Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

La protein homolog (La autoantigen homolog) (La ribonucleoprotein)

 LHP1_YEAST              Reviewed;         275 AA.
P33399; D6VRU5;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 2.
12-SEP-2018, entry version 176.
RecName: Full=La protein homolog;
AltName: Full=La autoantigen homolog;
AltName: Full=La ribonucleoprotein;
Name=LHP1; Synonyms=LAH1, YLA1; OrderedLocusNames=YDL051W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
STRAIN=YPH501;
PubMed=8035818; DOI=10.1128/MCB.14.8.5412;
Yoo C.J., Wolin S.L.;
"La proteins from Drosophila melanogaster and Saccharomyces
cerevisiae: a yeast homolog of the La autoantigen is dispensable for
growth.";
Mol. Cell. Biol. 14:5412-5424(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-275, AND CHARACTERIZATION.
PubMed=7799435; DOI=10.1006/jmbi.1994.0008;
Lin-Marq N., Clarkson S.G.;
"A yeast RNA binding protein that resembles the human autoantigen
La.";
J. Mol. Biol. 245:81-85(1995).
[6]
NUCLEOTIDE SEQUENCE OF 1-252.
PubMed=8408076;
Nagiec M.M., Wells G.B., Lester R.L., Dickson R.C.;
"A suppressor gene that enables Saccharomyces cerevisiae to grow
without making sphingolipids encodes a protein that resembles an
Escherichia coli fatty acyltransferase.";
J. Biol. Chem. 268:22156-22163(1993).
[7]
FUNCTION.
PubMed=9150139; DOI=10.1016/S0092-8674(00)80220-2;
Yoo C.J., Wolin S.L.;
"The yeast La protein is required for the 3' endonucleolytic cleavage
that matures tRNA precursors.";
Cell 89:393-402(1997).
[8]
INTERACTION WITH SXM1, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9412461; DOI=10.1083/jcb.139.7.1655;
Rosenblum J.S., Pemberton L.F., Blobel G.;
"A nuclear import pathway for a protein involved in tRNA maturation.";
J. Cell Biol. 139:1655-1661(1997).
[9]
FUNCTION, AND U6 RNA-BINDING.
PubMed=9857199; DOI=10.1093/emboj/17.24.7442;
Pannone B.K., Xue D., Wolin S.L.;
"A role for the yeast La protein in U6 snRNP assembly: evidence that
the La protein is a molecular chaperone for RNA polymerase III
transcripts.";
EMBO J. 17:7442-7453(1998).
[10]
FUNCTION.
PubMed=9851972; DOI=10.1101/gad.12.23.3650;
Anderson J., Phan L., Cuesta R., Carlson B.A., Pak M., Asano K.,
Bjoerk G.R., Tamame M., Hinnebusch A.G.;
"The essential Gcd10p-Gcd14p nuclear complex is required for 1-
methyladenosine modification and maturation of initiator methionyl-
tRNA.";
Genes Dev. 12:3650-3662(1998).
[11]
INTERACTION WITH SXM1, AND SUBCELLULAR LOCATION.
PubMed=9817748; DOI=10.1083/jcb.143.4.887;
Rosenblum J.S., Pemberton L.F., Bonifaci N., Blobel G.;
"Nuclear import and the evolution of a multifunctional RNA-binding
protein.";
J. Cell Biol. 143:887-899(1998).
[12]
FUNCTION, AND RNA-BINDING.
PubMed=10385518; DOI=10.1083/jcb.145.7.1369;
Dechampesme A.M., Koroleva O., Leger-Silvestre I., Gas N., Camier S.;
"Assembly of 5S ribosomal RNA is required at a specific step of the
pre-rRNA processing pathway.";
J. Cell Biol. 145:1369-1380(1999).
[13]
SUBCELLULAR LOCATION.
PubMed=10564276; DOI=10.1091/mbc.10.11.3849;
Sobel S.G., Wolin S.L.;
"Two yeast La motif-containing proteins are RNA-binding proteins that
associate with polyribosomes.";
Mol. Biol. Cell 10:3849-3862(1999).
[14]
FUNCTION.
PubMed=10330157; DOI=10.1128/MCB.19.6.4167;
Calvo O., Cuesta R., Anderson J., Gutierrez N., Garcia-Barrio M.T.,
Hinnebusch A.G., Tamame M.;
"GCD14p, a repressor of GCN4 translation, cooperates with Gcd10p and
Lhp1p in the maturation of initiator methionyl-tRNA in Saccharomyces
cerevisiae.";
Mol. Cell. Biol. 19:4167-4181(1999).
[15]
FUNCTION, AND RNA-BINDING.
PubMed=10747032; DOI=10.1093/emboj/19.7.1650;
Xue D., Rubinson D.A., Pannone B.K., Yoo C.J., Wolin S.L.;
"U snRNP assembly in yeast involves the La protein.";
EMBO J. 19:1650-1660(2000).
[16]
FUNCTION, AND RNA-BINDING.
PubMed=10891482; DOI=10.1128/MCB.20.15.5415-5424.2000;
Kufel J., Allmang C., Chanfreau G., Petfalski E., Lafontaine D.L.,
Tollervey D.;
"Precursors to the U3 small nucleolar RNA lack small nucleolar RNP
proteins but are stabilized by La binding.";
Mol. Cell. Biol. 20:5415-5424(2000).
[17]
FUNCTION.
PubMed=11333229;
Pannone B.K., Kim S.D., Noe D.A., Wolin S.L.;
"Multiple functional interactions between components of the Lsm2-Lsm8
complex, U6 snRNA, and the yeast La protein.";
Genetics 158:187-196(2001).
[18]
PHOSPHORYLATION AT SER-15; SER-19 AND SER-235, IDENTIFICATION BY MASS
SPECTROMETRY, FUNCTION, AND MUTAGENESIS OF SER-15; SER-19 AND SER-235.
PubMed=11720288;
Long K.S., Cedervall T., Walch-Solimena C., Noe D.A., Huddleston M.J.,
Annan R.S., Wolin S.L.;
"Phosphorylation of the Saccharomyces cerevisiae La protein does not
appear to be required for its functions in tRNA maturation and nascent
RNA stabilization.";
RNA 7:1589-1602(2001).
[19]
FUNCTION, AND RNA-BINDING.
PubMed=12077351; DOI=10.1128/MCB.22.14.5248-5256.2002;
Kufel J., Allmang C., Verdone L., Beggs J.D., Tollervey D.;
"Lsm proteins are required for normal processing of pre-tRNAs and
their efficient association with La-homologous protein Lhp1p.";
Mol. Cell. Biol. 22:5248-5256(2002).
[20]
FUNCTION.
PubMed=14657028; DOI=10.1093/emboj/cdg625;
Chakshusmathi G., Kim S.D., Rubinson D.A., Wolin S.L.;
"A La protein requirement for efficient pre-tRNA folding.";
EMBO J. 22:6562-6572(2003).
[21]
FUNCTION.
PubMed=12828645; DOI=10.1046/j.1365-2958.2003.03568.x;
Aye M., Sandmeyer S.B.;
"Ty3 requires yeast La homologous protein for wild-type frequencies of
transposition.";
Mol. Microbiol. 49:501-515(2003).
[22]
FUNCTION.
PubMed=14627812; DOI=10.1093/nar/gkg904;
Kufel J., Allmang C., Verdone L., Beggs J., Tollervey D.;
"A complex pathway for 3' processing of the yeast U3 snoRNA.";
Nucleic Acids Res. 31:6788-6797(2003).
[23]
RNA-BINDING.
PubMed=14704279; DOI=10.1073/pnas.0307425100;
Inada M., Guthrie C.;
"Identification of Lhp1p-associated RNAs by microarray analysis in
Saccharomyces cerevisiae reveals association with coding and noncoding
RNAs.";
Proc. Natl. Acad. Sci. U.S.A. 101:434-439(2004).
[24]
FUNCTION.
PubMed=15579677; DOI=10.1534/genetics.104.028126;
Aye M., Irwin B., Beliakova-Bethell N., Chen E., Garrus J.,
Sandmeyer S.;
"Host factors that affect Ty3 retrotransposition in Saccharomyces
cerevisiae.";
Genetics 168:1159-1176(2004).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[26]
FUNCTION.
PubMed=16581807; DOI=10.1261/rna.2307206;
Copela L.A., Chakshusmathi G., Sherrer R.L., Wolin S.L.;
"The La protein functions redundantly with tRNA modification enzymes
to ensure tRNA structural stability.";
RNA 12:644-654(2006).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-19; SER-230;
SER-233 AND SER-235, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-19, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[32]
METHYLATION AT ARG-104.
PubMed=23865587; DOI=10.1021/pr400556c;
Low J.K., Hart-Smith G., Erce M.A., Wilkins M.R.;
"Analysis of the proteome of Saccharomyces cerevisiae for
methylarginine.";
J. Proteome Res. 12:3884-3899(2013).
-!- FUNCTION: Molecular chaperone that binds nascent RNA polymerase
III transcripts, stabilizing these RNAs against exonucleases.
Required for the 3' endonucleolytic cleavage that matures tRNA
precursors and for efficient folding of certain pre-tRNAs.
Cooperaes with GCD14 in the maturation of a subset of RNA
polymerase III transcripts. Functions also in the assembly of
certain RNA polymerase II-transcribed RNAs into RNPs. Binds and
stabilizes newly synthesized U6 snRNA as well as precursors of U3
snRNA from degradation. Facilitates efficient Sm protein binding,
thus assisting formation of the U4/U6 snRNP. Required fot Ty3
normal transposition frequency. {ECO:0000269|PubMed:10330157,
ECO:0000269|PubMed:10385518, ECO:0000269|PubMed:10747032,
ECO:0000269|PubMed:10891482, ECO:0000269|PubMed:11333229,
ECO:0000269|PubMed:11720288, ECO:0000269|PubMed:12077351,
ECO:0000269|PubMed:12828645, ECO:0000269|PubMed:14627812,
ECO:0000269|PubMed:14657028, ECO:0000269|PubMed:15579677,
ECO:0000269|PubMed:16581807, ECO:0000269|PubMed:9150139,
ECO:0000269|PubMed:9412461, ECO:0000269|PubMed:9851972,
ECO:0000269|PubMed:9857199}.
-!- SUBUNIT: Interacts with SXM1. {ECO:0000269|PubMed:9412461,
ECO:0000269|PubMed:9817748}.
-!- INTERACTION:
P33203:PRP40; NbExp=2; IntAct=EBI-10046, EBI-701;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10564276,
ECO:0000269|PubMed:9412461, ECO:0000269|PubMed:9817748}.
Note=Imported into nucleus by the nuclear transport factor SXM1.
-!- PTM: Phosphorylation is not required for the roles tRNA and snRNP
biogenesis. {ECO:0000269|PubMed:11720288}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; L33023; AAA21777.1; -; Genomic_DNA.
EMBL; Z74099; CAA98612.1; -; Genomic_DNA.
EMBL; AY558373; AAS56699.1; -; Genomic_DNA.
EMBL; L13282; AAA16515.1; -; Unassigned_DNA.
EMBL; X80801; CAA56782.1; -; Genomic_DNA.
EMBL; BK006938; DAA11805.1; -; Genomic_DNA.
PIR; B48600; B48600.
RefSeq; NP_010232.1; NM_001180110.1.
ProteinModelPortal; P33399; -.
SMR; P33399; -.
BioGrid; 32008; 145.
DIP; DIP-6444N; -.
IntAct; P33399; 21.
MINT; P33399; -.
STRING; 4932.YDL051W; -.
iPTMnet; P33399; -.
MaxQB; P33399; -.
PaxDb; P33399; -.
PRIDE; P33399; -.
EnsemblFungi; YDL051W; YDL051W; YDL051W.
GeneID; 851509; -.
KEGG; sce:YDL051W; -.
EuPathDB; FungiDB:YDL051W; -.
SGD; S000002209; LHP1.
GeneTree; ENSGT00830000128323; -.
InParanoid; P33399; -.
KO; K11090; -.
OMA; NDGWVEL; -.
OrthoDB; EOG092C4I3J; -.
BioCyc; YEAST:G3O-29469-MONOMER; -.
PRO; PR:P33399; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005730; C:nucleolus; IDA:SGD.
GO; GO:0005654; C:nucleoplasm; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:1990904; C:ribonucleoprotein complex; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IDA:SGD.
GO; GO:0000049; F:tRNA binding; IDA:SGD.
GO; GO:0008033; P:tRNA processing; IMP:SGD.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 3.30.70.330; -; 1.
InterPro; IPR006630; La_HTH.
InterPro; IPR002344; Lupus_La.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF05383; La; 1.
Pfam; PF00076; RRM_1; 1.
PRINTS; PR00302; LUPUSLA.
SMART; SM00715; LA; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50961; HTH_LA; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Methylation; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 275 La protein homolog.
/FTId=PRO_0000207608.
DOMAIN 23 112 HTH La-type RNA-binding.
{ECO:0000255|PROSITE-ProRule:PRU00332}.
DOMAIN 123 216 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
MOTIF 240 256 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:18407956,
ECO:0000269|PubMed:11720288}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:11720288}.
MOD_RES 104 104 Omega-N-methylarginine.
{ECO:0000269|PubMed:23865587}.
MOD_RES 230 230 Phosphoserine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 233 233 Phosphoserine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 235 235 Phosphoserine.
{ECO:0000244|PubMed:17287358,
ECO:0000269|PubMed:11720288}.
MUTAGEN 15 15 S->A: Prevents phosphorylation; when
associated with A-19 and A-235.
{ECO:0000269|PubMed:11720288}.
MUTAGEN 19 19 S->A: Prevents phosphorylation; when
associated with A-15 and A-235.
{ECO:0000269|PubMed:11720288}.
MUTAGEN 235 235 S->A: Prevents phosphorylation; when
associated with A-15 and A-19.
{ECO:0000269|PubMed:11720288}.
SEQUENCE 275 AA; 32104 MW; 43CDB2E6C740978D CRC64;
MSEKPQQEEQ EKPQSRRNSF AVIEFTPEVL DRCLKQVEFY FSEFNFPYDR FLRTTAEKND
GWVPISTIAT FNRMKKYRPV DKVIEALRSS EILEVSADGE NVKRRVPLDL TAARNARIEQ
NQRTLAVMNF PHEDVEASQI PELQENLEAF FKKLGEINQV RLRRDHRNKK FNGTVLVEFK
TIPECEAFLK SYSNDDESNE ILSYEGKKLS VLTKKQFDLQ REASKSKNFS GRSRSFNGHK
KKNLPKFPKN KKKNGKEESK EDSSAIADDD EEHKE


Related products :

Catalog number Product name Quantity
E0275b ELISA Bos taurus,Bovine,La autoantigen homolog,La ribonucleoprotein,Lupus La protein homolog,SSB 96T
E0275m ELISA La autoantigen homolog,La ribonucleoprotein,Lupus La protein homolog,Mouse,Mus musculus,Ssb,Ss-b 96T
E0275r ELISA kit La autoantigen homolog,La ribonucleoprotein,Lupus La protein homolog,Rat,Rattus norvegicus,Ssb,Ss-b 96T
E0275r ELISA La autoantigen homolog,La ribonucleoprotein,Lupus La protein homolog,Rat,Rattus norvegicus,Ssb,Ss-b 96T
E0275b ELISA kit Bos taurus,Bovine,La autoantigen homolog,La ribonucleoprotein,Lupus La protein homolog,SSB 96T
U0275r CLIA La autoantigen homolog,La ribonucleoprotein,Lupus La protein homolog,Rat,Rattus norvegicus,Ssb,Ss-b 96T
E0275m ELISA kit La autoantigen homolog,La ribonucleoprotein,Lupus La protein homolog,Mouse,Mus musculus,Ssb,Ss-b 96T
U0275m CLIA La autoantigen homolog,La ribonucleoprotein,Lupus La protein homolog,Mouse,Mus musculus,Ssb,Ss-b 96T
U0275b CLIA Bos taurus,Bovine,La autoantigen homolog,La ribonucleoprotein,Lupus La protein homolog,SSB 96T
E0275Rb ELISA kit La autoantigen homolog,La ribonucleoprotein,Lupus La protein homolog,Oryctolagus cuniculus,Rabbit,SSB 96T
E0275Rb ELISA La autoantigen homolog,La ribonucleoprotein,Lupus La protein homolog,Oryctolagus cuniculus,Rabbit,SSB 96T
U0275Rb CLIA La autoantigen homolog,La ribonucleoprotein,Lupus La protein homolog,Oryctolagus cuniculus,Rabbit,SSB 96T
EIAAB40005 Autoantigen p27 homolog,C184l,Mouse,Mus musculus,Protein C184L,Sjoegren syndrome_scleroderma autoantigen 1 homolog,Sssca1
EIAAB13505 Autoantigen PM_Scl 2 homolog,Exosc10,Exosome component 10,Mouse,Mus musculus,Pmscl2,Polymyositis_scleroderma autoantigen 2 homolog
10-663-45614 LA_SS-B Human - La ribonucleoprotein; La autoantigen homolog N_A 1 mg
10-663-45614 LA_SS-B Human - La ribonucleoprotein; La autoantigen homolog N_A 0.05 mg
10-663-45614 LA_SS-B Human - La ribonucleoprotein; La autoantigen homolog N_A 0.01 mg
EIAAB46719 DACA-1 homolog,Dermatomyositis associated with cancer putative autoantigen 1 homolog,Mouse,Mus musculus,YTH domain family protein 1,Ythdf1
EIAAB33722 Autoantigen p542,Heterogeneous nuclear ribonucleoprotein C-like 2,hnRNP associated with lethal yellow protein homolog,hnRNP core protein C-like 2,HNRPCL2,Homo sapiens,Human,P542,RALY,RNA-binding prote
EIAAB13308 CTF7 homolog 1,ECO1 homolog 1,EFO1,EFO1p,ESCO1,ESO1 homolog 1,Establishment factor-like protein 1,Establishment of cohesion 1 homolog 1,hEFO1,Homo sapiens,Human,KIAA1911,N-acetyltransferase ESCO1
EIAAB05141 Cage1,CAGE-1,Cancer_testis antigen 3 homolog,Cancer-associated gene 1 protein homolog,CT3 homolog,Ctag3,Rat,Rattus norvegicus
EIAAB05142 Cage1,CAGE-1,Cancer_testis antigen 3 homolog,Cancer-associated gene 1 protein homolog,CT3 homolog,Ctag3,Mouse,Mus musculus
18-003-43993 LAG1 longevity assurance homolog 4 - Translocating chain-associating membrane protein homolog 1; TRAM homolog 1 Polyclonal 0.1 mg Protein A
EIAAB40499 Mammalian homolog of Unc-18c,Mouse,MUNC-18-3,Munc-18c,Mus musculus,Protein unc-18 homolog 3,Protein unc-18 homolog C,Stxbp3,Stxbp3a,Syntaxin-binding protein 3,Unc18-3,Unc18c,Unc-18C
EIAAB11547 DnaJ homolog subfamily B member 4,DNAJB4,DNAJW,Heat shock 40 kDa protein 1 homolog,Heat shock protein 40 homolog,HLJ1,Homo sapiens,HSP40 homolog,Human,Human liver DnaJ-like protein


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur