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RM30_HUMAN
ID   RM30_HUMAN              Reviewed;         161 AA.
AC   Q8TCC3; A6NIC6; D3DVI0; D3DVI3; Q0D2Q7; Q6ZTP4; Q96Q69; Q9P0N0;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=39S ribosomal protein L30, mitochondrial;
DE            Short=L30mt;
DE            Short=MRP-L30;
DE   AltName: Full=39S ribosomal protein L28, mitochondrial;
DE            Short=L28mt;
DE            Short=MRP-L28;
DE   AltName: Full=Mitochondrial large ribosomal subunit protein uL30m {ECO:0000303|PubMed:25278503};
DE   Flags: Precursor;
GN   Name=MRPL30; Synonyms=MRPL28, RPML28; ORFNames=HSPC249;
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] (ISOFORM 3).
RC   TISSUE=Umbilical cord blood;
RX   PubMed=11042152; DOI=10.1101/gr.140200;
RA   Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA   Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA   Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT   "Cloning and functional analysis of cDNAs with open reading frames for 300
RT   previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT   cells.";
RL   Genome Res. 10:1546-1560(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-130.
RC   TISSUE=Uterus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-130.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-130.
RC   TISSUE=Brain, and Kidney;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-161.
RX   PubMed=11543634; DOI=10.1006/geno.2001.6622;
RA   Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S.,
RA   Watanabe K., Tanaka T.;
RT   "The human mitochondrial ribosomal protein genes: mapping of 54 genes to
RT   the chromosomes and implications for human disorders.";
RL   Genomics 77:65-70(2001).
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   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   [9] {ECO:0007744|PDB:3J7Y}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBCELLULAR LOCATION,
RP   AND SUBUNIT.
RX   PubMed=25278503; DOI=10.1126/science.1258026;
RA   Brown A., Amunts A., Bai X.C., Sugimoto Y., Edwards P.C., Murshudov G.,
RA   Scheres S.H., Ramakrishnan V.;
RT   "Structure of the large ribosomal subunit from human mitochondria.";
RL   Science 346:718-722(2014).
RN   [10] {ECO:0007744|PDB:3J9M}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR LOCATION,
RP   AND SUBUNIT.
RX   PubMed=25838379; DOI=10.1126/science.aaa1193;
RA   Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.;
RT   "Ribosome. The structure of the human mitochondrial ribosome.";
RL   Science 348:95-98(2015).
RN   [11] {ECO:0007744|PDB:5OOL, ECO:0007744|PDB:5OOM}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), SUBCELLULAR LOCATION,
RP   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   -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC       LSU) (PubMed:28892042, PubMed:25838379, PubMed:25278503). Mature
CC       mammalian 55S mitochondrial ribosomes consist of a small (28S) and a
CC       large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA
CC       (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains
CC       a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA
CC       (mt-tRNA(Val)), which plays an integral structural role, and 52
CC       different proteins. {ECO:0000269|PubMed:25278503,
CC       ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC       ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8TCC3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8TCC3-2; Sequence=VSP_021746;
CC       Name=3;
CC         IsoId=Q8TCC3-3; Sequence=VSP_021747;
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL30 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF36169.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF151083; AAF36169.1; ALT_FRAME; mRNA.
DR   EMBL; AK126402; BAC86542.1; -; mRNA.
DR   EMBL; AC092587; AAX88929.1; -; Genomic_DNA.
DR   EMBL; CH471127; EAX01876.1; -; Genomic_DNA.
DR   EMBL; CH471127; EAX01878.1; -; Genomic_DNA.
DR   EMBL; CH471127; EAX01880.1; -; Genomic_DNA.
DR   EMBL; CH471127; EAX01881.1; -; Genomic_DNA.
DR   EMBL; CH471127; EAX01882.1; -; Genomic_DNA.
DR   EMBL; CH471127; EAX01883.1; -; Genomic_DNA.
DR   EMBL; BC000217; AAH00217.1; -; mRNA.
DR   EMBL; BC022391; AAH22391.1; -; mRNA.
DR   EMBL; AB051342; BAB54932.1; -; Genomic_DNA.
DR   CCDS; CCDS2041.1; -. [Q8TCC3-1]
DR   RefSeq; NP_660213.1; NM_145212.3. [Q8TCC3-1]
DR   PDB; 3J7Y; EM; 3.40 A; Z=1-161.
DR   PDB; 3J9M; EM; 3.50 A; Z=1-161.
DR   PDB; 5OOL; EM; 3.06 A; Z=1-161.
DR   PDB; 5OOM; EM; 3.03 A; Z=1-161.
DR   PDB; 6I9R; EM; 3.90 A; Z=1-161.
DR   PDB; 6NU2; EM; 3.90 A; Z=35-154.
DR   PDB; 6NU3; EM; 4.40 A; Z=1-161.
DR   PDB; 6VLZ; EM; 2.97 A; Z=1-161.
DR   PDB; 6VMI; EM; 2.96 A; Z=1-161.
DR   PDB; 6ZM5; EM; 2.89 A; Z=1-161.
DR   PDB; 6ZM6; EM; 2.59 A; Z=1-161.
DR   PDB; 6ZS9; EM; 4.00 A; XZ=1-161.
DR   PDB; 6ZSA; EM; 4.00 A; XZ=1-161.
DR   PDB; 6ZSB; EM; 4.50 A; XZ=1-161.
DR   PDB; 6ZSC; EM; 3.50 A; XZ=1-161.
DR   PDB; 6ZSD; EM; 3.70 A; XZ=1-161.
DR   PDB; 6ZSE; EM; 5.00 A; XZ=1-161.
DR   PDB; 6ZSG; EM; 4.00 A; XZ=1-161.
DR   PDB; 7A5F; EM; 4.40 A; Z3=1-161.
DR   PDB; 7A5G; EM; 4.33 A; Z3=1-161.
DR   PDB; 7A5H; EM; 3.30 A; Z=1-161.
DR   PDB; 7A5I; EM; 3.70 A; Z3=1-161.
DR   PDB; 7A5J; EM; 3.10 A; Z=1-161.
DR   PDB; 7A5K; EM; 3.70 A; Z3=1-161.
DR   PDB; 7L08; EM; 3.49 A; Z=1-161.
DR   PDB; 7L20; EM; 3.15 A; Z=1-161.
DR   PDB; 7O9K; EM; 3.10 A; Z=1-161.
DR   PDB; 7O9M; EM; 2.50 A; Z=1-161.
DR   PDB; 7ODR; EM; 2.90 A; Z=1-161.
DR   PDB; 7ODS; EM; 3.10 A; Z=1-161.
DR   PDB; 7ODT; EM; 3.10 A; Z=1-161.
DR   PDB; 7OF0; EM; 2.20 A; Z=1-161.
DR   PDB; 7OF2; EM; 2.70 A; Z=1-161.
DR   PDB; 7OF3; EM; 2.70 A; Z=1-161.
DR   PDB; 7OF4; EM; 2.70 A; Z=1-161.
DR   PDB; 7OF5; EM; 2.90 A; Z=1-161.
DR   PDB; 7OF6; EM; 2.60 A; Z=1-161.
DR   PDB; 7OF7; EM; 2.50 A; Z=1-161.
DR   PDB; 7OG4; EM; 3.80 A; XZ=1-161.
DR   PDB; 7OI6; EM; 5.70 A; Z=1-161.
DR   PDB; 7OI7; EM; 3.50 A; Z=1-161.
DR   PDB; 7OI8; EM; 3.50 A; Z=1-161.
DR   PDB; 7OI9; EM; 3.30 A; Z=1-161.
DR   PDB; 7OIA; EM; 3.20 A; Z=1-161.
DR   PDB; 7OIB; EM; 3.30 A; Z=1-161.
DR   PDB; 7OIC; EM; 3.10 A; Z=1-161.
DR   PDB; 7OID; EM; 3.70 A; Z=1-161.
DR   PDB; 7OIE; EM; 3.50 A; Z=1-161.
DR   PDB; 7PD3; EM; 3.40 A; Z=1-161.
DR   PDB; 7QH6; EM; 3.08 A; Z=1-161.
DR   PDBsum; 3J7Y; -.
DR   PDBsum; 3J9M; -.
DR   PDBsum; 5OOL; -.
DR   PDBsum; 5OOM; -.
DR   PDBsum; 6I9R; -.
DR   PDBsum; 6NU2; -.
DR   PDBsum; 6NU3; -.
DR   PDBsum; 6VLZ; -.
DR   PDBsum; 6VMI; -.
DR   PDBsum; 6ZM5; -.
DR   PDBsum; 6ZM6; -.
DR   PDBsum; 6ZS9; -.
DR   PDBsum; 6ZSA; -.
DR   PDBsum; 6ZSB; -.
DR   PDBsum; 6ZSC; -.
DR   PDBsum; 6ZSD; -.
DR   PDBsum; 6ZSE; -.
DR   PDBsum; 6ZSG; -.
DR   PDBsum; 7A5F; -.
DR   PDBsum; 7A5G; -.
DR   PDBsum; 7A5H; -.
DR   PDBsum; 7A5I; -.
DR   PDBsum; 7A5J; -.
DR   PDBsum; 7A5K; -.
DR   PDBsum; 7L08; -.
DR   PDBsum; 7L20; -.
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; 7OF4; -.
DR   PDBsum; 7OF5; -.
DR   PDBsum; 7OF6; -.
DR   PDBsum; 7OF7; -.
DR   PDBsum; 7OG4; -.
DR   PDBsum; 7OI6; -.
DR   PDBsum; 7OI7; -.
DR   PDBsum; 7OI8; -.
DR   PDBsum; 7OI9; -.
DR   PDBsum; 7OIA; -.
DR   PDBsum; 7OIB; -.
DR   PDBsum; 7OIC; -.
DR   PDBsum; 7OID; -.
DR   PDBsum; 7OIE; -.
DR   PDBsum; 7PD3; -.
DR   PDBsum; 7QH6; -.
DR   AlphaFoldDB; Q8TCC3; -.
DR   SMR; Q8TCC3; -.
DR   BioGRID; 119417; 162.
DR   ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR   CORUM; Q8TCC3; -.
DR   IntAct; Q8TCC3; 27.
DR   MINT; Q8TCC3; -.
DR   STRING; 9606.ENSP00000338057; -.
DR   GlyGen; Q8TCC3; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8TCC3; -.
DR   PhosphoSitePlus; Q8TCC3; -.
DR   BioMuta; MRPL30; -.
DR   DMDM; 74730583; -.
DR   EPD; Q8TCC3; -.
DR   jPOST; Q8TCC3; -.
DR   MassIVE; Q8TCC3; -.
DR   MaxQB; Q8TCC3; -.
DR   PaxDb; Q8TCC3; -.
DR   PeptideAtlas; Q8TCC3; -.
DR   PRIDE; Q8TCC3; -.
DR   TopDownProteomics; Q8TCC3-1; -. [Q8TCC3-1]
DR   TopDownProteomics; Q8TCC3-2; -. [Q8TCC3-2]
DR   TopDownProteomics; Q8TCC3-3; -. [Q8TCC3-3]
DR   Antibodypedia; 65219; 68 antibodies from 17 providers.
DR   DNASU; 51263; -.
DR   Ensembl; ENST00000338148.8; ENSP00000338057.3; ENSG00000185414.20. [Q8TCC3-1]
DR   Ensembl; ENST00000409841.1; ENSP00000386752.1; ENSG00000185414.20. [Q8TCC3-1]
DR   GeneID; 51263; -.
DR   KEGG; hsa:51263; -.
DR   MANE-Select; ENST00000338148.8; ENSP00000338057.3; NM_145212.4; NP_660213.1.
DR   UCSC; uc002szv.4; human. [Q8TCC3-1]
DR   CTD; 51263; -.
DR   DisGeNET; 51263; -.
DR   GeneCards; MRPL30; -.
DR   HGNC; HGNC:14036; MRPL30.
DR   HPA; ENSG00000185414; Low tissue specificity.
DR   MIM; 611838; gene.
DR   neXtProt; NX_Q8TCC3; -.
DR   OpenTargets; ENSG00000185414; -.
DR   PharmGKB; PA30961; -.
DR   VEuPathDB; HostDB:ENSG00000185414; -.
DR   eggNOG; KOG4799; Eukaryota.
DR   GeneTree; ENSGT00390000016769; -.
DR   GeneTree; ENSGT00940000163829; -.
DR   HOGENOM; CLU_139849_0_0_1; -.
DR   InParanoid; Q8TCC3; -.
DR   OMA; VESFICT; -.
DR   OrthoDB; 1446797at2759; -.
DR   PhylomeDB; Q8TCC3; -.
DR   TreeFam; TF314611; -.
DR   PathwayCommons; Q8TCC3; -.
DR   Reactome; R-HSA-5368286; Mitochondrial translation initiation.
DR   Reactome; R-HSA-5389840; Mitochondrial translation elongation.
DR   Reactome; R-HSA-5419276; Mitochondrial translation termination.
DR   SignaLink; Q8TCC3; -.
DR   SIGNOR; Q8TCC3; -.
DR   BioGRID-ORCS; 51263; 141 hits in 1047 CRISPR screens.
DR   ChiTaRS; MRPL30; human.
DR   GeneWiki; MRPL30; -.
DR   GenomeRNAi; 51263; -.
DR   Pharos; Q8TCC3; Tdark.
DR   PRO; PR:Q8TCC3; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q8TCC3; protein.
DR   Bgee; ENSG00000185414; Expressed in tibialis anterior and 191 other tissues.
DR   ExpressionAtlas; Q8TCC3; baseline and differential.
DR   Genevisible; Q8TCC3; HS.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR   CDD; cd01658; Ribosomal_L30; 1.
DR   Gene3D; 3.30.1390.20; -; 1.
DR   InterPro; IPR036919; L30_ferredoxin-like_sf.
DR   InterPro; IPR005996; Ribosomal_L30_bac-type.
DR   InterPro; IPR016082; Ribosomal_L30_ferredoxin-like.
DR   PANTHER; PTHR15892; PTHR15892; 1.
DR   Pfam; PF00327; Ribosomal_L30; 1.
DR   SUPFAM; SSF55129; SSF55129; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Mitochondrion; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT         1..34
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           35..161
FT                   /note="39S ribosomal protein L30, mitochondrial"
FT                   /id="PRO_0000261649"
FT   VAR_SEQ         1
FT                   /note="M -> MSSTLGKLSNQVEETLPLLKKPLKRAITTLM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_021746"
FT   VAR_SEQ         119..161
FT                   /note="IKPLKLPQGLPAEENMSNTCLKSTGELVVQWHLKPVEQKAHES -> FVVSS
FT                   QLFLKCIA (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11042152"
FT                   /id="VSP_021747"
FT   VARIANT         130
FT                   /note="A -> T (in dbSNP:rs1044575)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT                   /id="VAR_034462"
FT   CONFLICT        45
FT                   /note="V -> A (in Ref. 2; BAC86542)"
FT                   /evidence="ECO:0000305"
FT   HELIX           43..46
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           50..56
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          60..62
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          65..71
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          75..78
FT                   /evidence="ECO:0007829|PDB:7OI9"
FT   HELIX           80..89
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:7OI8"
FT   STRAND          98..101
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           104..112
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   TURN            113..115
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          116..121
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   TURN            132..135
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          143..147
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   STRAND          151..153
FT                   /evidence="ECO:0007829|PDB:7OIA"
SQ   SEQUENCE   161 AA;  18546 MW;  E818AD8B8AA7DD23 CRC64;
     MAGILRLVVQ WPPGRLQTVT KGVESLICTD WIRHKFTRSR IPEKVFQASP EDHEKYGGDP
     QNPHKLHIVT RIKSTRRRPY WEKDIIKMLG LEKAHTPQVH KNIPSVNAKL KVVKHLIRIK
     PLKLPQGLPA EENMSNTCLK STGELVVQWH LKPVEQKAHE S
 
 
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