ID   SBDS_HUMAN              Reviewed;         250 AA.
AC   Q9Y3A5; Q96FX0; Q9NV53;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-APR-2008, entry version 66.
DE   Ribosome maturation protein SBDS (Shwachman-Bodian-Diamond syndrome
DE   protein).
GN   Name=SBDS; ORFNames=CGI-97;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SDS LYS-8; GLY-44; GLU-67;
RP   SER-87; THR-126; CYS-169 AND THR-212.
RX   MEDLINE=22397848; 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   MEDLINE=20272150; 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=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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-19, CLEAVAGE OF INITIATOR METHIONINE,
RP   ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
RC   TISSUE=Platelet;
RA   Bienvenut W.V., Claeys D.;
RL   Submitted (NOV-2005) to UniProtKB.
RN   [6]
RP   FUNCTION.
RX   PubMed=15701634; DOI=10.1074/jbc.M414421200;
RA   Savchenko A., Krogan N., Cort J.R., Evdokimova E., Lew J.M., Yee A.A.,
RA   Sanchez-Pulido L., Andrade M.A., Bochkarev A., Watson J.D.,
RA   Kennedy M.A., Greenblatt J., Hughes T., Arrowsmith C.H., Rommens J.M.,
RA   Edwards A.M.;
RT   "The Shwachman-Bodian-Diamond syndrome protein family is involved in
RT   RNA metabolism.";
RL   J. Biol. Chem. 280:19213-19220(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124 AND TYR-128, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=17924679; DOI=10.1021/pr070152u;
RA   Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT   "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT   cells and high confident phosphopeptide identification by cross-
RT   validation of MS/MS and MS/MS/MS spectra.";
RL   J. Proteome Res. 6:4150-4162(2007).
RN   [8]
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
RT   with HsNip7 and its down-regulation affects gene expression at the
RT   transcriptional and translational levels.";
RL   Exp. Cell Res. 313:4180-4195(2007).
CC   -!- FUNCTION: May be involved in the biogenesis of the 60S ribosomal
CC       subunit and translational activation of ribosomes. May trigger the
CC       GTP-dependent release of EIF6 from 60S pre-ribosomes in the
CC       cytoplasm, thereby activating ribosomes for translation competence
CC       by allowing 80S ribosome assembly and facilitating EIF6 recycling
CC       to the nucleus, where it is required for 60S rRNA processing and
CC       nuclear export (By similarity).
CC   -!- SUBUNIT: Associates with the 60S ribosomal subunit (By
CC       similarity). May interact with NIP7.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DISEASE: Defects in SBDS are the cause of Shwachman-Diamond
CC       syndrome (SDS) [MIM:260400]. SDS is an autosomal recessive
CC       disorder characterized by pancreatic exocrine insufficiency,
CC       hematologic dysfunction, and skeletal abnormalities.
CC   -!- SIMILARITY: Belongs to the SDO1/SBDS family.
CC   -!- WEB RESOURCE: Name=SBDSbase; Note=SBDS mutation db;
CC       URL="http://bioinf.uta.fi/SBDSbase/";
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.genetests.org/query?gene=SBDS";
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DR   EMBL; AY169963; AAN77490.1; -; mRNA.
DR   EMBL; AF151855; AAD34092.1; -; mRNA.
DR   EMBL; AK001779; BAA91905.1; -; mRNA.
DR   EMBL; BC065700; AAH65700.1; -; mRNA.
DR   RefSeq; NP_057122.2; -.
DR   UniGene; Hs.110445; -.
DR   PeptideAtlas; Q9Y3A5; -.
DR   Ensembl; ENSG00000126524; Homo sapiens.
DR   GeneID; 51119; -.
DR   KEGG; hsa:51119; -.
DR   HGNC; HGNC:19440; SBDS.
DR   MIM; 260400; phenotype.
DR   MIM; 607444; gene.
DR   Orphanet; 811; Shwachman-diamond syndrome.
DR   PharmGKB; PA134978742; -.
DR   LinkHub; Q9Y3A5; -.
DR   ArrayExpress; Q9Y3A5; -.
DR   CleanEx; HS_SBDS; -.
DR   GermOnline; ENSG00000126524; Homo sapiens.
DR   InterPro; IPR002140; SBDS.
DR   PANTHER; PTHR10927; SBDS; 1.
DR   Pfam; PF01172; SBDS; 1.
DR   ProDom; PD009796; UPF0023; 1.
DR   TIGRFAMs; TIGR00291; SBDS; 1.
DR   PROSITE; PS01267; UPF0023; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Disease mutation;
KW   Phosphoprotein; Ribosome biogenesis.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    250       Ribosome maturation protein SBDS.
FT                                /FTId=PRO_0000123762.
FT   MOD_RES       2      2       N-acetylserine.
FT   MOD_RES     124    124       Phosphothreonine.
FT   MOD_RES     128    128       Phosphotyrosine.
FT   VARIANT       8      8       N -> K (in SDS).
FT                                /FTId=VAR_015390.
FT   VARIANT      44     44       E -> G (in SDS).
FT                                /FTId=VAR_015391.
FT   VARIANT      67     67       K -> E (in SDS).
FT                                /FTId=VAR_015392.
FT   VARIANT      87     87       I -> S (in SDS).
FT                                /FTId=VAR_015393.
FT   VARIANT     126    126       R -> T (in SDS).
FT                                /FTId=VAR_015394.
FT   VARIANT     169    169       R -> C (in SDS).
FT                                /FTId=VAR_015395.
FT   VARIANT     212    212       I -> T (in SDS).
FT                                /FTId=VAR_015396.
FT   CONFLICT     41     43       SGV -> RAW (in Ref. 2; AAD34092).
FT   CONFLICT     89     89       T -> A (in Ref. 2; AAD34092).
FT   CONFLICT    105    105       E -> G (in Ref. 2; AAD34092).
FT   CONFLICT    114    114       I -> F (in Ref. 2; AAD34092).
FT   CONFLICT    126    126       R -> G (in Ref. 2; AAD34092).
FT   CONFLICT    143    143       S -> L (in Ref. 2; AAD34092).
FT   CONFLICT    146    146       T -> P (in Ref. 2; AAD34092).
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
//