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Centrosomal protein of 57 kDa (Cep57) (Testis-specific protein 57) (Translokin)

 CEP57_MOUSE             Reviewed;         500 AA.
Q8CEE0; B8JJE6; Q6ZQJ3; Q7TN18; Q80X65; Q810F2; Q9D4J4; Q9D5S4;
Q9D5W5;
21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 2.
25-OCT-2017, entry version 119.
RecName: Full=Centrosomal protein of 57 kDa;
Short=Cep57;
AltName: Full=Testis-specific protein 57;
AltName: Full=Translokin;
Name=Cep57; Synonyms=Kiaa0092, Tsp57;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION IN FGF2
TRAFFICKING.
STRAIN=C57BL/6J;
PubMed=12717444; DOI=10.1038/ncb979;
Bossard C., Laurell H., Van den Berghe L., Meunier S., Zanibellato C.,
Prats H.;
"Translokin is an intracellular mediator of FGF-2 trafficking.";
Nat. Cell Biol. 5:433-439(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND INTERACTION WITH RAP80.
STRAIN=Swiss Webster; TISSUE=Testis;
PubMed=12954732; DOI=10.1095/biolreprod.103.018465;
Kim Y.-S., Nakanishi G., Oudes A.J., Kim K.H., Wang H.,
Kilpatrick D.L., Jetten A.M.;
"Tsp57: a novel gene induced during a specific stage of
spermatogenesis.";
Biol. Reprod. 70:106-113(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
STRAIN=C57BL/6J; TISSUE=Skin, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-257 (ISOFORM 1).
TISSUE=Embryonic tail;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[8]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, SUBUNIT,
AND INTERACTION WITH MICROTUBULES.
PubMed=18294141; DOI=10.1042/BJ20071501;
Momotani K., Khromov A.S., Miyake T., Stukenberg P.T., Somlyo A.V.;
"Cep57, a multidomain protein with unique microtubule and centrosomal
localization domains.";
Biochem. J. 412:265-273(2008).
-!- FUNCTION: Centrosomal protein which may be required for
microtubule attachment to centrosomes. May act by forming ring-
like structures around microtubules. Mediates nuclear
translocation and mitogenic activity of the internalized growth
factor FGF2. {ECO:0000269|PubMed:12717444,
ECO:0000269|PubMed:18294141}.
-!- SUBUNIT: Interacts with FGF2 and RAP80. Does not interact with
FGF1 or FGF2 isoform 24 kDa (By similarity). Homodimer and
homooligomer. Interacts with microtubules. {ECO:0000250,
ECO:0000269|PubMed:12954732, ECO:0000269|PubMed:18294141}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing
center, centrosome {ECO:0000269|PubMed:12954732,
ECO:0000269|PubMed:18294141}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8CEE0-1; Sequence=Displayed;
Name=2;
IsoId=Q8CEE0-2; Sequence=VSP_012266;
Name=3;
IsoId=Q8CEE0-3; Sequence=VSP_012265;
-!- TISSUE SPECIFICITY: Ubiquitous (at protein level). Expressed in
testis, predominantly in round spermatids. Low expression is
detected in other tissues. {ECO:0000269|PubMed:12954732,
ECO:0000269|PubMed:18294141}.
-!- DOMAIN: The C-terminal region mediates the interaction with
microtubules and is able to nucleate and bundles microtubules in
vitro. {ECO:0000269|PubMed:18294141}.
-!- DOMAIN: The centrosome localization domain (CLD) region mediates
the localization to centrosomes and homooligomerization.
{ECO:0000269|PubMed:18294141}.
-!- SIMILARITY: Belongs to the translokin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH50785.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAC97863.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY225093; AAO73939.1; -; mRNA.
EMBL; AY251192; AAP32743.1; -; mRNA.
EMBL; AK014873; BAB29596.1; -; mRNA.
EMBL; AK014982; BAB29652.1; -; mRNA.
EMBL; AK016484; BAB30264.1; -; mRNA.
EMBL; AK028458; BAC25962.1; -; mRNA.
EMBL; CT010488; CAX15658.1; -; Genomic_DNA.
EMBL; CH466522; EDL24979.1; -; Genomic_DNA.
EMBL; BC050785; AAH50785.1; ALT_INIT; mRNA.
EMBL; AK129053; BAC97863.1; ALT_INIT; mRNA.
CCDS; CCDS52724.1; -. [Q8CEE0-1]
RefSeq; NP_001297650.1; NM_001310721.1.
RefSeq; NP_080941.3; NM_026665.4. [Q8CEE0-1]
RefSeq; XP_006510712.1; XM_006510649.1. [Q8CEE0-3]
UniGene; Mm.157212; -.
ProteinModelPortal; Q8CEE0; -.
SMR; Q8CEE0; -.
BioGrid; 216689; 1.
STRING; 10090.ENSMUSP00000034398; -.
iPTMnet; Q8CEE0; -.
PhosphoSitePlus; Q8CEE0; -.
PaxDb; Q8CEE0; -.
PRIDE; Q8CEE0; -.
Ensembl; ENSMUST00000034398; ENSMUSP00000034398; ENSMUSG00000031922. [Q8CEE0-1]
Ensembl; ENSMUST00000124883; ENSMUSP00000119081; ENSMUSG00000031922. [Q8CEE0-3]
Ensembl; ENSMUST00000148086; ENSMUSP00000114665; ENSMUSG00000031922. [Q8CEE0-2]
GeneID; 74360; -.
KEGG; mmu:74360; -.
UCSC; uc009oea.2; mouse. [Q8CEE0-3]
UCSC; uc009oeb.2; mouse. [Q8CEE0-1]
CTD; 9702; -.
MGI; MGI:1915551; Cep57.
eggNOG; ENOG410IESE; Eukaryota.
eggNOG; ENOG410XPJC; LUCA.
GeneTree; ENSGT00530000063695; -.
HOVERGEN; HBG050917; -.
InParanoid; Q8CEE0; -.
KO; K16762; -.
OMA; LCLGDMP; -.
OrthoDB; EOG091G07B7; -.
PhylomeDB; Q8CEE0; -.
TreeFam; TF329178; -.
Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-MMU-8854518; AURKA Activation by TPX2.
ChiTaRS; Cep57; mouse.
PRO; PR:Q8CEE0; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000031922; -.
CleanEx; MM_CEP57; -.
ExpressionAtlas; Q8CEE0; baseline and differential.
Genevisible; Q8CEE0; MM.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0005874; C:microtubule; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:HGNC.
GO; GO:0017134; F:fibroblast growth factor binding; ISS:UniProtKB.
GO; GO:0043015; F:gamma-tubulin binding; IEA:InterPro.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0034453; P:microtubule anchoring; IEA:InterPro.
GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
GO; GO:0051260; P:protein homooligomerization; IPI:UniProtKB.
GO; GO:0000060; P:protein import into nucleus, translocation; IMP:UniProtKB.
GO; GO:0007286; P:spermatid development; IEP:HGNC.
InterPro; IPR010597; Centrosomal_protein_57kDa.
InterPro; IPR025913; Cep57_CLD.
InterPro; IPR024957; Cep57_MT-bd_dom.
PANTHER; PTHR19336:SF11; PTHR19336:SF11; 1.
Pfam; PF14073; Cep57_CLD; 1.
Pfam; PF06657; Cep57_MT_bd; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Microtubule; Nucleus; Phosphoprotein;
Reference proteome.
CHAIN 1 500 Centrosomal protein of 57 kDa.
/FTId=PRO_0000189533.
REGION 58 239 centrosome localization domain (CLD).
REGION 278 491 Mediates interaction with microtubules.
COILED 63 242 {ECO:0000255}.
COILED 389 449 {ECO:0000255}.
COMPBIAS 259 266 Poly-Lys.
MOD_RES 53 53 Phosphoserine.
{ECO:0000250|UniProtKB:Q86XR8}.
VAR_SEQ 1 149 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_012265.
VAR_SEQ 1 27 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_012266.
CONFLICT 5 5 S -> P (in Ref. 3; BAB29596).
{ECO:0000305}.
CONFLICT 16 24 SVLAEPSRS -> VRGGGASRC (in Ref. 2;
AAP32743). {ECO:0000305}.
CONFLICT 295 296 GT -> EK (in Ref. 1; AAO73939).
{ECO:0000305}.
CONFLICT 353 353 S -> N (in Ref. 3; BAC25962).
{ECO:0000305}.
CONFLICT 386 386 E -> K (in Ref. 3; BAB29652).
{ECO:0000305}.
CONFLICT 417 417 V -> F (in Ref. 3; BAB29652).
{ECO:0000305}.
CONFLICT 425 425 E -> K (in Ref. 3; BAB29652).
{ECO:0000305}.
CONFLICT 431 431 K -> R (in Ref. 3; BAB29652).
{ECO:0000305}.
CONFLICT 435 435 E -> K (in Ref. 3; BAB29652).
{ECO:0000305}.
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


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