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Centrosomal protein of 57 kDa (Cep57) (FGF2-interacting protein) (Testis-specific protein 57) (Translokin)

 CEP57_HUMAN             Reviewed;         500 AA.
Q86XR8; A0PJH1; A8K5D0; B4DDP5; F5H5F7; Q14704; Q5JB46; Q8IXP0;
Q9BVF9;
21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 2.
25-OCT-2017, entry version 132.
RecName: Full=Centrosomal protein of 57 kDa;
Short=Cep57;
AltName: Full=FGF2-interacting protein;
AltName: Full=Testis-specific protein 57;
AltName: Full=Translokin;
Name=CEP57; Synonyms=KIAA0092, TSP57;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, SUBUNIT, INTERACTION WITH FGF2, AND VARIANT GLY-448.
TISSUE=Placenta;
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).
Kim J.W.;
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Bone marrow;
PubMed=7788527; DOI=10.1093/dnares/2.1.37;
Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. III.
The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:37-43(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
GLY-448.
TISSUE=Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Kidney, Mammary gland, and Placenta;
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]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
Mann M.;
"Proteomic characterization of the human centrosome by protein
correlation profiling.";
Nature 426:570-574(2003).
[8]
INVOLVEMENT IN MVA2.
PubMed=21552266; DOI=10.1038/ng.822;
Snape K., Hanks S., Ruark E., Barros-Nunez P., Elliott A., Murray A.,
Lane A.H., Shannon N., Callier P., Chitayat D., Clayton-Smith J.,
Fitzpatrick D.R., Gisselsson D., Jacquemont S., Asakura-Hay K.,
Micale M.A., Tolmie J., Turnpenny P.D., Wright M., Douglas J.,
Rahman N.;
"Mutations in CEP57 cause mosaic variegated aneuploidy syndrome.";
Nat. Genet. 43:527-529(2011).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[10]
FUNCTION.
PubMed=22321063; DOI=10.1111/j.1600-0854.2012.01341.x;
Zhen Y., Sorensen V., Skjerpen C.S., Haugsten E.M., Jin Y.,
Walchli S., Olsnes S., Wiedlocha A.;
"Nuclear import of exogenous FGF1 requires the ER-protein LRRC59 and
the importins Kpnalpha1 and Kpnbeta1.";
Traffic 13:650-664(2012).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53 AND SER-55, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- 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, but that of FGF1. {ECO:0000269|PubMed:22321063}.
-!- SUBUNIT: Homodimer and homooligomer. Interacts with microtubules.
Interacts with FGF2 and RAP80. Does not interact with FGF1 or FGF2
isoform 24 kDa. {ECO:0000269|PubMed:12717444}.
-!- INTERACTION:
Q96MT8:CEP63; NbExp=3; IntAct=EBI-308614, EBI-741977;
Q96MT8-3:CEP63; NbExp=3; IntAct=EBI-11752486, EBI-11522539;
O15320:CTAGE5; NbExp=3; IntAct=EBI-308614, EBI-1050253;
Q96CN9:GCC1; NbExp=4; IntAct=EBI-308614, EBI-746252;
O75031:HSF2BP; NbExp=4; IntAct=EBI-11752486, EBI-7116203;
A1A4E9:KRT13; NbExp=3; IntAct=EBI-308614, EBI-10171552;
P19012:KRT15; NbExp=3; IntAct=EBI-308614, EBI-739566;
Q15323:KRT31; NbExp=3; IntAct=EBI-308614, EBI-948001;
Q6A162:KRT40; NbExp=3; IntAct=EBI-308614, EBI-10171697;
P43356:MAGEA2B; NbExp=4; IntAct=EBI-11752486, EBI-5650739;
Q96E03:MAGEA2B; NbExp=3; IntAct=EBI-308614, EBI-10239285;
P01106:MYC; NbExp=3; IntAct=EBI-308614, EBI-447544;
Q15311:RALBP1; NbExp=4; IntAct=EBI-308614, EBI-749285;
Q9UBB9:TFIP11; NbExp=3; IntAct=EBI-308614, EBI-1105213;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q86XR8-1; Sequence=Displayed;
Name=2;
IsoId=Q86XR8-2; Sequence=VSP_012262;
Name=3;
IsoId=Q86XR8-3; Sequence=VSP_012263, VSP_012264;
Name=4;
IsoId=Q86XR8-4; Sequence=VSP_037839, VSP_037840;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q86XR8-5; Sequence=VSP_037839;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12717444}.
-!- DOMAIN: The C-terminal region mediates the interaction with
microtubules and is able to nucleate and bundles microtubules in
vitro. {ECO:0000250}.
-!- DOMAIN: The centrosome localization domain (CLD) region mediates
the localization to centrosomes and homooligomerization.
{ECO:0000250}.
-!- DISEASE: Mosaic variegated aneuploidy syndrome 2 (MVA2)
[MIM:614114]: A severe developmental disorder characterized by
mosaic aneuploidies, predominantly trisomies and monosomies,
involving multiple different chromosomes and tissues. Affected
individuals typically present with severe intrauterine growth
retardation and microcephaly. Eye anomalies, mild dysmorphism,
variable developmental delay, and a broad spectrum of additional
congenital abnormalities and medical conditions may also occur.
The risk of malignancy is high, with rhabdomyosarcoma, Wilms tumor
and leukemia reported in several cases.
{ECO:0000269|PubMed:21552266}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the translokin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH29385.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA07654.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CEP57ID43008ch11q21.html";
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EMBL; AY225092; AAO73938.1; -; mRNA.
EMBL; AY239292; AAP72184.1; -; mRNA.
EMBL; D42054; BAA07654.2; ALT_INIT; mRNA.
EMBL; AK291245; BAF83934.1; -; mRNA.
EMBL; AK293277; BAG56806.1; -; mRNA.
EMBL; AP001877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001233; AAH01233.1; -; mRNA.
EMBL; BC029385; AAH29385.1; ALT_SEQ; mRNA.
EMBL; BC039711; AAH39711.1; -; mRNA.
CCDS; CCDS58166.1; -. [Q86XR8-2]
CCDS; CCDS58167.1; -. [Q86XR8-5]
CCDS; CCDS8304.1; -. [Q86XR8-1]
RefSeq; NP_001230705.1; NM_001243776.1. [Q86XR8-5]
RefSeq; NP_001230706.1; NM_001243777.1. [Q86XR8-2]
RefSeq; NP_055494.2; NM_014679.4. [Q86XR8-1]
RefSeq; XP_016874081.1; XM_017018592.1. [Q86XR8-5]
UniGene; Hs.101014; -.
PDB; 4L0R; X-ray; 2.49 A; A/B=334-433.
PDBsum; 4L0R; -.
ProteinModelPortal; Q86XR8; -.
SMR; Q86XR8; -.
BioGrid; 115054; 121.
IntAct; Q86XR8; 27.
MINT; MINT-4989031; -.
STRING; 9606.ENSP00000317902; -.
iPTMnet; Q86XR8; -.
PhosphoSitePlus; Q86XR8; -.
BioMuta; CEP57; -.
DMDM; 56748768; -.
EPD; Q86XR8; -.
MaxQB; Q86XR8; -.
PaxDb; Q86XR8; -.
PeptideAtlas; Q86XR8; -.
PRIDE; Q86XR8; -.
Ensembl; ENST00000325486; ENSP00000317487; ENSG00000166037. [Q86XR8-2]
Ensembl; ENST00000325542; ENSP00000317902; ENSG00000166037. [Q86XR8-1]
Ensembl; ENST00000538658; ENSP00000445706; ENSG00000166037. [Q86XR8-3]
Ensembl; ENST00000541150; ENSP00000443436; ENSG00000166037. [Q86XR8-5]
GeneID; 9702; -.
KEGG; hsa:9702; -.
UCSC; uc001pfo.3; human. [Q86XR8-1]
CTD; 9702; -.
DisGeNET; 9702; -.
EuPathDB; HostDB:ENSG00000166037.10; -.
GeneCards; CEP57; -.
HGNC; HGNC:30794; CEP57.
HPA; HPA018315; -.
MalaCards; CEP57; -.
MIM; 607951; gene.
MIM; 614114; phenotype.
neXtProt; NX_Q86XR8; -.
OpenTargets; ENSG00000166037; -.
Orphanet; 1052; Mosaic variegated aneuploidy syndrome.
PharmGKB; PA142672123; -.
eggNOG; ENOG410IESE; Eukaryota.
eggNOG; ENOG410XPJC; LUCA.
GeneTree; ENSGT00530000063695; -.
HOVERGEN; HBG050917; -.
InParanoid; Q86XR8; -.
KO; K16762; -.
OMA; LCLGDMP; -.
OrthoDB; EOG091G07B7; -.
PhylomeDB; Q86XR8; -.
TreeFam; TF329178; -.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
GeneWiki; CEP57; -.
GenomeRNAi; 9702; -.
PRO; PR:Q86XR8; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000166037; -.
CleanEx; HS_CEP57; -.
ExpressionAtlas; Q86XR8; baseline and differential.
Genevisible; Q86XR8; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:HGNC.
GO; GO:0017134; F:fibroblast growth factor binding; IPI:UniProtKB.
GO; GO:0043015; F:gamma-tubulin binding; IEA:InterPro.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IPI:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
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; IEA:Ensembl.
GO; GO:0000060; P:protein import into nucleus, translocation; ISS:UniProtKB.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0007286; P:spermatid development; ISS: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;
3D-structure; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Microtubule; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 500 Centrosomal protein of 57 kDa.
/FTId=PRO_0000189532.
REGION 58 239 centrosome localization domain (CLD).
{ECO:0000250}.
REGION 277 491 Mediates interaction with microtubules.
{ECO:0000250}.
COILED 63 242 {ECO:0000255}.
COILED 392 492 {ECO:0000255}.
COMPBIAS 260 265 Poly-Lys.
MOD_RES 53 53 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 55 55 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 15 MAAASVSAASGSHLS -> MLTRID (in isoform 4
and isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037839.
VAR_SEQ 270 295 Missing (in isoform 2).
{ECO:0000303|PubMed:7788527}.
/FTId=VSP_012262.
VAR_SEQ 270 270 K -> V (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012263.
VAR_SEQ 271 500 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012264.
VAR_SEQ 498 500 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037840.
VARIANT 448 448 R -> G (in dbSNP:rs644799).
{ECO:0000269|PubMed:12717444,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_059839.
CONFLICT 45 45 F -> S (in Ref. 4; BAF83934).
{ECO:0000305}.
CONFLICT 182 182 V -> A (in Ref. 4; BAG56806).
{ECO:0000305}.
CONFLICT 188 188 K -> E (in Ref. 4; BAF83934).
{ECO:0000305}.
CONFLICT 468 468 L -> Q (in Ref. 3; BAA07654).
{ECO:0000305}.
HELIX 356 386 {ECO:0000244|PDB:4L0R}.
HELIX 391 426 {ECO:0000244|PDB:4L0R}.
SEQUENCE 500 AA; 57089 MW; 88FC47E7B33CE328 CRC64;
MAAASVSAAS GSHLSNSFAE PSRSNGSMVR HSSSPYVVYP SDKPFLNSDL RRSPSKPTLA
YPESNSRAIF SALKNLQDKI RRLELERIQA EESVKTLSRE TIEYKKVLDE QIQERENSKN
EESKHNQELT SQLLAAENKC NLLEKQLEYM RNMIKHAEME RTSVLEKQVS LERERQHDQT
HVQSQLEKLD LLEQEYNKLT TMQALAEKKM QELEAKLHEE EQERKRMQAK AAELQTGLET
NRLIFEDKAT PCVPNARRIK KKKSKPPEKK SSRNYFGAQP HYRLCLGDMP FVAGKSTSPS
HAVVANVQLV LHLMKQHSKA LCNDRVINSI PLAKQVSSRG GKSKKLSVTP PSSNGINEEL
SEVLQTLQDE FGQMSFDHQQ LAKLIQESPT VELKDKLECE LEALVGRMEA KANQITKVRK
YQAQLEKQKL EKQKKELKAT KKTLDEERNS SSRSGITGTT NKKDFMKLRP GEKRRKNLQL
LKDMQSIQNS LQSSSLCWDY


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EIAAB44357 CASK-interacting nucleosome assembly protein,Cinap,Dentt,Differentially-expressed nucleolar TGF-beta1 target protein,DXBwg1396e,Mouse,Mus musculus,Testis-specific Y-encoded-like protein 2,Tspx,Tspyl2,


 

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