Full text data of LARP1
LARP1
(KIAA0731, LARP)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
La-related protein 1 (La ribonucleoprotein domain family member 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
La-related protein 1 (La ribonucleoprotein domain family member 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q6PKG0
ID LARP1_HUMAN Reviewed; 1096 AA.
AC Q6PKG0; O94836; Q8N4M2; Q8NB73; Q9UFD7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2005, sequence version 2.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=La-related protein 1;
DE AltName: Full=La ribonucleoprotein domain family member 1;
GN Name=LARP1; Synonyms=KIAA0731, LARP;
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] (ISOFORM 2).
RC TISSUE=Cervix, 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-816 (ISOFORM 1).
RC TISSUE=Brain;
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 [3]
RP PROTEIN SEQUENCE OF 2-26; 115-123; 167-185; 252-265; 357-366; 410-422;
RP 429-473; 524-539; 579-597; 643-654; 695-703; 718-778; 904-924;
RP 937-944; 949-964 AND 1004-1017, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, PHOSPHORYLATION AT THR-526 AND SER-774, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma, Colon carcinoma, and Mammary carcinoma;
RA Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Kolch W.,
RA Heiserich L., Boulahbel H., Gottlieb E.;
RL Submitted (FEB-2008) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-1096 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1096.
RC TISSUE=Mammary cancer;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-521; THR-526;
RP SER-627; SER-766 AND SER-774, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-845, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
RA Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate
RT reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT Wnt signal transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-90, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627, AND MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-143; SER-165;
RP SER-517; SER-521; THR-526; SER-627; SER-631; THR-649; THR-724;
RP SER-774; SER-824 AND SER-851, AND MASS 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; THR-526 AND SER-774,
RP AND MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-90; SER-627;
RP SER-631; THR-724; SER-824; THR-865 AND SER-868, AND MASS 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).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-892 AND LYS-1017, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-220; THR-376;
RP SER-521; THR-526; SER-548; SER-627; SER-631; THR-649; SER-766 AND
RP SER-774, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
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.,
RA Buerckstuemmer T., 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-143; SER-215;
RP SER-220; SER-521; THR-526; SER-548; SER-627; SER-631; SER-766; SER-774
RP AND TYR-777, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PKG0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PKG0-3; Sequence=VSP_015114, VSP_015115;
CC -!- SIMILARITY: Belongs to the LARP family.
CC -!- SIMILARITY: Contains 1 HTH La-type RNA-binding domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH33856.1; Type=Erroneous initiation;
CC Sequence=BAA34451.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing;
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DR EMBL; BC001460; AAH01460.2; -; mRNA.
DR EMBL; BC033856; AAH33856.1; ALT_INIT; mRNA.
DR EMBL; AK091465; BAC03668.1; -; mRNA.
DR EMBL; AB018274; BAA34451.1; ALT_SEQ; mRNA.
DR EMBL; AL133034; CAB61364.1; -; mRNA.
DR PIR; T42646; T42646.
DR RefSeq; NP_056130.2; NM_015315.4.
DR RefSeq; XP_005268461.1; XM_005268404.1.
DR UniGene; Hs.292078; -.
DR ProteinModelPortal; Q6PKG0; -.
DR SMR; Q6PKG0; 397-473.
DR IntAct; Q6PKG0; 19.
DR MINT; MINT-1631511; -.
DR STRING; 9606.ENSP00000366871; -.
DR PhosphoSite; Q6PKG0; -.
DR DMDM; 73621135; -.
DR PaxDb; Q6PKG0; -.
DR PRIDE; Q6PKG0; -.
DR DNASU; 23367; -.
DR Ensembl; ENST00000336314; ENSP00000336721; ENSG00000155506.
DR Ensembl; ENST00000518297; ENSP00000428589; ENSG00000155506.
DR GeneID; 23367; -.
DR KEGG; hsa:23367; -.
DR UCSC; uc010jie.1; human.
DR CTD; 23367; -.
DR GeneCards; GC05P154092; -.
DR HGNC; HGNC:29531; LARP1.
DR HPA; CAB015222; -.
DR MIM; 612059; gene.
DR neXtProt; NX_Q6PKG0; -.
DR PharmGKB; PA142671564; -.
DR eggNOG; COG5193; -.
DR HOGENOM; HOG000113283; -.
DR HOVERGEN; HBG054322; -.
DR InParanoid; Q6PKG0; -.
DR OMA; NARTPRT; -.
DR OrthoDB; EOG7HB59K; -.
DR ChiTaRS; LARP1; human.
DR GeneWiki; LARP1; -.
DR GenomeRNAi; 23367; -.
DR NextBio; 45430; -.
DR PMAP-CutDB; Q6PKG0; -.
DR PRO; PR:Q6PKG0; -.
DR ArrayExpress; Q6PKG0; -.
DR Bgee; Q6PKG0; -.
DR CleanEx; HS_LARP1; -.
DR Genevestigator; Q6PKG0; -.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:BHF-UCL.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR006607; DM15.
DR InterPro; IPR006630; Lupus_La_RNA-bd.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF05383; La; 1.
DR SMART; SM00684; DM15; 3.
DR SMART; SM00715; LA; 1.
DR PROSITE; PS50961; HTH_LA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1096 La-related protein 1.
FT /FTId=PRO_0000207609.
FT DOMAIN 397 487 HTH La-type RNA-binding.
FT COMPBIAS 1044 1050 Poly-Gly.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 75 75 Phosphoserine.
FT MOD_RES 90 90 Phosphoserine.
FT MOD_RES 143 143 Phosphoserine.
FT MOD_RES 165 165 Phosphoserine.
FT MOD_RES 215 215 Phosphoserine.
FT MOD_RES 220 220 Phosphoserine.
FT MOD_RES 324 324 Phosphoserine (By similarity).
FT MOD_RES 327 327 Phosphoserine (By similarity).
FT MOD_RES 376 376 Phosphothreonine.
FT MOD_RES 517 517 Phosphoserine.
FT MOD_RES 521 521 Phosphoserine.
FT MOD_RES 526 526 Phosphothreonine.
FT MOD_RES 548 548 Phosphoserine.
FT MOD_RES 627 627 Phosphoserine.
FT MOD_RES 631 631 Phosphoserine.
FT MOD_RES 649 649 Phosphothreonine.
FT MOD_RES 724 724 Phosphothreonine.
FT MOD_RES 766 766 Phosphoserine.
FT MOD_RES 774 774 Phosphoserine.
FT MOD_RES 777 777 Phosphotyrosine.
FT MOD_RES 824 824 Phosphoserine.
FT MOD_RES 845 845 Phosphothreonine.
FT MOD_RES 851 851 Phosphoserine.
FT MOD_RES 865 865 Phosphothreonine.
FT MOD_RES 868 868 Phosphoserine.
FT MOD_RES 892 892 N6-acetyllysine.
FT MOD_RES 1017 1017 N6-acetyllysine.
FT VAR_SEQ 1 77 Missing (in isoform 2).
FT /FTId=VSP_015114.
FT VAR_SEQ 78 144 PLQLPGAEGPAISDGEEGGGEPGAGGGAAGAAGAGRRDFVE
FT APPPKVNPWTKNALPPVLTTVNGQSP -> MLWRVLLSKRP
FT PFPHPELDFQEAPIPSCPGRLPGRKNSVALAAAPRKEPTGD
FT REKPLPFPVLAPFSN (in isoform 2).
FT /FTId=VSP_015115.
FT CONFLICT 778 780 RNT -> TRP (in Ref. 1; AAH33856).
FT CONFLICT 979 979 V -> L (in Ref. 5; CAB61364).
SQ SEQUENCE 1096 AA; 123510 MW; CA3E9D30BBC101B7 CRC64;
MATQVEPLLP GGATLLQAEE HGGLVRKKPP PAPEGKGEPG PNDVRGGEPD GSARRPRPPC
AKPHKEGTGQ QERESPRPLQ LPGAEGPAIS DGEEGGGEPG AGGGAAGAAG AGRRDFVEAP
PPKVNPWTKN ALPPVLTTVN GQSPPEHSAP AKVVRAAVPK QRKGSKVGDF GDAINWPTPG
EIAHKSVQPQ SHKPQPTRKL PPKKDMKEQE KGEGSDSKES PKTKSDESGE EKNGDEDCQR
GGQKKKGNKH KWVPLQIDMK PEVPREKLAS RPTRPPEPRH IPANRGEIKG SESATYVPVA
PPTPAWQPEI KPEPAWHDQD ETSSVKSDGA GGARASFRGR GRGRGRGRGR GRGGTRTHFD
YQFGYRKFDG VEGPRTPKYM NNITYYFDNV SSTELYSVDQ ELLKDYIKRQ IEYYFSVDNL
ERDFFLRRKM DADGFLPITL IASFHRVQAL TTDISLIFAA LKDSKVVEIV DEKVRRREEP
EKWPLPPIVD YSQTDFSQLL NCPEFVPRQH YQKETESAPG SPRAVTPVPT KTEEVSNLKT
LPKGLSASLP DLDSENWIEV KKRPRPSPAR PKKSEESRFS HLTSLPQQLP SQQLMSKDQD
EQEELDFLFD EEMEQMDGRK NTFTAWSDEE SDYEIDDRDV NKILIVTQTP HYMRRHPGGD
RTGNHTSRAK MSAELAKVIN DGLFYYEQDL WAEKFEPEYS QIKQEVENFK KVNMISREQF
DTLTPEPPVD PNQEVPPGPP RFQQVPTDAL ANKLFGAPEP STIARSLPTT VPESPNYRNT
RTPRTPRTPQ LKDSSQTSRF YPVVKEGRTL DAKMPRKRKT RHSSNPPLES HVGWVMDSRE
HRPRTASISS SPSEGTPTVG SYGCTPQSLP KFQHPSHELL KENGFTQHVY HKYRRRCLNE
RKRLGIGQSQ EMNTLFRFWS FFLRDHFNKK MYEEFKQLAL EDAKEGYRYG LECLFRYYSY
GLEKKFRLDI FKDFQEETVK DYEAGQLYGL EKFWAFLKYS KAKNLDIDPK LQEYLGKFRR
LEDFRVDPPM GEEGNHKRHS VVAGGGGGEG RKRCPSQSSS RPAAMISQPP TPPTGQPVRE
DAKWTSQHSN TQTLGK
//
ID LARP1_HUMAN Reviewed; 1096 AA.
AC Q6PKG0; O94836; Q8N4M2; Q8NB73; Q9UFD7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2005, sequence version 2.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=La-related protein 1;
DE AltName: Full=La ribonucleoprotein domain family member 1;
GN Name=LARP1; Synonyms=KIAA0731, LARP;
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] (ISOFORM 2).
RC TISSUE=Cervix, 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-816 (ISOFORM 1).
RC TISSUE=Brain;
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 [3]
RP PROTEIN SEQUENCE OF 2-26; 115-123; 167-185; 252-265; 357-366; 410-422;
RP 429-473; 524-539; 579-597; 643-654; 695-703; 718-778; 904-924;
RP 937-944; 949-964 AND 1004-1017, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, PHOSPHORYLATION AT THR-526 AND SER-774, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma, Colon carcinoma, and Mammary carcinoma;
RA Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Kolch W.,
RA Heiserich L., Boulahbel H., Gottlieb E.;
RL Submitted (FEB-2008) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-1096 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1096.
RC TISSUE=Mammary cancer;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-521; THR-526;
RP SER-627; SER-766 AND SER-774, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-845, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
RA Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate
RT reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT Wnt signal transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-90, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627, AND MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-143; SER-165;
RP SER-517; SER-521; THR-526; SER-627; SER-631; THR-649; THR-724;
RP SER-774; SER-824 AND SER-851, AND MASS 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; THR-526 AND SER-774,
RP AND MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-90; SER-627;
RP SER-631; THR-724; SER-824; THR-865 AND SER-868, AND MASS 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).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-892 AND LYS-1017, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-220; THR-376;
RP SER-521; THR-526; SER-548; SER-627; SER-631; THR-649; SER-766 AND
RP SER-774, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
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.,
RA Buerckstuemmer T., 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-143; SER-215;
RP SER-220; SER-521; THR-526; SER-548; SER-627; SER-631; SER-766; SER-774
RP AND TYR-777, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PKG0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PKG0-3; Sequence=VSP_015114, VSP_015115;
CC -!- SIMILARITY: Belongs to the LARP family.
CC -!- SIMILARITY: Contains 1 HTH La-type RNA-binding domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH33856.1; Type=Erroneous initiation;
CC Sequence=BAA34451.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing;
CC -----------------------------------------------------------------------
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DR EMBL; BC001460; AAH01460.2; -; mRNA.
DR EMBL; BC033856; AAH33856.1; ALT_INIT; mRNA.
DR EMBL; AK091465; BAC03668.1; -; mRNA.
DR EMBL; AB018274; BAA34451.1; ALT_SEQ; mRNA.
DR EMBL; AL133034; CAB61364.1; -; mRNA.
DR PIR; T42646; T42646.
DR RefSeq; NP_056130.2; NM_015315.4.
DR RefSeq; XP_005268461.1; XM_005268404.1.
DR UniGene; Hs.292078; -.
DR ProteinModelPortal; Q6PKG0; -.
DR SMR; Q6PKG0; 397-473.
DR IntAct; Q6PKG0; 19.
DR MINT; MINT-1631511; -.
DR STRING; 9606.ENSP00000366871; -.
DR PhosphoSite; Q6PKG0; -.
DR DMDM; 73621135; -.
DR PaxDb; Q6PKG0; -.
DR PRIDE; Q6PKG0; -.
DR DNASU; 23367; -.
DR Ensembl; ENST00000336314; ENSP00000336721; ENSG00000155506.
DR Ensembl; ENST00000518297; ENSP00000428589; ENSG00000155506.
DR GeneID; 23367; -.
DR KEGG; hsa:23367; -.
DR UCSC; uc010jie.1; human.
DR CTD; 23367; -.
DR GeneCards; GC05P154092; -.
DR HGNC; HGNC:29531; LARP1.
DR HPA; CAB015222; -.
DR MIM; 612059; gene.
DR neXtProt; NX_Q6PKG0; -.
DR PharmGKB; PA142671564; -.
DR eggNOG; COG5193; -.
DR HOGENOM; HOG000113283; -.
DR HOVERGEN; HBG054322; -.
DR InParanoid; Q6PKG0; -.
DR OMA; NARTPRT; -.
DR OrthoDB; EOG7HB59K; -.
DR ChiTaRS; LARP1; human.
DR GeneWiki; LARP1; -.
DR GenomeRNAi; 23367; -.
DR NextBio; 45430; -.
DR PMAP-CutDB; Q6PKG0; -.
DR PRO; PR:Q6PKG0; -.
DR ArrayExpress; Q6PKG0; -.
DR Bgee; Q6PKG0; -.
DR CleanEx; HS_LARP1; -.
DR Genevestigator; Q6PKG0; -.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:BHF-UCL.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR006607; DM15.
DR InterPro; IPR006630; Lupus_La_RNA-bd.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF05383; La; 1.
DR SMART; SM00684; DM15; 3.
DR SMART; SM00715; LA; 1.
DR PROSITE; PS50961; HTH_LA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1096 La-related protein 1.
FT /FTId=PRO_0000207609.
FT DOMAIN 397 487 HTH La-type RNA-binding.
FT COMPBIAS 1044 1050 Poly-Gly.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 75 75 Phosphoserine.
FT MOD_RES 90 90 Phosphoserine.
FT MOD_RES 143 143 Phosphoserine.
FT MOD_RES 165 165 Phosphoserine.
FT MOD_RES 215 215 Phosphoserine.
FT MOD_RES 220 220 Phosphoserine.
FT MOD_RES 324 324 Phosphoserine (By similarity).
FT MOD_RES 327 327 Phosphoserine (By similarity).
FT MOD_RES 376 376 Phosphothreonine.
FT MOD_RES 517 517 Phosphoserine.
FT MOD_RES 521 521 Phosphoserine.
FT MOD_RES 526 526 Phosphothreonine.
FT MOD_RES 548 548 Phosphoserine.
FT MOD_RES 627 627 Phosphoserine.
FT MOD_RES 631 631 Phosphoserine.
FT MOD_RES 649 649 Phosphothreonine.
FT MOD_RES 724 724 Phosphothreonine.
FT MOD_RES 766 766 Phosphoserine.
FT MOD_RES 774 774 Phosphoserine.
FT MOD_RES 777 777 Phosphotyrosine.
FT MOD_RES 824 824 Phosphoserine.
FT MOD_RES 845 845 Phosphothreonine.
FT MOD_RES 851 851 Phosphoserine.
FT MOD_RES 865 865 Phosphothreonine.
FT MOD_RES 868 868 Phosphoserine.
FT MOD_RES 892 892 N6-acetyllysine.
FT MOD_RES 1017 1017 N6-acetyllysine.
FT VAR_SEQ 1 77 Missing (in isoform 2).
FT /FTId=VSP_015114.
FT VAR_SEQ 78 144 PLQLPGAEGPAISDGEEGGGEPGAGGGAAGAAGAGRRDFVE
FT APPPKVNPWTKNALPPVLTTVNGQSP -> MLWRVLLSKRP
FT PFPHPELDFQEAPIPSCPGRLPGRKNSVALAAAPRKEPTGD
FT REKPLPFPVLAPFSN (in isoform 2).
FT /FTId=VSP_015115.
FT CONFLICT 778 780 RNT -> TRP (in Ref. 1; AAH33856).
FT CONFLICT 979 979 V -> L (in Ref. 5; CAB61364).
SQ SEQUENCE 1096 AA; 123510 MW; CA3E9D30BBC101B7 CRC64;
MATQVEPLLP GGATLLQAEE HGGLVRKKPP PAPEGKGEPG PNDVRGGEPD GSARRPRPPC
AKPHKEGTGQ QERESPRPLQ LPGAEGPAIS DGEEGGGEPG AGGGAAGAAG AGRRDFVEAP
PPKVNPWTKN ALPPVLTTVN GQSPPEHSAP AKVVRAAVPK QRKGSKVGDF GDAINWPTPG
EIAHKSVQPQ SHKPQPTRKL PPKKDMKEQE KGEGSDSKES PKTKSDESGE EKNGDEDCQR
GGQKKKGNKH KWVPLQIDMK PEVPREKLAS RPTRPPEPRH IPANRGEIKG SESATYVPVA
PPTPAWQPEI KPEPAWHDQD ETSSVKSDGA GGARASFRGR GRGRGRGRGR GRGGTRTHFD
YQFGYRKFDG VEGPRTPKYM NNITYYFDNV SSTELYSVDQ ELLKDYIKRQ IEYYFSVDNL
ERDFFLRRKM DADGFLPITL IASFHRVQAL TTDISLIFAA LKDSKVVEIV DEKVRRREEP
EKWPLPPIVD YSQTDFSQLL NCPEFVPRQH YQKETESAPG SPRAVTPVPT KTEEVSNLKT
LPKGLSASLP DLDSENWIEV KKRPRPSPAR PKKSEESRFS HLTSLPQQLP SQQLMSKDQD
EQEELDFLFD EEMEQMDGRK NTFTAWSDEE SDYEIDDRDV NKILIVTQTP HYMRRHPGGD
RTGNHTSRAK MSAELAKVIN DGLFYYEQDL WAEKFEPEYS QIKQEVENFK KVNMISREQF
DTLTPEPPVD PNQEVPPGPP RFQQVPTDAL ANKLFGAPEP STIARSLPTT VPESPNYRNT
RTPRTPRTPQ LKDSSQTSRF YPVVKEGRTL DAKMPRKRKT RHSSNPPLES HVGWVMDSRE
HRPRTASISS SPSEGTPTVG SYGCTPQSLP KFQHPSHELL KENGFTQHVY HKYRRRCLNE
RKRLGIGQSQ EMNTLFRFWS FFLRDHFNKK MYEEFKQLAL EDAKEGYRYG LECLFRYYSY
GLEKKFRLDI FKDFQEETVK DYEAGQLYGL EKFWAFLKYS KAKNLDIDPK LQEYLGKFRR
LEDFRVDPPM GEEGNHKRHS VVAGGGGGEG RKRCPSQSSS RPAAMISQPP TPPTGQPVRE
DAKWTSQHSN TQTLGK
//
MIM
612059
*RECORD*
*FIELD* NO
612059
*FIELD* TI
*612059 La RIBONUCLEOPROTEIN DOMAIN FAMILY, MEMBER 1; LARP1
;;La-RELATED PROTEIN; LARP;;
read moreKIAA0731
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated human brain cDNA
library, Nagase et al. (1998) cloned LARP1, which they designated
KIAA0731. The deduced protein contains 1,096 amino acids. RT-PCR ELISA
detected high LARP1 expression in all tissues examined, with highest
level in heart.
Chauvet et al. (2000) cloned fly and mouse Larp, and they identified
orthologs in several species. All LARP proteins, including human LARP,
contain 2 conserved regions. The first conserved region shares homology
with La proteins (see SSB; 109090) from various species, whereas the
second conserved region is restricted to LARP proteins. In situ
hybridization of mouse embryos showed expression of Larp in dorsal root
ganglia and spinal cord, as well as in developing organs characterized
by epithelial-mesenchymal interactions.
MAPPING
By radiation hybrid analysis, Nagase et al. (1998) mapped the LARP1 gene
to chromosome 10. However, Hartz (2008) mapped the LARP1 gene to
chromosome 5q33.2 based on an alignment of the LARP1 sequence (GenBank
GENBANK AB018274) with the genomic sequence (build 36.1).
*FIELD* RF
1. Chauvet, S.; Maurel-Zaffran, C.; Miassod, R.; Jullien, N.; Pradel,
J.; Aragnol, D.: dlarp, a new candidate Hox target in Drosophila
whose orthologue in mouse is expressed at sites of epithelium/mesenchymal
interactions. Dev. Dyn. 218: 401-413, 2000.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 5/16/2008.
3. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XI. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 5: 277-286, 1998.
*FIELD* CD
Patricia A. Hartz: 5/16/2008
*FIELD* ED
mgross: 05/16/2008
*RECORD*
*FIELD* NO
612059
*FIELD* TI
*612059 La RIBONUCLEOPROTEIN DOMAIN FAMILY, MEMBER 1; LARP1
;;La-RELATED PROTEIN; LARP;;
read moreKIAA0731
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated human brain cDNA
library, Nagase et al. (1998) cloned LARP1, which they designated
KIAA0731. The deduced protein contains 1,096 amino acids. RT-PCR ELISA
detected high LARP1 expression in all tissues examined, with highest
level in heart.
Chauvet et al. (2000) cloned fly and mouse Larp, and they identified
orthologs in several species. All LARP proteins, including human LARP,
contain 2 conserved regions. The first conserved region shares homology
with La proteins (see SSB; 109090) from various species, whereas the
second conserved region is restricted to LARP proteins. In situ
hybridization of mouse embryos showed expression of Larp in dorsal root
ganglia and spinal cord, as well as in developing organs characterized
by epithelial-mesenchymal interactions.
MAPPING
By radiation hybrid analysis, Nagase et al. (1998) mapped the LARP1 gene
to chromosome 10. However, Hartz (2008) mapped the LARP1 gene to
chromosome 5q33.2 based on an alignment of the LARP1 sequence (GenBank
GENBANK AB018274) with the genomic sequence (build 36.1).
*FIELD* RF
1. Chauvet, S.; Maurel-Zaffran, C.; Miassod, R.; Jullien, N.; Pradel,
J.; Aragnol, D.: dlarp, a new candidate Hox target in Drosophila
whose orthologue in mouse is expressed at sites of epithelium/mesenchymal
interactions. Dev. Dyn. 218: 401-413, 2000.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 5/16/2008.
3. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XI. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 5: 277-286, 1998.
*FIELD* CD
Patricia A. Hartz: 5/16/2008
*FIELD* ED
mgross: 05/16/2008