MISP_MOUSE
ID MISP_MOUSE Reviewed; 648 AA.
AC Q9D279; Q3UI04;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Mitotic interactor and substrate of PLK1 {ECO:0000250|UniProtKB:Q8IVT2};
DE AltName: Full=Mitotic spindle positioning protein {ECO:0000312|MGI:MGI:1926156};
GN Name=Misp {ECO:0000312|MGI:MGI:1926156};
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].
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220 AND SER-364, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Pancreas;
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: Plays a role in mitotic spindle orientation and mitotic
CC progression. Regulates the distribution of dynactin at the cell cortex
CC in a PLK1-dependent manner, thus stabilizing cortical and astral
CC microtubule attachments required for proper mitotic spindle
CC positioning. May link microtubules to the actin cytoskeleton and focal
CC adhesions. May be required for directed cell migration and centrosome
CC orientation. May also be necessary for proper stacking of the Golgi
CC apparatus (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Associates with F-actin. Interacts with DCTN1; this
CC interaction regulates DCTN1 distribution at the cell cortex. Interacts
CC with PTK2/FAK and MAPRE1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex
CC {ECO:0000250}. Note=Predominantly localizes to cortical actin
CC structures during interphase and mitosis. Present in retraction fibers,
CC which are formed at former adhesion sites during mitosis, and at
CC spicular membrane protrusions in re-attaching cytokinetic cells.
CC Partially colocalizes with cytoplasmic F-actin. Not detected at
CC microtubules at interphase, nor at spindle during mitosis (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by CDK1 and PLK1. CDK1 is the priming kinase for
CC PLK1 phosphorylation. Phosphorylation by PLK1 is required for proper
CC spindle orientation at metaphase (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MISP family. {ECO:0000305}.
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DR EMBL; AK020266; BAB32049.1; -; mRNA.
DR EMBL; AK146817; BAE27456.1; -; mRNA.
DR EMBL; AK147132; BAE27702.1; -; mRNA.
DR EMBL; BC013508; AAH13508.1; -; mRNA.
DR CCDS; CCDS23992.1; -.
DR RefSeq; NP_084494.1; NM_030218.2.
DR RefSeq; XP_006514391.1; XM_006514328.1.
DR RefSeq; XP_006514392.1; XM_006514329.1.
DR RefSeq; XP_006514393.1; XM_006514330.1.
DR RefSeq; XP_006514394.1; XM_006514331.1.
DR RefSeq; XP_006514395.1; XM_006514332.3.
DR RefSeq; XP_006514396.1; XM_006514333.3.
DR AlphaFoldDB; Q9D279; -.
DR STRING; 10090.ENSMUSP00000130071; -.
DR iPTMnet; Q9D279; -.
DR PhosphoSitePlus; Q9D279; -.
DR EPD; Q9D279; -.
DR MaxQB; Q9D279; -.
DR PaxDb; Q9D279; -.
DR PeptideAtlas; Q9D279; -.
DR PRIDE; Q9D279; -.
DR ProteomicsDB; 295568; -.
DR Antibodypedia; 22380; 121 antibodies from 21 providers.
DR DNASU; 78906; -.
DR Ensembl; ENSMUST00000046833; ENSMUSP00000048893; ENSMUSG00000035852.
DR Ensembl; ENSMUST00000169041; ENSMUSP00000130071; ENSMUSG00000035852.
DR Ensembl; ENSMUST00000219305; ENSMUSP00000151529; ENSMUSG00000035852.
DR GeneID; 78906; -.
DR KEGG; mmu:78906; -.
DR UCSC; uc007fzy.1; mouse.
DR CTD; 126353; -.
DR MGI; MGI:1926156; Misp.
DR VEuPathDB; HostDB:ENSMUSG00000035852; -.
DR eggNOG; ENOG502RZZI; Eukaryota.
DR GeneTree; ENSGT00940000154739; -.
DR HOGENOM; CLU_404873_0_0_1; -.
DR InParanoid; Q9D279; -.
DR OMA; WGQDEPQ; -.
DR OrthoDB; 481627at2759; -.
DR PhylomeDB; Q9D279; -.
DR TreeFam; TF334067; -.
DR BioGRID-ORCS; 78906; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q9D279; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9D279; protein.
DR Bgee; ENSMUSG00000035852; Expressed in intestinal villus and 126 other tissues.
DR ExpressionAtlas; Q9D279; baseline and differential.
DR Genevisible; Q9D279; MM.
DR GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:1905721; C:mitotic spindle astral microtubule end; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0031616; C:spindle pole centrosome; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0051660; P:establishment of centrosome localization; ISS:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0051640; P:organelle localization; ISS:UniProtKB.
DR GO; GO:1904776; P:regulation of protein localization to cell cortex; ISS:UniProtKB.
DR InterPro; IPR029304; AKAP2_C.
DR InterPro; IPR042779; MISP/MISP3.
DR PANTHER; PTHR18839; PTHR18839; 1.
DR Pfam; PF15304; AKAP2_C; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell cycle; Cell division; Cell junction; Coiled coil;
KW Cytoplasm; Cytoskeleton; Mitosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..648
FT /note="Mitotic interactor and substrate of PLK1"
FT /id="PRO_0000079382"
FT REGION 242..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 511..534
FT /evidence="ECO:0000255"
FT COMPBIAS 242..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 149
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 190
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 253
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 256
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 347
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 365
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 439
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 541
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 554
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IVT2"
SQ SEQUENCE 648 AA; 72281 MW; 1E395B70763B3D1F CRC64;
MDRVTRYPIF SNPRSARVTS LVLDEDTSYT VELVGVGPEA GWSQGDLQAW STEYQTRPDV
KRTNVSSNRR VFLGQQSPRS LYLEDEDEEI KSYHLDDSSD TLCRQRRELE AERWAVIQSQ
AVRKGGTVAT LQAASDHGDL RIARQPQSTV TEEILVDTEQ IDFLAARQQF LSLEKANTNP
VPCGLTARET FPRTPPGINQ APKASTGPHL ANGYTTAVTS PMKEVTLEKS FHVSPARSIH
IVNDPGSQTQ AESPETPKET PIEREIRLAQ EREAELREQR GLGRAAGHQE LVQIPSRPLL
SKMSLTETPP RRDRGRPSLY VQRDMVQETQ REEDHRREGL QVGRASTPDW PSQDPQPGLQ
RSLSSDCILS PDARATDPAP EARKVNRIPL DAYQPYLGPG TPKLEFSAFG VYSKPSGVST
EDTKATVFQK ATESPRHVSE SSGRSLSSKQ EWSKPPGKAT NVGVVRLGNF HLRPLRFKVP
DVPQGTETPH TWGWEVAGGP ILRLQKSQSS DLLEREMESV LRREREVAEE RRNAFFPEVF
SPVPAEDESH EQDSRSSSRA SGITGSYSVS ESPLFTPVHL NSGLVWKVEA PEDSAPPGQK
TRKEMWYAGI NPSDSVNSEV LGATRVKRHK NLLAERWEAH IYASEDEN
