CEP72_MOUSE
ID CEP72_MOUSE Reviewed; 646 AA.
AC Q9D3R3; E9QQ95; Q3TU12; Q497H8; Q69ZH7; Q8BM53; Q9D0B7;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Centrosomal protein of 72 kDa;
DE Short=Cep72;
GN Name=Cep72; Synonyms=Kiaa1519;
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 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Liver, and Testis;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-646 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 231-646 (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Involved in the recruitment of key centrosomal proteins to
CC the centrosome. Provides centrosomal microtubule-nucleation activity on
CC the gamma-tubulin ring complexes (gamma-TuRCs) and has critical roles
CC in forming a focused bipolar spindle, which is needed for proper
CC tension generation between sister chromatids. Required for localization
CC of KIZ, AKAP9 and gamma-tubulin ring complexes (gamma-TuRCs) (By
CC similarity). Involved in centriole duplication. Required for CDK5RAP22,
CC CEP152, WDR62 and CEP63 centrosomal localization and promotes the
CC centrosomal localization of CDK2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9P209}.
CC -!- SUBUNIT: Interacts with KIZ, PCM1 and CDK5RAP2.
CC {ECO:0000250|UniProtKB:Q9P209}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q9P209}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriolar
CC satellite {ECO:0000250|UniProtKB:Q9P209}. Note=Localizes to the
CC centrosome and centrosome-surrounding particles throughout the cell
CC cycle. These particles disappear after microtubules are depolymerized
CC using nocodazole, suggesting that CEP72-associating particles localize
CC in a microtubule-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q9P209}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D3R3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D3R3-2; Sequence=VSP_012748, VSP_012749;
CC -!- SIMILARITY: Belongs to the CEP72 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC28870.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD32467.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence={ECO:0000305};
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DR EMBL; AK011607; BAB27729.1; -; mRNA.
DR EMBL; AK017134; BAB30613.2; -; mRNA.
DR EMBL; AK034892; BAC28870.1; ALT_INIT; mRNA.
DR EMBL; AK161033; BAE36159.1; -; mRNA.
DR EMBL; CT010471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC100549; AAI00550.1; -; mRNA.
DR EMBL; AK173189; BAD32467.1; ALT_SEQ; Transcribed_RNA.
DR CCDS; CCDS26639.1; -. [Q9D3R3-1]
DR RefSeq; NP_083235.3; NM_028959.3. [Q9D3R3-1]
DR AlphaFoldDB; Q9D3R3; -.
DR SMR; Q9D3R3; -.
DR BioGRID; 216776; 53.
DR IntAct; Q9D3R3; 52.
DR MINT; Q9D3R3; -.
DR STRING; 10090.ENSMUSP00000037788; -.
DR iPTMnet; Q9D3R3; -.
DR PhosphoSitePlus; Q9D3R3; -.
DR EPD; Q9D3R3; -.
DR jPOST; Q9D3R3; -.
DR MaxQB; Q9D3R3; -.
DR PaxDb; Q9D3R3; -.
DR PeptideAtlas; Q9D3R3; -.
DR PRIDE; Q9D3R3; -.
DR ProteomicsDB; 280001; -. [Q9D3R3-1]
DR ProteomicsDB; 280002; -. [Q9D3R3-2]
DR Antibodypedia; 22247; 184 antibodies from 25 providers.
DR Ensembl; ENSMUST00000036456; ENSMUSP00000037788; ENSMUSG00000021572. [Q9D3R3-1]
DR GeneID; 74470; -.
DR KEGG; mmu:74470; -.
DR UCSC; uc007rep.2; mouse. [Q9D3R3-2]
DR UCSC; uc007req.2; mouse. [Q9D3R3-1]
DR CTD; 55722; -.
DR MGI; MGI:1921720; Cep72.
DR VEuPathDB; HostDB:ENSMUSG00000021572; -.
DR eggNOG; ENOG502QV2Y; Eukaryota.
DR GeneTree; ENSGT00530000063884; -.
DR HOGENOM; CLU_027497_0_0_1; -.
DR InParanoid; Q9D3R3; -.
DR OMA; KITHLGH; -.
DR OrthoDB; 881430at2759; -.
DR PhylomeDB; Q9D3R3; -.
DR TreeFam; TF338646; -.
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; 74470; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Cep72; mouse.
DR PRO; PR:Q9D3R3; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9D3R3; protein.
DR Bgee; ENSMUSG00000021572; Expressed in spermatocyte and 101 other tissues.
DR ExpressionAtlas; Q9D3R3; baseline and differential.
DR Genevisible; Q9D3R3; MM.
DR GO; GO:0034451; C:centriolar satellite; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0007099; P:centriole replication; ISO:MGI.
DR GO; GO:0033566; P:gamma-tubulin complex localization; ISS:UniProtKB.
DR GO; GO:1904779; P:regulation of protein localization to centrosome; ISO:MGI.
DR GO; GO:0007051; P:spindle organization; ISS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR040146; CEP72.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR PANTHER; PTHR23311:SF7; PTHR23311:SF7; 1.
DR SMART; SM00369; LRR_TYP; 2.
DR SMART; SM00446; LRRcap; 1.
DR PROSITE; PS51450; LRR; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Leucine-rich repeat; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..646
FT /note="Centrosomal protein of 72 kDa"
FT /id="PRO_0000089500"
FT REPEAT 28..49
FT /note="LRR 1"
FT REPEAT 54..75
FT /note="LRR 2"
FT REPEAT 76..97
FT /note="LRR 3"
FT DOMAIN 110..149
FT /note="LRRCT"
FT REGION 300..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 476..622
FT /evidence="ECO:0000255"
FT COMPBIAS 300..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P209"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P209"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P209"
FT VAR_SEQ 1..286
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012748"
FT VAR_SEQ 321..400
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012749"
FT CONFLICT 18..19
FT /note="SG -> RA (in Ref. 1; BAB30613)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="V -> L (in Ref. 1; BAB27729)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 646 AA; 72433 MW; 9E2A803B0E0883AC CRC64;
MAPGQRLVLC EETVRERSGL GPHRDLAELR SLSIPGTYQE KITHLGNSLM HLTALKSLDL
SRNSLVSLEG IQYLVSLESL NLYYNCISSL AEVFRLHTLL ELQDVDFRLN PVVKNESDYR
LFVVHMLPKL RQLDDRPVRE SERKASQLHF APEDSLNSKE NFSTTLTVGR PHHLRNRCTE
TSAKKCLVMD ADDEAVLNLI AECEWDLSNP PGNMSSSQKE HEADLHYAQE SRHLLSPLSI
QHQCGDSARR GHEKKKVTSR GCPGHSPQDQ LCGELPLQHG LPEACHMHVQ HARITSQPDS
VDVEDCASSA QKSSLSSQKT VNPLPVPEKY RKRRMPGGRF QVPSDRECLS FLERADGPSS
LEDSLSRQDG LEGQSQVALS HSEALEAEER TSHGTSDPRV LSPKLCSAAV PERRSTLEVA
LLEALLDLID RCSSGSGSLH GNEAFLAQAK HVLSSLQEFT ATRDSSALEK EGIGYLSLEN
KTLQSRLAEQ QQQYTATVTK MTAELNNTKR ELDTLRQHLD KSLEENSHLK SLLYNVKKEV
KTADTSTALT LQITGLQASM KQLSGEVVEL KQHVEHYDKI QELTQMLQES HSSLVSTNEH
LLQELSRTRA QHRAEVEQMR WSFQEFKKTT ALIPHRSSRR GGRQSC
