RS27_HUMAN
ID RS27_HUMAN Reviewed; 84 AA.
AC P42677; Q5T4L6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 221.
DE RecName: Full=40S ribosomal protein S27;
DE AltName: Full=Metallopan-stimulin 1;
DE Short=MPS-1;
DE AltName: Full=Small ribosomal subunit protein eS27 {ECO:0000303|PubMed:24524803};
GN Name=RPS27; Synonyms=MPS1;
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].
RC TISSUE=Mammary carcinoma;
RX PubMed=8407955; DOI=10.1016/s0021-9258(19)36910-8;
RA Fernandez-Pol J.A., Klos D.J., Hamilton P.D.;
RT "A growth factor-inducible gene encodes a novel nuclear protein with zinc
RT finger structure.";
RL J. Biol. Chem. 268:21198-21204(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=8908372; DOI=10.1080/15216549600201203;
RA Tsui S.K.W., Lee S.M.Y., Fung K.P., Waye M.M.Y., Lee C.Y.;
RT "Primary structures and sequence analysis of human ribosomal proteins L39
RT and S27.";
RL Biochem. Mol. Biol. Int. 40:611-616(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative analysis of
RT 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [8]
RP PROTEIN SEQUENCE OF 2-11, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP FUNCTION.
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-74.
RX PubMed=9582194; DOI=10.1101/gr.8.5.509;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J.,
RA Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, 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 IDENTIFICATION BY 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 FUNCTION, AND INVOLVEMENT IN DBA17.
RX PubMed=25424902; DOI=10.1111/bjh.13229;
RA Wang R., Yoshida K., Toki T., Sawada T., Uechi T., Okuno Y.,
RA Sato-Otsubo A., Kudo K., Kamimaki I., Kanezaki R., Shiraishi Y., Chiba K.,
RA Tanaka H., Terui K., Sato T., Iribe Y., Ohga S., Kuramitsu M.,
RA Hamaguchi I., Ohara A., Hara J., Goi K., Matsubara K., Koike K.,
RA Ishiguro A., Okamoto Y., Watanabe K., Kanno H., Kojima S., Miyano S.,
RA Kenmochi N., Ogawa S., Ito E.;
RT "Loss of function mutations in RPL27 and RPS27 identified by whole-exome
RT sequencing in Diamond-Blackfan anaemia.";
RL Br. J. Haematol. 168:854-864(2015).
RN [20]
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 -!- FUNCTION: Component of the small ribosomal subunit (PubMed:8706699).
CC Required for proper rRNA processing and maturation of 18S rRNAs
CC (PubMed:25424902). {ECO:0000269|PubMed:25424902,
CC ECO:0000305|PubMed:8706699}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBUNIT: Component of the small ribosomal subunit.
CC {ECO:0000305|PubMed:8706699}.
CC -!- INTERACTION:
CC P42677; P54132: BLM; NbExp=4; IntAct=EBI-356336, EBI-621372;
CC P42677; Q5S007: LRRK2; NbExp=4; IntAct=EBI-356336, EBI-5323863;
CC P42677; Q00987: MDM2; NbExp=5; IntAct=EBI-356336, EBI-389668;
CC P42677; P61289: PSME3; NbExp=3; IntAct=EBI-356336, EBI-355546;
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of actively
CC proliferating cells and tumor tissues.
CC -!- DISEASE: Diamond-Blackfan anemia 17 (DBA17) [MIM:617409]: A form of
CC Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic
CC anemia that usually presents early in infancy. Diamond-Blackfan anemia
CC is characterized by a moderate to severe macrocytic anemia,
CC erythroblastopenia, and an increased risk of malignancy. 30 to 40% of
CC Diamond-Blackfan anemia patients present with short stature and
CC congenital anomalies, the most frequent being craniofacial (Pierre-
CC Robin syndrome and cleft palate), thumb and urogenital anomalies.
CC {ECO:0000269|PubMed:25424902}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS27 family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:8407955) thought to be a protein that
CC could have played a role as a potentially important mediator of
CC cellular proliferative responses to various growth factors and other
CC environmental signals. Capable of specific binding to a cAMP response
CC element in DNA. {ECO:0000305|PubMed:8407955}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RPS27ID45550ch1q21.html";
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DR EMBL; L19739; AAA59867.1; -; mRNA.
DR EMBL; U57847; AAB02266.1; -; mRNA.
DR EMBL; AB061845; BAB79483.1; -; Genomic_DNA.
DR EMBL; AK312070; BAG35006.1; -; mRNA.
DR EMBL; AL358472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53239.1; -; Genomic_DNA.
DR EMBL; CH471055; EAW64624.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88871.1; -; Genomic_DNA.
DR EMBL; BC002658; AAH02658.1; -; mRNA.
DR EMBL; BC070219; AAH70219.1; -; mRNA.
DR EMBL; AB007162; BAA25825.1; -; Genomic_DNA.
DR CCDS; CCDS1059.1; -.
DR PIR; A48045; A48045.
DR RefSeq; NP_001021.1; NM_001030.4.
DR PDB; 4UG0; EM; -; Sb=1-84.
DR PDB; 4V6X; EM; 5.00 A; Ab=1-84.
DR PDB; 5A2Q; EM; 3.90 A; b=2-83.
DR PDB; 5AJ0; EM; 3.50 A; Bb=1-84.
DR PDB; 5FLX; EM; 3.90 A; b=1-84.
DR PDB; 5LKS; EM; 3.60 A; Sb=1-84.
DR PDB; 5OA3; EM; 4.30 A; b=2-83.
DR PDB; 5T2C; EM; 3.60 A; AV=1-84.
DR PDB; 5VYC; X-ray; 6.00 A; b1/b2/b3/b4/b5/b6=1-84.
DR PDB; 6FEC; EM; 6.30 A; Y=1-84.
DR PDB; 6G18; EM; 3.60 A; b=1-84.
DR PDB; 6G4S; EM; 4.00 A; b=1-84.
DR PDB; 6G4W; EM; 4.50 A; b=1-84.
DR PDB; 6G51; EM; 4.10 A; b=1-84.
DR PDB; 6G53; EM; 4.50 A; b=1-84.
DR PDB; 6G5H; EM; 3.60 A; b=1-84.
DR PDB; 6G5I; EM; 3.50 A; b=1-84.
DR PDB; 6IP5; EM; 3.90 A; 3P=1-84.
DR PDB; 6IP6; EM; 4.50 A; 3P=1-84.
DR PDB; 6IP8; EM; 3.90 A; 3P=1-84.
DR PDB; 6OLE; EM; 3.10 A; Sb=2-83.
DR PDB; 6OLF; EM; 3.90 A; Sb=2-83.
DR PDB; 6OLG; EM; 3.40 A; Bb=4-83.
DR PDB; 6OLI; EM; 3.50 A; Sb=2-83.
DR PDB; 6OLZ; EM; 3.90 A; Bb=4-83.
DR PDB; 6OM0; EM; 3.10 A; Sb=2-83.
DR PDB; 6OM7; EM; 3.70 A; Sb=2-83.
DR PDB; 6QZP; EM; 2.90 A; Sb=2-84.
DR PDB; 6XA1; EM; 2.80 A; Sb=2-83.
DR PDB; 6Y0G; EM; 3.20 A; Sb=1-84.
DR PDB; 6Y2L; EM; 3.00 A; Sb=1-84.
DR PDB; 6Y57; EM; 3.50 A; Sb=1-84.
DR PDB; 6YBD; EM; 3.30 A; H=1-84.
DR PDB; 6YBW; EM; 3.10 A; H=1-84.
DR PDB; 6Z6L; EM; 3.00 A; Sb=1-84.
DR PDB; 6Z6M; EM; 3.10 A; Sb=1-84.
DR PDB; 6Z6N; EM; 2.90 A; Sb=1-84.
DR PDB; 6ZLW; EM; 2.60 A; b=1-84.
DR PDB; 6ZM7; EM; 2.70 A; Sb=1-84.
DR PDB; 6ZME; EM; 3.00 A; Sb=1-84.
DR PDB; 6ZMI; EM; 2.60 A; Sb=1-84.
DR PDB; 6ZMO; EM; 3.10 A; Sb=1-84.
DR PDB; 6ZMT; EM; 3.00 A; b=1-84.
DR PDB; 6ZMW; EM; 3.70 A; H=1-84.
DR PDB; 6ZN5; EM; 3.20 A; b=2-83.
DR PDB; 6ZOJ; EM; 2.80 A; b=2-83.
DR PDB; 6ZOK; EM; 2.80 A; b=2-83.
DR PDB; 6ZON; EM; 3.00 A; R=1-84.
DR PDB; 6ZP4; EM; 2.90 A; R=1-84.
DR PDB; 6ZUO; EM; 3.10 A; b=1-84.
DR PDB; 6ZV6; EM; 2.90 A; b=1-84.
DR PDB; 6ZVH; EM; 2.90 A; b=2-84.
DR PDB; 6ZVJ; EM; 3.80 A; R=2-83.
DR PDB; 6ZXD; EM; 3.20 A; b=1-84.
DR PDB; 6ZXE; EM; 3.00 A; b=1-84.
DR PDB; 6ZXF; EM; 3.70 A; b=1-84.
DR PDB; 6ZXG; EM; 2.60 A; b=1-84.
DR PDB; 6ZXH; EM; 2.70 A; b=1-84.
DR PDB; 7A09; EM; 3.50 A; R=1-84.
DR PDB; 7K5I; EM; 2.90 A; b=1-84.
DR PDB; 7MQ8; EM; 3.60 A; NQ=1-84.
DR PDB; 7MQ9; EM; 3.87 A; NQ=1-84.
DR PDB; 7MQA; EM; 2.70 A; NQ=1-84.
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; 6ZVJ; -.
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; P42677; -.
DR SMR; P42677; -.
DR BioGRID; 112146; 273.
DR CORUM; P42677; -.
DR DIP; DIP-44182N; -.
DR IntAct; P42677; 101.
DR MINT; P42677; -.
DR STRING; 9606.ENSP00000357555; -.
DR BindingDB; P42677; -.
DR ChEMBL; CHEMBL1932893; -.
DR GlyGen; P42677; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P42677; -.
DR MetOSite; P42677; -.
DR PhosphoSitePlus; P42677; -.
DR SwissPalm; P42677; -.
DR BioMuta; RPS27; -.
DR DMDM; 1171014; -.
DR EPD; P42677; -.
DR jPOST; P42677; -.
DR MassIVE; P42677; -.
DR PaxDb; P42677; -.
DR PeptideAtlas; P42677; -.
DR PRIDE; P42677; -.
DR ProteomicsDB; 55523; -.
DR TopDownProteomics; P42677; -.
DR Antibodypedia; 20391; 263 antibodies from 33 providers.
DR DNASU; 6232; -.
DR Ensembl; ENST00000651669.1; ENSP00000499044.1; ENSG00000177954.14.
DR GeneID; 6232; -.
DR KEGG; hsa:6232; -.
DR MANE-Select; ENST00000651669.1; ENSP00000499044.1; NM_001030.6; NP_001021.1.
DR UCSC; uc001fdv.4; human.
DR CTD; 6232; -.
DR DisGeNET; 6232; -.
DR GeneCards; RPS27; -.
DR GeneReviews; RPS27; -.
DR HGNC; HGNC:10416; RPS27.
DR HPA; ENSG00000177954; Low tissue specificity.
DR MalaCards; RPS27; -.
DR MIM; 603702; gene.
DR MIM; 617409; phenotype.
DR neXtProt; NX_P42677; -.
DR OpenTargets; ENSG00000177954; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34820; -.
DR VEuPathDB; HostDB:ENSG00000177954; -.
DR eggNOG; KOG1779; Eukaryota.
DR GeneTree; ENSGT00950000182891; -.
DR HOGENOM; CLU_130128_3_0_1; -.
DR InParanoid; P42677; -.
DR OMA; VYSHANT; -.
DR OrthoDB; 1537724at2759; -.
DR PhylomeDB; P42677; -.
DR TreeFam; TF300265; -.
DR PathwayCommons; P42677; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
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-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
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-9648025; EML4 and NUDC in mitotic spindle formation.
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; P42677; -.
DR SIGNOR; P42677; -.
DR BioGRID-ORCS; 6232; 418 hits in 634 CRISPR screens.
DR ChiTaRS; RPS27; human.
DR GeneWiki; RPS27; -.
DR GenomeRNAi; 6232; -.
DR Pharos; P42677; Tchem.
DR PRO; PR:P42677; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P42677; protein.
DR Bgee; ENSG00000177954; Expressed in ganglionic eminence and 94 other tissues.
DR ExpressionAtlas; P42677; baseline and differential.
DR Genevisible; P42677; HS.
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:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0005840; C:ribosome; NAS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR Gene3D; 2.20.25.100; -; 1.
DR HAMAP; MF_00371; Ribosomal_S27e; 1.
DR InterPro; IPR000592; Ribosomal_S27.
DR InterPro; IPR023407; Ribosomal_S27_Zn-bd_dom_sf.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR PANTHER; PTHR11594; PTHR11594; 1.
DR Pfam; PF01667; Ribosomal_S27e; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
DR PROSITE; PS01168; RIBOSOMAL_S27E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Diamond-Blackfan anemia; Direct protein sequencing;
KW Metal-binding; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8706699"
FT CHAIN 2..84
FT /note="40S ribosomal protein S27"
FT /id="PRO_0000149051"
FT ZN_FING 37..59
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CONFLICT 5
FT /note="K -> R (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6ZMT"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:6ZLW"
SQ SEQUENCE 84 AA; 9461 MW; 242C4466AC8A8900 CRC64;
MPLAKDLLHP SPEEEKRKHK KKRLVQSPNS YFMDVKCPGC YKITTVFSHA QTVVLCVGCS
TVLCQPTGGK ARLTEGCSFR RKQH
