MASU1_HUMAN
ID MASU1_HUMAN Reviewed; 234 AA.
AC Q96EH3; A4D154;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Mitochondrial assembly of ribosomal large subunit protein 1;
GN Name=MALSU1; Synonyms=C7orf30;
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 [LARGE SCALE MRNA].
RC TISSUE=Cerebellum, and Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16548050; DOI=10.1002/elps.200500704;
RA Chevallet M., Lescuyer P., Diemer H., van Dorsselaer A., Leize-Wagner E.,
RA Rabilloud T.;
RT "Alterations of the mitochondrial proteome caused by the absence of
RT mitochondrial DNA: A proteomic view.";
RL Electrophoresis 27:1574-1583(2006).
RN [7]
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 [8]
RP SUBCELLULAR LOCATION, FUNCTION, AND ASSOCIATION WITH MITOCHONDRIAL RIBOSOME
RP LARGE SUBUNIT.
RX PubMed=22238376; DOI=10.1093/nar/gkr1282;
RA Rorbach J., Gammage P.A., Minczuk M.;
RT "C7orf30 is necessary for biogenesis of the large subunit of the
RT mitochondrial ribosome.";
RL Nucleic Acids Res. 40:4097-4109(2012).
RN [9]
RP SUBCELLULAR LOCATION, INTERACTION WITH MRPL12, AND FUNCTION.
RX PubMed=22238375; DOI=10.1093/nar/gkr1271;
RA Wanschers B.F., Szklarczyk R., Pajak A., van den Brand M.A., Gloerich J.,
RA Rodenburg R.J., Lightowlers R.N., Nijtmans L.G., Huynen M.A.;
RT "C7orf30 specifically associates with the large subunit of the
RT mitochondrial ribosome and is involved in translation.";
RL Nucleic Acids Res. 40:4040-4051(2012).
RN [10]
RP POSSIBLE FUNCTION IN RIBOSOMAL SILENCING, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH MRPL14.
RX PubMed=22829778; DOI=10.1371/journal.pgen.1002815;
RA Hauser R., Pech M., Kijek J., Yamamoto H., Titz B., Naeve F.,
RA Tovchigrechko A., Yamamoto K., Szaflarski W., Takeuchi N., Stellberger T.,
RA Diefenbacher M.E., Nierhaus K.H., Uetz P.;
RT "RsfA (YbeB) proteins are conserved ribosomal silencing factors.";
RL PLoS Genet. 8:E1002815-E1002815(2012).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH MRPL14.
RX PubMed=23171548; DOI=10.1091/mbc.e12-09-0651;
RA Fung S., Nishimura T., Sasarman F., Shoubridge E.A.;
RT "The conserved interaction of C7orf30 with MRPL14 promotes biogenesis of
RT the mitochondrial large ribosomal subunit and mitochondrial translation.";
RL Mol. Biol. Cell 24:184-193(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13] {ECO:0007744|PDB:5OOL, ECO:0007744|PDB:5OOM}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=28892042; DOI=10.1038/nsmb.3464;
RA Brown A., Rathore S., Kimanius D., Aibara S., Bai X.C., Rorbach J.,
RA Amunts A., Ramakrishnan V.;
RT "Structures of the human mitochondrial ribosome in native states of
RT assembly.";
RL Nat. Struct. Mol. Biol. 24:866-869(2017).
CC -!- FUNCTION: Required for normal mitochondrial ribosome function and
CC mitochondrial translation (PubMed:22238375, PubMed:23171548). May play
CC a role in ribosome biogenesis by preventing premature association of
CC the 28S and 39S ribosomal subunits (Probable). Interacts with
CC mitochondrial ribosomal protein L14 (MRPL14), probably blocking
CC formation of intersubunit bridge B8, preventing association of the 28S
CC and 39S ribosomal subunits (Probable). Addition to isolated
CC mitochondrial ribosomal subunits partially inhibits translation,
CC probably by interfering with the association of the 28S and 39S
CC ribosomal subunits and the formation of functional ribosomes
CC (Probable). May also participate in the assembly and/or regulation of
CC the stability of the large subunit of the mitochondrial ribosome
CC (PubMed:22238376, PubMed:23171548). May function as a ribosomal
CC silencing factor (Probable). {ECO:0000269|PubMed:22238375,
CC ECO:0000269|PubMed:22238376, ECO:0000269|PubMed:23171548,
CC ECO:0000305|PubMed:22829778, ECO:0000305|PubMed:28892042}.
CC -!- SUBUNIT: Associates with the mitochondrial ribosome large subunit (39S)
CC via interaction with MRPL12 and/or MRPL14 (PubMed:22238375,
CC PubMed:23171548, PubMed:28892042). The interaction generates steric
CC hindrance that is expected to prevent premature association of the 28S
CC and 39S ribosomal subunits (PubMed:28892042). Identified in a complex
CC composed of MALSU1, MIEF1 upstream open reading frame protein and
CC NDUFAB1; within the trimeric complex, MIEF1 upstream open reading frame
CC protein functions as a bridging scaffold that interacts with MALSU1 on
CC one side, and with NDUFAB1 on the other side (PubMed:28892042).
CC Interacts with MRPL12 and MRPL14 (PubMed:23171548, PubMed:22829778,
CC PubMed:22238375). {ECO:0000269|PubMed:22238375,
CC ECO:0000269|PubMed:22829778, ECO:0000269|PubMed:23171548,
CC ECO:0000269|PubMed:28892042}.
CC -!- INTERACTION:
CC Q96EH3; P32321: DCTD; NbExp=6; IntAct=EBI-2339737, EBI-739870;
CC Q96EH3; P42858: HTT; NbExp=6; IntAct=EBI-2339737, EBI-466029;
CC Q96EH3; Q0VD86: INCA1; NbExp=3; IntAct=EBI-2339737, EBI-6509505;
CC Q96EH3; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2339737, EBI-11742507;
CC Q96EH3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2339737, EBI-16439278;
CC Q96EH3; A2RUH7: MYBPHL; NbExp=3; IntAct=EBI-2339737, EBI-9088235;
CC Q96EH3; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-2339737, EBI-741158;
CC Q96EH3; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-2339737, EBI-949255;
CC Q96EH3; Q3SY56: SP6; NbExp=3; IntAct=EBI-2339737, EBI-11175533;
CC Q96EH3; Q8TF47: ZFP90; NbExp=3; IntAct=EBI-2339737, EBI-11419867;
CC Q96EH3; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-2339737, EBI-743265;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:16548050, ECO:0000269|PubMed:22238375,
CC ECO:0000269|PubMed:22238376, ECO:0000269|PubMed:22829778,
CC ECO:0000269|PubMed:23171548, ECO:0000305|PubMed:28892042}.
CC Note=Colocalizes with MRPL12 and/or MRPL14.
CC {ECO:0000269|PubMed:22238375, ECO:0000269|PubMed:22829778}.
CC -!- SIMILARITY: Belongs to the Iojap/RsfS family. {ECO:0000305}.
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DR EMBL; AK316559; BAG38148.1; -; mRNA.
DR EMBL; AK127742; BAG54562.1; -; mRNA.
DR EMBL; AC005082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236948; EAL24258.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93785.1; -; Genomic_DNA.
DR EMBL; BC012331; AAH12331.1; -; mRNA.
DR CCDS; CCDS5381.1; -.
DR RefSeq; NP_612455.1; NM_138446.1.
DR PDB; 5OOL; EM; 3.06 A; u=1-234.
DR PDB; 5OOM; EM; 3.03 A; u=1-234.
DR PDB; 7A5H; EM; 3.30 A; u=1-234.
DR PDB; 7A5J; EM; 3.10 A; u=1-234.
DR PDB; 7O9K; EM; 3.10 A; u=1-234.
DR PDB; 7O9M; EM; 2.50 A; u=1-234.
DR PDB; 7ODR; EM; 2.90 A; u=1-234.
DR PDB; 7ODS; EM; 3.10 A; u=1-234.
DR PDB; 7ODT; EM; 3.10 A; u=1-234.
DR PDB; 7OF0; EM; 2.20 A; u=1-234.
DR PDB; 7OF2; EM; 2.70 A; u=1-234.
DR PDB; 7OF3; EM; 2.70 A; u=1-234.
DR PDB; 7OF5; EM; 2.90 A; u=1-234.
DR PDB; 7OF7; EM; 2.50 A; u=1-234.
DR PDB; 7OI6; EM; 5.70 A; u=1-234.
DR PDB; 7OI7; EM; 3.50 A; u=1-234.
DR PDB; 7OI8; EM; 3.50 A; u=1-234.
DR PDB; 7OI9; EM; 3.30 A; u=1-234.
DR PDB; 7OIC; EM; 3.10 A; u=1-234.
DR PDB; 7OID; EM; 3.70 A; u=1-234.
DR PDB; 7OIE; EM; 3.50 A; u=1-234.
DR PDB; 7PD3; EM; 3.40 A; u=1-234.
DR PDB; 7QH6; EM; 3.08 A; u=1-234.
DR PDBsum; 5OOL; -.
DR PDBsum; 5OOM; -.
DR PDBsum; 7A5H; -.
DR PDBsum; 7A5J; -.
DR PDBsum; 7O9K; -.
DR PDBsum; 7O9M; -.
DR PDBsum; 7ODR; -.
DR PDBsum; 7ODS; -.
DR PDBsum; 7ODT; -.
DR PDBsum; 7OF0; -.
DR PDBsum; 7OF2; -.
DR PDBsum; 7OF3; -.
DR PDBsum; 7OF5; -.
DR PDBsum; 7OF7; -.
DR PDBsum; 7OI6; -.
DR PDBsum; 7OI7; -.
DR PDBsum; 7OI8; -.
DR PDBsum; 7OI9; -.
DR PDBsum; 7OIC; -.
DR PDBsum; 7OID; -.
DR PDBsum; 7OIE; -.
DR PDBsum; 7PD3; -.
DR PDBsum; 7QH6; -.
DR AlphaFoldDB; Q96EH3; -.
DR SMR; Q96EH3; -.
DR BioGRID; 125433; 188.
DR IntAct; Q96EH3; 49.
DR MINT; Q96EH3; -.
DR STRING; 9606.ENSP00000419370; -.
DR iPTMnet; Q96EH3; -.
DR PhosphoSitePlus; Q96EH3; -.
DR BioMuta; MALSU1; -.
DR DMDM; 74731563; -.
DR EPD; Q96EH3; -.
DR jPOST; Q96EH3; -.
DR MassIVE; Q96EH3; -.
DR MaxQB; Q96EH3; -.
DR PaxDb; Q96EH3; -.
DR PeptideAtlas; Q96EH3; -.
DR PRIDE; Q96EH3; -.
DR ProteomicsDB; 76407; -.
DR Antibodypedia; 12100; 55 antibodies from 15 providers.
DR DNASU; 115416; -.
DR Ensembl; ENST00000466681.2; ENSP00000419370.1; ENSG00000156928.5.
DR GeneID; 115416; -.
DR KEGG; hsa:115416; -.
DR MANE-Select; ENST00000466681.2; ENSP00000419370.1; NM_138446.2; NP_612455.1.
DR UCSC; uc003swd.2; human.
DR CTD; 115416; -.
DR DisGeNET; 115416; -.
DR GeneCards; MALSU1; -.
DR HGNC; HGNC:21721; MALSU1.
DR HPA; ENSG00000156928; Low tissue specificity.
DR MIM; 614624; gene.
DR neXtProt; NX_Q96EH3; -.
DR OpenTargets; ENSG00000156928; -.
DR PharmGKB; PA134866345; -.
DR VEuPathDB; HostDB:ENSG00000156928; -.
DR eggNOG; KOG3212; Eukaryota.
DR GeneTree; ENSGT00390000015035; -.
DR HOGENOM; CLU_1277285_0_0_1; -.
DR InParanoid; Q96EH3; -.
DR OMA; HLKCKHD; -.
DR OrthoDB; 1590818at2759; -.
DR PhylomeDB; Q96EH3; -.
DR TreeFam; TF326763; -.
DR PathwayCommons; Q96EH3; -.
DR SignaLink; Q96EH3; -.
DR BioGRID-ORCS; 115416; 96 hits in 1078 CRISPR screens.
DR ChiTaRS; MALSU1; human.
DR GeneWiki; C7orf30; -.
DR GenomeRNAi; 115416; -.
DR Pharos; Q96EH3; Tbio.
DR PRO; PR:Q96EH3; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96EH3; protein.
DR Bgee; ENSG00000156928; Expressed in sperm and 190 other tissues.
DR Genevisible; Q96EH3; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central.
DR GO; GO:0070130; P:negative regulation of mitochondrial translation; IDA:UniProtKB.
DR GO; GO:0090071; P:negative regulation of ribosome biogenesis; IBA:GO_Central.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:UniProtKB.
DR Gene3D; 3.30.460.10; -; 1.
DR HAMAP; MF_01477; Iojap_RsfS; 1.
DR InterPro; IPR004394; Iojap/RsfS/C7orf30.
DR InterPro; IPR043519; NT_sf.
DR PANTHER; PTHR21043; PTHR21043; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR00090; rsfS_iojap_ybeB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..234
FT /note="Mitochondrial assembly of ribosomal large subunit
FT protein 1"
FT /id="PRO_0000228108"
FT REGION 63..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 132..149
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:5OOM"
SQ SEQUENCE 234 AA; 26170 MW; D0B1CD0C9562FF2A CRC64;
MGPGGRVARL LAPLMWRRAV SSVAGSAVGA EPGLRLLAVQ RLPVGAAFCR ACQTPNFVRG
LHSEPGLEER AEGTVNEGRP ESDAADHTGP KFDIDMMVSL LRQENARDIC VIQVPPEMRY
TDYFVIVSGT STRHLHAMAF YVVKMYKHLK CKRDPHVKIE GKDTDDWLCV DFGSMVIHLM
LPETREIYEL EKLWTLRSYD DQLAQIAPET VPEDFILGIE DDTSSVTPVE LKCE
