CEP57_MOUSE
ID CEP57_MOUSE Reviewed; 500 AA.
AC Q8CEE0; B8JJE6; Q6ZQJ3; Q7TN18; Q80X65; Q810F2; Q9D4J4; Q9D5S4; Q9D5W5;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Centrosomal protein of 57 kDa;
DE Short=Cep57;
DE AltName: Full=Testis-specific protein 57;
DE AltName: Full=Translokin;
GN Name=Cep57; Synonyms=Kiaa0092, Tsp57;
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), AND FUNCTION IN FGF2 TRAFFICKING.
RC STRAIN=C57BL/6J;
RX PubMed=12717444; DOI=10.1038/ncb979;
RA Bossard C., Laurell H., Van den Berghe L., Meunier S., Zanibellato C.,
RA Prats H.;
RT "Translokin is an intracellular mediator of FGF-2 trafficking.";
RL Nat. Cell Biol. 5:433-439(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH RAP80.
RC STRAIN=Swiss Webster; TISSUE=Testis;
RX PubMed=12954732; DOI=10.1095/biolreprod.103.018465;
RA Kim Y.-S., Nakanishi G., Oudes A.J., Kim K.H., Wang H., Kilpatrick D.L.,
RA Jetten A.M.;
RT "Tsp57: a novel gene induced during a specific stage of spermatogenesis.";
RL Biol. Reprod. 70:106-113(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Skin, 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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-257 (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, SUBUNIT, AND
RP INTERACTION WITH MICROTUBULES.
RX PubMed=18294141; DOI=10.1042/bj20071501;
RA Momotani K., Khromov A.S., Miyake T., Stukenberg P.T., Somlyo A.V.;
RT "Cep57, a multidomain protein with unique microtubule and centrosomal
RT localization domains.";
RL Biochem. J. 412:265-273(2008).
CC -!- FUNCTION: Centrosomal protein which may be required for microtubule
CC attachment to centrosomes. May act by forming ring-like structures
CC around microtubules. Mediates nuclear translocation and mitogenic
CC activity of the internalized growth factor FGF2.
CC {ECO:0000269|PubMed:12717444, ECO:0000269|PubMed:18294141}.
CC -!- SUBUNIT: Interacts with FGF2 and RAP80. Does not interact with FGF1 or
CC FGF2 isoform 24 kDa (By similarity). Homodimer and homooligomer.
CC Interacts with microtubules. {ECO:0000250, ECO:0000269|PubMed:12954732,
CC ECO:0000269|PubMed:18294141}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:12954732, ECO:0000269|PubMed:18294141}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CEE0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CEE0-2; Sequence=VSP_012266;
CC Name=3;
CC IsoId=Q8CEE0-3; Sequence=VSP_012265;
CC -!- TISSUE SPECIFICITY: Ubiquitous (at protein level). Expressed in testis,
CC predominantly in round spermatids. Low expression is detected in other
CC tissues. {ECO:0000269|PubMed:12954732, ECO:0000269|PubMed:18294141}.
CC -!- DOMAIN: The C-terminal region mediates the interaction with
CC microtubules and is able to nucleate and bundles microtubules in vitro.
CC {ECO:0000269|PubMed:18294141}.
CC -!- DOMAIN: The centrosome localization domain (CLD) region mediates the
CC localization to centrosomes and homooligomerization.
CC {ECO:0000269|PubMed:18294141}.
CC -!- SIMILARITY: Belongs to the translokin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50785.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC97863.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY225093; AAO73939.1; -; mRNA.
DR EMBL; AY251192; AAP32743.1; -; mRNA.
DR EMBL; AK014873; BAB29596.1; -; mRNA.
DR EMBL; AK014982; BAB29652.1; -; mRNA.
DR EMBL; AK016484; BAB30264.1; -; mRNA.
DR EMBL; AK028458; BAC25962.1; -; mRNA.
DR EMBL; CT010488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466522; EDL24979.1; -; Genomic_DNA.
DR EMBL; BC050785; AAH50785.1; ALT_INIT; mRNA.
DR EMBL; AK129053; BAC97863.1; ALT_INIT; mRNA.
DR CCDS; CCDS52724.1; -. [Q8CEE0-1]
DR RefSeq; NP_001297650.1; NM_001310721.1.
DR RefSeq; NP_080941.3; NM_026665.4. [Q8CEE0-1]
DR RefSeq; XP_006510712.1; XM_006510649.1. [Q8CEE0-3]
DR AlphaFoldDB; Q8CEE0; -.
DR SMR; Q8CEE0; -.
DR BioGRID; 216689; 5.
DR STRING; 10090.ENSMUSP00000034398; -.
DR iPTMnet; Q8CEE0; -.
DR PhosphoSitePlus; Q8CEE0; -.
DR EPD; Q8CEE0; -.
DR jPOST; Q8CEE0; -.
DR MaxQB; Q8CEE0; -.
DR PaxDb; Q8CEE0; -.
DR PRIDE; Q8CEE0; -.
DR ProteomicsDB; 281196; -. [Q8CEE0-1]
DR ProteomicsDB; 281197; -. [Q8CEE0-2]
DR ProteomicsDB; 281198; -. [Q8CEE0-3]
DR Antibodypedia; 17918; 238 antibodies from 27 providers.
DR DNASU; 74360; -.
DR Ensembl; ENSMUST00000034398; ENSMUSP00000034398; ENSMUSG00000031922. [Q8CEE0-1]
DR Ensembl; ENSMUST00000124883; ENSMUSP00000119081; ENSMUSG00000031922. [Q8CEE0-3]
DR Ensembl; ENSMUST00000148086; ENSMUSP00000114665; ENSMUSG00000031922. [Q8CEE0-2]
DR GeneID; 74360; -.
DR KEGG; mmu:74360; -.
DR UCSC; uc009oea.2; mouse. [Q8CEE0-3]
DR UCSC; uc009oeb.2; mouse. [Q8CEE0-1]
DR CTD; 9702; -.
DR MGI; MGI:1915551; Cep57.
DR VEuPathDB; HostDB:ENSMUSG00000031922; -.
DR eggNOG; ENOG502QTZR; Eukaryota.
DR GeneTree; ENSGT00530000063695; -.
DR HOGENOM; CLU_034321_2_0_1; -.
DR InParanoid; Q8CEE0; -.
DR OMA; QHTKALC; -.
DR OrthoDB; 1255254at2759; -.
DR PhylomeDB; Q8CEE0; -.
DR TreeFam; TF329178; -.
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; 74360; 9 hits in 74 CRISPR screens.
DR ChiTaRS; Cep57; mouse.
DR PRO; PR:Q8CEE0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8CEE0; protein.
DR Bgee; ENSMUSG00000031922; Expressed in seminiferous tubule of testis and 237 other tissues.
DR ExpressionAtlas; Q8CEE0; baseline and differential.
DR Genevisible; Q8CEE0; MM.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISS:UniProtKB.
DR GO; GO:0043015; F:gamma-tubulin binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0034453; P:microtubule anchoring; IEA:InterPro.
DR GO; GO:0051260; P:protein homooligomerization; IPI:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IEP:HGNC-UCL.
DR InterPro; IPR010597; Centrosomal_protein_57kDa.
DR InterPro; IPR025913; Cep57_CLD.
DR InterPro; IPR024957; Cep57_MT-bd_dom.
DR PANTHER; PTHR19336:SF11; PTHR19336:SF11; 1.
DR Pfam; PF14073; Cep57_CLD; 1.
DR Pfam; PF06657; Cep57_MT_bd; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..500
FT /note="Centrosomal protein of 57 kDa"
FT /id="PRO_0000189533"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..239
FT /note="centrosome localization domain (CLD)"
FT REGION 256..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..491
FT /note="Mediates interaction with microtubules"
FT REGION 432..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 63..242
FT /evidence="ECO:0000255"
FT COILED 389..449
FT /evidence="ECO:0000255"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XR8"
FT VAR_SEQ 1..149
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_012265"
FT VAR_SEQ 1..27
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012266"
FT CONFLICT 5
FT /note="S -> P (in Ref. 3; BAB29596)"
FT /evidence="ECO:0000305"
FT CONFLICT 16..24
FT /note="SVLAEPSRS -> VRGGGASRC (in Ref. 2; AAP32743)"
FT /evidence="ECO:0000305"
FT CONFLICT 295..296
FT /note="GT -> EK (in Ref. 1; AAO73939)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="S -> N (in Ref. 3; BAC25962)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="E -> K (in Ref. 3; BAB29652)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="V -> F (in Ref. 3; BAB29652)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="E -> K (in Ref. 3; BAB29652)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="K -> R (in Ref. 3; BAB29652)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="E -> K (in Ref. 3; BAB29652)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 56909 MW; D57490F4B22E7707 CRC64;
MAAASVSAAS DSQFSSVLAE PSRSNGNMVR HSSSPYVLYP PDKPFLNSDL RRSPNKPTFA
YPESNSRAIF SALKNLQDKI RRLELERIQA EESVKTLSRE TIEYKKVLDE QIQERENSKN
EESKHNQELA SQLVAAENKC NLLEKQLEYM RNMIKHAEME RTSVLEKQVS LERERQHDQT
HVQSQLEKLD LLEQEYNKLT AMQALAEKKM QELESKLREE EQERKRMQAR AAELQSGLEA
NRLIFEDKTT SCVSTSTRKI KKKKSKPPEK KGSRTYFGAQ PHYRLCLGDM PFVAGTSTSP
SHAVVANVQH VLHLMKHHSK ALCNDRVVNS VPLAKQACSR VSKSKKSVVP PSSSVNEELS
DVLQTLQDEF GQMSFDHQQL TKLIQESPTV ELKDNLECEL EALVGRMEAK ANQITKVRKY
QAQLEKQNID KQKKELKANK KTLDEEGNSS GRSSGVPRTA SKKDLAKQRP GEKSRKNLQL
LKDMQTIQNS LQSSNLCWDY
