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   27-MAR-2024, entry version 230.
DE   RecName: Full=Small ribosomal subunit protein eS27 {ECO:0000303|PubMed:24524803};
DE   AltName: Full=40S ribosomal protein S27;
DE   AltName: Full=Metallopan-stimulin 1;
DE            Short=MPS-1;
GN   Name=RPS27 {ECO:0000312|HGNC:HGNC:10416}; 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], AND TISSUE SPECIFICITY.
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) OF 80S RIBOSOME, FUNCTION,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
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).
RN   [21] {ECO:0007744|PDB:7MQ8, ECO:0007744|PDB:7MQ9, ECO:0007744|PDB:7MQA}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=34516797; DOI=10.1126/science.abj5338;
RA   Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.;
RT   "Nucleolar maturation of the human small subunit processome.";
RL   Science 373:eabj5338-eabj5338(2021).
CC   -!- FUNCTION: Component of the small ribosomal subunit (PubMed:8706699,
CC       PubMed:23636399). The ribosome is a large ribonucleoprotein complex
CC       responsible for the synthesis of proteins in the cell
CC       (PubMed:23636399). Required for proper rRNA processing and maturation
CC       of 18S rRNAs (PubMed:25424902). Part of the small subunit (SSU)
CC       processome, first precursor of the small eukaryotic ribosomal subunit.
CC       During the assembly of the SSU processome in the nucleolus, many
CC       ribosome biogenesis factors, an RNA chaperone and ribosomal proteins
CC       associate with the nascent pre-rRNA and work in concert to generate RNA
CC       folding, modifications, rearrangements and cleavage as well as targeted
CC       degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797).
CC       {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25424902,
CC       ECO:0000269|PubMed:34516797, ECO:0000269|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 (PubMed:23636399)
CC       (Probable). Part of the small subunit (SSU) processome, composed of
CC       more than 70 proteins and the RNA chaperone small nucleolar RNA
CC       (snoRNA) U3 (PubMed:34516797). {ECO:0000269|PubMed:23636399,
CC       ECO:0000269|PubMed:34516797, 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:34516797}.
CC   -!- TISSUE SPECIFICITY: Expressed in a wide variety of actively
CC       proliferating cells and tumor tissues. {ECO:0000269|PubMed:8407955}.
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="https://atlasgeneticsoncology.org/gene/45550/RPS27";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   PDB; 7QP6; EM; 4.70 A; H=1-84.
DR   PDB; 7QP7; EM; 3.70 A; H=1-84.
DR   PDB; 7R4X; EM; 2.15 A; b=1-84.
DR   PDB; 7TQL; EM; 3.40 A; b=2-83.
DR   PDB; 7WTS; EM; 3.20 A; b=1-84.
DR   PDB; 7WTT; EM; 3.10 A; b=1-84.
DR   PDB; 7WTU; EM; 3.00 A; b=1-84.
DR   PDB; 7WTV; EM; 3.50 A; b=1-84.
DR   PDB; 7WTW; EM; 3.20 A; b=1-84.
DR   PDB; 7WTX; EM; 3.10 A; b=1-84.
DR   PDB; 7WTZ; EM; 3.00 A; b=1-84.
DR   PDB; 7WU0; EM; 3.30 A; b=1-84.
DR   PDB; 7XNX; EM; 2.70 A; Sb=1-84.
DR   PDB; 7XNY; EM; 2.50 A; Sb=1-84.
DR   PDB; 8G5Y; EM; 2.29 A; Sb=1-84.
DR   PDB; 8G60; EM; 2.54 A; Sb=1-84.
DR   PDB; 8G61; EM; 2.94 A; Sb=1-84.
DR   PDB; 8G6J; EM; 2.80 A; Sb=1-84.
DR   PDB; 8GLP; EM; 1.67 A; Sb=1-84.
DR   PDB; 8JDJ; EM; 2.50 A; AN=1-84.
DR   PDB; 8JDK; EM; 2.26 A; AN=1-84.
DR   PDB; 8JDL; EM; 2.42 A; AN=1-84.
DR   PDB; 8JDM; EM; 2.67 A; AN=1-84.
DR   PDB; 8PPK; EM; 2.98 A; b=1-84.
DR   PDB; 8PPL; EM; 2.65 A; Ab=1-84.
DR   PDB; 8T4S; EM; 2.60 A; b=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   PDBsum; 7QP6; -.
DR   PDBsum; 7QP7; -.
DR   PDBsum; 7R4X; -.
DR   PDBsum; 7TQL; -.
DR   PDBsum; 7WTS; -.
DR   PDBsum; 7WTT; -.
DR   PDBsum; 7WTU; -.
DR   PDBsum; 7WTV; -.
DR   PDBsum; 7WTW; -.
DR   PDBsum; 7WTX; -.
DR   PDBsum; 7WTZ; -.
DR   PDBsum; 7WU0; -.
DR   PDBsum; 7XNX; -.
DR   PDBsum; 7XNY; -.
DR   PDBsum; 8G5Y; -.
DR   PDBsum; 8G60; -.
DR   PDBsum; 8G61; -.
DR   PDBsum; 8G6J; -.
DR   PDBsum; 8GLP; -.
DR   PDBsum; 8JDJ; -.
DR   PDBsum; 8JDK; -.
DR   PDBsum; 8JDL; -.
DR   PDBsum; 8JDM; -.
DR   PDBsum; 8PPK; -.
DR   PDBsum; 8PPL; -.
DR   PDBsum; 8T4S; -.
DR   AlphaFoldDB; P42677; -.
DR   EMDB; EMD-10668; -.
DR   EMDB; EMD-10674; -.
DR   EMDB; EMD-10690; -.
DR   EMDB; EMD-10769; -.
DR   EMDB; EMD-10775; -.
DR   EMDB; EMD-11098; -.
DR   EMDB; EMD-11099; -.
DR   EMDB; EMD-11100; -.
DR   EMDB; EMD-11276; -.
DR   EMDB; EMD-11288; -.
DR   EMDB; EMD-11289; -.
DR   EMDB; EMD-11292; -.
DR   EMDB; EMD-11299; -.
DR   EMDB; EMD-11301; -.
DR   EMDB; EMD-11302; -.
DR   EMDB; EMD-11310; -.
DR   EMDB; EMD-11320; -.
DR   EMDB; EMD-11321; -.
DR   EMDB; EMD-11325; -.
DR   EMDB; EMD-11335; -.
DR   EMDB; EMD-11440; -.
DR   EMDB; EMD-11441; -.
DR   EMDB; EMD-11456; -.
DR   EMDB; EMD-11458; -.
DR   EMDB; EMD-11517; -.
DR   EMDB; EMD-11518; -.
DR   EMDB; EMD-11519; -.
DR   EMDB; EMD-11520; -.
DR   EMDB; EMD-11521; -.
DR   EMDB; EMD-11602; -.
DR   EMDB; EMD-14113; -.
DR   EMDB; EMD-14114; -.
DR   EMDB; EMD-14317; -.
DR   EMDB; EMD-17804; -.
DR   EMDB; EMD-17805; -.
DR   EMDB; EMD-22681; -.
DR   EMDB; EMD-23936; -.
DR   EMDB; EMD-23937; -.
DR   EMDB; EMD-23938; -.
DR   EMDB; EMD-26067; -.
DR   EMDB; EMD-29757; -.
DR   EMDB; EMD-29758; -.
DR   EMDB; EMD-29759; -.
DR   EMDB; EMD-29760; -.
DR   EMDB; EMD-29771; -.
DR   EMDB; EMD-32799; -.
DR   EMDB; EMD-32800; -.
DR   EMDB; EMD-32801; -.
DR   EMDB; EMD-32802; -.
DR   EMDB; EMD-32803; -.
DR   EMDB; EMD-32804; -.
DR   EMDB; EMD-32806; -.
DR   EMDB; EMD-32807; -.
DR   EMDB; EMD-33329; -.
DR   EMDB; EMD-33330; -.
DR   EMDB; EMD-3770; -.
DR   EMDB; EMD-3883; -.
DR   EMDB; EMD-40205; -.
DR   EMDB; EMD-4070; -.
DR   EMDB; EMD-41039; -.
DR   EMDB; EMD-4242; -.
DR   EMDB; EMD-4337; -.
DR   EMDB; EMD-4348; -.
DR   EMDB; EMD-4349; -.
DR   EMDB; EMD-4350; -.
DR   EMDB; EMD-4351; -.
DR   EMDB; EMD-4352; -.
DR   EMDB; EMD-4353; -.
DR   EMDB; EMD-9701; -.
DR   EMDB; EMD-9702; -.
DR   EMDB; EMD-9703; -.
DR   SMR; P42677; -.
DR   BioGRID; 112146; 333.
DR   CORUM; P42677; -.
DR   DIP; DIP-44182N; -.
DR   IntAct; P42677; 103.
DR   MINT; P42677; -.
DR   STRING; 9606.ENSP00000499044; -.
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; 9606-ENSP00000357555; -.
DR   PeptideAtlas; P42677; -.
DR   ProteomicsDB; 55523; -.
DR   Pumba; P42677; -.
DR   TopDownProteomics; P42677; -.
DR   Antibodypedia; 20391; 281 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   AGR; HGNC:10416; -.
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; Diamond-Blackfan 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; CASILCQ; -.
DR   OrthoDB; 5470875at2759; -.
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-9735869; SARS-CoV-1 modulates host translation machinery.
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; 448 hits in 705 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 96 other cell types or tissues.
DR   ExpressionAtlas; P42677; baseline and differential.
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:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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:0032040; C:small-subunit processome; IDA: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:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB.
DR   GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR   GO; GO:0006412; P:translation; NAS:UniProtKB.
DR   Gene3D; 2.20.25.100; Zn-binding ribosomal proteins; 1.
DR   HAMAP; MF_00371; Ribosomal_eS27; 1.
DR   InterPro; IPR000592; Ribosomal_eS27.
DR   InterPro; IPR023407; Ribosomal_eS27_Zn-bd_dom_sf.
DR   InterPro; IPR011332; Ribosomal_zn-bd.
DR   PANTHER; PTHR11594; 40S RIBOSOMAL PROTEIN S27; 1.
DR   PANTHER; PTHR11594:SF1; 40S RIBOSOMAL PROTEIN S27; 1.
DR   Pfam; PF01667; Ribosomal_S27e; 1.
DR   SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR   PROSITE; PS01168; RIBOSOMAL_S27E; 1.
DR   Genevisible; P42677; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Diamond-Blackfan anemia;
KW   Direct protein sequencing; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; Zinc;
KW   Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8706699"
FT   CHAIN           2..84
FT                   /note="Small ribosomal subunit protein eS27"
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   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:34516797,
FT                   ECO:0007744|PDB:7MQ8"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:34516797,
FT                   ECO:0007744|PDB:7MQ8"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:34516797,
FT                   ECO:0007744|PDB:7MQ8"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:34516797,
FT                   ECO:0007744|PDB:7MQ8"
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:7R4X"
FT   HELIX           20..22
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   STRAND          32..36
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   STRAND          38..41
FT                   /evidence="ECO:0007829|PDB:6ZXG"
FT   STRAND          43..47
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:6ZMT"
FT   STRAND          57..60
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:7R4X"
SQ   SEQUENCE   84 AA;  9461 MW;  242C4466AC8A8900 CRC64;
     MPLAKDLLHP SPEEEKRKHK KKRLVQSPNS YFMDVKCPGC YKITTVFSHA QTVVLCVGCS
     TVLCQPTGGK ARLTEGCSFR RKQH
//