MRT4_HUMAN
ID MRT4_HUMAN Reviewed; 239 AA.
AC Q9UKD2; B3KNB3; Q5TG55; Q96SS6; Q9BPV9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=mRNA turnover protein 4 homolog {ECO:0000250|UniProtKB:P33201};
DE AltName: Full=Ribosome assembly factor MRTO4 {ECO:0000250|UniProtKB:P33201, ECO:0000305};
GN Name=MRTO4; Synonyms=C1orf33, MRT4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ge H.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RA Zou S.W., Miao S.Y., Zhang X.D., Qiao Y., Wang L.F.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [8]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=20083226; DOI=10.1016/j.biocel.2010.01.011;
RA Michalec B., Krokowski D., Grela P., Wawiorka L., Sawa-Makarska J.,
RA Grankowski N., Tchorzewski M.;
RT "Subcellular localization of ribosomal P0-like protein MRT4 is determined
RT by its N-terminal domain.";
RL Int. J. Biochem. Cell Biol. 42:736-748(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP INTERACTION WITH MINAS-60.
RX PubMed=35393574; DOI=10.1038/s41589-022-01003-9;
RA Cao X., Khitun A., Harold C.M., Bryant C.J., Zheng S.J., Baserga S.J.,
RA Slavoff S.A.;
RT "Nascent alt-protein chemoproteomics reveals a pre-60S assembly checkpoint
RT inhibitor.";
RL Nat. Chem. Biol. 0:0-0(2022).
CC -!- FUNCTION: Component of the ribosome assembly machinery. Nuclear paralog
CC of the ribosomal protein P0, it binds pre-60S subunits at an early
CC stage of assembly in the nucleolus, and is replaced by P0 in
CC cytoplasmic pre-60S subunits and mature 80S ribosomes.
CC {ECO:0000269|PubMed:20083226}.
CC -!- SUBUNIT: Associates with the pre-60S ribosomal particle
CC (PubMed:20083226). Interacts with MINAS-60 (product of an alternative
CC open reading frame of RBM10) (PubMed:35393574).
CC {ECO:0000269|PubMed:20083226, ECO:0000269|PubMed:35393574}.
CC -!- INTERACTION:
CC Q9UKD2; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-1046493, EBI-750109;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:20083226}. Cytoplasm {ECO:0000269|PubMed:20083226}.
CC Note=Shuttles between the nucleus and the cytoplasm.
CC {ECO:0000269|PubMed:20083226}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000305}.
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DR EMBL; AF173378; AAD52608.1; -; mRNA.
DR EMBL; AY303790; AAP68821.1; -; mRNA.
DR EMBL; AK024227; BAG51275.1; -; mRNA.
DR EMBL; AK027569; BAB55205.1; -; mRNA.
DR EMBL; AL035413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471134; EAW94873.1; -; Genomic_DNA.
DR EMBL; BC003013; AAH03013.1; -; mRNA.
DR EMBL; BC006504; AAH06504.1; -; mRNA.
DR CCDS; CCDS191.1; -.
DR RefSeq; NP_057267.2; NM_016183.3.
DR AlphaFoldDB; Q9UKD2; -.
DR SMR; Q9UKD2; -.
DR BioGRID; 119337; 135.
DR IntAct; Q9UKD2; 53.
DR MINT; Q9UKD2; -.
DR STRING; 9606.ENSP00000364320; -.
DR GlyGen; Q9UKD2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UKD2; -.
DR PhosphoSitePlus; Q9UKD2; -.
DR SwissPalm; Q9UKD2; -.
DR BioMuta; MRTO4; -.
DR DMDM; 51316541; -.
DR SWISS-2DPAGE; Q9UKD2; -.
DR EPD; Q9UKD2; -.
DR jPOST; Q9UKD2; -.
DR MassIVE; Q9UKD2; -.
DR MaxQB; Q9UKD2; -.
DR PaxDb; Q9UKD2; -.
DR PeptideAtlas; Q9UKD2; -.
DR PRIDE; Q9UKD2; -.
DR ProteomicsDB; 84768; -.
DR Antibodypedia; 29590; 213 antibodies from 25 providers.
DR DNASU; 51154; -.
DR Ensembl; ENST00000330263.5; ENSP00000364320.3; ENSG00000053372.5.
DR GeneID; 51154; -.
DR KEGG; hsa:51154; -.
DR MANE-Select; ENST00000330263.5; ENSP00000364320.3; NM_016183.4; NP_057267.2.
DR UCSC; uc001bbs.4; human.
DR CTD; 51154; -.
DR GeneCards; MRTO4; -.
DR HGNC; HGNC:18477; MRTO4.
DR HPA; ENSG00000053372; Low tissue specificity.
DR neXtProt; NX_Q9UKD2; -.
DR OpenTargets; ENSG00000053372; -.
DR PharmGKB; PA162396216; -.
DR VEuPathDB; HostDB:ENSG00000053372; -.
DR eggNOG; KOG0816; Eukaryota.
DR GeneTree; ENSGT00390000006238; -.
DR HOGENOM; CLU_071690_3_0_1; -.
DR InParanoid; Q9UKD2; -.
DR OMA; LEWAENY; -.
DR OrthoDB; 1181992at2759; -.
DR PhylomeDB; Q9UKD2; -.
DR TreeFam; TF300111; -.
DR PathwayCommons; Q9UKD2; -.
DR SignaLink; Q9UKD2; -.
DR BioGRID-ORCS; 51154; 610 hits in 1088 CRISPR screens.
DR ChiTaRS; MRTO4; human.
DR GenomeRNAi; 51154; -.
DR Pharos; Q9UKD2; Tbio.
DR PRO; PR:Q9UKD2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UKD2; protein.
DR Bgee; ENSG00000053372; Expressed in oocyte and 174 other tissues.
DR ExpressionAtlas; Q9UKD2; baseline and differential.
DR Genevisible; Q9UKD2; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:InterPro.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR CDD; cd05796; Ribosomal_P0_like; 1.
DR Gene3D; 3.30.70.1730; -; 1.
DR Gene3D; 3.90.105.20; -; 1.
DR InterPro; IPR033867; Mrt4.
DR InterPro; IPR043141; Ribosomal_L10-like_sf.
DR InterPro; IPR001790; Ribosomal_L10P.
DR InterPro; IPR043164; RL10_insert_sf.
DR InterPro; IPR040637; RL10P_insert.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR Pfam; PF17777; RL10P_insert; 1.
DR SUPFAM; SSF160369; SSF160369; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis.
FT CHAIN 1..239
FT /note="mRNA turnover protein 4 homolog"
FT /id="PRO_0000154816"
FT REGION 215..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0I8"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0I8"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D0I8"
FT CONFLICT 95
FT /note="R -> T (in Ref. 1; AAD52608)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="S -> L (in Ref. 3; BAB55205)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 239 AA; 27560 MW; F1BFF6E566FF942F CRC64;
MPKSKRDKKV SLTKTAKKGL ELKQNLIEEL RKCVDTYKYL FIFSVANMRN SKLKDIRNAW
KHSRMFFGKN KVMMVALGRS PSDEYKDNLH QVSKRLRGEV GLLFTNRTKE EVNEWFTKYT
EMDYARAGNK AAFTVSLDPG PLEQFPHSME PQLRQLGLPT ALKRGVVTLL SDYEVCKEGD
VLTPEQARVL KLFGYEMAEF KVTIKYMWDS QSGRFQQMGD DLPESASEST EESDSEDDD
