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   05-OCT-2010, entry version 67.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-267.
RC   TISSUE=Testis;
RX   MEDLINE=21154917; 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.,
RA   Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA   Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA   Wambutt R., Korn B., Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and
RT   analysis of 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.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   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.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   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
RT   project: 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Scheffzek K., Pepperkok R.;
RT   "Human Lsg1 defines a family of essential GTPases that correlates with
RT   the evolution of compartmentalization.";
RL   BMC Biol. 3:21-21(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND MASS
RP   SPECTROMETRY.
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].
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND MASS
RP   SPECTROMETRY.
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).
CC   -!- FUNCTION: GTPase required for the XPO1/CRM1-mediated nuclear
CC       export of the 60S ribosomal subunit. Probably acts by mediating
CC       the release of NMD3 from the 60S ribosomal subunit after export
CC       into the cytoplasm (Probable).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. Nucleus,
CC       Cajal body. Note=Shuttles between the Cajal bodies in the nucleus
CC       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
CC       described by a G4-G1-G3 pattern.
CC   -!- SIMILARITY: Belongs to the MMR1/HSR1 GTP-binding protein family.
CC       LSG1 subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH15042.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH40119.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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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   IPI; IPI00300094; -.
DR   RefSeq; NP_060855.2; -.
DR   UniGene; Hs.518505; -.
DR   ProteinModelPortal; Q9H089; -.
DR   SMR; Q9H089; 85-445, 163-551.
DR   STRING; Q9H089; -.
DR   PhosphoSite; Q9H089; -.
DR   PRIDE; Q9H089; -.
DR   Ensembl; ENST00000265245; ENSP00000265245; ENSG00000041802.
DR   GeneID; 55341; -.
DR   KEGG; hsa:55341; -.
DR   UCSC; uc003fui.1; human.
DR   CTD; 55341; -.
DR   GeneCards; GC03M194361; -.
DR   HGNC; HGNC:25652; LSG1.
DR   MIM; 610780; gene.
DR   PharmGKB; PA142671501; -.
DR   eggNOG; prNOG12796; -.
DR   HOGENOM; HBG610636; -.
DR   HOVERGEN; HBG097657; -.
DR   InParanoid; Q9H089; -.
DR   OMA; CSGILPI; -.
DR   OrthoDB; EOG91ZHW6; -.
DR   NextBio; 59663; -.
DR   ArrayExpress; Q9H089; -.
DR   Bgee; Q9H089; -.
DR   CleanEx; HS_LSG1; -.
DR   Genevestigator; Q9H089; -.
DR   GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051168; P:nuclear export; IDA:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR006073; GTP1_OBG.
DR   InterPro; IPR002917; MMR_HSR1_GTP-bd.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   PRINTS; PR00326; GTP1OBG.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Endoplasmic reticulum; GTP-binding;
KW   Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Protein transport; Transport.
FT   CHAIN         1    658       Large subunit GTPase 1 homolog.
FT                                /FTId=PRO_0000324553.
FT   NP_BIND     212    215       GTP (Potential).
FT   NP_BIND     393    400       GTP (Potential).
FT   NP_BIND     437    440       GTP (Potential).
FT   MOD_RES     252    252       Phosphoserine.
FT   VARIANT      92     92       L -> P (in dbSNP:rs34423045).
FT                                /FTId=VAR_039826.
FT   VARIANT     267    267       K -> E (in dbSNP:rs1675953).
FT                                /FTId=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
//