ID KIZ_MOUSE Reviewed; 695 AA. AC Q3UXL4; A2AUS7; B2RX19; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 02-SEP-2026, entry version 126. DE RecName: Full=Centrosomal protein kizuna; DE AltName: Full=Polo-like kinase 1 substrate 1; GN Name=Kiz; Synonyms=Gm114, Plk1s1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Muellerian duct; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP PROTEIN SEQUENCE OF 73-82; 76-87 AND 132-158, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667 AND SER-670, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). 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:0000250|UniProtKB:Q2M2Z5}. CC -!- SUBUNIT: Interacts with AKAP9, CEP72, ODF2, PCNT and TUBGCP2. CC {ECO:0000250|UniProtKB:Q2M2Z5}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000250|UniProtKB:Q2M2Z5}. Cytoplasm, CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q2M2Z5}. 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 CC centrosome- surrounding area in a microtubule-independent and dependent CC manner, respectively. {ECO:0000250|UniProtKB:Q2M2Z5}. CC -!- PTM: Phosphorylation at Thr-391 by PLK1 is not needed for centrosomal CC localization or pericentriolar material expansion but is indispensable CC for spindle-pole stabilization. {ECO:0000250|UniProtKB:Q2M2Z5}. CC -!- SIMILARITY: Belongs to the kizuna family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAM27275.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK135486; BAE22549.1; -; mRNA. DR EMBL; AL929215; CAM27275.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL929215; CAM27276.1; -; Genomic_DNA. DR EMBL; BC150844; AAI50845.1; -; mRNA. DR EMBL; BC150845; AAI50846.1; -; mRNA. DR CCDS; CCDS16832.1; -. DR RefSeq; NP_001028470.1; NM_001033298.4. DR AlphaFoldDB; Q3UXL4; -. DR SMR; Q3UXL4; -. DR FunCoup; Q3UXL4; 787. DR IntAct; Q3UXL4; 1. DR STRING; 10090.ENSMUSP00000096884; -. DR iPTMnet; Q3UXL4; -. DR PhosphoSitePlus; Q3UXL4; -. DR jPOST; Q3UXL4; -. DR PaxDb; 10090-ENSMUSP00000096884; -. DR PeptideAtlas; Q3UXL4; -. DR ProteomicsDB; 263446; -. DR Pumba; Q3UXL4; -. DR Antibodypedia; 24776; 130 antibodies from 26 providers. DR Ensembl; ENSMUST00000099278.9; ENSMUSP00000096884.3; ENSMUSG00000074749.11. DR GeneID; 228730; -. DR KEGG; mmu:228730; -. DR UCSC; uc008mso.1; mouse. DR AGR; MGI:2684960; -. DR CTD; 55857; -. DR MGI; MGI:2684960; Kiz. DR VEuPathDB; HostDB:ENSMUSG00000074749; -. DR eggNOG; ENOG502R72X; Eukaryota. DR GeneTree; ENSGT00390000010121; -. DR HOGENOM; CLU_026235_0_0_1; -. DR InParanoid; Q3UXL4; -. DR OMA; EKEQTHC; -. DR OrthoDB; 8015657at2759; -. DR PhylomeDB; Q3UXL4; -. DR BioGRID-ORCS; 228730; 3 hits in 78 CRISPR screens. DR PRO; PR:Q3UXL4; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; Q3UXL4; protein. DR Bgee; ENSMUSG00000074749; Expressed in interventricular septum and 239 other cell types or tissues. DR ExpressionAtlas; Q3UXL4; baseline and differential. DR GO; GO:0005813; C:centrosome; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0019901; F:protein kinase binding; ISO:GO_Central. DR GO; GO:0007051; P:spindle organization; ISS:UniProtKB. DR InterPro; IPR026742; Centrosomal_kizuma. DR InterPro; IPR060349; Kizuna_N. DR PANTHER; PTHR16299; CENTROSOMAL PROTEIN KIZUNA; 1. DR PANTHER; PTHR16299:SF2; CENTROSOMAL PROTEIN KIZUNA; 1. DR Pfam; PF28416; Kizuna_N; 1. PE 1: Evidence at protein level; KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Phosphoprotein; Reference proteome. FT CHAIN 1..695 FT /note="Centrosomal protein kizuna" FT /id="PRO_0000301852" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 261..313 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 351..391 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 444..465 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 633..695 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 29..57 FT /evidence="ECO:0000255" FT COILED 102..132 FT /evidence="ECO:0000255" FT COMPBIAS 1..12 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 15..24 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 263..274 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 282..297 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 299..313 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 360..377 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 382..391 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 448..465 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 633..645 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 676..686 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 391 FT /note="Phosphothreonine; by PLK1" FT /evidence="ECO:0000250|UniProtKB:Q2M2Z5" FT MOD_RES 667 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 670 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 672 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q2M2Z5" SQ SEQUENCE 695 AA; 76542 MW; 71DDC7CB94FD6EBF CRC64; MPRGRGGGGG GLRQASATSA PLASPSYYER VGQLQQALRD SEKKRLDLED KLYEYNKSDK CRAKLKCAKL KKYLKEVCES ERRAQVRNQG YLKKFECVQT YVEHLTTNTE KLQKLKTEYE AEVKRMRLLS KDSLGMSDED GAKDAVQAGI NSGTAMSRGL YQPATIFMGR QMSAISSIED FSTELKSNQP TKNFSISDPH SHQQTAQSSC VTDSCVVQTN GDTQCLNKSD KIHGKTSLQT GEKAPVTSYV LSAEEQTHCL EIGSSTQHSK SNLSEGRKSA ELHSSLQERL SPENSITDLK CDSSSRSEGS DREILTQEHI EVREERAGPL VPMMAASEHC TSAKKWAGEK HSAWEASSDD LDHGDSKSQK AVLKHEEEQE EGSSCSSSDL TVSVSEDDLI LESLAALSNP GAKMAGKDGM QALRAAHTEP RQDSLFTEYV LQTQSFPDSK REPSPDSPRQ PEKVPDCHLL KTRGQCMKEH DNSLKEEATT LLKKVLTEEC DHRSAIHSNE SSCSMPSILN DNNGIKEAKP ALRLNSVLTR EQEVSSGCGD ESKEESIAAA PGTGHREADL VPSELFQFSL GAAMKETKAY QLLKKSTLQD NSNQAEERFE SQFSGLDIGG SMFTTKTAHK IASEASFSSS EGSPLSRHES KRDPVTTIKS NAFWGESDDS NSEIEAALRP RDHDMPDDFD DFYDT //