RL1D1_MOUSE
ID RL1D1_MOUSE Reviewed; 452 AA.
AC Q8BVY0; Q8K235;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ribosomal L1 domain-containing protein 1;
GN Name=Rsl1d1 {ECO:0000312|MGI:MGI:1913659};
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;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, 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).
CC -!- FUNCTION: Regulates cellular senescence through inhibition of PTEN
CC translation. Acts as a pro-apoptotic regulator in response to DNA
CC damage. {ECO:0000250|UniProtKB:O76021}.
CC -!- SUBUNIT: Interacts with ING1. {ECO:0000250|UniProtKB:O76021}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:O76021}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC Highly divergent. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34355.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK075933; BAC36063.1; -; mRNA.
DR EMBL; AK136025; BAE22779.1; -; mRNA.
DR EMBL; AK166579; BAE38868.1; -; mRNA.
DR EMBL; BC034355; AAH34355.1; ALT_FRAME; mRNA.
DR EMBL; AC087541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49763.1; -.
DR RefSeq; NP_079822.1; NM_025546.2.
DR AlphaFoldDB; Q8BVY0; -.
DR SMR; Q8BVY0; -.
DR BioGRID; 211453; 27.
DR IntAct; Q8BVY0; 3.
DR MINT; Q8BVY0; -.
DR STRING; 10090.ENSMUSP00000113431; -.
DR iPTMnet; Q8BVY0; -.
DR PhosphoSitePlus; Q8BVY0; -.
DR SwissPalm; Q8BVY0; -.
DR jPOST; Q8BVY0; -.
DR MaxQB; Q8BVY0; -.
DR PaxDb; Q8BVY0; -.
DR PRIDE; Q8BVY0; -.
DR ProteomicsDB; 253308; -.
DR Antibodypedia; 11546; 161 antibodies from 30 providers.
DR Ensembl; ENSMUST00000119953; ENSMUSP00000113431; ENSMUSG00000005846.
DR GeneID; 66409; -.
DR KEGG; mmu:66409; -.
DR UCSC; uc007yfb.1; mouse.
DR CTD; 26156; -.
DR MGI; MGI:1913659; Rsl1d1.
DR VEuPathDB; HostDB:ENSMUSG00000005846; -.
DR eggNOG; KOG1685; Eukaryota.
DR GeneTree; ENSGT00440000038603; -.
DR HOGENOM; CLU_026457_0_0_1; -.
DR InParanoid; Q8BVY0; -.
DR OMA; KNEAIWL; -.
DR OrthoDB; 1000750at2759; -.
DR PhylomeDB; Q8BVY0; -.
DR TreeFam; TF354254; -.
DR BioGRID-ORCS; 66409; 28 hits in 73 CRISPR screens.
DR ChiTaRS; Rsl1d1; mouse.
DR PRO; PR:Q8BVY0; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BVY0; protein.
DR Bgee; ENSMUSG00000005846; Expressed in embryonic post-anal tail and 255 other tissues.
DR ExpressionAtlas; Q8BVY0; baseline and differential.
DR Genevisible; Q8BVY0; MM.
DR GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:2000772; P:regulation of cellular senescence; ISS:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR CDD; cd00403; Ribosomal_L1; 1.
DR Gene3D; 3.40.50.790; -; 1.
DR InterPro; IPR023674; Ribosomal_L1-like.
DR InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR Pfam; PF00687; Ribosomal_L1; 1.
DR SUPFAM; SSF56808; SSF56808; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..452
FT /note="Ribosomal L1 domain-containing protein 1"
FT /id="PRO_0000430629"
FT REGION 283..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 277..350
FT /evidence="ECO:0000255"
FT COMPBIAS 283..307
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 344
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 360
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 399
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 407
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 429
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 432
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O76021"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O76021"
SQ SEQUENCE 452 AA; 50421 MW; D40EA836C21D6B48 CRC64;
MKGSASESPS ASVAEATTTD VQVTPTALLQ LDREQIRKAV EVISNRSKSK KNNNELLLSG
SENLFLMVIL WKIPEKELRV KVPLPHSILS ESSDVCLFTK DEFDSPEQTE GFYKKLLKKH
GVNTISQIIP FKTLKTEYKA YEAKLRLLGS FEVFITDARI RRHLPSHIGR HFYQRKKVPV
SVNLLAKNLS KEINRCITGT VLNISKRGSC STIRIGHTGM ETEHIVDNIL AVSEMLSEKL
PEKWQSVKLL FLKTEKSVSL PIFSSFVTSQ DENAVSLRSL RKQELKKRKR ENAKLKKESK
MLRKKSKKAT SLLTQSGLAS SAPAKSPGAQ KKKTNKAHKK QKVTEECEEA IPQLVPIGET
PDKENVKMQE NITGKTPKSK SDPSTPKGKK RKALLATETP EASAPGTSGK KQKKDVQEFR
KPEASSFSTP RKSGKKASNT PRDKKTKAAH SN
