MPP9_MOUSE
ID MPP9_MOUSE Reviewed; 991 AA.
AC A6H5Y1; E9QPF8; Q8BUK7; Q8BV15; V9GX48;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=M-phase phosphoprotein 9;
GN Name=Mphosph9;
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 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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-508.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Heart;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=30375385; DOI=10.1038/s41467-018-06990-9;
RA Huang N., Zhang D., Li F., Chai P., Wang S., Teng J., Chen J.;
RT "M-Phase Phosphoprotein 9 regulates ciliogenesis by modulating CP110-CEP97
RT complex localization at the mother centriole.";
RL Nat. Commun. 9:4511-4511(2018).
CC -!- FUNCTION: Negatively regulates cilia formation by recruiting the CP110-
CC CEP97 complex (a negative regulator of ciliogenesis) at the distal end
CC of the mother centriole in ciliary cells (PubMed:30375385). At the
CC beginning of cilia formation, MPHOSPH9 undergoes TTBK2-mediated
CC phosphorylation and degradation via the ubiquitin-proteasome system and
CC removes itself and the CP110-CEP97 complex from the distal end of the
CC mother centriole, which subsequently promotes cilia formation (By
CC similarity). {ECO:0000250|UniProtKB:Q99550,
CC ECO:0000269|PubMed:30375385}.
CC -!- SUBUNIT: Interacts with CCP110, CEP97 and KIF24.
CC {ECO:0000250|UniProtKB:Q99550}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:Q99550}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:Q99550}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q99550}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:30375385}. Note=Localizes to the distal and
CC proximal end of centriole pairs in duplicated centrosomes. In ciliated
CC cells, localizes to the distal and proximal end of daughter centriole
CC and proximal of the mother centriole but not in the distal end of the
CC mother centriole (By similarity). Recruited by KIF24 to the distal end
CC of mother centriole where it forms a ring-like structure (By
CC similarity). {ECO:0000250|UniProtKB:Q99550}.
CC -!- PTM: TTBK2-mediated phosphorylation at Ser-587 and Ser-594, promotes
CC its ubiquitination at Lys-590 leading to proteasomal degradation, loss
CC of MPHOSPH9 facilitates the removal of the CP110-CEP97 complex from the
CC mother centrioles, promoting the initiation of ciliogenesis (By
CC similarity). Phosphorylated in M (mitotic) phase (By similarity).
CC {ECO:0000250|UniProtKB:Q99550}.
CC -!- PTM: Ubiquitinated at Lys-590, leading to proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q99550}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice show decreased body weight when
CC compared with wild-type mice around 1 month after birth
CC (PubMed:30375385). An increased percentage of ciliated cells in the
CC proximal and distal tubules is observed in the kidneys of knockout mice
CC at 1 and 4 months after birth (PubMed:30375385).
CC {ECO:0000269|PubMed:30375385}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC38158.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC138423; AAI38424.1; -; mRNA.
DR EMBL; BC145681; AAI45682.1; -; mRNA.
DR EMBL; AK081178; BAC38158.1; ALT_INIT; mRNA.
DR EMBL; AK084586; BAC39220.1; -; mRNA.
DR EMBL; GL456120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001074792.1; NM_001081323.2.
DR AlphaFoldDB; A6H5Y1; -.
DR SMR; A6H5Y1; -.
DR BioGRID; 234701; 6.
DR STRING; 10090.ENSMUSP00000031344; -.
DR iPTMnet; A6H5Y1; -.
DR PhosphoSitePlus; A6H5Y1; -.
DR jPOST; A6H5Y1; -.
DR MaxQB; A6H5Y1; -.
DR PaxDb; A6H5Y1; -.
DR PRIDE; A6H5Y1; -.
DR ProteomicsDB; 290305; -.
DR ProteomicsDB; 347094; -.
DR ProteomicsDB; 367800; -.
DR Antibodypedia; 31757; 175 antibodies from 24 providers.
DR DNASU; 269702; -.
DR GeneID; 269702; -.
DR KEGG; mmu:269702; -.
DR UCSC; uc008zpi.2; mouse.
DR CTD; 10198; -.
DR MGI; MGI:2443138; Mphosph9.
DR VEuPathDB; HostDB:ENSMUSG00000038126; -.
DR eggNOG; KOG4713; Eukaryota.
DR HOGENOM; CLU_008784_0_0_1; -.
DR InParanoid; A6H5Y1; -.
DR OMA; NKQMPDQ; -.
DR OrthoDB; 572984at2759; -.
DR PhylomeDB; A6H5Y1; -.
DR TreeFam; TF336168; -.
DR BioGRID-ORCS; 269702; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Mphosph9; mouse.
DR PRO; PR:A6H5Y1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; A6H5Y1; protein.
DR Bgee; ENSMUSG00000038126; Expressed in saccule of membranous labyrinth and 240 other tissues.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1902018; P:negative regulation of cilium assembly; IMP:UniProtKB.
DR InterPro; IPR026636; MPHOSPH9.
DR PANTHER; PTHR14926; PTHR14926; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus; Isopeptide bond;
KW Membrane; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..991
FT /note="M-phase phosphoprotein 9"
FT /id="PRO_0000355083"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..606
FT /note="Required for its centrosomal localization"
FT /evidence="ECO:0000250|UniProtKB:Q99550"
FT REGION 259..308
FT /note="Interaction with CEP97"
FT /evidence="ECO:0000250|UniProtKB:Q99550"
FT REGION 287..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..840
FT /note="Interaction with KIF24"
FT /evidence="ECO:0000250|UniProtKB:Q99550"
FT REGION 717..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 451..610
FT /evidence="ECO:0000255"
FT COILED 917..982
FT /evidence="ECO:0000255"
FT COMPBIAS 287..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 587
FT /note="Phosphoserine; by TTBK2"
FT /evidence="ECO:0000250|UniProtKB:Q99550"
FT MOD_RES 594
FT /note="Phosphoserine; by TTBK2"
FT /evidence="ECO:0000250|UniProtKB:Q99550"
FT MOD_RES 803
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99550"
FT CROSSLNK 590
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q99550"
SQ SEQUENCE 991 AA; 109953 MW; 3B8CDC9A257274CB CRC64;
MGFFSENSER NESVVSSPAS KEPETQPASS TSYPDCHVDS SSVSSGYGTF CILDMNTHKA
KEPTEPLEPG AASQGQHPAS VVQAHGPAGG AAAINFFTQT PEELCASLKE DGSTFPGEFD
RNFLGENKIS EVYSGKANSG KSVTSWAQRL KQNQSKQAHT EDDCSGPKPG SELNWKPPAD
TFDLAADAAR PCAFYINKPA ESPSSWLSDS GTGLTYWKLE EKDMYHSLPE TLEKTFAPSP
AERPLSQVLT LDPGAIRMKP KEHVAGIQAH GFLHALDDRI SFSPDSVLEP SLSRHSDTDS
SSQASHNPSQ VSGFSKYPST TRASPVDTWK NHAFQRESRT SSTIPSRYTI TSNDISVKTV
DEENTVTVAS VSQSQLPGTA NSVPECISLA SLEDPVMLSK IRQNLKEKHA RHVADLRAYY
ESEISSLKQK LEAKDISAVE EWKKKNEILA DRCGQLDSAL NEATSRVRTL EKNNNLLEIE
VSDLRERFNA ASSASKVLQE RIEEMRTSNK EKDNTITRLK CRLQDLEEAF ENAYKLSDDK
EARLRQENKM FQDLLGEYES LGKEHGRVKD TLNTTENKLL DAHTQISDLK RTISKLEAQV
KQAEHESMLS LRNGAKVPER PSRSNSVATS DVSRRKWLIP GAEYSIFTGQ PLDPRDRKLD
KQLEEALVPG YHSPPEKDSS LGSSPASLLV KKKRDTPDTP PIIKALKELD EERVFKSWGT
QTEKEDSSSK LVNSRQTEPS VNTGRSPEKC AQQRPKRQTS ASQRSSSLPP SSRKANTPTK
REIMLTPVTV AYSPKRSPKE NLSPGFSHLL SKNESSPVRF DILLDDLDTV PVSTLQQTTA
KKQLQFLLDD SEEKKYSEKN SDDPVNPSSC PEHSPNGLKK VSTRQAWEKS KSVSLEQCQP
GSAAPQDNGF EYTAKIRTLA ETERFFDELT KEKDQIEAAL SRMPSPGGRI TLQTRLNQEA
LEDRLEKINR ELGSVRMTLK KFHVLRSSAN L
