RS7_HUMAN
ID RS7_HUMAN Reviewed; 194 AA.
AC P62081; P23821; P24818; Q57Z92; Q6IPH1;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=40S ribosomal protein S7;
DE AltName: Full=Small ribosomal subunit protein eS7 {ECO:0000303|PubMed:24524803};
GN Name=RPS7;
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 / MRNA].
RX PubMed=8522193; DOI=10.1016/0378-1119(95)00405-u;
RA Annilo T., Laan M., Stahl J., Metspalu A.;
RT "The human ribosomal protein S7-encoding gene: isolation, structure and
RT localization in 2p25.";
RL Gene 165:297-302(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Liver, and Lung;
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 PROTEIN SEQUENCE OF 170-177.
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 [7]
RP INTERACTION WITH IPO5; IPO7 AND KPNB1, AND SUBCELLULAR LOCATION.
RX PubMed=9687515; DOI=10.1093/emboj/17.15.4491;
RA Jaekel S., Goerlich D.;
RT "Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of
RT ribosomal proteins in mammalian cells.";
RL EMBO J. 17:4491-4502(1998).
RN [8]
RP INTERACTION WITH IPO9.
RX PubMed=11823430; DOI=10.1093/emboj/21.3.377;
RA Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.;
RT "Importins fulfill a dual function as nuclear import receptors and
RT cytoplasmic chaperones for exposed basic domains.";
RL EMBO J. 21:377-386(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
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 FUNCTION, AND INVOLVEMENT IN DBA8.
RX PubMed=19061985; DOI=10.1016/j.ajhg.2008.11.004;
RA Gazda H.T., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.-F.,
RA Schneider H., Darras N., Hasman C., Sieff C.A., Newburger P.E., Ball S.E.,
RA Niewiadomska E., Matysiak M., Zaucha J.M., Glader B., Niemeyer C.,
RA Meerpohl J.J., Atsidaftos E., Lipton J.M., Gleizes P.-E., Beggs A.H.;
RT "Ribosomal protein L5 and L11 mutations are associated with cleft palate
RT and abnormal thumbs in Diamond-Blackfan anemia patients.";
RL Am. J. Hum. Genet. 83:769-780(2008).
RN [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP SUBCELLULAR LOCATION, INTERACTION WITH NEK6, AND PHOSPHORYLATION BY NEK6.
RX PubMed=20873783; DOI=10.1021/pr100562w;
RA Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J.,
RA Paes Leme A.F., Kobarg J.;
RT "Characterization of hNek6 interactome reveals an important role for its
RT short N-terminal domain and colocalization with proteins at the
RT centrosome.";
RL J. Proteome Res. 9:6298-6316(2010).
RN [15]
RP IDENTIFICATION BY 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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-74, AND IDENTIFICATION
RP 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 [22]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
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 [23]
RP INTERACTION WITH DESI2, AND DEUBIQUITINATION BY DESI2.
RX PubMed=28483520; DOI=10.1016/j.bbrc.2017.04.161;
RA Xie X., Wang X., Jiang D., Wang J., Fei R., Cong X., Wei L., Wang Y.,
RA Chen H.;
RT "PPPDE1 is a novel deubiquitinase belonging to a cysteine isopeptidase
RT family.";
RL Biochem. Biophys. Res. Commun. 488:291-296(2017).
CC -!- FUNCTION: Required for rRNA maturation. {ECO:0000269|PubMed:19061985}.
CC -!- SUBUNIT: Binds IPO9 with high affinity (PubMed:11823430). Interacts
CC with NEK6 (PubMed:20873783). Interacts with DESI2 (PubMed:28483520).
CC Interacts with IPO5, IPO7 and KPNB1; these interactions may be involved
CC in RPS7 nuclear import for the assembly of ribosomal subunits
CC (PubMed:9687515). {ECO:0000269|PubMed:11823430,
CC ECO:0000269|PubMed:20873783, ECO:0000269|PubMed:28483520,
CC ECO:0000269|PubMed:9687515}.
CC -!- INTERACTION:
CC P62081; Q00987: MDM2; NbExp=15; IntAct=EBI-354360, EBI-389668;
CC P62081; Q15843: NEDD8; NbExp=2; IntAct=EBI-354360, EBI-716247;
CC P62081; O43829: ZBTB14; NbExp=4; IntAct=EBI-354360, EBI-10176632;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:20873783}. Cytoplasm {ECO:0000269|PubMed:9687515}.
CC Nucleus {ECO:0000269|PubMed:9687515}. Note=Although RPS7 is functional
CC within the cytoplasm, the assembly of ribosomal subunits occurs in the
CC nucleus. RPS7 nuclear import is mediated by IPO5/RanBP5, IPO7/RanBP7,
CC KPNB1/importin-beta or TPNO1/Trn (PubMed:9687515). Colocalizes with
CC NEK6 in the centrosome (PubMed:20873783). {ECO:0000269|PubMed:20873783,
CC ECO:0000269|PubMed:9687515}.
CC -!- PTM: Phosphorylated by NEK6. {ECO:0000269|PubMed:20873783}.
CC -!- PTM: Ubiquitinated. Deubiquitinated by DESI2, leading to its
CC stabilization. {ECO:0000269|PubMed:28483520}.
CC -!- DISEASE: Diamond-Blackfan anemia 8 (DBA8) [MIM:612563]: 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:19061985}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS7 family.
CC {ECO:0000305}.
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DR EMBL; M77233; AAB00969.1; -; mRNA.
DR EMBL; Z25749; CAA81022.1; -; Genomic_DNA.
DR EMBL; AK311794; BAG34737.1; -; mRNA.
DR EMBL; AC108488; AAX82027.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01057.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01058.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01059.1; -; Genomic_DNA.
DR EMBL; BC002866; AAH02866.1; -; mRNA.
DR EMBL; BC061901; AAH61901.1; -; mRNA.
DR EMBL; BC071919; AAH71919.1; -; mRNA.
DR CCDS; CCDS1648.1; -.
DR PIR; JC4388; JC4388.
DR RefSeq; NP_001002.1; NM_001011.3.
DR PDB; 4UG0; EM; -; SH=1-194.
DR PDB; 4V6X; EM; 5.00 A; AH=1-194.
DR PDB; 5A2Q; EM; 3.90 A; H=1-194.
DR PDB; 5AJ0; EM; 3.50 A; BH=1-194.
DR PDB; 5FLX; EM; 3.90 A; H=1-194.
DR PDB; 5LKS; EM; 3.60 A; SH=1-194.
DR PDB; 5OA3; EM; 4.30 A; H=1-194.
DR PDB; 5T2C; EM; 3.60 A; At=1-194.
DR PDB; 5VYC; X-ray; 6.00 A; H1/H2/H3/H4/H5/H6=1-194.
DR PDB; 6FEC; EM; 6.30 A; X=5-194.
DR PDB; 6G18; EM; 3.60 A; H=1-194.
DR PDB; 6G4S; EM; 4.00 A; H=1-194.
DR PDB; 6G4W; EM; 4.50 A; H=1-194.
DR PDB; 6G51; EM; 4.10 A; H=1-194.
DR PDB; 6G53; EM; 4.50 A; H=1-194.
DR PDB; 6G5H; EM; 3.60 A; H=1-194.
DR PDB; 6G5I; EM; 3.50 A; H=1-194.
DR PDB; 6IP5; EM; 3.90 A; 2s=1-194.
DR PDB; 6IP6; EM; 4.50 A; 2s=1-194.
DR PDB; 6IP8; EM; 3.90 A; 2s=1-194.
DR PDB; 6OLE; EM; 3.10 A; SH=5-193.
DR PDB; 6OLF; EM; 3.90 A; SH=5-193.
DR PDB; 6OLG; EM; 3.40 A; BH=12-194.
DR PDB; 6OLI; EM; 3.50 A; SH=5-193.
DR PDB; 6OLZ; EM; 3.90 A; BH=12-194.
DR PDB; 6OM0; EM; 3.10 A; SH=5-193.
DR PDB; 6OM7; EM; 3.70 A; SH=5-193.
DR PDB; 6QZP; EM; 2.90 A; SH=5-193.
DR PDB; 6XA1; EM; 2.80 A; SH=6-194.
DR PDB; 6Y0G; EM; 3.20 A; SH=1-194.
DR PDB; 6Y2L; EM; 3.00 A; SH=1-194.
DR PDB; 6Y57; EM; 3.50 A; SH=1-194.
DR PDB; 6YBD; EM; 3.30 A; G=1-194.
DR PDB; 6YBW; EM; 3.10 A; G=1-194.
DR PDB; 6Z6L; EM; 3.00 A; SH=1-194.
DR PDB; 6Z6M; EM; 3.10 A; SH=1-194.
DR PDB; 6Z6N; EM; 2.90 A; SH=1-194.
DR PDB; 6ZLW; EM; 2.60 A; H=1-194.
DR PDB; 6ZM7; EM; 2.70 A; SH=1-194.
DR PDB; 6ZME; EM; 3.00 A; SH=1-194.
DR PDB; 6ZMI; EM; 2.60 A; SH=1-194.
DR PDB; 6ZMO; EM; 3.10 A; SH=1-194.
DR PDB; 6ZMT; EM; 3.00 A; H=1-194.
DR PDB; 6ZMW; EM; 3.70 A; G=1-194.
DR PDB; 6ZN5; EM; 3.20 A; H=8-193.
DR PDB; 6ZOJ; EM; 2.80 A; H=1-194.
DR PDB; 6ZOK; EM; 2.80 A; H=1-194.
DR PDB; 6ZON; EM; 3.00 A; s=1-194.
DR PDB; 6ZP4; EM; 2.90 A; s=1-194.
DR PDB; 6ZUO; EM; 3.10 A; H=1-194.
DR PDB; 6ZV6; EM; 2.90 A; H=1-194.
DR PDB; 6ZVH; EM; 2.90 A; H=5-193.
DR PDB; 6ZVJ; EM; 3.80 A; s=13-193.
DR PDB; 6ZXD; EM; 3.20 A; H=1-194.
DR PDB; 6ZXE; EM; 3.00 A; H=1-194.
DR PDB; 6ZXF; EM; 3.70 A; H=1-194.
DR PDB; 6ZXG; EM; 2.60 A; H=1-194.
DR PDB; 6ZXH; EM; 2.70 A; H=1-194.
DR PDB; 7A09; EM; 3.50 A; s=1-194.
DR PDB; 7K5I; EM; 2.90 A; H=1-194.
DR PDB; 7MQ8; EM; 3.60 A; L7=1-194.
DR PDB; 7MQ9; EM; 3.87 A; L7=1-194.
DR PDB; 7MQA; EM; 2.70 A; L7=1-194.
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; P62081; -.
DR SMR; P62081; -.
DR BioGRID; 112115; 301.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62081; -.
DR IntAct; P62081; 79.
DR MINT; P62081; -.
DR STRING; 9606.ENSP00000339095; -.
DR MoonProt; P62081; -.
DR GlyGen; P62081; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62081; -.
DR MetOSite; P62081; -.
DR PhosphoSitePlus; P62081; -.
DR SwissPalm; P62081; -.
DR BioMuta; RPS7; -.
DR DMDM; 49065831; -.
DR EPD; P62081; -.
DR jPOST; P62081; -.
DR MassIVE; P62081; -.
DR PaxDb; P62081; -.
DR PeptideAtlas; P62081; -.
DR PRIDE; P62081; -.
DR ProteomicsDB; 57364; -.
DR TopDownProteomics; P62081; -.
DR Antibodypedia; 26343; 189 antibodies from 28 providers.
DR DNASU; 6201; -.
DR Ensembl; ENST00000403564.5; ENSP00000385018.1; ENSG00000171863.15.
DR Ensembl; ENST00000406376.1; ENSP00000385286.1; ENSG00000171863.15.
DR Ensembl; ENST00000462576.5; ENSP00000495273.1; ENSG00000171863.15.
DR Ensembl; ENST00000645674.2; ENSP00000496757.1; ENSG00000171863.15.
DR Ensembl; ENST00000646909.1; ENSP00000496654.1; ENSG00000171863.15.
DR GeneID; 6201; -.
DR KEGG; hsa:6201; -.
DR MANE-Select; ENST00000645674.2; ENSP00000496757.1; NM_001011.4; NP_001002.1.
DR UCSC; uc002qxw.4; human.
DR CTD; 6201; -.
DR DisGeNET; 6201; -.
DR GeneCards; RPS7; -.
DR GeneReviews; RPS7; -.
DR HGNC; HGNC:10440; RPS7.
DR HPA; ENSG00000171863; Low tissue specificity.
DR MalaCards; RPS7; -.
DR MIM; 603658; gene.
DR MIM; 612563; phenotype.
DR neXtProt; NX_P62081; -.
DR OpenTargets; ENSG00000171863; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34855; -.
DR VEuPathDB; HostDB:ENSG00000171863; -.
DR eggNOG; KOG3320; Eukaryota.
DR GeneTree; ENSGT00390000014122; -.
DR HOGENOM; CLU_088621_1_2_1; -.
DR InParanoid; P62081; -.
DR OMA; AAYHKVQ; -.
DR OrthoDB; 1289550at2759; -.
DR PhylomeDB; P62081; -.
DR TreeFam; TF343364; -.
DR PathwayCommons; P62081; -.
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; P62081; -.
DR SIGNOR; P62081; -.
DR BioGRID-ORCS; 6201; 770 hits in 1013 CRISPR screens.
DR ChiTaRS; RPS7; human.
DR GeneWiki; RPS7; -.
DR GenomeRNAi; 6201; -.
DR Pharos; P62081; Tbio.
DR PRO; PR:P62081; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P62081; protein.
DR Bgee; ENSG00000171863; Expressed in left ovary and 96 other tissues.
DR ExpressionAtlas; P62081; baseline and differential.
DR Genevisible; P62081; 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:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0005840; C:ribosome; HDA:UniProtKB.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:CAFA.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:CAFA.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:1990948; F:ubiquitin ligase inhibitor activity; IDA:CAFA.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IDA:CAFA.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IDA:CAFA.
DR GO; GO:0014033; P:neural crest cell differentiation; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:CAFA.
DR GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IMP:CAFA.
DR GO; GO:0050821; P:protein stabilization; IMP:CAFA.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR InterPro; IPR000554; Ribosomal_S7e.
DR PANTHER; PTHR11278; PTHR11278; 1.
DR Pfam; PF01251; Ribosomal_S7e; 1.
DR PROSITE; PS00948; RIBOSOMAL_S7E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton;
KW Diamond-Blackfan anemia; Direct protein sequencing; Isopeptide bond;
KW Nucleus; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT CHAIN 1..194
FT /note="40S ribosomal protein S7"
FT /id="PRO_0000174190"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT MOD_RES 74
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 70
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 74
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:6ZVH"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6ZXH"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:6ZOJ"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 122..133
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:6ZVH"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:6ZLW"
FT TURN 161..165
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:6ZLW"
SQ SEQUENCE 194 AA; 22127 MW; E21089929CC061E9 CRC64;
MFSSSAKIVK PNGEKPDEFE SGISQALLEL EMNSDLKAQL RELNITAAKE IEVGGGRKAI
IIFVPVPQLK SFQKIQVRLV RELEKKFSGK HVVFIAQRRI LPKPTRKSRT KNKQKRPRSR
TLTAVHDAIL EDLVFPSEIV GKRIRVKLDG SRLIKVHLDK AQQNNVEHKV ETFSGVYKKL
TGKDVNFEFP EFQL
