RSSA_HUMAN
ID RSSA_HUMAN Reviewed; 295 AA.
AC P08865; P11085; P12030; Q16471; Q6IPD1; Q6IPD2; Q6NSD1; Q6NXQ8; Q86VC0;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 237.
DE RecName: Full=40S ribosomal protein SA {ECO:0000255|HAMAP-Rule:MF_03016};
DE AltName: Full=37 kDa laminin receptor precursor {ECO:0000255|HAMAP-Rule:MF_03016};
DE Short=37LRP {ECO:0000255|HAMAP-Rule:MF_03016};
DE AltName: Full=37/67 kDa laminin receptor {ECO:0000255|HAMAP-Rule:MF_03016};
DE Short=LRP/LR {ECO:0000255|HAMAP-Rule:MF_03016};
DE AltName: Full=67 kDa laminin receptor {ECO:0000255|HAMAP-Rule:MF_03016};
DE Short=67LR {ECO:0000255|HAMAP-Rule:MF_03016};
DE AltName: Full=Colon carcinoma laminin-binding protein;
DE AltName: Full=Laminin receptor 1 {ECO:0000255|HAMAP-Rule:MF_03016};
DE Short=LamR {ECO:0000255|HAMAP-Rule:MF_03016};
DE AltName: Full=Laminin-binding protein precursor p40 {ECO:0000255|HAMAP-Rule:MF_03016};
DE Short=LBP/p40 {ECO:0000255|HAMAP-Rule:MF_03016};
DE AltName: Full=Multidrug resistance-associated protein MGr1-Ag;
DE AltName: Full=NEM/1CHD4;
DE AltName: Full=Small ribosomal subunit protein uS2 {ECO:0000303|PubMed:24524803};
GN Name=RPSA {ECO:0000255|HAMAP-Rule:MF_03016}; Synonyms=LAMBR, LAMR1;
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].
RX PubMed=2970639; DOI=10.1073/pnas.85.17.6394;
RA Yow H., Wong J.M., Chen H.S., Lee C., Steele G.D. Jr., Chen L.B.;
RT "Increased mRNA expression of a laminin-binding protein in human colon
RT carcinoma: complete sequence of a full-length cDNA encoding the protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6394-6398(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2543954; DOI=10.1093/nar/17.10.3829;
RA van den Ouweland A.M.W., van Duijnhoven H.L.P., Deichmann K.A.,
RA van Groningen J.J.M., de Leij L., van de Ven W.J.M.;
RT "Characteristics of a multicopy gene family predominantly consisting of
RT processed pseudogenes.";
RL Nucleic Acids Res. 17:3829-3843(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=1534510; DOI=10.1016/0304-3835(92)90096-e;
RA Satoh K., Narumi K., Sakai T., Abe T., Kikuchi T., Matsushima K.,
RA Sindoh S., Motomiya M.;
RT "Cloning of 67-kDa laminin receptor cDNA and gene expression in normal and
RT malignant cell lines of the human lung.";
RL Cancer Lett. 62:199-203(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8760291;
RA Jackers P., Minoletti F., Belotti D., Clausse N., Sozzi G., Sobel M.E.,
RA Castronovo V.;
RT "Isolation from a multigene family of the active human gene of the
RT metastasis-associated multifunctional protein 37LRP/p40 at chromosome
RT 3p21.3.";
RL Oncogene 13:495-503(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shi Y., Zhai H., Wang X., Wu H., Ning X., Han Y., Zhang D., Xiao B., Wu K.,
RA Fan D.;
RT "Multidrug resistance associated protein MGr1-Ag is identical to human 67-
RT KDa laminin receptor precursor.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TRP-117.
RC TISSUE=Bone marrow, Brain, Cervix, Hippocampus, Liver, Lung, Lymph,
RC Placenta, Prostate, Skin, and Urinary bladder;
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 2-17, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V., Potts A., Barblan J., Quadroni M.;
RL Submitted (JUL-2004) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-295.
RA Siyanova E.Y., Lukashev V.A., Blinov V.M., Troyanovskii S.M.;
RT "Determination and analysis of the primary sequence of human laminin-
RT binding protein.";
RL Dokl. Biochem. 313:227-231(1990).
RN [10]
RP PROTEIN SEQUENCE OF 16-26 AND 90-99.
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 [11]
RP PROTEIN SEQUENCE OF 43-52; 64-80; 103-117; 129-155 AND 192-205, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-209.
RC TISSUE=Blood;
RX PubMed=8586453;
RA Selvamurugan N., Eliceiri G.L.;
RT "The gene for human E2 small nucleolar RNA resides in an intron of a
RT laminin-binding protein gene.";
RL Genomics 30:400-401(1995).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 161-295, AND PROTEIN SEQUENCE OF 177-184.
RX PubMed=2429301; DOI=10.1073/pnas.83.19.7137;
RA Wewer U.M., Liotta L.A., Jaye M., Ricca G.A., Drohan W.N., Claysmith A.P.,
RA Rao C.N., Wirth P., Coligan J.E., Albrechtsen R., Mudryj M., Sobel M.E.;
RT "Altered levels of laminin receptor mRNA in various human carcinoma cells
RT that have different abilities to bind laminin.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:7137-7141(1986).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 225-295.
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 [15]
RP FUNCTION, AND INTERACTION WITH LAMININ-1.
RX PubMed=6300843; DOI=10.1073/pnas.80.2.444;
RA Terranova V.P., Rao C.N., Kalebic T., Margulies I.M., Liotta L.A.;
RT "Laminin receptor on human breast carcinoma cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:444-448(1983).
RN [16]
RP DOMAINS, AND INTERACTION WITH LAMININ-1.
RX PubMed=1834645; DOI=10.1016/s0021-9258(18)54943-7;
RA Castronovo V., Taraboletti G., Sobel M.E.;
RT "Functional domains of the 67-kDa laminin receptor precursor.";
RL J. Biol. Chem. 266:20440-20446(1991).
RN [17]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH SINDBIS VIRUS E2
RP ENVELOPE GLYCOPROTEIN.
RX PubMed=1385835; DOI=10.1128/jvi.66.8.4992-5001.1992;
RA Wang K.-S., Kuhn R.J., Strauss E.G., Ou S., Strauss J.H.;
RT "High-affinity laminin receptor is a receptor for Sindbis virus in
RT mammalian cells.";
RL J. Virol. 66:4992-5001(1992).
RN [18]
RP INTERACTION WITH LAMININ-1.
RX PubMed=8433567; DOI=10.1038/ki.1993.7;
RA Cioce V., Margulies I.M.K., Sobel M.E., Castronovo V.;
RT "Interaction between the 67 kilodalton metastasis-associated laminin
RT receptor and laminin.";
RL Kidney Int. 43:30-37(1993).
RN [19]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH VENEZUELAN EQUINE
RP ENCEPHALITIS VIRUS E2 GLYCOPROTEIN.
RX PubMed=8764073; DOI=10.1128/jvi.70.8.5592-5599.1996;
RA Ludwig G.V., Kondig J.P., Smith J.F.;
RT "A putative receptor for Venezuelan equine encephalitis virus from mosquito
RT cells.";
RL J. Virol. 70:5592-5599(1996).
RN [20]
RP INTERACTION WITH PRNP.
RX PubMed=9396609; DOI=10.1038/nm1297-1383;
RA Rieger R., Edenhofer F., Lasmezas C.I., Weiss S.;
RT "The human 37-kDa laminin receptor precursor interacts with the prion
RT protein in eukaryotic cells.";
RL Nat. Med. 3:1383-1388(1997).
RN [21]
RP ACYLATION.
RX PubMed=9581863;
RX DOI=10.1002/(sici)1097-4644(19980601)69:3<244::aid-jcb2>3.0.co;2-r;
RA Buto S., Tagliabue E., Ardini E., Magnifico A., Ghirelli C.,
RA van den Brule F., Castronovo V., Colnaghi M.I., Sobel M.E., Menard S.;
RT "Formation of the 67-kDa laminin receptor by acylation of the precursor.";
RL J. Cell. Biochem. 69:244-251(1998).
RN [22]
RP INTERACTION WITH LAMININ-5.
RX PubMed=9718729; DOI=10.1093/oxfordjournals.molbev.a026000;
RA Ardini E., Pesole G., Tagliabue E., Magnifico A., Castronovo V.,
RA Sobel M.E., Colnaghi M.I., Menard S.;
RT "The 67-kDa laminin receptor originated from a ribosomal protein that
RT acquired a dual function during evolution.";
RL Mol. Biol. Evol. 15:1017-1025(1998).
RN [23]
RP INTERACTION WITH RPS21.
RX PubMed=10079194; DOI=10.1006/bbrc.1999.0343;
RA Sato M., Saeki Y., Tanaka K., Kaneda Y.;
RT "Ribosome-associated protein LBP/p40 binds to S21 protein of 40S ribosome:
RT analysis using a yeast two-hybrid system.";
RL Biochem. Biophys. Res. Commun. 256:385-390(1999).
RN [24]
RP INTERACTION WITH LAMB1.
RX PubMed=10772861; DOI=10.1006/jmbi.2000.3680;
RA Kazmin D.A., Hoyt T.R., Taubner L., Teintze M., Starkey J.R.;
RT "Phage display mapping for peptide 11 sensitive sequences binding to
RT laminin-1.";
RL J. Mol. Biol. 298:431-445(2000).
RN [25]
RP PRION-BINDING, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11689427; DOI=10.1093/emboj/20.21.5863;
RA Gauczynski S., Peyrin J.-M., Haik S., Leucht C., Hundt C., Rieger R.,
RA Krasemann S., Deslys J.-P., Dormont D., Lasmezas C.I., Weiss S.;
RT "The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for
RT the cellular prion protein.";
RL EMBO J. 20:5863-5875(2001).
RN [26]
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 [27]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH DENGUE VIRUS ENVELOPE
RP PROTEIN E.
RX PubMed=15507651; DOI=10.1128/jvi.78.22.12647-12656.2004;
RA Thepparit C., Smith D.R.;
RT "Serotype-specific entry of dengue virus into liver cells: identification
RT of the 37-kilodalton/67-kilodalton high-affinity laminin receptor as a
RT dengue virus serotype 1 receptor.";
RL J. Virol. 78:12647-12656(2004).
RN [28]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
RP PPP1R16B AND PPP1CA.
RX PubMed=16263087; DOI=10.1016/j.bbrc.2005.10.089;
RA Kim K., Li L., Kozlowski K., Suh H.S., Cao W., Ballermann B.J.;
RT "The protein phosphatase-1 targeting subunit TIMAP regulates LAMR1
RT phosphorylation.";
RL Biochem. Biophys. Res. Commun. 338:1327-1334(2005).
RN [29]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=15516338; DOI=10.1074/jbc.m410176200;
RA Kim K.J., Chung J.W., Kim K.S.;
RT "67-kDa laminin receptor promotes internalization of cytotoxic necrotizing
RT factor 1-expressing Escherichia coli K1 into human brain microvascular
RT endothelial cells.";
RL J. Biol. Chem. 280:1360-1368(2005).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [31]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ADENO-ASSOCIATED VIRUS
RP CAPSID PROTEINS.
RX PubMed=16973587; DOI=10.1128/jvi.00878-06;
RA Akache B., Grimm D., Pandey K., Yant S.R., Xu H., Kay M.A.;
RT "The 37/67-kilodalton laminin receptor is a receptor for adeno-associated
RT virus serotypes 8, 2, 3, and 9.";
RL J. Virol. 80:9831-9836(2006).
RN [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, 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 [34]
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 [35]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND THR-97, AND
RP IDENTIFICATION BY 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 [37]
RP INVOLVEMENT IN ICAS, VARIANTS ICAS ASN-54; PHE-58; GLY-180; TRP-180 AND
RP CYS-186, CHARACTERIZATION OF VARIANTS ICAS ASN-54; PHE-58; GLY-180; TRP-180
RP AND CYS-186, AND VARIANTS VAL-185; GLY-257 AND THR-278.
RX PubMed=23579497; DOI=10.1126/science.1234864;
RA Bolze A., Mahlaoui N., Byun M., Turner B., Trede N., Ellis S.R.,
RA Abhyankar A., Itan Y., Patin E., Brebner S., Sackstein P., Puel A.,
RA Picard C., Abel L., Quintana-Murci L., Faust S.N., Williams A.P.,
RA Baretto R., Duddridge M., Kini U., Pollard A.J., Gaud C., Frange P.,
RA Orbach D., Emile J.F., Stephan J.L., Sorensen R., Plebani A.,
RA Hammarstrom L., Conley M.E., Selleri L., Casanova J.L.;
RT "Ribosomal protein SA haploinsufficiency in humans with isolated congenital
RT asplenia.";
RL Science 340:976-978(2013).
RN [38]
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 [39]
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 [40]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [41]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-89, AND IDENTIFICATION BY MASS
RP 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 [42]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 9-205.
RX PubMed=18063583; DOI=10.1074/jbc.c700206200;
RA Jamieson K.V., Wu J., Hubbard S.R., Meruelo D.;
RT "Crystal structure of the human laminin receptor precursor.";
RL J. Biol. Chem. 283:3002-3005(2008).
CC -!- FUNCTION: Required for the assembly and/or stability of the 40S
CC ribosomal subunit. Required for the processing of the 20S rRNA-
CC precursor to mature 18S rRNA in a late step of the maturation of 40S
CC ribosomal subunits. Also functions as a cell surface receptor for
CC laminin. Plays a role in cell adhesion to the basement membrane and in
CC the consequent activation of signaling transduction pathways. May play
CC a role in cell fate determination and tissue morphogenesis. Acts as a
CC PPP1R16B-dependent substrate of PPP1CA. {ECO:0000255|HAMAP-
CC Rule:MF_03016, ECO:0000269|PubMed:16263087,
CC ECO:0000269|PubMed:6300843}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for the Adeno-
CC associated viruses 2,3,8 and 9. {ECO:0000269|PubMed:16973587}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for the Dengue
CC virus. {ECO:0000269|PubMed:15507651}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for the Sindbis
CC virus. {ECO:0000269|PubMed:1385835}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for the Venezuelan
CC equine encephalitis virus. {ECO:0000269|PubMed:1385835}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for the pathogenic
CC prion protein. {ECO:0000269|PubMed:11689427,
CC ECO:0000269|PubMed:9396609}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for bacteria.
CC {ECO:0000269|PubMed:15516338}.
CC -!- SUBUNIT: Monomer (37LRP) and homodimer (67LR). Component of the small
CC ribosomal subunit. Mature ribosomes consist of a small (40S) and a
CC large (60S) subunit. The 40S subunit contains about 33 different
CC proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49
CC different proteins and 3 molecules of RNA (28S, 5.8S and 5S). Interacts
CC with RPS21. Interacts with several laminins including at least LAMB1.
CC Interacts with MDK (By similarity). The mature dimeric form interacts
CC with PPP1R16B (via its fourth ankyrin repeat). Interacts with PPP1CA
CC only in the presence of PPP1R16B. {ECO:0000255|HAMAP-Rule:MF_03016,
CC ECO:0000269|PubMed:10079194, ECO:0000269|PubMed:10772861,
CC ECO:0000269|PubMed:11689427, ECO:0000269|PubMed:15507651,
CC ECO:0000269|PubMed:16263087, ECO:0000269|PubMed:1834645,
CC ECO:0000269|PubMed:6300843, ECO:0000269|PubMed:8433567,
CC ECO:0000269|PubMed:9396609, ECO:0000269|PubMed:9718729}.
CC -!- SUBUNIT: (Microbial infection) 67LR interacts with capsid protein of
CC Adeno-associated virus 2,3,8 and 9. {ECO:0000269|PubMed:16973587}.
CC -!- SUBUNIT: (Microbial infection) 67LR interacts with envelope protein of
CC dengue virus. {ECO:0000269|PubMed:15507651}.
CC -!- SUBUNIT: (Microbial infection) 6s7LR interacts with E2 glycoprotein of
CC Sindbis and Venezuelan equine encephalitis virus (PubMed:8764073,
CC PubMed:1385835). {ECO:0000269|PubMed:1385835,
CC ECO:0000269|PubMed:8764073}.
CC -!- INTERACTION:
CC P08865; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-354112, EBI-10961312;
CC P08865; P02489: CRYAA; NbExp=3; IntAct=EBI-354112, EBI-6875961;
CC P08865; Q9UQC2: GAB2; NbExp=3; IntAct=EBI-354112, EBI-975200;
CC P08865; P04792: HSPB1; NbExp=4; IntAct=EBI-354112, EBI-352682;
CC P08865; Q15046: KARS1; NbExp=9; IntAct=EBI-354112, EBI-356367;
CC P08865; Q9Y2W7: KCNIP3; NbExp=3; IntAct=EBI-354112, EBI-751501;
CC P08865; O60333-2: KIF1B; NbExp=3; IntAct=EBI-354112, EBI-10975473;
CC P08865; O60260-5: PRKN; NbExp=3; IntAct=EBI-354112, EBI-21251460;
CC P08865; P00441: SOD1; NbExp=3; IntAct=EBI-354112, EBI-990792;
CC P08865; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-354112, EBI-717399;
CC P08865; O76024: WFS1; NbExp=3; IntAct=EBI-354112, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm. Nucleus
CC {ECO:0000255|HAMAP-Rule:MF_03016}. Note=67LR is found at the surface of
CC the plasma membrane, with its C-terminal laminin-binding domain
CC accessible to extracellular ligands. 37LRP is found at the cell
CC surface, in the cytoplasm and in the nucleus (By similarity).
CC Colocalizes with PPP1R16B in the cell membrane. {ECO:0000255|HAMAP-
CC Rule:MF_03016}.
CC -!- PTM: Acylated. Acylation may be a prerequisite for conversion of the
CC monomeric 37 kDa laminin receptor precursor (37LRP) to the mature
CC dimeric 67 kDa laminin receptor (67LR), and may provide a mechanism for
CC membrane association (PubMed:9581863). {ECO:0000255|HAMAP-
CC Rule:MF_03016, ECO:0000269|PubMed:9581863}.
CC -!- PTM: Cleaved by stromelysin-3 (ST3) at the cell surface. Cleavage by
CC stromelysin-3 may be a mechanism to alter cell-extracellular matrix
CC interactions. {ECO:0000255|HAMAP-Rule:MF_03016}.
CC -!- DISEASE: Asplenia, isolated congenital (ICAS) [MIM:271400]: A rare
CC primary immunodeficiency and life-threatening condition, often
CC presenting with pneumococcal sepsis. Most affected individuals die of
CC severe bacterial infections in early childhood. Isolated asplenia is
CC distinct from asplenia associated with other complex visceral defects,
CC notably heterotaxy syndromes such as Ivemark syndrome.
CC {ECO:0000269|PubMed:23579497}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: This protein appears to have acquired a second function
CC as a laminin receptor specifically in the vertebrate lineage.
CC -!- MISCELLANEOUS: It is thought that in vertebrates 37/67 kDa laminin
CC receptor acquired a dual function during evolution. It developed from
CC the ribosomal protein SA, playing an essential role in the protein
CC biosynthesis lacking any laminin binding activity, to a cell surface
CC receptor with laminin binding activity.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC {ECO:0000255|HAMAP-Rule:MF_03016}.
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DR EMBL; J03799; AAA36161.1; -; mRNA.
DR EMBL; X15005; CAA33112.1; -; mRNA.
DR EMBL; S37431; AAB22299.1; -; mRNA.
DR EMBL; U43901; AAC50652.1; -; Genomic_DNA.
DR EMBL; AF503367; AAM33304.1; -; mRNA.
DR EMBL; BT007219; AAP35883.1; -; mRNA.
DR EMBL; BC005391; AAH05391.1; -; mRNA.
DR EMBL; BC008867; AAH08867.1; -; mRNA.
DR EMBL; BC010418; AAH10418.1; -; mRNA.
DR EMBL; BC013827; AAH13827.1; -; mRNA.
DR EMBL; BC034537; AAH34537.1; -; mRNA.
DR EMBL; BC050688; AAH50688.1; -; mRNA.
DR EMBL; BC053370; AAH53370.1; -; mRNA.
DR EMBL; BC062714; AAH62714.1; -; mRNA.
DR EMBL; BC066941; AAH66941.1; -; mRNA.
DR EMBL; BC068062; AAH68062.1; -; mRNA.
DR EMBL; BC070263; AAH70263.1; -; mRNA.
DR EMBL; BC071693; AAH71693.1; -; mRNA.
DR EMBL; BC071968; AAH71968.1; -; mRNA.
DR EMBL; BC071969; AAH71969.1; -; mRNA.
DR EMBL; BC071970; AAH71970.1; -; mRNA.
DR EMBL; BC073863; AAH73863.1; -; mRNA.
DR EMBL; BC107567; AAI07568.1; -; mRNA.
DR EMBL; X61156; CAA43469.1; -; mRNA.
DR EMBL; U36484; AAC50313.1; -; Genomic_DNA.
DR EMBL; M14199; AAA36165.1; -; mRNA.
DR EMBL; AB007146; BAA25812.1; -; Genomic_DNA.
DR CCDS; CCDS2686.1; -.
DR PIR; A31233; A31233.
DR RefSeq; NP_001291217.1; NM_001304288.1.
DR RefSeq; NP_002286.2; NM_002295.5.
DR PDB; 3BCH; X-ray; 2.15 A; A=2-220.
DR PDB; 4UG0; EM; -; SA=1-295.
DR PDB; 4V6X; EM; 5.00 A; AA=1-295.
DR PDB; 5A2Q; EM; 3.90 A; A=1-295.
DR PDB; 5AJ0; EM; 3.50 A; BA=1-295.
DR PDB; 5FLX; EM; 3.90 A; A=1-295.
DR PDB; 5LKS; EM; 3.60 A; SA=1-295.
DR PDB; 5OA3; EM; 4.30 A; A=1-295.
DR PDB; 5T2C; EM; 3.60 A; Ao=1-295.
DR PDB; 5VYC; X-ray; 6.00 A; A1/A2/A3/A4/A5/A6=1-295.
DR PDB; 6FEC; EM; 6.30 A; f=2-209.
DR PDB; 6G18; EM; 3.60 A; A=1-295.
DR PDB; 6G4S; EM; 4.00 A; A=1-295.
DR PDB; 6G51; EM; 4.10 A; A=1-295.
DR PDB; 6G53; EM; 4.50 A; A=1-295.
DR PDB; 6G5H; EM; 3.60 A; A=1-295.
DR PDB; 6G5I; EM; 3.50 A; A=1-295.
DR PDB; 6IP5; EM; 3.90 A; 2n=1-295.
DR PDB; 6IP6; EM; 4.50 A; 2n=1-295.
DR PDB; 6IP8; EM; 3.90 A; 2n=1-295.
DR PDB; 6OLE; EM; 3.10 A; SA=3-223.
DR PDB; 6OLF; EM; 3.90 A; SA=3-223.
DR PDB; 6OLG; EM; 3.40 A; BA=5-219.
DR PDB; 6OLI; EM; 3.50 A; SA=3-223.
DR PDB; 6OLZ; EM; 3.90 A; BA=5-219.
DR PDB; 6OM0; EM; 3.10 A; SA=3-223.
DR PDB; 6OM7; EM; 3.70 A; SA=3-223.
DR PDB; 6QZP; EM; 2.90 A; SA=3-223.
DR PDB; 6XA1; EM; 2.80 A; SA=2-217.
DR PDB; 6Y0G; EM; 3.20 A; SA=1-295.
DR PDB; 6Y2L; EM; 3.00 A; SA=1-295.
DR PDB; 6Y57; EM; 3.50 A; SA=1-295.
DR PDB; 6YBD; EM; 3.30 A; N=1-295.
DR PDB; 6YBW; EM; 3.10 A; N=1-295.
DR PDB; 6Z6L; EM; 3.00 A; SA=1-295.
DR PDB; 6Z6M; EM; 3.10 A; SA=1-295.
DR PDB; 6Z6N; EM; 2.90 A; SA=1-295.
DR PDB; 6ZLW; EM; 2.60 A; B=1-295.
DR PDB; 6ZM7; EM; 2.70 A; SA=1-295.
DR PDB; 6ZME; EM; 3.00 A; SA=1-295.
DR PDB; 6ZMI; EM; 2.60 A; SA=1-295.
DR PDB; 6ZMO; EM; 3.10 A; SA=1-295.
DR PDB; 6ZMT; EM; 3.00 A; B=1-295.
DR PDB; 6ZMW; EM; 3.70 A; N=1-295.
DR PDB; 6ZN5; EM; 3.20 A; B=2-207.
DR PDB; 6ZOJ; EM; 2.80 A; A=1-295.
DR PDB; 6ZOK; EM; 2.80 A; A=1-295.
DR PDB; 6ZON; EM; 3.00 A; a=1-295.
DR PDB; 6ZP4; EM; 2.90 A; a=1-295.
DR PDB; 6ZUO; EM; 3.10 A; A=1-295.
DR PDB; 6ZV6; EM; 2.90 A; A=1-295.
DR PDB; 6ZVH; EM; 2.90 A; A=3-223.
DR PDB; 6ZVJ; EM; 3.80 A; a=2-217.
DR PDB; 6ZXD; EM; 3.20 A; A=1-295.
DR PDB; 6ZXE; EM; 3.00 A; A=1-295.
DR PDB; 6ZXF; EM; 3.70 A; A=1-295.
DR PDB; 6ZXG; EM; 2.60 A; A=1-295.
DR PDB; 6ZXH; EM; 2.70 A; A=1-295.
DR PDB; 7A09; EM; 3.50 A; a=1-295.
DR PDB; 7K5I; EM; 2.90 A; A=1-295.
DR PDBsum; 3BCH; -.
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; 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 AlphaFoldDB; P08865; -.
DR SMR; P08865; -.
DR BioGRID; 110115; 445.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P08865; -.
DR DIP; DIP-32878N; -.
DR IntAct; P08865; 123.
DR MINT; P08865; -.
DR STRING; 9606.ENSP00000346067; -.
DR ChEMBL; CHEMBL6119; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB04985; Tigapotide.
DR GlyGen; P08865; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P08865; -.
DR MetOSite; P08865; -.
DR PhosphoSitePlus; P08865; -.
DR SwissPalm; P08865; -.
DR BioMuta; RPSA; -.
DR DMDM; 125969; -.
DR EPD; P08865; -.
DR jPOST; P08865; -.
DR MassIVE; P08865; -.
DR MaxQB; P08865; -.
DR PaxDb; P08865; -.
DR PeptideAtlas; P08865; -.
DR PRIDE; P08865; -.
DR ProteomicsDB; 52170; -.
DR TopDownProteomics; P08865; -.
DR Antibodypedia; 4030; 421 antibodies from 37 providers.
DR DNASU; 3921; -.
DR Ensembl; ENST00000301821.11; ENSP00000346067.4; ENSG00000168028.14.
DR GeneID; 3921; -.
DR KEGG; hsa:3921; -.
DR MANE-Select; ENST00000301821.11; ENSP00000346067.4; NM_002295.6; NP_002286.2.
DR UCSC; uc003cjp.4; human.
DR CTD; 3921; -.
DR DisGeNET; 3921; -.
DR GeneCards; RPSA; -.
DR HGNC; HGNC:6502; RPSA.
DR HPA; ENSG00000168028; Low tissue specificity.
DR MalaCards; RPSA; -.
DR MIM; 150370; gene.
DR MIM; 271400; phenotype.
DR neXtProt; NX_P08865; -.
DR OpenTargets; ENSG00000168028; -.
DR Orphanet; 101351; Familial isolated congenital asplenia.
DR PharmGKB; PA30287; -.
DR VEuPathDB; HostDB:ENSG00000168028; -.
DR eggNOG; KOG0830; Eukaryota.
DR GeneTree; ENSGT00950000183099; -.
DR InParanoid; P08865; -.
DR OrthoDB; 1129610at2759; -.
DR PhylomeDB; P08865; -.
DR TreeFam; TF300100; -.
DR PathwayCommons; P08865; -.
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-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; P08865; -.
DR SIGNOR; P08865; -.
DR BioGRID-ORCS; 3921; 746 hits in 1088 CRISPR screens.
DR ChiTaRS; RPSA; human.
DR EvolutionaryTrace; P08865; -.
DR GeneWiki; Ribosomal_protein_SA; -.
DR GenomeRNAi; 3921; -.
DR Pharos; P08865; Tbio.
DR PRO; PR:P08865; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P08865; protein.
DR Bgee; ENSG00000168028; Expressed in right uterine tube and 108 other tissues.
DR ExpressionAtlas; P08865; baseline and differential.
DR Genevisible; P08865; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043236; F:laminin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005055; F:laminin receptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome 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:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd01425; RPS2; 1.
DR HAMAP; MF_03015; Ribosomal_S2_euk; 1.
DR HAMAP; MF_03016; Ribosomal_S2_laminin_receptor; 1.
DR InterPro; IPR027504; 40S_ribosomal_SA.
DR InterPro; IPR032281; 40S_SA_C.
DR InterPro; IPR001865; Ribosomal_S2.
DR InterPro; IPR018130; Ribosomal_S2_CS.
DR InterPro; IPR027498; Ribosomal_S2_euk.
DR InterPro; IPR005707; Ribosomal_S2_euk/arc.
DR InterPro; IPR023591; Ribosomal_S2_flav_dom_sf.
DR PANTHER; PTHR11489; PTHR11489; 1.
DR Pfam; PF16122; 40S_SA_C; 1.
DR Pfam; PF00318; Ribosomal_S2; 2.
DR PRINTS; PR00395; RIBOSOMALS2.
DR SUPFAM; SSF52313; SSF52313; 1.
DR TIGRFAMs; TIGR01012; uS2_euk_arch; 1.
DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
DR PROSITE; PS00963; RIBOSOMAL_S2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Disease variant;
KW Host cell receptor for virus entry; Host-virus interaction;
KW Isopeptide bond; Membrane; Nucleus; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016,
FT ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT CHAIN 2..295
FT /note="40S ribosomal protein SA"
FT /id="PRO_0000134358"
FT REPEAT 230..232
FT /note="[DE]-W-[ST] 1"
FT REPEAT 247..249
FT /note="[DE]-W-[ST] 2"
FT REPEAT 266..268
FT /note="[DE]-W-[ST] 3"
FT REPEAT 275..277
FT /note="[DE]-W-[ST] 4"
FT REPEAT 293..295
FT /note="[DE]-W-[ST] 5"
FT REGION 54..113
FT /note="Interaction with PPP1R16B"
FT /evidence="ECO:0000269|PubMed:16263087"
FT REGION 161..180
FT /note="Laminin-binding"
FT REGION 205..229
FT /note="Laminin-binding"
FT REGION 242..295
FT /note="Laminin-binding"
FT REGION 266..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 115..116
FT /note="Cleavage; by ST3; site 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016"
FT SITE 133..134
FT /note="Cleavage; by ST3; site 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03016,
FT ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 52
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 89
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14206"
FT MOD_RES 97
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 54
FT /note="T -> N (in ICAS; reduced protein levels;
FT dbSNP:rs397514762)"
FT /evidence="ECO:0000269|PubMed:23579497"
FT /id="VAR_075092"
FT VARIANT 58
FT /note="L -> F (in ICAS; reduced protein levels;
FT dbSNP:rs397514763)"
FT /evidence="ECO:0000269|PubMed:23579497"
FT /id="VAR_075093"
FT VARIANT 117
FT /note="R -> W (in dbSNP:rs17856150)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025522"
FT VARIANT 180
FT /note="R -> G (in ICAS; reduced protein levels;
FT dbSNP:rs397514760)"
FT /evidence="ECO:0000269|PubMed:23579497"
FT /id="VAR_075094"
FT VARIANT 180
FT /note="R -> W (in ICAS; reduced protein levels;
FT dbSNP:rs397514760)"
FT /evidence="ECO:0000269|PubMed:23579497"
FT /id="VAR_075095"
FT VARIANT 185
FT /note="M -> V (in dbSNP:rs1214087389)"
FT /evidence="ECO:0000269|PubMed:23579497"
FT /id="VAR_075096"
FT VARIANT 186
FT /note="R -> C (in ICAS; reduced protein levels;
FT dbSNP:rs397514761)"
FT /evidence="ECO:0000269|PubMed:23579497"
FT /id="VAR_075097"
FT VARIANT 257
FT /note="V -> G (in dbSNP:rs369708612)"
FT /evidence="ECO:0000269|PubMed:23579497"
FT /id="VAR_075098"
FT VARIANT 278
FT /note="A -> T (in dbSNP:rs143085301)"
FT /evidence="ECO:0000269|PubMed:23579497"
FT /id="VAR_075099"
FT CONFLICT 60
FT /note="L -> V (in Ref. 9; CAA43469)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="Q -> QVCGTV (in Ref. 2; CAA33112)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="A -> T (in Ref. 7; AAH50688)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="T -> S (in Ref. 7; AAH70263)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="E -> G (in Ref. 3; AAB22299)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="E -> G (in Ref. 7; AAH66941)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="Q -> L (in Ref. 3; AAB22299)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:3BCH"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:3BCH"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:3BCH"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:3BCH"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:3BCH"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:3BCH"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3BCH"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:3BCH"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:3BCH"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:3BCH"
FT TURN 105..109
FT /evidence="ECO:0007829|PDB:3BCH"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:3BCH"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:3BCH"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:3BCH"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:3BCH"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:6ZN5"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:3BCH"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6ZVH"
FT HELIX 168..185
FT /evidence="ECO:0007829|PDB:3BCH"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:6ZV6"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:3BCH"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:3BCH"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:6ZXG"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:6ZUO"
SQ SEQUENCE 295 AA; 32854 MW; C68DDB16B759E79E CRC64;
MSGALDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYIYK RKSDGIYIIN LKRTWEKLLL
AARAIVAIEN PADVSVISSR NTGQRAVLKF AAATGATPIA GRFTPGTFTN QIQAAFREPR
LLVVTDPRAD HQPLTEASYV NLPTIALCNT DSPLRYVDIA IPCNNKGAHS VGLMWWMLAR
EVLRMRGTIS REHPWEVMPD LYFYRDPEEI EKEEQAAAEK AVTKEEFQGE WTAPAPEFTA
TQPEVADWSE GVQVPSVPIQ QFPTEDWSAQ PATEDWSAAP TAQATEWVGA TTDWS
