ID   CEP57_HUMAN             Reviewed;         500 AA.
AC   Q86XR8; A0PJH1; A8K5D0; B4DDP5; F5H5F7; Q14704; Q5JB46; Q8IXP0; Q9BVF9;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 2.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Centrosomal protein of 57 kDa;
DE            Short=Cep57;
DE   AltName: Full=FGF2-interacting protein;
DE   AltName: Full=Testis-specific protein 57;
DE   AltName: Full=Translokin;
GN   Name=CEP57; Synonyms=KIAA0092, TSP57;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, SUBUNIT, INTERACTION WITH FGF2, AND VARIANT GLY-448.
RC   TISSUE=Placenta;
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).
RA   Kim J.W.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Bone marrow;
RX   PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA   Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA   Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. III. The
RT   coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 2:37-43(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP   GLY-448.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Kidney, Mammary gland, and Placenta;
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   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [8]
RP   INVOLVEMENT IN MVA2.
RX   PubMed=21552266; DOI=10.1038/ng.822;
RA   Snape K., Hanks S., Ruark E., Barros-Nunez P., Elliott A., Murray A.,
RA   Lane A.H., Shannon N., Callier P., Chitayat D., Clayton-Smith J.,
RA   Fitzpatrick D.R., Gisselsson D., Jacquemont S., Asakura-Hay K.,
RA   Micale M.A., Tolmie J., Turnpenny P.D., Wright M., Douglas J., Rahman N.;
RT   "Mutations in CEP57 cause mosaic variegated aneuploidy syndrome.";
RL   Nat. Genet. 43:527-529(2011).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [10]
RP   FUNCTION.
RX   PubMed=22321063; DOI=10.1111/j.1600-0854.2012.01341.x;
RA   Zhen Y., Sorensen V., Skjerpen C.S., Haugsten E.M., Jin Y., Walchli S.,
RA   Olsnes S., Wiedlocha A.;
RT   "Nuclear import of exogenous FGF1 requires the ER-protein LRRC59 and the
RT   importins Kpnalpha1 and Kpnbeta1.";
RL   Traffic 13:650-664(2012).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53 AND SER-55, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
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, but that of FGF1.
CC       {ECO:0000269|PubMed:22321063}.
CC   -!- SUBUNIT: Homodimer and homooligomer. Interacts with microtubules.
CC       Interacts with FGF2 and RAP80. Does not interact with FGF1 or FGF2
CC       isoform 24 kDa. {ECO:0000269|PubMed:12717444}.
CC   -!- INTERACTION:
CC       Q86XR8; Q96MT8: CEP63; NbExp=4; IntAct=EBI-308614, EBI-741977;
CC       Q86XR8; P22607: FGFR3; NbExp=3; IntAct=EBI-308614, EBI-348399;
CC       Q86XR8; Q96CN9: GCC1; NbExp=5; IntAct=EBI-308614, EBI-746252;
CC       Q86XR8; P01112: HRAS; NbExp=3; IntAct=EBI-308614, EBI-350145;
CC       Q86XR8; A1A4E9: KRT13; NbExp=3; IntAct=EBI-308614, EBI-10171552;
CC       Q86XR8; P19012: KRT15; NbExp=3; IntAct=EBI-308614, EBI-739566;
CC       Q86XR8; Q15323: KRT31; NbExp=3; IntAct=EBI-308614, EBI-948001;
CC       Q86XR8; Q6A162: KRT40; NbExp=3; IntAct=EBI-308614, EBI-10171697;
CC       Q86XR8; Q96E03: MAGEA2B; NbExp=3; IntAct=EBI-308614, EBI-10239285;
CC       Q86XR8; Q96PC5: MIA2; NbExp=3; IntAct=EBI-308614, EBI-1050253;
CC       Q86XR8; P01106: MYC; NbExp=3; IntAct=EBI-308614, EBI-447544;
CC       Q86XR8; Q15311: RALBP1; NbExp=4; IntAct=EBI-308614, EBI-749285;
CC       Q86XR8; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-308614, EBI-5235340;
CC       Q86XR8; Q9UBB9: TFIP11; NbExp=4; IntAct=EBI-308614, EBI-1105213;
CC       Q86XR8; Q9Y649; NbExp=3; IntAct=EBI-308614, EBI-25900580;
CC       Q86XR8-3; Q4LEZ3: AARD; NbExp=3; IntAct=EBI-11752486, EBI-5463075;
CC       Q86XR8-3; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-11752486, EBI-11096309;
CC       Q86XR8-3; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-11752486, EBI-1166928;
CC       Q86XR8-3; Q96M89-2: CCDC138; NbExp=3; IntAct=EBI-11752486, EBI-10972887;
CC       Q86XR8-3; Q8N715: CCDC185; NbExp=3; IntAct=EBI-11752486, EBI-740814;
CC       Q86XR8-3; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-11752486, EBI-10175300;
CC       Q86XR8-3; Q96MT8-3: CEP63; NbExp=4; IntAct=EBI-11752486, EBI-11522539;
CC       Q86XR8-3; Q05D60: DEUP1; NbExp=3; IntAct=EBI-11752486, EBI-748597;
CC       Q86XR8-3; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-11752486, EBI-11988027;
CC       Q86XR8-3; Q9UKT7: FBXL3; NbExp=3; IntAct=EBI-11752486, EBI-2557269;
CC       Q86XR8-3; Q96CN9: GCC1; NbExp=3; IntAct=EBI-11752486, EBI-746252;
CC       Q86XR8-3; O75031: HSF2BP; NbExp=6; IntAct=EBI-11752486, EBI-7116203;
CC       Q86XR8-3; O60341: KDM1A; NbExp=3; IntAct=EBI-11752486, EBI-710124;
CC       Q86XR8-3; Q9NSK0: KLC4; NbExp=3; IntAct=EBI-11752486, EBI-949319;
CC       Q86XR8-3; P19013: KRT4; NbExp=3; IntAct=EBI-11752486, EBI-2371606;
CC       Q86XR8-3; O95678: KRT75; NbExp=3; IntAct=EBI-11752486, EBI-2949715;
CC       Q86XR8-3; P05787: KRT8; NbExp=3; IntAct=EBI-11752486, EBI-297852;
CC       Q86XR8-3; P78385: KRT83; NbExp=3; IntAct=EBI-11752486, EBI-10221390;
CC       Q86XR8-3; O43790: KRT86; NbExp=3; IntAct=EBI-11752486, EBI-9996498;
CC       Q86XR8-3; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-11752486, EBI-11742507;
CC       Q86XR8-3; P43356: MAGEA2B; NbExp=3; IntAct=EBI-11752486, EBI-5650739;
CC       Q86XR8-3; O43482: OIP5; NbExp=3; IntAct=EBI-11752486, EBI-536879;
CC       Q86XR8-3; Q16512: PKN1; NbExp=3; IntAct=EBI-11752486, EBI-602382;
CC       Q86XR8-3; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-11752486, EBI-1105153;
CC       Q86XR8-3; Q15276: RABEP1; NbExp=3; IntAct=EBI-11752486, EBI-447043;
CC       Q86XR8-3; A6NK89: RASSF10; NbExp=3; IntAct=EBI-11752486, EBI-6912267;
CC       Q86XR8-3; Q7L8J4: SH3BP5L; NbExp=3; IntAct=EBI-11752486, EBI-747389;
CC       Q86XR8-3; O95238: SPDEF; NbExp=3; IntAct=EBI-11752486, EBI-12811275;
CC       Q86XR8-3; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-11752486, EBI-12090309;
CC       Q86XR8-3; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-11752486, EBI-1105213;
CC       Q86XR8-3; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-11752486, EBI-744794;
CC       Q86XR8-3; Q9UJ04: TSPYL4; NbExp=3; IntAct=EBI-11752486, EBI-308511;
CC       Q86XR8-3; P40222: TXLNA; NbExp=3; IntAct=EBI-11752486, EBI-359793;
CC       Q86XR8-3; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-11752486, EBI-6116822;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:14654843}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q86XR8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86XR8-2; Sequence=VSP_012262;
CC       Name=3;
CC         IsoId=Q86XR8-3; Sequence=VSP_012263, VSP_012264;
CC       Name=4;
CC         IsoId=Q86XR8-4; Sequence=VSP_037839, VSP_037840;
CC       Name=5;
CC         IsoId=Q86XR8-5; Sequence=VSP_037839;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12717444}.
CC   -!- DOMAIN: The C-terminal region mediates the interaction with
CC       microtubules and is able to nucleate and bundles microtubules in vitro.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The centrosome localization domain (CLD) region mediates the
CC       localization to centrosomes and homooligomerization. {ECO:0000250}.
CC   -!- DISEASE: Mosaic variegated aneuploidy syndrome 2 (MVA2) [MIM:614114]: A
CC       severe developmental disorder characterized by mosaic aneuploidies,
CC       predominantly trisomies and monosomies, involving multiple different
CC       chromosomes and tissues. Affected individuals typically present with
CC       severe intrauterine growth retardation and microcephaly. Eye anomalies,
CC       mild dysmorphism, variable developmental delay, and a broad spectrum of
CC       additional congenital abnormalities and medical conditions may also
CC       occur. The risk of malignancy is high, with rhabdomyosarcoma, Wilms
CC       tumor and leukemia reported in several cases.
CC       {ECO:0000269|PubMed:21552266}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the translokin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH29385.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=BAA07654.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/43008/CEP57";
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DR   EMBL; AY225092; AAO73938.1; -; mRNA.
DR   EMBL; AY239292; AAP72184.1; -; mRNA.
DR   EMBL; D42054; BAA07654.2; ALT_INIT; mRNA.
DR   EMBL; AK291245; BAF83934.1; -; mRNA.
DR   EMBL; AK293277; BAG56806.1; -; mRNA.
DR   EMBL; AP001877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC001233; AAH01233.1; -; mRNA.
DR   EMBL; BC029385; AAH29385.1; ALT_SEQ; mRNA.
DR   EMBL; BC039711; AAH39711.1; -; mRNA.
DR   CCDS; CCDS58166.1; -. [Q86XR8-2]
DR   CCDS; CCDS58167.1; -. [Q86XR8-5]
DR   CCDS; CCDS8304.1; -. [Q86XR8-1]
DR   RefSeq; NP_001230705.1; NM_001243776.1. [Q86XR8-5]
DR   RefSeq; NP_001230706.1; NM_001243777.1. [Q86XR8-2]
DR   RefSeq; NP_055494.2; NM_014679.4. [Q86XR8-1]
DR   RefSeq; XP_016874081.1; XM_017018592.1. [Q86XR8-5]
DR   PDB; 4L0R; X-ray; 2.49 A; A/B=334-433.
DR   PDBsum; 4L0R; -.
DR   AlphaFoldDB; Q86XR8; -.
DR   SMR; Q86XR8; -.
DR   BioGRID; 115054; 160.
DR   IntAct; Q86XR8; 55.
DR   MINT; Q86XR8; -.
DR   STRING; 9606.ENSP00000317902; -.
DR   GlyCosmos; Q86XR8; 1 site, 2 glycans.
DR   GlyGen; Q86XR8; 2 sites, 2 O-linked glycans (2 sites).
DR   iPTMnet; Q86XR8; -.
DR   PhosphoSitePlus; Q86XR8; -.
DR   BioMuta; CEP57; -.
DR   DMDM; 56748768; -.
DR   EPD; Q86XR8; -.
DR   jPOST; Q86XR8; -.
DR   MassIVE; Q86XR8; -.
DR   MaxQB; Q86XR8; -.
DR   PaxDb; 9606-ENSP00000317902; -.
DR   PeptideAtlas; Q86XR8; -.
DR   ProteomicsDB; 26863; -.
DR   ProteomicsDB; 70324; -. [Q86XR8-1]
DR   ProteomicsDB; 70325; -. [Q86XR8-2]
DR   ProteomicsDB; 70326; -. [Q86XR8-3]
DR   ProteomicsDB; 70327; -. [Q86XR8-4]
DR   Pumba; Q86XR8; -.
DR   Antibodypedia; 17918; 256 antibodies from 27 providers.
DR   DNASU; 9702; -.
DR   Ensembl; ENST00000325486.9; ENSP00000317487.5; ENSG00000166037.11. [Q86XR8-2]
DR   Ensembl; ENST00000325542.10; ENSP00000317902.5; ENSG00000166037.11. [Q86XR8-1]
DR   Ensembl; ENST00000538658.5; ENSP00000445706.1; ENSG00000166037.11. [Q86XR8-3]
DR   Ensembl; ENST00000541150.5; ENSP00000443436.1; ENSG00000166037.11. [Q86XR8-5]
DR   GeneID; 9702; -.
DR   KEGG; hsa:9702; -.
DR   MANE-Select; ENST00000325542.10; ENSP00000317902.5; NM_014679.5; NP_055494.2.
DR   UCSC; uc001pfo.3; human. [Q86XR8-1]
DR   AGR; HGNC:30794; -.
DR   CTD; 9702; -.
DR   DisGeNET; 9702; -.
DR   GeneCards; CEP57; -.
DR   HGNC; HGNC:30794; CEP57.
DR   HPA; ENSG00000166037; Low tissue specificity.
DR   MalaCards; CEP57; -.
DR   MIM; 607951; gene.
DR   MIM; 614114; phenotype.
DR   neXtProt; NX_Q86XR8; -.
DR   OpenTargets; ENSG00000166037; -.
DR   Orphanet; 1052; Mosaic variegated aneuploidy syndrome.
DR   PharmGKB; PA142672123; -.
DR   VEuPathDB; HostDB:ENSG00000166037; -.
DR   eggNOG; ENOG502QTZR; Eukaryota.
DR   GeneTree; ENSGT00530000063695; -.
DR   HOGENOM; CLU_939967_0_0_1; -.
DR   InParanoid; Q86XR8; -.
DR   OMA; DLQRSPW; -.
DR   OrthoDB; 5396442at2759; -.
DR   PhylomeDB; Q86XR8; -.
DR   TreeFam; TF329178; -.
DR   PathwayCommons; Q86XR8; -.
DR   Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR   Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR   Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR   SignaLink; Q86XR8; -.
DR   BioGRID-ORCS; 9702; 94 hits in 1166 CRISPR screens.
DR   ChiTaRS; CEP57; human.
DR   GeneWiki; CEP57; -.
DR   GenomeRNAi; 9702; -.
DR   Pharos; Q86XR8; Tbio.
DR   PRO; PR:Q86XR8; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q86XR8; Protein.
DR   Bgee; ENSG00000166037; Expressed in oocyte and 205 other cell types or tissues.
DR   ExpressionAtlas; Q86XR8; baseline and differential.
DR   GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR   GO; GO:0005813; C:centrosome; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR   GO; GO:0017134; F:fibroblast growth factor binding; IPI:UniProtKB.
DR   GO; GO:0043015; F:gamma-tubulin binding; IEA:InterPro.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IPI:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR   GO; GO:0007286; P:spermatid development; ISS:HGNC-UCL.
DR   Gene3D; 1.20.58.90; -; 1.
DR   InterPro; IPR025913; Cep57_CLD.
DR   InterPro; IPR024957; Cep57_MT-bd_dom.
DR   PANTHER; PTHR19336:SF11; CENTROSOMAL PROTEIN OF 57 KDA; 1.
DR   PANTHER; PTHR19336; UNCHARACTERIZED DUF1167; 1.
DR   Pfam; PF14073; Cep57_CLD; 1.
DR   Pfam; PF06657; Cep57_MT_bd; 1.
DR   Genevisible; Q86XR8; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..500
FT                   /note="Centrosomal protein of 57 kDa"
FT                   /id="PRO_0000189532"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          43..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          58..239
FT                   /note="centrosome localization domain (CLD)"
FT                   /evidence="ECO:0000250"
FT   REGION          277..491
FT                   /note="Mediates interaction with microtubules"
FT                   /evidence="ECO:0000250"
FT   REGION          434..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          63..242
FT                   /evidence="ECO:0000255"
FT   COILED          392..492
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        8..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..449
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         53
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         55
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..15
FT                   /note="MAAASVSAASGSHLS -> MLTRID (in isoform 4 and isoform
FT                   5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_037839"
FT   VAR_SEQ         270..295
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:7788527"
FT                   /id="VSP_012262"
FT   VAR_SEQ         270
FT                   /note="K -> V (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012263"
FT   VAR_SEQ         271..500
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012264"
FT   VAR_SEQ         498..500
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_037840"
FT   VARIANT         448
FT                   /note="R -> G (in dbSNP:rs644799)"
FT                   /evidence="ECO:0000269|PubMed:12717444,
FT                   ECO:0000269|PubMed:14702039"
FT                   /id="VAR_059839"
FT   CONFLICT        45
FT                   /note="F -> S (in Ref. 4; BAF83934)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        182
FT                   /note="V -> A (in Ref. 4; BAG56806)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188
FT                   /note="K -> E (in Ref. 4; BAF83934)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        468
FT                   /note="L -> Q (in Ref. 3; BAA07654)"
FT                   /evidence="ECO:0000305"
FT   HELIX           356..386
FT                   /evidence="ECO:0007829|PDB:4L0R"
FT   HELIX           391..426
FT                   /evidence="ECO:0007829|PDB:4L0R"
SQ   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
//