BYST_RAT
ID BYST_RAT Reviewed; 436 AA.
AC Q80WL2; Q6AYI7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Bystin;
GN Name=Bysl {ECO:0000312|EMBL:AAH79030.1, ECO:0000312|RGD:727959};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAP22286.4}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAP22286.4};
RA Yang S., Li Z., Xu L., Zhou J.;
RT "Identification of rat bystin gene.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAH79030.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAH79030.1};
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Required for processing of 20S pre-rRNA precursor and
CC biogenesis of 40S ribosomal subunits. {ECO:0000250|UniProtKB:O54825}.
CC -!- SUBUNIT: Binds trophinin, tastin and cytokeratins.
CC {ECO:0000250|UniProtKB:Q13895}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13895}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q13895}. Note=Associated with
CC 40S ribosomal subunits. {ECO:0000250|UniProtKB:Q13895}.
CC -!- SIMILARITY: Belongs to the bystin family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH79030.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP22286.4; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY257675; AAP22286.4; ALT_INIT; mRNA.
DR EMBL; BC079030; AAH79030.1; ALT_INIT; mRNA.
DR RefSeq; NP_872615.3; NM_182674.3.
DR AlphaFoldDB; Q80WL2; -.
DR SMR; Q80WL2; -.
DR IntAct; Q80WL2; 1.
DR MINT; Q80WL2; -.
DR STRING; 10116.ENSRNOP00000067656; -.
DR iPTMnet; Q80WL2; -.
DR PhosphoSitePlus; Q80WL2; -.
DR jPOST; Q80WL2; -.
DR PaxDb; Q80WL2; -.
DR PRIDE; Q80WL2; -.
DR GeneID; 359727; -.
DR KEGG; rno:359727; -.
DR CTD; 705; -.
DR RGD; 727959; Bysl.
DR eggNOG; KOG3871; Eukaryota.
DR InParanoid; Q80WL2; -.
DR OrthoDB; 1193442at2759; -.
DR PhylomeDB; Q80WL2; -.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q80WL2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IBA:GO_Central.
DR GO; GO:0030515; F:snoRNA binding; IBA:GO_Central.
DR GO; GO:0001825; P:blastocyst formation; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISO:RGD.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR GO; GO:0001829; P:trophectodermal cell differentiation; ISO:RGD.
DR InterPro; IPR007955; Bystin.
DR PANTHER; PTHR12821; PTHR12821; 1.
DR Pfam; PF05291; Bystin; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis.
FT CHAIN 1..436
FT /note="Bystin"
FT /id="PRO_0000294934"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13895"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 155
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13895"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13895"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13895"
FT CONFLICT 112
FT /note="Missing (in Ref. 2; AAH79030)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="I -> K (in Ref. 2; AAH79030)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 50012 MW; 6DE83191F5135D5F CRC64;
MPKLKVTRGA RNQERHAPLA EQILAGDAVR AGTREKRRRH GVEEEEEYVG PRLSRRILQQ
ARQQQEELET EHATGDRPAK PRERATRLGP GVPQDGSDEE DEEWPTLEKA AKMTVVNHQA
EVVVDPEDER AIEMFMNKNP PVRRTLADII MEKLTEKQTE VETVMSEVSG FPMPQLDPRV
LEVYRGVREV LCKYRSGILP KAFKIIPALS NWEQILYVTE PEAWTAAAMY QATRIFASNL
KERMAQRFYN LVLLPRVRDD IAEYKRLNFH LYMALKKALF KPGAWFKGIL IPLCESGTCT
LREAIIVGSI ISKCSIPVLH SSAAMLKIAE MEYSGASSIF LRLLLDKKYA LPYRVLDALV
FHFLAFRTEK RQLPVLWHQC LLTLAQRYKA DLATEQKEAL LELLRLQPHP QLSPEIRREL
QSAVPRDVED VVVTME
