LAS1L_MOUSE
ID LAS1L_MOUSE Reviewed; 776 AA.
AC A2BE28; A2BE30; Q6KAR5; Q8C742;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ribosomal biogenesis protein LAS1L;
DE AltName: Full=Protein LAS1 homolog;
GN Name=Las1l;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 253-575 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Stomach;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 541-776.
RC TISSUE=Spleen;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, 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 [6]
RP FUNCTION, IDENTIFICATION IN THE 5FMC COMPLEX, INTERACTION OF THE 5FMC
RP COMPLEX WITH CHTOP AND ZNF148, AND SUBCELLULAR LOCATION.
RX PubMed=22872859; DOI=10.1074/mcp.m112.017194;
RA Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
RA Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.;
RT "Five friends of methylated chromatin target of protein-arginine-
RT methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation
RT to desumoylation.";
RL Mol. Cell. Proteomics 11:1263-1273(2012).
CC -!- FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit.
CC Required for maturation of the 28S rRNA (By similarity). Functions as a
CC component of the Five Friends of Methylated CHTOP (5FMC) complex; the
CC 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to
CC desumoylation of ZNF148 and subsequent transactivation of ZNF148 target
CC genes. {ECO:0000250, ECO:0000269|PubMed:22872859}.
CC -!- SUBUNIT: Component of some MLL1/MLL complex, at least composed of the
CC core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well
CC as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1,
CC LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10 (By similarity). Component of the 5FMC complex, at least composed
CC of PELP1, LAS1L, TEX10, WDR18 and SENP3; the complex interacts with
CC methylated CHTOP and ZNF148. {ECO:0000250,
CC ECO:0000269|PubMed:22872859}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:22872859}. Cytoplasm
CC {ECO:0000269|PubMed:22872859}. Note=Localizes mainly to the granular
CC component, the region implicated in the later steps of rRNA processing
CC and subunit assembly and export (By similarity). Mainly found in the
CC nucleoplasm, with low levels detected in the cytoplasmic and chromatin
CC fractions. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2BE28-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2BE28-2; Sequence=VSP_038670;
CC -!- SIMILARITY: Belongs to the LAS1 family. {ECO:0000305}.
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DR EMBL; BX005184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC141155; AAI41156.1; -; mRNA.
DR EMBL; AK052578; BAC35047.1; -; mRNA.
DR EMBL; AK131142; BAD21392.1; -; mRNA.
DR CCDS; CCDS30287.1; -. [A2BE28-2]
DR RefSeq; NP_690035.2; NM_152822.3. [A2BE28-2]
DR RefSeq; XP_006528397.1; XM_006528334.2.
DR AlphaFoldDB; A2BE28; -.
DR SMR; A2BE28; -.
DR BioGRID; 217980; 15.
DR IntAct; A2BE28; 2.
DR MINT; A2BE28; -.
DR STRING; 10090.ENSMUSP00000078901; -.
DR iPTMnet; A2BE28; -.
DR PhosphoSitePlus; A2BE28; -.
DR EPD; A2BE28; -.
DR MaxQB; A2BE28; -.
DR PaxDb; A2BE28; -.
DR PeptideAtlas; A2BE28; -.
DR PRIDE; A2BE28; -.
DR ProteomicsDB; 265044; -. [A2BE28-1]
DR ProteomicsDB; 265045; -. [A2BE28-2]
DR Antibodypedia; 13076; 163 antibodies from 26 providers.
DR Ensembl; ENSMUST00000079987; ENSMUSP00000078901; ENSMUSG00000057421. [A2BE28-2]
DR Ensembl; ENSMUST00000113864; ENSMUSP00000109495; ENSMUSG00000057421. [A2BE28-1]
DR GeneID; 76130; -.
DR KEGG; mmu:76130; -.
DR UCSC; uc009tud.2; mouse. [A2BE28-2]
DR CTD; 81887; -.
DR MGI; MGI:1923380; Las1l.
DR VEuPathDB; HostDB:ENSMUSG00000057421; -.
DR eggNOG; KOG2425; Eukaryota.
DR GeneTree; ENSGT00390000014785; -.
DR HOGENOM; CLU_028117_0_0_1; -.
DR InParanoid; A2BE28; -.
DR OMA; PTCKTGT; -.
DR OrthoDB; 263288at2759; -.
DR TreeFam; TF314042; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 76130; 28 hits in 75 CRISPR screens.
DR ChiTaRS; Las1l; mouse.
DR PRO; PR:A2BE28; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; A2BE28; protein.
DR Bgee; ENSMUSG00000057421; Expressed in ectoplacental cone and 263 other tissues.
DR Genevisible; A2BE28; MM.
DR GO; GO:0090730; C:Las1 complex; IEA:InterPro.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR InterPro; IPR007174; Las1.
DR PANTHER; PTHR15002; PTHR15002; 2.
DR Pfam; PF04031; Las1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; rRNA processing.
FT CHAIN 1..776
FT /note="Ribosomal biogenesis protein LAS1L"
FT /id="PRO_0000390998"
FT REGION 185..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..223
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..605
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..646
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4W2"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4W2"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4W2"
FT VAR_SEQ 332..349
FT /note="DGQTEVQKGEVTEPNSHK -> E (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038670"
SQ SEQUENCE 776 AA; 89414 MW; 6855167CD37D57EC CRC64;
MDRVWRAWDG QSFKENQPES PSARGIVVSW LSRAEWEQVT VYLFCDDHKL QQYALNRITV
WRSRLGNELP LAVASTADLV RCKLIDAAGT LGTDELRLLY GMALVRFVNL ISERKTKCSN
LPLKYLAQEV NIPDWIVELR HNLTHKKMPH INECRRGCYF VLNWLQKTYW SRQLEGSLKE
TWELDEDQLD AEDPEEEERE IIADDVLEEI PEPQDDDKDE ELAVEDDANT KGNEEVASHP
EPSSRHKELY EKARELLVSY EEEQFKVLEK HRHLLQAIKV WNNLSPRVQC ILEELKSISW
ENRDAVLDAF LDDGFLIPTF EQLAALQIEY EDGQTEVQKG EVTEPNSHKN IDLNEVLVPK
PFSQFWQPLL RGLHSQTFTQ ALLERMFSEL STVGSTGIRP TYILRWTVEL IVANTKTGRN
ARRFSASQWE ARKSWRLFNC SATLDWPQVI ESCLGSPCWA SPQLLQVVFK AMGQVLPDEE
QEKLLRVCSI YTQNGENGLA KAIEGSSSSS TGKAPYTLDT LHEDLQPPGT NCESEESIQQ
KEQGNLKDVK QEEKKENEEE EKEEEEMEEE EEEEEEEKEE EEEEQEQEEH QEEEQEEEEE
EENQKVFQDQ MEADVEESDD VEEEEEVDDE EEDEDDDYDD DEEEDRMEVG AFSLAQGSSV
FENTRTTSRK REALQGSAWQ VSSEDVRWGT FPLGRLPGQT EDPAELMLDN YDTMYLLDQP
VIEHRLEPQK SKSSTLSLCC GGSNTNSSSS SSSGNMEGLL WNQGQMHGLK AGLQLF
