SBDS_MOUSE
ID SBDS_MOUSE Reviewed; 250 AA.
AC P70122; Q3TG78; Q9CR18;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ribosome maturation protein SBDS;
DE AltName: Full=Protein 22A3;
DE AltName: Full=Shwachman-Bodian-Diamond syndrome protein homolog;
GN Name=Sbds;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, Liver, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE.
RC STRAIN=BALB/cJ; TISSUE=Cochlea;
RA Crozet F.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=16914746; DOI=10.1128/mcb.00091-06;
RA Zhang S., Shi M., Hui C.C., Rommens J.M.;
RT "Loss of the mouse ortholog of the shwachman-diamond syndrome gene (Sbds)
RT results in early embryonic lethality.";
RL Mol. Cell. Biol. 26:6656-6663(2006).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
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).
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 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:19602484, ECO:0000269|PubMed:21536732}.
CC -!- SUBUNIT: Associates with the 60S ribosomal subunit. Interacts with
CC NPM1, RPA1 and PRKDC. May interact with NIP7. Found in a complex
CC consisting of the 60S ribosomal subunit, SBDS and EFL1. Interacts with
CC CLN3 (By similarity). {ECO:0000250|UniProtKB:Q9Y3A5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus {ECO:0000250}.
CC Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC Note=Detected in the cytoplasm, but not in the nucleus
CC (PubMed:21536732). Primarily detected in the cytoplasm, and at low
CC levels in nucleus (PubMed:19602484). 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 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:19602484,
CC ECO:0000269|PubMed:21536732}.
CC -!- TISSUE SPECIFICITY: Detected in adult liver, brain, heart, spleen,
CC pancreas, kidney, lung and testis (at protein level). Detected in
CC heart, brain, lung, liver, kidney and testis.
CC {ECO:0000269|PubMed:16914746}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality. Embryos cease to develop
CC prior to 6.5 dpc. Reduced assembly of 60S ribosomes and accumulation of
CC halfmer ribosomes. {ECO:0000269|PubMed:16914746,
CC ECO:0000269|PubMed:21536732}.
CC -!- SIMILARITY: Belongs to the SDO1/SBDS family. {ECO:0000305}.
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DR EMBL; AK005079; BAB23803.1; -; mRNA.
DR EMBL; AK014648; BAB29487.1; -; mRNA.
DR EMBL; AK019228; BAB31612.1; -; mRNA.
DR EMBL; AK168847; BAE40670.1; -; mRNA.
DR EMBL; BC003849; AAH03849.1; -; mRNA.
DR EMBL; X99668; CAA67982.1; ALT_SEQ; mRNA.
DR CCDS; CCDS19710.1; -.
DR RefSeq; NP_075737.1; NM_023248.2.
DR AlphaFoldDB; P70122; -.
DR BMRB; P70122; -.
DR SMR; P70122; -.
DR BioGRID; 211663; 5.
DR IntAct; P70122; 1.
DR MINT; P70122; -.
DR STRING; 10090.ENSMUSP00000026387; -.
DR iPTMnet; P70122; -.
DR PhosphoSitePlus; P70122; -.
DR SwissPalm; P70122; -.
DR EPD; P70122; -.
DR jPOST; P70122; -.
DR MaxQB; P70122; -.
DR PaxDb; P70122; -.
DR PeptideAtlas; P70122; -.
DR PRIDE; P70122; -.
DR ProteomicsDB; 256709; -.
DR Antibodypedia; 14141; 244 antibodies from 31 providers.
DR DNASU; 66711; -.
DR Ensembl; ENSMUST00000026387; ENSMUSP00000026387; ENSMUSG00000025337.
DR GeneID; 66711; -.
DR KEGG; mmu:66711; -.
DR UCSC; uc008zuj.1; mouse.
DR CTD; 51119; -.
DR MGI; MGI:1913961; Sbds.
DR VEuPathDB; HostDB:ENSMUSG00000025337; -.
DR eggNOG; KOG2917; Eukaryota.
DR GeneTree; ENSGT00390000008135; -.
DR HOGENOM; CLU_043216_1_1_1; -.
DR InParanoid; P70122; -.
DR OMA; AVNPQMD; -.
DR OrthoDB; 1217666at2759; -.
DR PhylomeDB; P70122; -.
DR TreeFam; TF300881; -.
DR BioGRID-ORCS; 66711; 24 hits in 73 CRISPR screens.
DR ChiTaRS; Sbds; mouse.
DR PRO; PR:P70122; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P70122; protein.
DR Bgee; ENSMUSG00000025337; Expressed in undifferentiated genital tubercle and 258 other tissues.
DR ExpressionAtlas; P70122; baseline and differential.
DR Genevisible; P70122; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; ISO:MGI.
DR GO; GO:0048539; P:bone marrow development; ISO:MGI.
DR GO; GO:0030282; P:bone mineralization; ISO:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISS:UniProtKB.
DR GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
DR GO; GO:0030595; P:leukocyte chemotaxis; ISO:MGI.
DR GO; GO:0042256; P:mature ribosome assembly; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; ISO:MGI.
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 Acetylation; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3A5"
FT CHAIN 2..250
FT /note="Ribosome maturation protein SBDS"
FT /id="PRO_0000123763"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3A5"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 250 AA; 28781 MW; 3137CA2807DD250A CRC64;
MSIFTPTNQI RLTNVAVVRM KRGGKRFEIA CYKNKVVGWR SGVEKDLDEV LQTHSVFVNV
SKGQVAKKED LISAFGTDDQ TEICKQILTK GEVQVSDKER HTQLEQMFRD IATIVADKCV
NPETKRPYTV ILIERAMKDI HYSVKPNKST KQQALEVIKQ LKEKMKIERA HMRLRFILPV
NEGKKLKEKL KPLMKVVESE DYSQQLEIVC LIDPGCFREI DELIKKETKG RGSLEVLSLK
DVEEGDEKFE
