LAS1L_HUMAN
ID LAS1L_HUMAN Reviewed; 734 AA.
AC Q9Y4W2; A9X410; Q5JXQ0; Q8TEN5; Q9H9V5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Ribosomal biogenesis protein LAS1L;
DE AltName: Full=Protein LAS1 homolog;
GN Name=LAS1L; ORFNames=MSTP060;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Aorta;
RA Zhao B., Xu Y.Y., Liu Y.Q., Wang X.Y., Liu B., Ye J., Song L., Zhao Y.,
RA Cao H.Q., Zhao X.W., Gao Y., Liu L.S., Ding J.F., Gao R.L., Wu Q.Y.,
RA Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, Lung, and Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 345-377.
RX PubMed=17623809; DOI=10.1101/gr.6320607;
RA Krull M., Petrusma M., Makalowski W., Brosius J., Schmitz J.;
RT "Functional persistence of exonized mammalian-wide interspersed repeat
RT elements (MIRs).";
RL Genome Res. 17:1139-1145(2007).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [8]
RP IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT "Physical association and coordinate function of the H3 K4
RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL Cell 121:873-885(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20647540; DOI=10.1128/mcb.00358-10;
RA Castle C.D., Cassimere E.K., Lee J., Denicourt C.;
RT "Las1L is a nucleolar protein required for cell proliferation and ribosome
RT biogenesis.";
RL Mol. Cell. Biol. 30:4404-4414(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND SER-617, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND SER-617, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP FUNCTION, AND IDENTIFICATION IN THE 5FMC COMPLEX.
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).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441; SER-523; SER-560 AND
RP SER-617, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP INVOLVEMENT IN WTS, AND VARIANTS WTS GLY-269 AND TRP-415.
RX PubMed=25644381; DOI=10.1038/mp.2014.193;
RA Hu H., Haas S.A., Chelly J., Van Esch H., Raynaud M., de Brouwer A.P.,
RA Weinert S., Froyen G., Frints S.G., Laumonnier F., Zemojtel T., Love M.I.,
RA Richard H., Emde A.K., Bienek M., Jensen C., Hambrock M., Fischer U.,
RA Langnick C., Feldkamp M., Wissink-Lindhout W., Lebrun N., Castelnau L.,
RA Rucci J., Montjean R., Dorseuil O., Billuart P., Stuhlmann T., Shaw M.,
RA Corbett M.A., Gardner A., Willis-Owen S., Tan C., Friend K.L., Belet S.,
RA van Roozendaal K.E., Jimenez-Pocquet M., Moizard M.P., Ronce N., Sun R.,
RA O'Keeffe S., Chenna R., van Boemmel A., Goeke J., Hackett A., Field M.,
RA Christie L., Boyle J., Haan E., Nelson J., Turner G., Baynam G.,
RA Gillessen-Kaesbach G., Mueller U., Steinberger D., Budny B.,
RA Badura-Stronka M., Latos-Bielenska A., Ousager L.B., Wieacker P.,
RA Rodriguez Criado G., Bondeson M.L., Anneren G., Dufke A., Cohen M.,
RA Van Maldergem L., Vincent-Delorme C., Echenne B., Simon-Bouy B.,
RA Kleefstra T., Willemsen M., Fryns J.P., Devriendt K., Ullmann R.,
RA Vingron M., Wrogemann K., Wienker T.F., Tzschach A., van Bokhoven H.,
RA Gecz J., Jentsch T.J., Chen W., Ropers H.H., Kalscheuer V.M.;
RT "X-exome sequencing of 405 unresolved families identifies seven novel
RT intellectual disability genes.";
RL Mol. Psychiatry 21:133-148(2016).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-215 AND LYS-226, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [22]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-170.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit.
CC Required for maturation of the 28S rRNA. Functions as a component of
CC the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex
CC is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of
CC ZNF148 and subsequent transactivation of ZNF148 target genes.
CC {ECO:0000269|PubMed:20647540, 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, KAT8/MOF, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10. Component of the 5FMC complex, at least composed of PELP1,
CC LAS1L, TEX10, WDR18 and SENP3; the complex interacts with methylated
CC CHTOP and ZNF148. {ECO:0000269|PubMed:15960975,
CC ECO:0000269|PubMed:22872859}.
CC -!- INTERACTION:
CC Q9Y4W2; PRO_0000037309 [P0C6X7]: rep; Xeno; NbExp=2; IntAct=EBI-1051591, EBI-25475797;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:20647540}. Nucleus, nucleoplasm {ECO:0000250}.
CC Cytoplasm {ECO:0000250}. Note=Mainly found in the nucleoplasm, with low
CC levels detected in the cytoplasmic and chromatin fractions (By
CC similarity). Localizes mainly to the granular component, the region
CC implicated in the later steps of rRNA processing and subunit assembly
CC and export. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9Y4W2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4W2-2; Sequence=VSP_015181;
CC Name=3;
CC IsoId=Q9Y4W2-3; Sequence=VSP_015178, VSP_015181;
CC Name=4;
CC IsoId=Q9Y4W2-4; Sequence=VSP_015179, VSP_015180;
CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic,
CC Wilson-Turner type (WTS) [MIM:309585]: A neurologic disorder
CC characterized by severe intellectual disability, dysmorphic facial
CC features, hypogonadism, short stature, and truncal obesity. Affected
CC females have a milder phenotype than affected males.
CC {ECO:0000269|PubMed:25644381}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the LAS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB84913.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF116730; AAO15306.1; -; mRNA.
DR EMBL; AK074087; BAB84913.1; ALT_INIT; mRNA.
DR EMBL; AK022587; BAB14114.1; -; mRNA.
DR EMBL; AL050306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014545; AAH14545.1; -; mRNA.
DR EMBL; BC018610; AAH18610.1; -; mRNA.
DR EMBL; BC019302; AAH19302.1; -; mRNA.
DR EMBL; DQ323624; ABD39127.1; -; mRNA.
DR CCDS; CCDS14381.1; -. [Q9Y4W2-1]
DR CCDS; CCDS55433.1; -. [Q9Y4W2-3]
DR CCDS; CCDS55434.1; -. [Q9Y4W2-2]
DR RefSeq; NP_001164120.1; NM_001170649.1. [Q9Y4W2-2]
DR RefSeq; NP_001164121.1; NM_001170650.1. [Q9Y4W2-3]
DR RefSeq; NP_112483.1; NM_031206.4. [Q9Y4W2-1]
DR AlphaFoldDB; Q9Y4W2; -.
DR SMR; Q9Y4W2; -.
DR BioGRID; 123620; 119.
DR CORUM; Q9Y4W2; -.
DR ELM; Q9Y4W2; -.
DR IntAct; Q9Y4W2; 62.
DR MINT; Q9Y4W2; -.
DR STRING; 9606.ENSP00000363944; -.
DR GlyGen; Q9Y4W2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y4W2; -.
DR PhosphoSitePlus; Q9Y4W2; -.
DR BioMuta; LAS1L; -.
DR DMDM; 73920837; -.
DR SWISS-2DPAGE; Q9Y4W2; -.
DR EPD; Q9Y4W2; -.
DR jPOST; Q9Y4W2; -.
DR MassIVE; Q9Y4W2; -.
DR MaxQB; Q9Y4W2; -.
DR PaxDb; Q9Y4W2; -.
DR PeptideAtlas; Q9Y4W2; -.
DR PRIDE; Q9Y4W2; -.
DR ProteomicsDB; 86250; -. [Q9Y4W2-1]
DR ProteomicsDB; 86251; -. [Q9Y4W2-2]
DR ProteomicsDB; 86252; -. [Q9Y4W2-3]
DR ProteomicsDB; 86253; -. [Q9Y4W2-4]
DR Antibodypedia; 13076; 163 antibodies from 26 providers.
DR DNASU; 81887; -.
DR Ensembl; ENST00000374804.9; ENSP00000363937.5; ENSG00000001497.18. [Q9Y4W2-3]
DR Ensembl; ENST00000374807.9; ENSP00000363940.5; ENSG00000001497.18. [Q9Y4W2-2]
DR Ensembl; ENST00000374811.8; ENSP00000363944.3; ENSG00000001497.18. [Q9Y4W2-1]
DR Ensembl; ENST00000484069.1; ENSP00000473471.1; ENSG00000001497.18. [Q9Y4W2-4]
DR GeneID; 81887; -.
DR KEGG; hsa:81887; -.
DR MANE-Select; ENST00000374811.8; ENSP00000363944.3; NM_031206.7; NP_112483.1.
DR UCSC; uc004dwa.3; human. [Q9Y4W2-1]
DR CTD; 81887; -.
DR DisGeNET; 81887; -.
DR GeneCards; LAS1L; -.
DR HGNC; HGNC:25726; LAS1L.
DR HPA; ENSG00000001497; Low tissue specificity.
DR MalaCards; LAS1L; -.
DR MIM; 300964; gene.
DR MIM; 309585; phenotype.
DR neXtProt; NX_Q9Y4W2; -.
DR OpenTargets; ENSG00000001497; -.
DR Orphanet; 404521; Spinal muscular atrophy with respiratory distress type 2.
DR Orphanet; 3459; Wilson-Turner syndrome.
DR PharmGKB; PA128394732; -.
DR VEuPathDB; HostDB:ENSG00000001497; -.
DR eggNOG; KOG2425; Eukaryota.
DR GeneTree; ENSGT00390000014785; -.
DR HOGENOM; CLU_028117_0_0_1; -.
DR InParanoid; Q9Y4W2; -.
DR OMA; PTCKTGT; -.
DR OrthoDB; 1070386at2759; -.
DR PhylomeDB; Q9Y4W2; -.
DR TreeFam; TF314042; -.
DR PathwayCommons; Q9Y4W2; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9Y4W2; -.
DR SIGNOR; Q9Y4W2; -.
DR BioGRID-ORCS; 81887; 401 hits in 676 CRISPR screens.
DR ChiTaRS; LAS1L; human.
DR GeneWiki; LAS1L; -.
DR GenomeRNAi; 81887; -.
DR Pharos; Q9Y4W2; Tbio.
DR PRO; PR:Q9Y4W2; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9Y4W2; protein.
DR Bgee; ENSG00000001497; Expressed in right hemisphere of cerebellum and 200 other tissues.
DR ExpressionAtlas; Q9Y4W2; baseline and differential.
DR Genevisible; Q9Y4W2; HS.
DR GO; GO:0090730; C:Las1 complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
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; 1.
DR Pfam; PF04031; Las1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disease variant; Intellectual disability;
KW Isopeptide bond; Nucleus; Obesity; Phosphoprotein; Reference proteome;
KW rRNA processing; Ubl conjugation.
FT CHAIN 1..734
FT /note="Ribosomal biogenesis protein LAS1L"
FT /id="PRO_0000211559"
FT REGION 204..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..606
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 226
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 79..120
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_015178"
FT VAR_SEQ 283..291
FT /note="VLEKFRYLP -> GGCAGCFSG (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_015179"
FT VAR_SEQ 292..734
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_015180"
FT VAR_SEQ 348..365
FT /note="DGQTEVQRGEGTDPKSHK -> E (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015181"
FT VARIANT 170
FT /note="R -> C (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1371889606)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036587"
FT VARIANT 269
FT /note="A -> G (in WTS; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:25644381"
FT /id="VAR_077824"
FT VARIANT 415
FT /note="R -> W (in WTS; unknown pathological significance;
FT dbSNP:rs1057518699)"
FT /evidence="ECO:0000269|PubMed:25644381"
FT /id="VAR_077825"
SQ SEQUENCE 734 AA; 83065 MW; A35CC38F95C39F7D CRC64;
MSWESGAGPG LGSQGMDLVW SAWYGKCVKG KGSLPLSAHG IVVAWLSRAE WDQVTVYLFC
DDHKLQRYAL NRITVWRSRS GNELPLAVAS TADLIRCKLL DVTGGLGTDE LRLLYGMALV
RFVNLISERK TKFAKVPLKC LAQEVNIPDW IVDLRHELTH KKMPHINDCR RGCYFVLDWL
QKTYWCRQLE NSLRETWELE EFREGIEEED QEEDKNIVVD DITEQKPEPQ DDGKSTESDV
KADGDSKGSE EVDSHCKKAL SHKELYERAR ELLVSYEEEQ FTVLEKFRYL PKAIKAWNNP
SPRVECVLAE LKGVTCENRE AVLDAFLDDG FLVPTFEQLA ALQIEYEDGQ TEVQRGEGTD
PKSHKNVDLN DVLVPKPFSQ FWQPLLRGLH SQNFTQALLE RMLSELPALG ISGIRPTYIL
RWTVELIVAN TKTGRNARRF SAGQWEARRG WRLFNCSASL DWPRMVESCL GSPCWASPQL
LRIIFKAMGQ GLPDEEQEKL LRICSIYTQS GENSLVQEGS EASPIGKSPY TLDSLYWSVK
PASSSFGSEA KAQQQEEQGS VNDVKEEEKE EKEVLPDQVE EEEENDDQEE EEEDEDDEDD
EEEDRMEVGP FSTGQESPTA ENARLLAQKR GALQGSAWQV SSEDVRWDTF PLGRMPGQTE
DPAELMLENY DTMYLLDQPV LEQRLEPSTC KTDTLGLSCG VGSGNCSNSS SSNFEGLLWS
QGQLHGLKTG LQLF
