CEP57_HUMAN
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 03-AUG-2022, entry version 159.
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=3; 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="http://atlasgeneticsoncology.org/Genes/CEP57ID43008ch11q21.html";
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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; 54.
DR MINT; Q86XR8; -.
DR STRING; 9606.ENSP00000317902; -.
DR GlyGen; Q86XR8; 1 site, 2 O-linked glycans (1 site).
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; Q86XR8; -.
DR PeptideAtlas; Q86XR8; -.
DR PRIDE; 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 Antibodypedia; 17918; 238 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 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; QHTKALC; -.
DR OrthoDB; 1255254at2759; -.
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; 83 hits in 1087 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 203 other tissues.
DR ExpressionAtlas; Q86XR8; baseline and differential.
DR Genevisible; Q86XR8; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0034453; P:microtubule anchoring; IEA:InterPro.
DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR GO; GO:0007286; P:spermatid development; ISS: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 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
