MPLKI_MOUSE
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 03-AUG-2022, entry version 122.
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}.
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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; Q9D011; -.
DR PRIDE; Q9D011; -.
DR ProteomicsDB; 291488; -.
DR DNASU; 66308; -.
DR Ensembl; ENSMUST00000049744; ENSMUSP00000059154; ENSMUSG00000012429.
DR GeneID; 66308; -.
DR KEGG; mmu:66308; -.
DR UCSC; uc007poa.1; mouse.
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; WSGQFRR; -.
DR OrthoDB; 1543160at2759; -.
DR PhylomeDB; Q9D011; -.
DR TreeFam; TF335586; -.
DR BioGRID-ORCS; 66308; 7 hits in 73 CRISPR screens.
DR PRO; PR:Q9D011; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9D011; protein.
DR Bgee; ENSMUSG00000012429; Expressed in ventricular zone and 201 other tissues.
DR ExpressionAtlas; Q9D011; baseline and differential.
DR Genevisible; Q9D011; MM.
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; PTHR22446; 1.
DR Pfam; PF15502; MPLKIP; 1.
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
