LSG1_HUMAN
ID LSG1_HUMAN Reviewed; 658 AA.
AC Q9H089; A0JLT4; A0PJK3; A6NI18; Q7L9H8; Q9NUK8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Large subunit GTPase 1 homolog;
DE Short=hLsg1;
DE EC=3.6.1.-;
GN Name=LSG1;
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], AND VARIANT GLU-267.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-267.
RC TISSUE=Duodenum, Placenta, and Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-642, AND VARIANT GLU-267.
RC TISSUE=Placenta;
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 [5]
RP FUNCTION, GTP-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=16209721; DOI=10.1186/1741-7007-3-21;
RA Reynaud E.G., Andrade M.A., Bonneau F., Ly T.B., Knop M., Scheffzek K.,
RA Pepperkok R.;
RT "Human Lsg1 defines a family of essential GTPases that correlates with the
RT evolution of compartmentalization.";
RL BMC Biol. 3:21-21(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-97, AND
RP 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).
CC -!- FUNCTION: GTPase required for the XPO1/CRM1-mediated nuclear export of
CC the 60S ribosomal subunit. Probably acts by mediating the release of
CC NMD3 from the 60S ribosomal subunit after export into the cytoplasm
CC (Probable). {ECO:0000305|PubMed:16209721}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16209721}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:16209721}. Nucleus, Cajal
CC body {ECO:0000269|PubMed:16209721}. Note=Shuttles between the Cajal
CC bodies in the nucleus and the endoplasmic reticulum.
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs described
CC by a G4-G1-G3 pattern.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. LSG1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH15042.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH40119.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AL136897; CAB66831.1; -; mRNA.
DR EMBL; AC046143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015042; AAH15042.1; ALT_SEQ; mRNA.
DR EMBL; BC040119; AAH40119.1; ALT_SEQ; mRNA.
DR EMBL; BC068500; AAH68500.1; -; mRNA.
DR EMBL; AK002163; BAA92116.1; -; mRNA.
DR CCDS; CCDS33922.1; -.
DR RefSeq; NP_060855.2; NM_018385.2.
DR PDB; 6LSR; EM; 3.13 A; 1=1-658.
DR PDBsum; 6LSR; -.
DR AlphaFoldDB; Q9H089; -.
DR SMR; Q9H089; -.
DR BioGRID; 120622; 132.
DR IntAct; Q9H089; 23.
DR MINT; Q9H089; -.
DR STRING; 9606.ENSP00000265245; -.
DR GlyGen; Q9H089; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H089; -.
DR PhosphoSitePlus; Q9H089; -.
DR BioMuta; LSG1; -.
DR DMDM; 172045910; -.
DR EPD; Q9H089; -.
DR jPOST; Q9H089; -.
DR MassIVE; Q9H089; -.
DR MaxQB; Q9H089; -.
DR PaxDb; Q9H089; -.
DR PeptideAtlas; Q9H089; -.
DR PRIDE; Q9H089; -.
DR ProteomicsDB; 80217; -.
DR Antibodypedia; 46856; 46 antibodies from 16 providers.
DR DNASU; 55341; -.
DR Ensembl; ENST00000265245.10; ENSP00000265245.5; ENSG00000041802.11.
DR GeneID; 55341; -.
DR KEGG; hsa:55341; -.
DR MANE-Select; ENST00000265245.10; ENSP00000265245.5; NM_018385.3; NP_060855.2.
DR UCSC; uc003fui.3; human.
DR CTD; 55341; -.
DR DisGeNET; 55341; -.
DR GeneCards; LSG1; -.
DR HGNC; HGNC:25652; LSG1.
DR HPA; ENSG00000041802; Low tissue specificity.
DR MIM; 610780; gene.
DR neXtProt; NX_Q9H089; -.
DR OpenTargets; ENSG00000041802; -.
DR PharmGKB; PA142671501; -.
DR VEuPathDB; HostDB:ENSG00000041802; -.
DR eggNOG; KOG1424; Eukaryota.
DR GeneTree; ENSGT00940000156442; -.
DR HOGENOM; CLU_011072_7_0_1; -.
DR InParanoid; Q9H089; -.
DR OMA; VNKADMM; -.
DR OrthoDB; 839833at2759; -.
DR PhylomeDB; Q9H089; -.
DR TreeFam; TF105747; -.
DR PathwayCommons; Q9H089; -.
DR SignaLink; Q9H089; -.
DR BioGRID-ORCS; 55341; 675 hits in 1083 CRISPR screens.
DR ChiTaRS; LSG1; human.
DR GeneWiki; LSG1; -.
DR GenomeRNAi; 55341; -.
DR Pharos; Q9H089; Tbio.
DR PRO; PR:Q9H089; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9H089; protein.
DR Bgee; ENSG00000041802; Expressed in granulocyte and 204 other tissues.
DR ExpressionAtlas; Q9H089; baseline and differential.
DR Genevisible; Q9H089; HS.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0051168; P:nuclear export; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR043358; GNL1-like.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45709; PTHR45709; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endoplasmic reticulum; GTP-binding; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..658
FT /note="Large subunit GTPase 1 homolog"
FT /id="PRO_0000324553"
FT DOMAIN 164..444
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..324
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 212..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 393..400
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 437..440
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 92
FT /note="L -> P (in dbSNP:rs34423045)"
FT /id="VAR_039826"
FT VARIANT 267
FT /note="K -> E (in dbSNP:rs1675953)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_039827"
SQ SEQUENCE 658 AA; 75225 MW; 7C1B0AEF1C960E78 CRC64;
MGRRRAPAGG SLGRALMRHQ TQRSRSHRHT DSWLHTSELN DGYDWGRLNL QSVTEQSSLD
DFLATAELAG TEFVAEKLNI KFVPAEARTG LLSFEESQRI KKLHEENKQF LCIPRRPNWN
QNTTPEELKQ AEKDNFLEWR RQLVRLEEEQ KLILTPFERN LDFWRQLWRV IERSDIVVQI
VDARNPLLFR CEDLECYVKE MDANKENVIL INKADLLTAE QRSAWAMYFE KEDVKVIFWS
ALAGAIPLNG DSEEEANRDD RQSNTTKFGH SSFDQAEISH SESEHLPARD SPSLSENPTT
DEDDSEYEDC PEEEEDDWQT CSEEDGPKEE DCSQDWKESS TADSEARSRK TPQKRQIHNF
SHLVSKQELL ELFKELHTGR KVKDGQLTVG LVGYPNVGKS STINTIMGNK KVSVSATPGH
TKHFQTLYVE PGLCLCDCPG LVMPSFVSTK AEMTCSGILP IDQMRDHVPP VSLVCQNIPR
HVLEATYGIN IITPREDEDP HRPPTSEELL TAYGYMRGFM TAHGQPDQPR SARYILKDYV
SGKLLYCHPP PGRDPVTFQH QHQRLLENKM NSDEIKMQLG RNKKAKQIEN IVDKTFFHQE
NVRALTKGVQ AVMGYKPGSG VVTASTASSE NGAGKPWKKH GNRNKKEKSR RLYKHLDM
