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UniProtKB/Swiss-Prot entry Q6PKG0


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LARP1_HUMAN
Primary accession number Q6PKG0
Secondary accession numbers O94836 Q8N4M2 Q8NB73 Q9UFD7
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on August 16, 2005 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 51)
Name and origin of the protein
Protein name La-related protein 1
Synonym La ribonucleoprotein domain family member 1
Gene name
Name: LARP1
Synonyms: KIAA0731, LARP
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Cervix, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
DOI=10.1093/dnares/5.5.277; PubMed=9872452 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-816 (ISOFORM 1).
TISSUE=Brain;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
PROTEIN SEQUENCE OF 2-26; 115-123; 167-185; 252-265; 357-366; 410-422; 429-473; 524-539; 579-597; 643-654; 695-703; 718-778; 904-924; 937-944; 949-964 AND 1004-1017, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT THR-526 AND SER-774, AND MASS SPECTROMETRY.
TISSUE=Cervix carcinoma, Colon carcinoma, and Mammary carcinoma;
Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Kolch W., Heiserich L., Boulahbel H., Gottlieb E.;
Submitted (FEB-2008) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1096.
TISSUE=Mammary cancer;
The German cDNA consortium;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526; SER-548; SER-627 AND SER-774, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-517; SER-521; THR-526; SER-627; SER-631; SER-766; SER-774; SER-824 AND THR-1071, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526; THR-785 AND THR-788, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526 AND THR-649, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND THR-526, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700120-MCP200; PubMed=17693683 [NCBI, ExPASy, EBI, Israel, Japan]
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517; SER-521; THR-526; THR-622; THR-624; SER-627; THR-785 AND THR-788, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1056 AND THR-1071, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526 AND SER-774, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-90; SER-766; SER-774; SER-823 AND SER-824, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
BC001460; AAH01460.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC033856; AAH33856.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB018274; BAA34451.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK091465; BAC03668.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133034; CAB61364.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T42646; T42646.
RefSeq NP_056130.2; -.
NP_291029.2; -.
UniGene Hs.292078
3D structure databases
ModBase Q6PKG0.
Protein-protein interaction databases
IntAct Q6PKG0; -.
PTM databases
PhosphoSite Q6PKG0; -.
Organism-specific databases
H-InvDB HIX0005343; -.
HGNC HGNC:29531; LARP1.
GenAtlas LARP1.
HPA CAB015222; -.
PharmGKB PA142671564; -.
GeneCards Q6PKG0.
HUGE KIAA0731.
Gene expression databases
ArrayExpress Q6PKG0; -.
CleanEx HS_LARP1; -.
GermOnline ENSG00000155506; Homo sapiens.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR006607; DM15.
IPR006630; Lupus_La_RNA_bd.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.
Gene3D G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
Pfam PF05383; La; 1.
Pfam graphical view of domain structure.
SMART SM00684; DM15; 3.
SM00715; LA; 1.
SMART graphical view of domain structure.
PROSITE PS50961; HTH_LA; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q6PKG0.
Genome annotation databases
Ensembl ENSG00000155506; Homo sapiens. [Contig view]
GeneID 23367; -.
KEGG hsa:23367; -.
Phylogenomic databases
HOGENOM Q6PKG0; -.
HOVERGEN Q6PKG0; -.
Other
LinkHub Q6PKG0; -.
ProtoNet Q6PKG0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Alternative splicing; Direct protein sequencing; Phosphoprotein; RNA-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
INIT_MET   1      1        Removed. 
CHAIN   2   1096  1095     La-related protein 1. PRO_0000207609
DOMAIN   397    487  91     HTH La-type RNA-binding. 
COMPBIAS   1044   1050  7     Poly-Gly. 
MOD_RES   2      2        N-acetylalanine. 
MOD_RES   75     75        Phosphoserine. 
MOD_RES   90     90        Phosphoserine. 
MOD_RES   517    517        Phosphoserine. 
MOD_RES   521    521        Phosphoserine. 
MOD_RES   526    526        Phosphothreonine. 
MOD_RES   548    548        Phosphoserine. 
MOD_RES   622    622        Phosphothreonine. 
MOD_RES   624    624        Phosphothreonine. 
MOD_RES   627    627        Phosphoserine. 
MOD_RES   631    631        Phosphoserine. 
MOD_RES   649    649        Phosphothreonine. 
MOD_RES   766    766        Phosphoserine. 
MOD_RES   774    774        Phosphoserine. 
MOD_RES   785    785        Phosphothreonine. 
MOD_RES   788    788        Phosphothreonine. 
MOD_RES   823    823        Phosphoserine. 
MOD_RES   824    824        Phosphoserine. 
MOD_RES   851    851        Phosphoserine (By similarity). 
MOD_RES   1056   1056        Phosphoserine. 
MOD_RES   1071   1071        Phosphothreonine. 
VAR_SEQ   1    122        MATQVEPLLPGGATLLQAEEHGGLVRKKPPPAPEGKGEPG PNDVRGGEPDGSARRPRPPCAKPHKEGTGQQERESPRPLQ LPGAEGPAISDGEEGGGEPGAGGGAAGAAGAGRRDFV EAPPP -> AADRVVCLARRASPPSVHIAAAPEPGSPGRPGGGGEGGTG LEACRARGGGVLRGTGGGGRTPRRPGLQSGGPSSPPAPLV GLGFTAAASNWEGAAPRVNPDPSLQGLGPSAPEEGVA GALLA (in isoform 2). VSP_015113
VAR_SEQ   1     77        Missing (in isoform 3). VSP_015114
VAR_SEQ   78    144        PLQLPGAEGPAISDGEEGGGEPGAGGGAAGAAGAGRRDFV EAPPPKVNPWTKNALPPVLTTVNGQSP -> MLWRVLLSKRPPFPHPELDFQEAPIPSCPGRLPGRKNSVA LAAAPRKEPTGDREKPLPFPVLAPFSN (in isoform 3). VSP_015115
CONFLICT   778    780        RNT -> TRP (in Ref. 1; AAH33856). 
CONFLICT   979    979        V -> L (in Ref. 5). 
Sequence information
Length: 1096 AA [This is the length of the unprocessed precursor] Molecular weight: 123510 Da [This is the MW of the unprocessed precursor] CRC64: CA3E9D30BBC101B7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATQVEPLLP GGATLLQAEE HGGLVRKKPP PAPEGKGEPG PNDVRGGEPD GSARRPRPPC 

        70         80         90        100        110        120 
AKPHKEGTGQ QERESPRPLQ LPGAEGPAIS DGEEGGGEPG AGGGAAGAAG AGRRDFVEAP 

       130        140        150        160        170        180 
PPKVNPWTKN ALPPVLTTVN GQSPPEHSAP AKVVRAAVPK QRKGSKVGDF GDAINWPTPG 

       190        200        210        220        230        240 
EIAHKSVQPQ SHKPQPTRKL PPKKDMKEQE KGEGSDSKES PKTKSDESGE EKNGDEDCQR 

       250        260        270        280        290        300 
GGQKKKGNKH KWVPLQIDMK PEVPREKLAS RPTRPPEPRH IPANRGEIKG SESATYVPVA 

       310        320        330        340        350        360 
PPTPAWQPEI KPEPAWHDQD ETSSVKSDGA GGARASFRGR GRGRGRGRGR GRGGTRTHFD 

       370        380        390        400        410        420 
YQFGYRKFDG VEGPRTPKYM NNITYYFDNV SSTELYSVDQ ELLKDYIKRQ IEYYFSVDNL 

       430        440        450        460        470        480 
ERDFFLRRKM DADGFLPITL IASFHRVQAL TTDISLIFAA LKDSKVVEIV DEKVRRREEP 

       490        500        510        520        530        540 
EKWPLPPIVD YSQTDFSQLL NCPEFVPRQH YQKETESAPG SPRAVTPVPT KTEEVSNLKT 

       550        560        570        580        590        600 
LPKGLSASLP DLDSENWIEV KKRPRPSPAR PKKSEESRFS HLTSLPQQLP SQQLMSKDQD 

       610        620        630        640        650        660 
EQEELDFLFD EEMEQMDGRK NTFTAWSDEE SDYEIDDRDV NKILIVTQTP HYMRRHPGGD 

       670        680        690        700        710        720 
RTGNHTSRAK MSAELAKVIN DGLFYYEQDL WAEKFEPEYS QIKQEVENFK KVNMISREQF 

       730        740        750        760        770        780 
DTLTPEPPVD PNQEVPPGPP RFQQVPTDAL ANKLFGAPEP STIARSLPTT VPESPNYRNT 

       790        800        810        820        830        840 
RTPRTPRTPQ LKDSSQTSRF YPVVKEGRTL DAKMPRKRKT RHSSNPPLES HVGWVMDSRE 

       850        860        870        880        890        900 
HRPRTASISS SPSEGTPTVG SYGCTPQSLP KFQHPSHELL KENGFTQHVY HKYRRRCLNE 

       910        920        930        940        950        960 
RKRLGIGQSQ EMNTLFRFWS FFLRDHFNKK MYEEFKQLAL EDAKEGYRYG LECLFRYYSY 

       970        980        990       1000       1010       1020 
GLEKKFRLDI FKDFQEETVK DYEAGQLYGL EKFWAFLKYS KAKNLDIDPK LQEYLGKFRR 

      1030       1040       1050       1060       1070       1080 
LEDFRVDPPM GEEGNHKRHS VVAGGGGGEG RKRCPSQSSS RPAAMISQPP TPPTGQPVRE 

      1090 
DAKWTSQHSN TQTLGK 

Q6PKG0 in FASTA format

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