MPH6_MOUSE
ID MPH6_MOUSE Reviewed; 161 AA.
AC Q9D1Q1;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=M-phase phosphoprotein 6;
GN Name=Mphosph6 {ECO:0000312|MGI:MGI:1915783};
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;
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=Mammary gland;
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 PROTEIN SEQUENCE OF 16-21, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: RNA-binding protein that associates with the RNA exosome
CC complex. Involved in the 3'-processing of the 7S pre-RNA to the mature
CC 5.8S rRNA and plays a role in recruiting the RNA exosome complex to
CC pre-rRNA; this function may include C1D.
CC {ECO:0000250|UniProtKB:Q99547}.
CC -!- SUBUNIT: Associates with the RNA exosome complex, probably mediated by
CC EXOSC10. Interacts with ARHGAP18, EXOSC10 and MTREX.
CC {ECO:0000250|UniProtKB:Q99547}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q99547}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q99547}. Note=Cytoplasmic in M phase.
CC {ECO:0000250|UniProtKB:Q99547}.
CC -!- PTM: Phosphorylated in M (mitotic) phase.
CC {ECO:0000250|UniProtKB:Q99547}.
CC -!- SIMILARITY: Belongs to the MPP6 family. {ECO:0000305}.
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DR EMBL; AK003245; BAB22664.1; -; mRNA.
DR EMBL; BC008161; AAH08161.1; -; mRNA.
DR CCDS; CCDS22702.1; -.
DR RefSeq; NP_081034.1; NM_026758.3.
DR AlphaFoldDB; Q9D1Q1; -.
DR SMR; Q9D1Q1; -.
DR STRING; 10090.ENSMUSP00000034303; -.
DR iPTMnet; Q9D1Q1; -.
DR PhosphoSitePlus; Q9D1Q1; -.
DR EPD; Q9D1Q1; -.
DR MaxQB; Q9D1Q1; -.
DR PaxDb; Q9D1Q1; -.
DR PeptideAtlas; Q9D1Q1; -.
DR PRIDE; Q9D1Q1; -.
DR ProteomicsDB; 252607; -.
DR Antibodypedia; 3289; 172 antibodies from 25 providers.
DR DNASU; 68533; -.
DR Ensembl; ENSMUST00000034303; ENSMUSP00000034303; ENSMUSG00000031843.
DR GeneID; 68533; -.
DR KEGG; mmu:68533; -.
DR UCSC; uc009npg.1; mouse.
DR CTD; 10200; -.
DR MGI; MGI:1915783; Mphosph6.
DR VEuPathDB; HostDB:ENSMUSG00000031843; -.
DR eggNOG; KOG4531; Eukaryota.
DR GeneTree; ENSGT00390000009212; -.
DR HOGENOM; CLU_139852_1_0_1; -.
DR InParanoid; Q9D1Q1; -.
DR OMA; EKLMVLM; -.
DR OrthoDB; 1436304at2759; -.
DR PhylomeDB; Q9D1Q1; -.
DR TreeFam; TF323810; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 68533; 24 hits in 73 CRISPR screens.
DR ChiTaRS; Mphosph6; mouse.
DR PRO; PR:Q9D1Q1; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9D1Q1; protein.
DR Bgee; ENSMUSG00000031843; Expressed in animal zygote and 254 other tissues.
DR Genevisible; Q9D1Q1; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000178; C:exosome (RNase complex); ISS:UniProtKB.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; ISO:MGI.
DR InterPro; IPR019324; MPP6.
DR PANTHER; PTHR13582; PTHR13582; 1.
DR Pfam; PF10175; MPP6; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; rRNA processing;
KW Ubl conjugation.
FT CHAIN 1..161
FT /note="M-phase phosphoprotein 6"
FT /id="PRO_0000122438"
FT MOTIF 117..134
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99547"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99547"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99547"
FT CROSSLNK 128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99547"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99547"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99547"
SQ SEQUENCE 161 AA; 19086 MW; 58762841641C0DC4 CRC64;
MASERKTKLS KNLLRMKFMQ RGLDSETKKQ LEEEERKMIS DEHWYLDLPE LKEKESFIVE
EQSFSLCEDL LYGRMSFRGF NPEVEKLMLQ MNSKNRAEAA EEDETVEVDV SDEEMARRYE
TLVGTIGKKF VKKRDRANYE EDENGTIKAI KPKKMFLKPQ D
