RS14_HUMAN
ID RS14_HUMAN Reviewed; 151 AA.
AC P62263; B2R5G5; D3DQG5; P06366; Q5BJI0;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=40S ribosomal protein S14;
DE AltName: Full=Small ribosomal subunit protein uS11 {ECO:0000303|PubMed:24524803};
GN Name=RPS14; ORFNames=PRO2640;
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 [GENOMIC DNA].
RX PubMed=3529092; DOI=10.1073/pnas.83.18.6907;
RA Chen I.-T., Dixit A., Rhoads D.D., Roufa D.J.;
RT "Homologous ribosomal proteins in bacteria, yeast, and humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6907-6911(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3785212; DOI=10.1128/mcb.6.8.2774-2783.1986;
RA Rhoads D.D., Dixit A., Roufa D.J.;
RT "Primary structure of human ribosomal protein S14 and the gene that encodes
RT it.";
RL Mol. Cell. Biol. 6:2774-2783(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 121 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, Placenta, and Skin;
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 PROTEIN SEQUENCE OF 2-15.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A.,
RA Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [8]
RP MUTAGENESIS.
RX PubMed=1549121; DOI=10.1128/mcb.12.4.1680-1686.1992;
RA Diaz J.-J., Roufa D.J.;
RT "Fine-structure map of the human ribosomal protein gene RPS14.";
RL Mol. Cell. Biol. 12:1680-1686(1992).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP 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 [17]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
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 [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-61; LYS-63 AND LYS-106, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- INTERACTION:
CC P62263; Q9Y3D8: AK6; NbExp=4; IntAct=EBI-352783, EBI-2896123;
CC P62263; Q13601: KRR1; NbExp=4; IntAct=EBI-352783, EBI-744525;
CC P62263; O00233: PSMD9; NbExp=3; IntAct=EBI-352783, EBI-750973;
CC P62263; P61247: RPS3A; NbExp=2; IntAct=EBI-352783, EBI-352378;
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS11 family.
CC {ECO:0000305}.
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DR EMBL; M13934; AAB59505.1; -; Genomic_DNA.
DR EMBL; AF116710; AAF71130.1; -; mRNA.
DR EMBL; AK312179; BAG35112.1; -; mRNA.
DR EMBL; CH471062; EAW61723.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61724.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61725.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61726.1; -; Genomic_DNA.
DR EMBL; BC001126; AAH01126.1; -; mRNA.
DR EMBL; BC003401; AAH03401.1; -; mRNA.
DR EMBL; BC006784; AAH06784.1; -; mRNA.
DR EMBL; BC020515; AAH20515.1; -; mRNA.
DR EMBL; BC091474; AAH91474.1; -; mRNA.
DR CCDS; CCDS4307.1; -.
DR PIR; A25220; A25220.
DR RefSeq; NP_001020241.1; NM_001025070.1.
DR RefSeq; NP_001020242.1; NM_001025071.1.
DR RefSeq; NP_005608.1; NM_005617.3.
DR PDB; 4UG0; EM; -; SO=1-151.
DR PDB; 4V6X; EM; 5.00 A; AO=1-151.
DR PDB; 5A2Q; EM; 3.90 A; O=1-151.
DR PDB; 5AJ0; EM; 3.50 A; BO=1-151.
DR PDB; 5FLX; EM; 3.90 A; O=1-151.
DR PDB; 5LKS; EM; 3.60 A; SO=1-151.
DR PDB; 5OA3; EM; 4.30 A; O=1-151.
DR PDB; 5T2C; EM; 3.60 A; AO=1-151.
DR PDB; 5VYC; X-ray; 6.00 A; O1/O2/O3/O4/O5/O6=1-151.
DR PDB; 6FEC; EM; 6.30 A; j=16-151.
DR PDB; 6G18; EM; 3.60 A; O=1-151.
DR PDB; 6G4S; EM; 4.00 A; O=1-151.
DR PDB; 6G4W; EM; 4.50 A; O=1-151.
DR PDB; 6G51; EM; 4.10 A; O=1-151.
DR PDB; 6G53; EM; 4.50 A; O=1-151.
DR PDB; 6G5H; EM; 3.60 A; O=1-151.
DR PDB; 6G5I; EM; 3.50 A; O=1-151.
DR PDB; 6IP5; EM; 3.90 A; 3L=1-151.
DR PDB; 6IP6; EM; 4.50 A; 3L=1-151.
DR PDB; 6IP8; EM; 3.90 A; 3L=1-151.
DR PDB; 6OLE; EM; 3.10 A; SO=15-151.
DR PDB; 6OLF; EM; 3.90 A; SO=15-151.
DR PDB; 6OLG; EM; 3.40 A; BO=16-151.
DR PDB; 6OLI; EM; 3.50 A; SO=15-151.
DR PDB; 6OLZ; EM; 3.90 A; BO=16-151.
DR PDB; 6OM0; EM; 3.10 A; SO=15-151.
DR PDB; 6OM7; EM; 3.70 A; SO=15-151.
DR PDB; 6QZP; EM; 2.90 A; SO=12-151.
DR PDB; 6XA1; EM; 2.80 A; SO=17-151.
DR PDB; 6Y0G; EM; 3.20 A; SO=1-151.
DR PDB; 6Y2L; EM; 3.00 A; SO=1-151.
DR PDB; 6Y57; EM; 3.50 A; SO=1-151.
DR PDB; 6YBD; EM; 3.30 A; P=1-151.
DR PDB; 6YBW; EM; 3.10 A; P=1-151.
DR PDB; 6Z6L; EM; 3.00 A; SO=1-151.
DR PDB; 6Z6M; EM; 3.10 A; SO=1-151.
DR PDB; 6Z6N; EM; 2.90 A; SO=1-151.
DR PDB; 6ZLW; EM; 2.60 A; P=1-151.
DR PDB; 6ZM7; EM; 2.70 A; SO=1-151.
DR PDB; 6ZME; EM; 3.00 A; SO=1-151.
DR PDB; 6ZMI; EM; 2.60 A; SO=1-151.
DR PDB; 6ZMO; EM; 3.10 A; SO=1-151.
DR PDB; 6ZMT; EM; 3.00 A; P=1-151.
DR PDB; 6ZMW; EM; 3.70 A; P=1-151.
DR PDB; 6ZN5; EM; 3.20 A; P=17-151.
DR PDB; 6ZOJ; EM; 2.80 A; O=1-151.
DR PDB; 6ZOK; EM; 2.80 A; O=1-151.
DR PDB; 6ZON; EM; 3.00 A; i=1-151.
DR PDB; 6ZP4; EM; 2.90 A; i=1-151.
DR PDB; 6ZUO; EM; 3.10 A; O=1-151.
DR PDB; 6ZV6; EM; 2.90 A; O=1-151.
DR PDB; 6ZVH; EM; 2.90 A; O=12-151.
DR PDB; 6ZXD; EM; 3.20 A; O=1-151.
DR PDB; 6ZXE; EM; 3.00 A; O=1-151.
DR PDB; 6ZXF; EM; 3.70 A; O=1-151.
DR PDB; 6ZXG; EM; 2.60 A; O=1-151.
DR PDB; 6ZXH; EM; 2.70 A; O=1-151.
DR PDB; 7A09; EM; 3.50 A; i=1-151.
DR PDB; 7K5I; EM; 2.90 A; O=1-151.
DR PDB; 7MQ8; EM; 3.60 A; NG=1-151.
DR PDB; 7MQ9; EM; 3.87 A; NG=1-151.
DR PDB; 7MQA; EM; 2.70 A; NG=1-151.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5FLX; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5OA3; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 5VYC; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6G18; -.
DR PDBsum; 6G4S; -.
DR PDBsum; 6G4W; -.
DR PDBsum; 6G51; -.
DR PDBsum; 6G53; -.
DR PDBsum; 6G5H; -.
DR PDBsum; 6G5I; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6YBD; -.
DR PDBsum; 6YBW; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZLW; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZMT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOK; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZUO; -.
DR PDBsum; 6ZV6; -.
DR PDBsum; 6ZVH; -.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR PDBsum; 7A09; -.
DR PDBsum; 7K5I; -.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; P62263; -.
DR SMR; P62263; -.
DR BioGRID; 112122; 408.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62263; -.
DR IntAct; P62263; 159.
DR MINT; P62263; -.
DR STRING; 9606.ENSP00000385958; -.
DR MoonProt; P62263; -.
DR GlyGen; P62263; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62263; -.
DR MetOSite; P62263; -.
DR PhosphoSitePlus; P62263; -.
DR SwissPalm; P62263; -.
DR BioMuta; RPS14; -.
DR DMDM; 50403752; -.
DR SWISS-2DPAGE; P62263; -.
DR EPD; P62263; -.
DR jPOST; P62263; -.
DR MassIVE; P62263; -.
DR MaxQB; P62263; -.
DR PaxDb; P62263; -.
DR PeptideAtlas; P62263; -.
DR PRIDE; P62263; -.
DR ProteomicsDB; 57379; -.
DR TopDownProteomics; P62263; -.
DR Antibodypedia; 1243; 266 antibodies from 29 providers.
DR DNASU; 6208; -.
DR Ensembl; ENST00000312037.6; ENSP00000311028.5; ENSG00000164587.13.
DR Ensembl; ENST00000401695.8; ENSP00000385958.3; ENSG00000164587.13.
DR Ensembl; ENST00000407193.7; ENSP00000385425.1; ENSG00000164587.13.
DR Ensembl; ENST00000521466.5; ENSP00000428509.1; ENSG00000164587.13.
DR GeneID; 6208; -.
DR KEGG; hsa:6208; -.
DR MANE-Select; ENST00000407193.7; ENSP00000385425.1; NM_005617.4; NP_005608.1.
DR UCSC; uc003lsh.4; human.
DR CTD; 6208; -.
DR DisGeNET; 6208; -.
DR GeneCards; RPS14; -.
DR HGNC; HGNC:10387; RPS14.
DR HPA; ENSG00000164587; Low tissue specificity.
DR MalaCards; RPS14; -.
DR MIM; 130620; gene.
DR neXtProt; NX_P62263; -.
DR OpenTargets; ENSG00000164587; -.
DR Orphanet; 86841; Myelodysplastic syndrome associated with isolated del(5q) chromosome abnormality.
DR PharmGKB; PA34786; -.
DR VEuPathDB; HostDB:ENSG00000164587; -.
DR eggNOG; KOG0407; Eukaryota.
DR GeneTree; ENSGT00390000000703; -.
DR HOGENOM; CLU_072439_6_0_1; -.
DR InParanoid; P62263; -.
DR OMA; KWGVAHI; -.
DR OrthoDB; 1408000at2759; -.
DR PhylomeDB; P62263; -.
DR TreeFam; TF300125; -.
DR PathwayCommons; P62263; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P62263; -.
DR SIGNOR; P62263; -.
DR BioGRID-ORCS; 6208; 770 hits in 1053 CRISPR screens.
DR ChiTaRS; RPS14; human.
DR GeneWiki; RPS14; -.
DR GenomeRNAi; 6208; -.
DR Pharos; P62263; Tbio.
DR PRO; PR:P62263; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P62263; protein.
DR Bgee; ENSG00000164587; Expressed in upper leg skin and 212 other tissues.
DR ExpressionAtlas; P62263; baseline and differential.
DR Genevisible; P62263; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0045182; F:translation regulator activity; IMP:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0030490; P:maturation of SSU-rRNA; ISS:UniProtKB.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IMP:UniProtKB.
DR Gene3D; 3.30.420.80; -; 1.
DR HAMAP; MF_01310; Ribosomal_S11; 1.
DR InterPro; IPR001971; Ribosomal_S11.
DR InterPro; IPR018102; Ribosomal_S11_CS.
DR InterPro; IPR036967; Ribosomal_S11_sf.
DR PANTHER; PTHR11759; PTHR11759; 1.
DR Pfam; PF00411; Ribosomal_S11; 1.
DR PIRSF; PIRSF002131; Ribosomal_S11; 1.
DR PROSITE; PS00054; RIBOSOMAL_S11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8706699"
FT CHAIN 2..151
FT /note="40S ribosomal protein S14"
FT /id="PRO_0000123337"
FT REGION 131..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 133
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:6ZVH"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6ZOJ"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 47..57
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:6ZMT"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:6YBW"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:6ZLW"
SQ SEQUENCE 151 AA; 16273 MW; 4F4387F9FADAC278 CRC64;
MAPRKGKEKK EEQVISLGPQ VAEGENVFGV CHIFASFNDT FVHVTDLSGK ETICRVTGGM
KVKADRDESS PYAAMLAAQD VAQRCKELGI TALHIKLRAT GGNRTKTPGP GAQSALRALA
RSGMKIGRIE DVTPIPSDST RRKGGRRGRR L
