CE192_HUMAN
ID CE192_HUMAN Reviewed; 2537 AA.
AC Q8TEP8; A0A060A9S4; B7ZMF0; E9PF99; Q8WYT8; Q9H0F4; Q9NW27;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Centrosomal protein of 192 kDa {ECO:0000305};
DE Short=Cep192;
DE Short=Cep192/SPD-2 {ECO:0000303|PubMed:25042804};
GN Name=CEP192 {ECO:0000312|HGNC:HGNC:25515}; Synonyms=KIAA1569;
GN ORFNames=PP8407;
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 3), AND FUNCTION.
RX PubMed=25042804; DOI=10.1016/j.molcel.2014.06.016;
RA Joukov V., Walter J.C., De Nicolo A.;
RT "The Cep192-organized aurora A-Plk1 cascade is essential for centrosome
RT cycle and bipolar spindle assembly.";
RL Mol. Cell 55:578-591(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 757-2537 (ISOFORM 1), AND
RP VARIANTS MET-1365; HIS-1544; PRO-1552; PHE-1701; PRO-2121 AND LEU-2449.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 797-2537 (ISOFORM 1), AND
RP VARIANTS PRO-1552; PHE-1701; ASN-2051; PRO-2121; GLU-2271 AND LEU-2449.
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1453-2537 (ISOFORM 2), AND
RP VARIANTS HIS-1544; PRO-1552 AND PHE-1701.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1958-2537 (ISOFORM 1), AND
RP VARIANTS PRO-2121 AND LEU-2449.
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 [7]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS
RP PRO-1552; PHE-1701; PRO-2121 AND LEU-2449.
RC TISSUE=Brain;
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 [8]
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 [9]
RP INTERACTION WITH SHBG.
RX PubMed=15862967; DOI=10.1016/j.jsbmb.2005.01.007;
RA Pope S.N., Lee I.R.;
RT "Yeast two-hybrid identification of prostatic proteins interacting with
RT human sex hormone-binding globulin.";
RL J. Steroid Biochem. Mol. Biol. 94:203-208(2005).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17980596; DOI=10.1016/j.cub.2007.10.019;
RA Gomez-Ferreria M.A., Rath U., Buster D.W., Chanda S.K., Caldwell J.S.,
RA Rines D.R., Sharp D.J.;
RT "Human Cep192 is required for mitotic centrosome and spindle assembly.";
RL Curr. Biol. 17:1960-1966(2007).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18207742; DOI=10.1016/j.cub.2007.12.055;
RA Zhu F., Lawo S., Bird A., Pinchev D., Ralph A., Richter C.,
RA Mueller-Reichert T., Kittler R., Hyman A.A., Pelletier L.;
RT "The mammalian SPD-2 ortholog Cep192 regulates centrosome biogenesis.";
RL Curr. Biol. 18:136-141(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-812; SER-1755; SER-2098 AND
RP SER-2110, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP HYDROXYLATION AT PRO-2313, UBIQUITINATION, AND MUTAGENESIS OF PRO-2313.
RX PubMed=23932902; DOI=10.1016/j.devcel.2013.06.014;
RA Moser S.C., Bensaddek D., Ortmann B., Maure J.F., Mudie S., Blow J.J.,
RA Lamond A.I., Swedlow J.R., Rocha S.;
RT "PHD1 links cell-cycle progression to oxygen sensing through hydroxylation
RT of the centrosomal protein Cep192.";
RL Dev. Cell 26:381-392(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1755 AND SER-2110, 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).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=32060285; DOI=10.1038/s41467-020-14767-2;
RA Atorino E.S., Hata S., Funaya C., Neuner A., Schiebel E.;
RT "CEP44 ensures the formation of bona fide centriole wall, a requirement for
RT the centriole-to-centrosome conversion.";
RL Nat. Commun. 11:903-903(2020).
RN [19] {ECO:0007744|PDB:6W3J}
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 217-238 IN COMPLEXES WITH PLK4
RP AND TENTC.
RX PubMed=32433990; DOI=10.1016/j.str.2020.04.023;
RA Chen H., Lu D., Shang G., Gao G., Zhang X.;
RT "Structural and Functional Analyses of the FAM46C/Plk4 Complex.";
RL Structure 28:910-921.e4(2020).
CC -!- FUNCTION: Required for mitotic centrosome maturation and bipolar
CC spindle assembly (PubMed:25042804, PubMed:17980596, PubMed:18207742).
CC Appears to be a major regulator of pericentriolar material (PCM)
CC recruitment, centrosome maturation, and centriole duplication
CC (PubMed:25042804, PubMed:17980596, PubMed:18207742). Centrosome-
CC specific activating scaffold for AURKA and PLK1 (PubMed:25042804).
CC {ECO:0000269|PubMed:17980596, ECO:0000269|PubMed:18207742,
CC ECO:0000269|PubMed:25042804}.
CC -!- SUBUNIT: Interacts with SHBG (PubMed:15862967). Interacts with PLK4;
CC this interaction mediates the formation of a ternary complex composed
CC by PLK4, TENT5C and CEP192 (PubMed:32433990).
CC {ECO:0000269|PubMed:15862967, ECO:0000269|PubMed:32433990}.
CC -!- INTERACTION:
CC Q8TEP8; O00444: PLK4; NbExp=2; IntAct=EBI-2339778, EBI-746202;
CC Q8TEP8; P62136: PPP1CA; NbExp=2; IntAct=EBI-2339778, EBI-357253;
CC Q8TEP8-3; O00444: PLK4; NbExp=13; IntAct=EBI-16111881, EBI-746202;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:17980596, ECO:0000269|PubMed:18207742,
CC ECO:0000269|PubMed:32060285}. Note=Pericentriolar location in mitotic
CC centrosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=Q8TEP8-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8TEP8-1; Sequence=VSP_059657;
CC Name=2;
CC IsoId=Q8TEP8-2; Sequence=VSP_059657, VSP_059658, VSP_059659;
CC -!- PTM: Hydroxylation by PHD1/EGLN2 at Pro-2313 promotes ubiquitination.
CC {ECO:0000269|PubMed:23932902}.
CC -!- PTM: Ubiquitinated by a SCF(SKP2) complex following proline
CC hydroxylation. {ECO:0000269|PubMed:23932902}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL55870.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91559.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB66752.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB66752.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; KJ567064; AIA61642.1; -; mRNA.
DR EMBL; AP001357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136818; CAB66752.1; ALT_SEQ; mRNA.
DR EMBL; AK074074; BAB84900.1; -; mRNA.
DR EMBL; AF318363; AAL55870.1; ALT_INIT; mRNA.
DR EMBL; AK001214; BAA91559.1; ALT_INIT; mRNA.
DR EMBL; BC144481; AAI44482.1; -; mRNA.
DR CCDS; CCDS32792.2; -. [Q8TEP8-3]
DR RefSeq; NP_115518.3; NM_032142.3. [Q8TEP8-3]
DR PDB; 4N7Z; X-ray; 2.85 A; B=1134-1191.
DR PDB; 6FVI; X-ray; 1.00 A; A=2256-2402.
DR PDB; 6W3J; X-ray; 4.38 A; C=217-238.
DR PDB; 7PTB; X-ray; 2.08 A; A=1743-2092.
DR PDBsum; 4N7Z; -.
DR PDBsum; 6FVI; -.
DR PDBsum; 6W3J; -.
DR PDBsum; 7PTB; -.
DR AlphaFoldDB; Q8TEP8; -.
DR SMR; Q8TEP8; -.
DR ComplexPortal; CPX-1161; CEP192-PLK4 complex.
DR DIP; DIP-52779N; -.
DR IntAct; Q8TEP8; 56.
DR MINT; Q8TEP8; -.
DR STRING; 9606.ENSP00000427550; -.
DR iPTMnet; Q8TEP8; -.
DR PhosphoSitePlus; Q8TEP8; -.
DR BioMuta; CEP192; -.
DR DMDM; 162416230; -.
DR EPD; Q8TEP8; -.
DR jPOST; Q8TEP8; -.
DR MassIVE; Q8TEP8; -.
DR MaxQB; Q8TEP8; -.
DR PaxDb; Q8TEP8; -.
DR PeptideAtlas; Q8TEP8; -.
DR PRIDE; Q8TEP8; -.
DR ProteomicsDB; 20058; -.
DR ProteomicsDB; 74474; -. [Q8TEP8-1]
DR ProteomicsDB; 74475; -. [Q8TEP8-2]
DR Antibodypedia; 21958; 85 antibodies from 17 providers.
DR DNASU; 55125; -.
DR Ensembl; ENST00000506447.5; ENSP00000427550.1; ENSG00000101639.19. [Q8TEP8-3]
DR GeneID; 55125; -.
DR KEGG; hsa:55125; -.
DR MANE-Select; ENST00000506447.5; ENSP00000427550.1; NM_032142.4; NP_115518.3.
DR UCSC; uc010xac.3; human. [Q8TEP8-3]
DR CTD; 55125; -.
DR DisGeNET; 55125; -.
DR GeneCards; CEP192; -.
DR HGNC; HGNC:25515; CEP192.
DR HPA; ENSG00000101639; Low tissue specificity.
DR MIM; 616426; gene.
DR neXtProt; NX_Q8TEP8; -.
DR OpenTargets; ENSG00000101639; -.
DR PharmGKB; PA142672129; -.
DR VEuPathDB; HostDB:ENSG00000101639; -.
DR eggNOG; ENOG502QQMZ; Eukaryota.
DR GeneTree; ENSGT00510000048187; -.
DR InParanoid; Q8TEP8; -.
DR OMA; KFIRVQI; -.
DR OrthoDB; 19805at2759; -.
DR PhylomeDB; Q8TEP8; -.
DR TreeFam; TF329535; -.
DR PathwayCommons; Q8TEP8; -.
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; Q8TEP8; -.
DR SIGNOR; Q8TEP8; -.
DR BioGRID-ORCS; 55125; 544 hits in 1078 CRISPR screens.
DR ChiTaRS; CEP192; human.
DR GenomeRNAi; 55125; -.
DR Pharos; Q8TEP8; Tbio.
DR PRO; PR:Q8TEP8; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q8TEP8; protein.
DR Bgee; ENSG00000101639; Expressed in ventricular zone and 168 other tissues.
DR ExpressionAtlas; Q8TEP8; baseline and differential.
DR Genevisible; Q8TEP8; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000242; C:pericentriolar material; IBA:GO_Central.
DR GO; GO:0120098; C:procentriole; IDA:ComplexPortal.
DR GO; GO:0120099; C:procentriole replication complex; IPI:ComplexPortal.
DR GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0007099; P:centriole replication; IBA:GO_Central.
DR GO; GO:0090222; P:centrosome-templated microtubule nucleation; IMP:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR039103; Spd-2/CEP192.
DR PANTHER; PTHR16029; PTHR16029; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton; Hydroxylation;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..2537
FT /note="Centrosomal protein of 192 kDa"
FT /id="PRO_0000312495"
FT REGION 69..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 812
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2098
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2313
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:23932902"
FT VAR_SEQ 1..603
FT /note="MEDFRGIAEESFPSFLTNSLFGNSGILENVTLSSNLGLPVAVSTLARDRSST
FT DNRYPDIQASYLVEGRFSVPSGSSPGSQSDAEPRERLQLSFQDDDSISRKKSYVESQRL
FT SNALSKQSALQMETAGPEEEPAGATESLQGQDLFNRASPLEQAQDSPIDFHLQSWMNNK
FT EPKIVVLDAGKHFEDKTLKSDLSHTSLLENEKLILPTSLEDSSDDDIDDEMFYDDHLEA
FT YFEQLAIPGMIYEDLEGPEPPEKGFKLPTNGLRQANENGSLNCKFQSENNSSLISLDSH
FT SSETTHKESEESQVICLPGTSNSIGTGDSRRYTDGMLPFSSGTWGTEKEIENLKGIVPD
FT LNSECASKDVLVKTLRAIDVKLNSDNFHDANANRGGFDLTDPVKQGAECPHQNKTVLHM
FT DGCLDTETPTVSIQENVDVASLKPISDSGINFTDAIWSPTCERRTCECHESIEKNKDKT
FT DLPQSVVYQNEEGRWVTDLAYYTSFNSKQNLNVSLSDEMNEDFRSGSEAFDLIAQDEEE
FT FNKEHQFIQEENIDAHNTSVALGDTSWGATINYSLLRKSRSTSDLDKDDASYLRLSLGE
FT FFAQRSEALGCLGGGNNVKR -> MKTSDLV (in isoform 1 and isoform
FT 2)"
FT /id="VSP_059657"
FT VAR_SEQ 1999..2003
FT /note="ALLHK -> QGPAT (in isoform 2)"
FT /id="VSP_059658"
FT VAR_SEQ 2004..2537
FT /note="Missing (in isoform 2)"
FT /id="VSP_059659"
FT VARIANT 1053
FT /note="T -> A (in dbSNP:rs10048340)"
FT /id="VAR_037514"
FT VARIANT 1109
FT /note="Q -> P (in dbSNP:rs11080623)"
FT /id="VAR_050782"
FT VARIANT 1365
FT /note="V -> M (in dbSNP:rs2282542)"
FT /evidence="ECO:0000269|PubMed:11230166"
FT /id="VAR_037515"
FT VARIANT 1544
FT /note="R -> H (in dbSNP:rs7228940)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:15498874"
FT /id="VAR_050783"
FT VARIANT 1552
FT /note="S -> P (in dbSNP:rs578208)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:12693554, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15498874"
FT /id="VAR_050784"
FT VARIANT 1701
FT /note="L -> F (in dbSNP:rs6505780)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:12693554, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15498874"
FT /id="VAR_050785"
FT VARIANT 2051
FT /note="S -> N (in dbSNP:rs2027698)"
FT /evidence="ECO:0000269|PubMed:12693554"
FT /id="VAR_050786"
FT VARIANT 2121
FT /note="L -> P (in dbSNP:rs474337)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:12693554, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_050787"
FT VARIANT 2271
FT /note="K -> E (in dbSNP:rs3737379)"
FT /evidence="ECO:0000269|PubMed:12693554"
FT /id="VAR_050788"
FT VARIANT 2449
FT /note="R -> L (in dbSNP:rs1786263)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:12693554, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_050789"
FT MUTAGEN 2313
FT /note="P->A: Increased presence on interphasic centrosomes,
FT and decreased presence on mitotic centrosomes; no
FT ubiquitination and unchanged levels in response to
FT hypoxia."
FT /evidence="ECO:0000269|PubMed:23932902"
FT CONFLICT 357
FT /note="V -> I (in Ref. 1; AIA61642)"
FT /evidence="ECO:0000305"
FT CONFLICT 1402
FT /note="R -> L (in Ref. 4; BAB84900)"
FT /evidence="ECO:0000305"
FT CONFLICT 1453
FT /note="P -> A (in Ref. 5; AAL55870)"
FT /evidence="ECO:0000305"
FT CONFLICT 2115
FT /note="R -> Q (in Ref. 3 and 7; AAI44482)"
FT /evidence="ECO:0000305"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:4N7Z"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:4N7Z"
FT HELIX 2268..2270
FT /evidence="ECO:0007829|PDB:6FVI"
FT STRAND 2272..2276
FT /evidence="ECO:0007829|PDB:6FVI"
FT STRAND 2278..2280
FT /evidence="ECO:0007829|PDB:6FVI"
FT STRAND 2290..2298
FT /evidence="ECO:0007829|PDB:6FVI"
FT STRAND 2300..2302
FT /evidence="ECO:0007829|PDB:6FVI"
FT STRAND 2304..2313
FT /evidence="ECO:0007829|PDB:6FVI"
FT STRAND 2315..2317
FT /evidence="ECO:0007829|PDB:6FVI"
FT STRAND 2319..2322
FT /evidence="ECO:0007829|PDB:6FVI"
FT STRAND 2332..2336
FT /evidence="ECO:0007829|PDB:6FVI"
FT STRAND 2339..2342
FT /evidence="ECO:0007829|PDB:6FVI"
FT STRAND 2347..2354
FT /evidence="ECO:0007829|PDB:6FVI"
FT STRAND 2357..2372
FT /evidence="ECO:0007829|PDB:6FVI"
FT STRAND 2380..2390
FT /evidence="ECO:0007829|PDB:6FVI"
SQ SEQUENCE 2537 AA; 279111 MW; CA0A92F264280C3B CRC64;
MEDFRGIAEE SFPSFLTNSL FGNSGILENV TLSSNLGLPV AVSTLARDRS STDNRYPDIQ
ASYLVEGRFS VPSGSSPGSQ SDAEPRERLQ LSFQDDDSIS RKKSYVESQR LSNALSKQSA
LQMETAGPEE EPAGATESLQ GQDLFNRASP LEQAQDSPID FHLQSWMNNK EPKIVVLDAG
KHFEDKTLKS DLSHTSLLEN EKLILPTSLE DSSDDDIDDE MFYDDHLEAY FEQLAIPGMI
YEDLEGPEPP EKGFKLPTNG LRQANENGSL NCKFQSENNS SLISLDSHSS ETTHKESEES
QVICLPGTSN SIGTGDSRRY TDGMLPFSSG TWGTEKEIEN LKGIVPDLNS ECASKDVLVK
TLRAIDVKLN SDNFHDANAN RGGFDLTDPV KQGAECPHQN KTVLHMDGCL DTETPTVSIQ
ENVDVASLKP ISDSGINFTD AIWSPTCERR TCECHESIEK NKDKTDLPQS VVYQNEEGRW
VTDLAYYTSF NSKQNLNVSL SDEMNEDFRS GSEAFDLIAQ DEEEFNKEHQ FIQEENIDAH
NTSVALGDTS WGATINYSLL RKSRSTSDLD KDDASYLRLS LGEFFAQRSE ALGCLGGGNN
VKRPSFGYFI RSPEKREPIA LIRKSDVSRG NLEKEMAHLN HDLYSGDLNE QSQAQLSEGS
ITLQVEAVES TSQVDENDVT LTADKGKTED TFFMSNKPQR YKDKLPDSGD SMLRISTIAS
AIAEASVNTD PSQLAAMIKA LSNKTRDKTF QEDEKQKDYS HVRHFLPNDL EKSNGSNALD
MEKYLKKTEV SRYESALENF SRASMSDTWD LSLPKEQTTQ DIHPVDLSAT SVSVRAPEEN
TAAIVYVENG ESENQESFRT INSSNSVTNR ENNSAVVDVK TCSIDNKLQD VGNDEKATSI
STPSDSYSSV RNPRITSLCL LKDCEEIRDN RENQRQNECV SEISNSEKHV TFENHRIVSP
KNSDLKNTSP EHGGRGSEDE QESFRPSTSP LSHSSPSEIS GTSSSGCALE SFGSAAQQQQ
PPCEQELSPL VCSPAGVSRL TYVSEPESSY PTTATDDALE DRKSDITSEL STTIIQGSPA
ALEERAMEKL REKVPFQNRG KGTLSSIIQN NSDTRKATET TSLSSKPEYV KPDFRWSKDP
SSKSGNLLET SEVGWTSNPE ELDPIRLALL GKSGLSCQVG SATSHPVSCQ EPIDEDQRIS
PKDKSTAGRE FSGQVSHQTT SENQCTPIPS STVHSSVADM QNMPAAVHAL LTQPSLSAAP
FAQRYLGTLP STGSTTLPQC HAGNATVCGF SGGLPYPAVA GEPVQNSVAV GICLGSNIGS
GWMGTSSLCN PYSNTLNQNL LSTTKPFPVP SVGTNCGIEP WDSGVTSGLG SVRVPEELKL
PHACCVGIAS QTLLSVLNPT DRWLQVSIGV LSISVNGEKV DLSTYRCLVF KNKAIIRPHA
TEEIKVLFIP SSPGVFRCTF SVASWPCSTD AETIVQAEAL ASTVTLTAIA ESPVIEVETE
KKDVLDFGDL TYGGWKALPL KLINRTHATV PIRLIINANA VAWRCFTFSK ESVRAPVEVA
PCADVVTRLA GPSVVNHMMP ASYDGQDPEF LMIWVLFHSP KKQISSSDIL DSAEEFSAKV
DIEVDSPNPT PVLRSVSLRA RAGIARIHAP RDLQTMHFLA KVASSRKQHL PLKNAGNIEV
YLDIKVPEQG SHFSVDPKNL LLKPGEEHEV IVSFTPKDPE ACEERILKIF VQPFGPQYEV
VLKGEVISSG SKPLSPGPCL DIPSILSNKQ FLAWGGVPLG RTQLQKLALR NNSASTTQHL
RLLIRGQDQD CFQLQNTFGS EQRLTSNCEI RIHPKEDIFI SVLFAPTRLS CMLARLEIKQ
LGNRSQPGIK FTIPLSGYGG TSNLILEGVK KLSDSYMVTV NGLVPGKESK IVFSVRNTGS
RAAFVKAVGF KDSQKKVLLD PKVLRIFPDK FVLKERTQEN VTLIYNPSDR GINNKTATEL
STVYLFGGDE ISRQQYRRAL LHKPEMIKQI LPEHSVLQNI NFVEAFQDEL LVTEVYDLPQ
RPNDVQLFYG SMCKIILSVI GEFRDCISSR EFLQPSSKAS LESTSDLGAS GKHGGNVSLD
VLPVKGPQGS PLLSRAARPP LDQLASEEPW TVLPEHLILV APSPCDMAKT GRFQIVNNSV
RLLRFELCWP AHCLTVTPQH GCVAPESKLQ ILVSPNSSLS TKQSMFPWSG LIYIHCDDGQ
KKIVKVQIRE DLTQVELLTR LTSKPFGILS PVSEPSVSHL VKPMTKPPST KVEIRNKSIT
FPTTEPGETS ESCLELENHG TTDVKWHLSS LAPPYVKGVD ESGDVFRATY AAFRCSPISG
LLESHGIQKV SITFLPRGRG DYAQFWDVEC HPLKEPHMKH TLRFQLSGQS IEAENEPENA
CLSTDSLIKI DHLVKPRRQA VSEASARIPE QLDVTARGVY APEDVYRFRP TSVGESRTLK
VNLRNNSFIT HSLKFLSPRE PFYVKHSKYS LRAQHYINMP VQFKPKSAGK FEALLVIQTD
EGKSIAIRLI GEALGKN
