SBDS_HUMAN
ID SBDS_HUMAN Reviewed; 250 AA.
AC Q9Y3A5; A8K0P4; Q96FX0; Q9NV53;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Ribosome maturation protein SBDS;
DE AltName: Full=Shwachman-Bodian-Diamond syndrome protein;
GN Name=SBDS; ORFNames=CGI-97;
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], VARIANTS SDS1 LYS-8; GLY-44; GLU-67; SER-87;
RP THR-126 AND CYS-169, AND VARIANT THR-212.
RX PubMed=12496757; DOI=10.1038/ng1062;
RA Boocock G.R.B., Morrison J.A., Popovic M., Richards N., Ellis L.,
RA Durie P.R., Rommens J.M.;
RT "Mutations in SBDS are associated with Shwachman-Diamond syndrome.";
RL Nat. Genet. 33:97-101(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Ovarian carcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=PNS;
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 2-19, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15860664; DOI=10.1182/blood-2005-02-0807;
RA Austin K.M., Leary R.J., Shimamura A.;
RT "The Shwachman-Diamond SBDS protein localizes to the nucleolus.";
RL Blood 106:1253-1258(2005).
RN [8]
RP INTERACTION WITH NPM1 AND THE 60S RIBOSOMAL SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17475909; DOI=10.1182/blood-2007-02-075184;
RA Ganapathi K.A., Austin K.M., Lee C.S., Dias A., Malsch M.M., Reed R.,
RA Shimamura A.;
RT "The human Shwachman-Diamond syndrome protein, SBDS, associates with
RT ribosomal RNA.";
RL Blood 110:1458-1465(2007).
RN [9]
RP FUNCTION, AND INTERACTION WITH NIP7.
RX PubMed=17643419; DOI=10.1016/j.yexcr.2007.06.024;
RA Hesling C., Oliveira C.C., Castilho B.A., Zanchin N.I.;
RT "The Shwachman-Bodian-Diamond syndrome associated protein interacts with
RT HsNip7 and its down-regulation affects gene expression at the
RT transcriptional and translational levels.";
RL Exp. Cell Res. 313:4180-4195(2007).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RPA1; PRKDC AND THE
RP 60S RIBOSOME SUBUNIT.
RX PubMed=19602484; DOI=10.1093/hmg/ddp316;
RA Ball H.L., Zhang B., Riches J.J., Gandhi R., Li J., Rommens J.M.,
RA Myers J.S.;
RT "Shwachman-Bodian Diamond syndrome is a multi-functional protein implicated
RT in cellular stress responses.";
RL Hum. Mol. Genet. 18:3684-3695(2009).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19759903; DOI=10.1371/journal.pone.0007084;
RA Orelio C., Verkuijlen P., Geissler J., van den Berg T.K., Kuijpers T.W.;
RT "SBDS expression and localization at the mitotic spindle in human myeloid
RT progenitors.";
RL PLoS ONE 4:E7084-E7084(2009).
RN [12]
RP INTERACTION WITH CLN3.
RX PubMed=20015955; DOI=10.1093/hmg/ddp560;
RA Vitiello S.P., Benedict J.W., Padilla-Lopez S., Pearce D.A.;
RT "Interaction between Sdo1p and Btn1p in the Saccharomyces cerevisiae model
RT for Batten disease.";
RL Hum. Mol. Genet. 19:931-942(2010).
RN [13]
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 [14]
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 [15]
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=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 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 [17]
RP INTERACTION WITH EFL1.
RX PubMed=25991726; DOI=10.1074/jbc.m114.626275;
RA Garcia-Marquez A., Gijsbers A., de la Mora E., Sanchez-Puig N.;
RT "Defective guanine nucleotide exchange in the elongation factor-like 1
RT (EFL1) GTPase by mutations in the Shwachman-Diamond syndrome protein.";
RL J. Biol. Chem. 290:17669-17678(2015).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP STRUCTURE BY NMR, AND RNA-BINDING.
RX PubMed=20053358; DOI=10.1016/j.jmb.2009.12.039;
RA de Oliveira J.F., Sforca M.L., Blumenschein T.M., Goldfeder M.B.,
RA Guimaraes B.G., Oliveira C.C., Zanchin N.I., Zeri A.C.;
RT "Structure, dynamics, and RNA interaction analysis of the human SBDS
RT protein.";
RL J. Mol. Biol. 396:1053-1069(2010).
RN [20]
RP STRUCTURE BY NMR, FUNCTION, CHARACTERIZATION OF VARIANT SDS1 THR-126, AND
RP MUTAGENESIS OF LYS-151.
RX PubMed=21536732; DOI=10.1101/gad.623011;
RA Finch A.J., Hilcenko C., Basse N., Drynan L.F., Goyenechea B., Menne T.F.,
RA Gonzalez Fernandez A., Simpson P., D'Santos C.S., Arends M.J., Donadieu J.,
RA Bellanne-Chantelot C., Costanzo M., Boone C., McKenzie A.N., Freund S.M.,
RA Warren A.J.;
RT "Uncoupling of GTP hydrolysis from eIF6 release on the ribosome causes
RT Shwachman-Diamond syndrome.";
RL Genes Dev. 25:917-929(2011).
RN [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), AND IDENTIFICATION IN A
RP COMPLEX WITH SBDS; 60S RIBOSOMAL SUBUNIT AND EFL1.
RX PubMed=26479198; DOI=10.1038/nsmb.3112;
RA Weis F., Giudice E., Churcher M., Jin L., Hilcenko C., Wong C.C.,
RA Traynor D., Kay R.R., Warren A.J.;
RT "Mechanism of eIF6 release from the nascent 60S ribosomal subunit.";
RL Nat. Struct. Mol. Biol. 22:914-919(2015).
RN [22]
RP VARIANT SDS1 THR-33.
RX PubMed=24898207; DOI=10.1186/1471-2350-15-64;
RA Carvalho C.M., Zuccherato L.W., Williams C.L., Neill N.J., Murdock D.R.,
RA Bainbridge M., Jhangiani S.N., Muzny D.M., Gibbs R.A., Ip W.,
RA Guillerman R.P., Lupski J.R., Bertuch A.A.;
RT "Structural variation and missense mutation in SBDS associated with
RT Shwachman-Diamond syndrome.";
RL BMC Med. Genet. 15:64-64(2014).
CC -!- FUNCTION: Required for the assembly of mature ribosomes and ribosome
CC biogenesis. Together with EFL1, triggers the GTP-dependent release of
CC EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating
CC ribosomes for translation competence by allowing 80S ribosome assembly
CC and facilitating EIF6 recycling to the nucleus, where it is required
CC for 60S rRNA processing and nuclear export. Required for normal levels
CC of protein synthesis. May play a role in cellular stress resistance.
CC May play a role in cellular response to DNA damage. May play a role in
CC cell proliferation. {ECO:0000269|PubMed:17643419,
CC ECO:0000269|PubMed:19602484, ECO:0000269|PubMed:19759903,
CC ECO:0000269|PubMed:21536732}.
CC -!- SUBUNIT: Associates with the 60S ribosomal subunit. Interacts with
CC NPM1, RPA1 and PRKDC. May interact with NIP7 (PubMed:17643419). Found
CC in a complex consisting of the 60S ribosomal subunit, SBDS and EFL1
CC (PubMed:26479198). Interacts with EFL1 (PubMed:25991726). Interacts
CC with CLN3 (PubMed:20015955). {ECO:0000269|PubMed:17475909,
CC ECO:0000269|PubMed:17643419, ECO:0000269|PubMed:19602484,
CC ECO:0000269|PubMed:20015955, ECO:0000269|PubMed:25991726,
CC ECO:0000269|PubMed:26479198}.
CC -!- INTERACTION:
CC Q9Y3A5; Q96AP0: ACD; NbExp=2; IntAct=EBI-1046471, EBI-717666;
CC Q9Y3A5; Q8WZ60: KLHL6; NbExp=3; IntAct=EBI-1046471, EBI-6426464;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus,
CC nucleoplasm. Cytoplasm, cytoskeleton, spindle. Note=Primarily detected
CC in the cytoplasm, and at low levels in nucleus and nucleolus
CC (PubMed:19602484 and PubMed:17475909). Detected in the nucleolus during
CC G1 and G2 phase of the cell cycle, and diffusely distributed in the
CC nucleus during S phase. Detected at the mitotic spindle. Colocalizes
CC with the microtubule organizing center during interphase
CC (PubMed:19759903). {ECO:0000269|PubMed:19759903}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DISEASE: Shwachman-Diamond syndrome 1 (SDS1) [MIM:260400]: A form of
CC Shwachman-Diamond syndrome, a disorder characterized by hematopoietic
CC abnormalities, exocrine pancreatic dysfunction, and skeletal dysplasia.
CC Intermittent or chronic neutropenia is the most common hematological
CC manifestation, followed by anemia and thrombocytopenia. Some patients
CC progress to bone marrow failure, myelodysplastic syndrome and malignant
CC transformation, with acute myelogenous leukemia being the most common.
CC Exocrine pancreatic dysfunction is generally the first presenting
CC symptom in infancy. Short stature and metaphyseal dysplasia are the
CC most frequent skeletal manifestations. SDS1 inheritance is autosomal
CC recessive. {ECO:0000269|PubMed:12496757, ECO:0000269|PubMed:21536732,
CC ECO:0000269|PubMed:24898207}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SDO1/SBDS family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SBDSbase; Note=SBDS mutation db;
CC URL="http://structure.bmc.lu.se/idbase/SBDSbase/";
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DR EMBL; AY169963; AAN77490.1; -; mRNA.
DR EMBL; AF151855; AAD34092.1; -; mRNA.
DR EMBL; AK001779; BAA91905.1; -; mRNA.
DR EMBL; AK289609; BAF82298.1; -; mRNA.
DR EMBL; CH471140; EAX07906.1; -; Genomic_DNA.
DR EMBL; BC065700; AAH65700.1; -; mRNA.
DR CCDS; CCDS5537.1; -.
DR RefSeq; NP_057122.2; NM_016038.3.
DR PDB; 2KDO; NMR; -; A=1-250.
DR PDB; 2L9N; NMR; -; A=1-250.
DR PDB; 5AN9; EM; 3.30 A; J=1-250.
DR PDB; 5ANB; EM; 4.10 A; J=1-250.
DR PDB; 5ANC; EM; 4.20 A; J=1-250.
DR PDB; 6QKL; EM; 3.30 A; J=1-250.
DR PDBsum; 2KDO; -.
DR PDBsum; 2L9N; -.
DR PDBsum; 5AN9; -.
DR PDBsum; 5ANB; -.
DR PDBsum; 5ANC; -.
DR PDBsum; 6QKL; -.
DR AlphaFoldDB; Q9Y3A5; -.
DR BMRB; Q9Y3A5; -.
DR SMR; Q9Y3A5; -.
DR BioGRID; 119307; 118.
DR IntAct; Q9Y3A5; 17.
DR MINT; Q9Y3A5; -.
DR STRING; 9606.ENSP00000246868; -.
DR GlyGen; Q9Y3A5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y3A5; -.
DR PhosphoSitePlus; Q9Y3A5; -.
DR BioMuta; SBDS; -.
DR DMDM; 28380824; -.
DR EPD; Q9Y3A5; -.
DR jPOST; Q9Y3A5; -.
DR MassIVE; Q9Y3A5; -.
DR MaxQB; Q9Y3A5; -.
DR PaxDb; Q9Y3A5; -.
DR PeptideAtlas; Q9Y3A5; -.
DR PRIDE; Q9Y3A5; -.
DR ProteomicsDB; 85997; -.
DR Antibodypedia; 14141; 244 antibodies from 31 providers.
DR DNASU; 51119; -.
DR Ensembl; ENST00000246868.7; ENSP00000246868.2; ENSG00000126524.11.
DR GeneID; 51119; -.
DR KEGG; hsa:51119; -.
DR MANE-Select; ENST00000246868.7; ENSP00000246868.2; NM_016038.4; NP_057122.2.
DR UCSC; uc003tvm.2; human.
DR CTD; 51119; -.
DR DisGeNET; 51119; -.
DR GeneCards; SBDS; -.
DR GeneReviews; SBDS; -.
DR HGNC; HGNC:19440; SBDS.
DR HPA; ENSG00000126524; Low tissue specificity.
DR MalaCards; SBDS; -.
DR MIM; 260400; phenotype.
DR MIM; 607444; gene.
DR neXtProt; NX_Q9Y3A5; -.
DR OpenTargets; ENSG00000126524; -.
DR Orphanet; 88; Idiopathic aplastic anemia.
DR Orphanet; 811; Shwachman-Diamond syndrome.
DR PharmGKB; PA134978742; -.
DR VEuPathDB; HostDB:ENSG00000126524; -.
DR eggNOG; KOG2917; Eukaryota.
DR GeneTree; ENSGT00390000008135; -.
DR HOGENOM; CLU_043216_1_1_1; -.
DR InParanoid; Q9Y3A5; -.
DR OrthoDB; 1217666at2759; -.
DR PhylomeDB; Q9Y3A5; -.
DR TreeFam; TF300881; -.
DR PathwayCommons; Q9Y3A5; -.
DR SignaLink; Q9Y3A5; -.
DR SIGNOR; Q9Y3A5; -.
DR BioGRID-ORCS; 51119; 739 hits in 1058 CRISPR screens.
DR ChiTaRS; SBDS; human.
DR EvolutionaryTrace; Q9Y3A5; -.
DR GeneWiki; SBDS; -.
DR GenomeRNAi; 51119; -.
DR Pharos; Q9Y3A5; Tbio.
DR PRO; PR:Q9Y3A5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y3A5; protein.
DR Bgee; ENSG00000126524; Expressed in popliteal artery and 102 other tissues.
DR ExpressionAtlas; Q9Y3A5; baseline and differential.
DR Genevisible; Q9Y3A5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IDA:UniProtKB.
DR GO; GO:0048539; P:bone marrow development; IMP:UniProtKB.
DR GO; GO:0030282; P:bone mineralization; IMP:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:UniProtKB.
DR GO; GO:0001833; P:inner cell mass cell proliferation; IEA:Ensembl.
DR GO; GO:0030595; P:leukocyte chemotaxis; IDA:UniProtKB.
DR GO; GO:0042256; P:mature ribosome assembly; IDA:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR Gene3D; 1.10.10.900; -; 1.
DR Gene3D; 3.30.1250.10; -; 1.
DR InterPro; IPR018023; Ribosome_mat_SBDS_CS.
DR InterPro; IPR036786; Ribosome_mat_SBDS_N_sf.
DR InterPro; IPR018978; Ribosome_mat_Sdo1/SBDS_C.
DR InterPro; IPR019783; Ribosome_mat_Sdo1/SBDS_N.
DR InterPro; IPR002140; Sdo1/SBDS.
DR InterPro; IPR039100; Sdo1/SBDS-like.
DR InterPro; IPR037188; Sdo1/SBDS_central_sf.
DR PANTHER; PTHR10927; PTHR10927; 1.
DR Pfam; PF01172; SBDS; 1.
DR Pfam; PF09377; SBDS_C; 1.
DR SUPFAM; SSF109728; SSF109728; 1.
DR SUPFAM; SSF89895; SSF89895; 1.
DR TIGRFAMs; TIGR00291; RNA_SBDS; 1.
DR PROSITE; PS01267; UPF0023; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disease variant; Nucleus; Reference proteome;
KW Ribosome biogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..250
FT /note="Ribosome maturation protein SBDS"
FT /id="PRO_0000123762"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT VARIANT 8
FT /note="N -> K (in SDS1; unknown pathological significance;
FT dbSNP:rs28942099)"
FT /evidence="ECO:0000269|PubMed:12496757"
FT /id="VAR_015390"
FT VARIANT 33
FT /note="K -> T (in SDS1; dbSNP:rs373730800)"
FT /evidence="ECO:0000269|PubMed:24898207"
FT /id="VAR_071673"
FT VARIANT 44
FT /note="E -> G (in SDS1; unknown pathological significance;
FT dbSNP:rs1554341516)"
FT /evidence="ECO:0000269|PubMed:12496757"
FT /id="VAR_015391"
FT VARIANT 67
FT /note="K -> E (in SDS1; unknown pathological significance;
FT dbSNP:rs1554341499)"
FT /evidence="ECO:0000269|PubMed:12496757"
FT /id="VAR_015392"
FT VARIANT 87
FT /note="I -> S (in SDS1; unknown pathological significance;
FT dbSNP:rs1554341363)"
FT /evidence="ECO:0000269|PubMed:12496757"
FT /id="VAR_015393"
FT VARIANT 126
FT /note="R -> T (in SDS1; strongly reduced release of EIF6
FT from pre-60S ribosome subunits; dbSNP:rs113993995)"
FT /evidence="ECO:0000269|PubMed:12496757,
FT ECO:0000269|PubMed:21536732"
FT /id="VAR_015394"
FT VARIANT 169
FT /note="R -> C (in SDS1; unknown pathological significance;
FT dbSNP:rs113993996)"
FT /evidence="ECO:0000269|PubMed:12496757"
FT /id="VAR_015395"
FT VARIANT 212
FT /note="I -> T (in dbSNP:rs79344818)"
FT /evidence="ECO:0000269|PubMed:12496757"
FT /id="VAR_015396"
FT MUTAGEN 151
FT /note="K->N: Strongly reduced release of EIF6 from pre-60S
FT ribosome subunits."
FT /evidence="ECO:0000269|PubMed:21536732"
FT CONFLICT 41..43
FT /note="SGV -> RAW (in Ref. 2; AAD34092)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="T -> A (in Ref. 2; AAD34092)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="E -> G (in Ref. 2; AAD34092)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="I -> F (in Ref. 2; AAD34092)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="R -> G (in Ref. 2; AAD34092)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="S -> L (in Ref. 2; AAD34092)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="T -> P (in Ref. 2; AAD34092)"
FT /evidence="ECO:0000305"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:2L9N"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:5AN9"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:5AN9"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:5AN9"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:5AN9"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2L9N"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5AN9"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:5AN9"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2KDO"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:5AN9"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:5AN9"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:5AN9"
FT HELIX 97..115
FT /evidence="ECO:0007829|PDB:5AN9"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:5AN9"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:5AN9"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:5AN9"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:5AN9"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:5AN9"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:5AN9"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:5AN9"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:5AN9"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:5AN9"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:5AN9"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:5AN9"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:2L9N"
FT HELIX 218..229
FT /evidence="ECO:0007829|PDB:5AN9"
FT STRAND 234..248
FT /evidence="ECO:0007829|PDB:5AN9"
SQ SEQUENCE 250 AA; 28764 MW; D35C43003C05F5A7 CRC64;
MSIFTPTNQI RLTNVAVVRM KRAGKRFEIA CYKNKVVGWR SGVEKDLDEV LQTHSVFVNV
SKGQVAKKED LISAFGTDDQ TEICKQILTK GEVQVSDKER HTQLEQMFRD IATIVADKCV
NPETKRPYTV ILIERAMKDI HYSVKTNKST KQQALEVIKQ LKEKMKIERA HMRLRFILPV
NEGKKLKEKL KPLIKVIESE DYGQQLEIVC LIDPGCFREI DELIKKETKG KGSLEVLNLK
DVEEGDEKFE
