KIZ_HUMAN
ID KIZ_HUMAN Reviewed; 673 AA.
AC Q2M2Z5; B4DDE9; B4DK54; Q4G0M8; Q4G0S5; Q5BKY3; Q6P0M6; Q71ME0; Q9NZ35;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Centrosomal protein kizuna;
DE AltName: Full=Polo-like kinase 1 substrate 1;
GN Name=KIZ; Synonyms=C20orf19, NCRNA00153, PLK1S1; ORFNames=HT013;
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 [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 202-672 (ISOFORM 4), AND VARIANT THR-236.
RC TISSUE=Neuroblastoma, and Thalamus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Hypothalamus;
RA Guo J.H., Yu L.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS GLN-139 AND
RP THR-236.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANTS
RP GLN-139 AND THR-236.
RC TISSUE=Hippocampus, Pituitary, and Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 280-673 (ISOFORMS 1/2).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-379, MUTAGENESIS OF
RP THR-249 AND THR-379, AND INTERACTION WITH AKAP9; ODF2; PCNT AND TUBGCP2.
RX PubMed=16980960; DOI=10.1038/ncb1474;
RA Oshimori N., Ohsugi M., Yamamoto T.;
RT "The Plk1 target Kizuna stabilizes mitotic centrosomes to ensure spindle
RT bipolarity.";
RL Nat. Cell Biol. 8:1095-1101(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317; SER-321; SER-647;
RP SER-650 AND SER-652, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [9]
RP INTERACTION WITH CEP72.
RX PubMed=19536135; DOI=10.1038/emboj.2009.161;
RA Oshimori N., Li X., Ohsugi M., Yamamoto T.;
RT "Cep72 regulates the localization of key centrosomal proteins and proper
RT bipolar spindle formation.";
RL EMBO J. 28:2066-2076(2009).
RN [10]
RP SUBCELLULAR LOCATION, AND INVOLVEMENT IN RP69.
RX PubMed=24680887; DOI=10.1016/j.ajhg.2014.03.005;
RA El Shamieh S., Neuille M., Terray A., Orhan E., Condroyer C., Demontant V.,
RA Michiels C., Antonio A., Boyard F., Lancelot M.E., Letexier M.,
RA Saraiva J.P., Leveillard T., Mohand-Said S., Goureau O., Sahel J.A.,
RA Zeitz C., Audo I.;
RT "Whole-exome sequencing identifies KIZ as a ciliary gene associated with
RT autosomal-recessive rod-cone dystrophy.";
RL Am. J. Hum. Genet. 94:625-633(2014).
CC -!- FUNCTION: Centrosomal protein required for establishing a robust
CC mitotic centrosome architecture that can endure the forces that
CC converge on the centrosomes during spindle formation. Required for
CC stabilizing the expanded pericentriolar material around the centriole.
CC {ECO:0000269|PubMed:16980960}.
CC -!- SUBUNIT: Interacts with AKAP9, CEP72, ODF2, PCNT and TUBGCP2.
CC {ECO:0000269|PubMed:16980960, ECO:0000269|PubMed:19536135}.
CC -!- INTERACTION:
CC Q2M2Z5; Q9P209: CEP72; NbExp=3; IntAct=EBI-2554344, EBI-739498;
CC Q2M2Z5; P22607: FGFR3; NbExp=3; IntAct=EBI-2554344, EBI-348399;
CC Q2M2Z5; P01112: HRAS; NbExp=3; IntAct=EBI-2554344, EBI-350145;
CC Q2M2Z5; P50222: MEOX2; NbExp=3; IntAct=EBI-2554344, EBI-748397;
CC Q2M2Z5; Q9Y6A5: TACC3; NbExp=6; IntAct=EBI-2554344, EBI-2554984;
CC Q2M2Z5; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-2554344, EBI-1105213;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:16980960}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000269|PubMed:24680887}.
CC Note=Localizes to centrosomes throughout the cell cycle. After
CC centrosome duplication, it usually remains associated only with the
CC mother centrosome, containing the older mature centriole and particles
CC surrounding it. During prophase, additional particles accumulate around
CC both separating centrosomes. Does not accumulate at the microtubule
CC minus ends, but instead localizes to the centrosomes and centrosome-
CC surrounding area in a microtubule-independent and dependent manner,
CC respectively. {ECO:0000269|PubMed:24680887}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q2M2Z5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2M2Z5-2; Sequence=VSP_027879, VSP_027880;
CC Name=3;
CC IsoId=Q2M2Z5-3; Sequence=VSP_027881;
CC Name=4;
CC IsoId=Q2M2Z5-4; Sequence=VSP_027882;
CC Name=5;
CC IsoId=Q2M2Z5-5; Sequence=VSP_037837, VSP_037838;
CC -!- PTM: Phosphorylation at Thr-379 by PLK1 is not needed for centrosomal
CC localization or pericentriolar material expansion but is indispensable
CC for spindle-pole stabilization. {ECO:0000269|PubMed:16980960}.
CC -!- DISEASE: Retinitis pigmentosa 69 (RP69) [MIM:615780]: A retinal
CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. {ECO:0000269|PubMed:24680887}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: Kizuna means 'bonds' in Japanese.
CC -!- SIMILARITY: Belongs to the kizuna family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF67652.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH39296.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAP97689.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAG59066.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK293166; BAG56710.1; -; mRNA.
DR EMBL; AK296399; BAG59066.1; ALT_INIT; mRNA.
DR EMBL; AF451990; AAP97689.1; ALT_FRAME; mRNA.
DR EMBL; AL110120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL117332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10188.1; -; Genomic_DNA.
DR EMBL; BC039296; AAH39296.1; ALT_FRAME; mRNA.
DR EMBL; BC045826; AAH45826.1; -; mRNA.
DR EMBL; BC065550; AAH65550.1; -; mRNA.
DR EMBL; BC090879; AAH90879.2; -; mRNA.
DR EMBL; BC105093; AAI05094.1; -; mRNA.
DR EMBL; BC113370; AAI13371.1; -; mRNA.
DR EMBL; AF220187; AAF67652.1; ALT_FRAME; mRNA.
DR CCDS; CCDS74706.1; -. [Q2M2Z5-1]
DR CCDS; CCDS74707.1; -. [Q2M2Z5-2]
DR CCDS; CCDS74708.1; -. [Q2M2Z5-5]
DR RefSeq; NP_001156494.1; NM_001163022.1. [Q2M2Z5-2]
DR RefSeq; NP_001156495.1; NM_001163023.1. [Q2M2Z5-5]
DR RefSeq; NP_060944.3; NM_018474.4. [Q2M2Z5-1]
DR AlphaFoldDB; Q2M2Z5; -.
DR SMR; Q2M2Z5; -.
DR BioGRID; 120959; 26.
DR IntAct; Q2M2Z5; 14.
DR MINT; Q2M2Z5; -.
DR STRING; 9606.ENSP00000479542; -.
DR iPTMnet; Q2M2Z5; -.
DR PhosphoSitePlus; Q2M2Z5; -.
DR BioMuta; KIZ; -.
DR DMDM; 257051030; -.
DR EPD; Q2M2Z5; -.
DR jPOST; Q2M2Z5; -.
DR MassIVE; Q2M2Z5; -.
DR MaxQB; Q2M2Z5; -.
DR PeptideAtlas; Q2M2Z5; -.
DR PRIDE; Q2M2Z5; -.
DR ProteomicsDB; 61359; -. [Q2M2Z5-1]
DR ProteomicsDB; 61360; -. [Q2M2Z5-2]
DR ProteomicsDB; 61361; -. [Q2M2Z5-3]
DR ProteomicsDB; 61362; -. [Q2M2Z5-4]
DR ProteomicsDB; 61363; -. [Q2M2Z5-5]
DR Antibodypedia; 24776; 136 antibodies from 25 providers.
DR DNASU; 55857; -.
DR Ensembl; ENST00000616848.4; ENSP00000480612.1; ENSG00000088970.16. [Q2M2Z5-5]
DR Ensembl; ENST00000619189.5; ENSP00000479542.1; ENSG00000088970.16. [Q2M2Z5-1]
DR Ensembl; ENST00000620891.4; ENSP00000478019.1; ENSG00000088970.16. [Q2M2Z5-2]
DR GeneID; 55857; -.
DR KEGG; hsa:55857; -.
DR MANE-Select; ENST00000619189.5; ENSP00000479542.1; NM_018474.6; NP_060944.3.
DR UCSC; uc032pdl.2; human. [Q2M2Z5-1]
DR CTD; 55857; -.
DR DisGeNET; 55857; -.
DR GeneCards; KIZ; -.
DR HGNC; HGNC:15865; KIZ.
DR HPA; ENSG00000088970; Low tissue specificity.
DR MalaCards; KIZ; -.
DR MIM; 615757; gene.
DR MIM; 615780; phenotype.
DR neXtProt; NX_Q2M2Z5; -.
DR OpenTargets; ENSG00000088970; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA165392491; -.
DR VEuPathDB; HostDB:ENSG00000088970; -.
DR eggNOG; ENOG502R72X; Eukaryota.
DR GeneTree; ENSGT00390000010121; -.
DR HOGENOM; CLU_026235_0_0_1; -.
DR InParanoid; Q2M2Z5; -.
DR OMA; ICESEKR; -.
DR OrthoDB; 573736at2759; -.
DR PhylomeDB; Q2M2Z5; -.
DR PathwayCommons; Q2M2Z5; -.
DR SignaLink; Q2M2Z5; -.
DR SIGNOR; Q2M2Z5; -.
DR BioGRID-ORCS; 55857; 4 hits in 207 CRISPR screens.
DR ChiTaRS; KIZ; human.
DR GenomeRNAi; 55857; -.
DR Pharos; Q2M2Z5; Tbio.
DR PRO; PR:Q2M2Z5; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q2M2Z5; protein.
DR Bgee; ENSG00000088970; Expressed in sperm and 205 other tissues.
DR ExpressionAtlas; Q2M2Z5; baseline and differential.
DR Genevisible; Q2M2Z5; HS.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
DR InterPro; IPR026742; Centrosomal_kizuma.
DR PANTHER; PTHR16299; PTHR16299; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Retinitis pigmentosa.
FT CHAIN 1..673
FT /note="Centrosomal protein kizuna"
FT /id="PRO_0000301851"
FT REGION 175..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 379
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000269|PubMed:16980960"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..133
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037837"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027879"
FT VAR_SEQ 104..105
FT /note="LK -> MQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027880"
FT VAR_SEQ 134..135
FT /note="EK -> MQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037838"
FT VAR_SEQ 628..673
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027881"
FT VAR_SEQ 642..673
FT /note="ALWDESDDSNSEIEAALRPRNHNTDDSDDFYD -> GERDNRTLDFLFLF
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_027882"
FT VARIANT 139
FT /note="H -> Q (in dbSNP:rs4815025)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_034909"
FT VARIANT 236
FT /note="M -> T (in dbSNP:rs2236178)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_034910"
FT MUTAGEN 249
FT /note="T->A: Does not affect phosphorylation status."
FT /evidence="ECO:0000269|PubMed:16980960"
FT MUTAGEN 379
FT /note="T->A: Abolishes phosphorylation by PLK1."
FT /evidence="ECO:0000269|PubMed:16980960"
FT MUTAGEN 379
FT /note="T->E: Phosphomimetic mutant able to partially
FT restore focused bipolar spindles to PLK1-depleted cells
FT that otherwise possess aberrant spindles with diffuse or
FT multiple gamma-tubulin signals."
FT /evidence="ECO:0000269|PubMed:16980960"
FT CONFLICT 369
FT /note="E -> G (in Ref. 5; AAF67652)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="Q -> R (in Ref. 1; BAG56710)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="S -> L (in Ref. 1; BAG59066)"
FT /evidence="ECO:0000305"
FT CONFLICT 642..672
FT /note="ALWDESDDSNSEIEAALRPRNHNTDDSDDFY -> GERDNRTLDFLFLF
FT (in Ref. 1; BAG59066)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 673 AA; 75111 MW; 3B6BDE3A479B5933 CRC64;
MSRTLASAVP LSSPDYYERL GQLQHGLRDS EKKRLDLEKK LYEYNQSDTC RVKLKYVKLK
NYLKEICESE KKAHTRNQEY LKRFERVQAH VVHFTTNTEK LQKLKLEYET QIKKMLCSKD
SLGLKEELTD EDREKVAVHE GINSGTAMSR GLYQPATIFM GRQMSAILSM RDFSTEHKSP
QPTKNFSIPD PHSHRQTAQS SNVTDSCVVQ TSNDTQCLNK SDNIDGKASL QIGEKMPVTA
SVLSEEEQTH CLEIGSNTRH GKSNLSEGKK SAELNSPLRE RLSPENRTTD LKCDSSSGSE
GEILTREHIE VEEKRASPPV SPIPVSEYCE SENKWSQEKH SPWEGVSDHL AHREPKSQKP
FRKMQEEEEE SWSTSSDLTI SISEDDLILE SPEPQPNPGG KMEGEDGIEA LKLIHAEQER
VALSTEKNCI LQTLSSPDSE KESSTNAPTR EPGQTPDSDV PRAQVGQHVA TLKEHDNSVK
EEATALLRKA LTEECGRRSA IHSSESSCSL PSILNDNSGI KEAKPAVWLN SVPTREQEVS
SGCGDKSKKE NVAADIPITE TEAYQLLKKA TLQDNTNQTE NRFQKTDASV SHLSGLNIGS
GAFETKTANK IASEASFSSS EGSPLSRHEN KKKPVINLKS NALWDESDDS NSEIEAALRP
RNHNTDDSDD FYD
