DR AlphaFoldDB; Q6IQY5; -.
DR SMR; Q6IQY5; -.
DR BioGRID; 212668; 5.
DR STRING; 10090.ENSMUSP00000091312; -.
DR iPTMnet; Q6IQY5; -.
DR PhosphoSitePlus; Q6IQY5; -.
DR MaxQB; Q6IQY5; -.
DR PaxDb; Q6IQY5; -.
DR PRIDE; Q6IQY5; -.
DR ProteomicsDB; 281380; -. [Q6IQY5-1]
DR ProteomicsDB; 281381; -. [Q6IQY5-2]
DR Antibodypedia; 46706; 222 antibodies from 26 providers.
DR Ensembl; ENSMUST00000093795; ENSMUSP00000091312; ENSMUSG00000056267. [Q6IQY5-1]
DR Ensembl; ENSMUST00000191335; ENSMUSP00000139816; ENSMUSG00000056267. [Q6IQY5-2]
DR GeneID; 68121; -.
DR KEGG; mmu:68121; -.
DR UCSC; uc009rdy.1; mouse. [Q6IQY5-2]
DR UCSC; uc009rdz.1; mouse. [Q6IQY5-1]
DR CTD; 80321; -.
DR MGI; MGI:1915371; Cep70.
DR VEuPathDB; HostDB:ENSMUSG00000056267; -.
DR eggNOG; ENOG502QS45; Eukaryota.
DR GeneTree; ENSGT00390000009029; -.
DR HOGENOM; CLU_032136_0_0_1; -.
DR InParanoid; Q6IQY5; -.
DR OMA; LNGIYPR; -.
DR OrthoDB; 1217382at2759; -.
DR PhylomeDB; Q6IQY5; -.
DR TreeFam; TF330986; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 68121; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Cep70; mouse.
DR PRO; PR:Q6IQY5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6IQY5; protein.
DR Bgee; ENSMUSG00000056267; Expressed in animal zygote and 233 other tissues.
DR ExpressionAtlas; Q6IQY5; baseline and differential.
DR Genevisible; Q6IQY5; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0043015; F:gamma-tubulin binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; IEA:InterPro.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:InterPro.
DR InterPro; IPR037692; CEP70.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14594; PTHR14594; 3.
DR PROSITE; PS50005; TPR; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Reference proteome; TPR repeat.
FT CHAIN 1..616
FT /note="Centrosomal protein of 70 kDa"
FT /id="PRO_0000089498"
FT REPEAT 502..535
FT /note="TPR"
FT COILED 96..210
FT /evidence="ECO:0000255"
FT COILED 273..335
FT /evidence="ECO:0000255"
FT VAR_SEQ 570..578
FT /note="SIIKKLEEH -> RYLLEMHLE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_042142"
FT VAR_SEQ 579..616
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_042143"
FT CONFLICT 18
FT /note="T -> I (in Ref. 2; BAE21486)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="T -> L (in Ref. 1; AAF97768)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="K -> Q (in Ref. 1; AAF97768)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="K -> R (in Ref. 1; AAF97768)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="L -> F (in Ref. 1; AAF97768)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 616 AA; 71065 MW; 57302F6297E3ECBF CRC64;
MTEGSQIFLL PISTSDSTKE PLSPVASKAQ DPSLLSNRLM IEKQQEEAEW ESINGLLMTH
GFKPLCLVKG ADLRDFIVFD KQSSQKMRQI LKTLMEETTR QQSMIRELIE TNQQLKSELQ
LEQNRAAHQE QRANDLQQIM DSVKSKIGEL EDESLNRVCQ QQNRIKDLQK EYKMLQMKCQ
QYKKNRMEQE GTIASLQKEI HRLAKEEEER ILTQNRVFAH LCRRVPHSVL DKQLLCLIDY
YECKLRKLHI QRQFEEDSQS EEKDFTNLGA SPNYKGVLMS LQKQLKESKS RIDVLVGEKL
SLQKDLENRP TEHELRLYKQ QVKKLEKTLK KNIKLQDLIG QKKSDDTEKK DEPSKDSHQQ
ALIEQSYFQV LCSINSIVHN PRAPVIIYKQ SKGRAPNGNK DIGQDCGFEH LVPIIEMWVD
ELTSLKDLYK SLKILSAELV PWHSLKKLDE KEGVKVGDLL FMVDTMLEEV ENQKETSSTP
NSQTLQAIVS HFQKLFDVQS LNGVFPRMNE VYTRLGEMNN AVRNLQELLE LDSSSSLCVV
VSTVGKLCEI INKDVSEQVK QVLGPEDLQS IIKKLEEHEE FFPAFQAFAN DLLEILEIDD
LDAIVPAVKK LKILSY
