ID MPLKI_MOUSE Reviewed; 178 AA. AC Q9D011; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 24-JAN-2024, entry version 129. DE RecName: Full=M-phase-specific PLK1-interacting protein; DE AltName: Full=TTD non-photosensitive 1 protein homolog; GN Name=Mplkip; Synonyms=Ttdn1; 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=Embryo, and Pituitary; 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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-36; ARG-58; ARG-67 AND ARG-76, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). CC -!- FUNCTION: May play a role in maintenance of cell cycle integrity by CC regulating mitosis or cytokinesis. {ECO:0000250}. CC -!- SUBUNIT: Interacts with PLK1; phosphorylation-dependent. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome {ECO:0000250}. Note=The CC subcellular location is regulated during cell cycle. During interphase CC located in the nucleus. During mitosis located at the centrosome and CC dispersed in the cytoplasm. During telophase located in the midbody. CC Colocalizes with PLK1 at the centrosome in M phase. CC -!- PTM: Phosphorylated during mitosis in the cell cycle probably by CDK1. CC {ECO:0000250}. 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; AK011919; BAB27916.1; -; mRNA. DR EMBL; AK030630; BAC27054.1; -; mRNA. DR CCDS; CCDS26253.1; -. DR RefSeq; NP_079755.1; NM_025479.5. DR AlphaFoldDB; Q9D011; -. DR STRING; 10090.ENSMUSP00000059154; -. DR iPTMnet; Q9D011; -. DR PhosphoSitePlus; Q9D011; -. DR jPOST; Q9D011; -. DR MaxQB; Q9D011; -. DR PaxDb; 10090-ENSMUSP00000059154; -. DR ProteomicsDB; 291488; -. DR Pumba; Q9D011; -. DR DNASU; 66308; -. DR Ensembl; ENSMUST00000049744.4; ENSMUSP00000059154.4; ENSMUSG00000012429.10. DR GeneID; 66308; -. DR KEGG; mmu:66308; -. DR UCSC; uc007poa.1; mouse. DR AGR; MGI:1913558; -. DR CTD; 136647; -. DR MGI; MGI:1913558; Mplkip. DR VEuPathDB; HostDB:ENSMUSG00000012429; -. DR eggNOG; ENOG502S6ND; Eukaryota. DR GeneTree; ENSGT00390000002582; -. DR HOGENOM; CLU_1510143_0_0_1; -. DR InParanoid; Q9D011; -. DR OMA; QTTCTGK; -. DR OrthoDB; 4496402at2759; -. DR PhylomeDB; Q9D011; -. DR TreeFam; TF335586; -. DR BioGRID-ORCS; 66308; 7 hits in 78 CRISPR screens. DR PRO; PR:Q9D011; -. DR Proteomes; UP000000589; Chromosome 13. DR RNAct; Q9D011; Protein. DR Bgee; ENSMUSG00000012429; Expressed in ventricular zone and 204 other cell types or tissues. DR ExpressionAtlas; Q9D011; baseline and differential. DR GO; GO:0005813; C:centrosome; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0030496; C:midbody; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR InterPro; IPR026618; MPLKIP-like_vertebrate. DR InterPro; IPR028265; TTDN1/SICKLE. DR PANTHER; PTHR22446:SF3; M-PHASE-SPECIFIC PLK1-INTERACTING PROTEIN; 1. DR PANTHER; PTHR22446; UNCHARACTERIZED; 1. DR Pfam; PF15502; MPLKIP; 1. DR Genevisible; Q9D011; MM. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Methylation; Mitosis; KW Nucleus; Phosphoprotein; Reference proteome. FT CHAIN 1..178 FT /note="M-phase-specific PLK1-interacting protein" FT /id="PRO_0000065675" FT REGION 1..134 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..16 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 90..121 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 36 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TAP9" FT MOD_RES 46 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TAP9" FT MOD_RES 50 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8TAP9" FT MOD_RES 56 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q8TAP9" FT MOD_RES 58 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 67 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 76 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 79 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TAP9" FT MOD_RES 81 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TAP9" FT MOD_RES 92 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TAP9" FT MOD_RES 103 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TAP9" FT MOD_RES 114 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TAP9" FT MOD_RES 116 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q8TAP9" FT MOD_RES 119 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8TAP9" FT MOD_RES 123 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TAP9" FT MOD_RES 132 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8TAP9" SQ SEQUENCE 178 AA; 19060 MW; 0DA799EDEB988986 CRC64; MHRPNFRPPT PPYPSPGIGG WGGGNNFRGA LGGGPRPPSP RDGYGSPHHT PPCGPRARPY GSSQSPRHGG NFSGARFGSP SPGGYPGSYS RSPAGSQHQF GYSPGQQQTY PQGSPRTSTP FGSGRGREKR MSNELESYFK PSMLEDPWAG LEPVSVVDIS QQYSNTQTFT GKKGRYFS //