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Heterogeneous nuclear ribonucleoprotein R (hnRNP R)

 HNRPR_HUMAN             Reviewed;         633 AA.
O43390; Q2L7G6; Q5TEH1; Q9BV64; S4R3J4;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
12-SEP-2018, entry version 192.
RecName: Full=Heterogeneous nuclear ribonucleoprotein R;
Short=hnRNP R;
Name=HNRNPR; Synonyms=HNRPR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9421497; DOI=10.1093/nar/26.2.439;
Hassfeld W., Chan E.K.L., Mathison D.A., Portman D., Dreyfuss G.,
Steiner G., Tan E.M.;
"Molecular definition of heterogeneous nuclear ribonucleoprotein R
(hnRNP R) using autoimmune antibody: immunological relationship with
hnRNP P.";
Nucleic Acids Res. 26:439-445(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=15858414; DOI=10.1097/00001756-200505120-00014;
Huang J., Chen X.H., Wu K., Xu P.;
"Cloning and expression of a novel isoform of heterogeneous nuclear
ribonucleoprotein-R.";
NeuroReport 16:727-730(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[5]
PROTEIN SEQUENCE OF 2-13; 32-41; 70-84; 95-103; 134-145; 175-216;
225-255; 258-285; 290-300; 347-366; 373-384; 398-414 AND 428-441,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[6]
PROTEIN SEQUENCE OF 32-41 AND 347-359, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Fetal brain;
Lubec G., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[7]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[8]
IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
Johnsen A.H., Christiansen J., Nielsen F.C.;
"Molecular composition of IMP1 ribonucleoprotein granules.";
Mol. Cell. Proteomics 6:798-811(2007).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-366, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
INTERACTION WITH GTPBP1.
PubMed=21515746; DOI=10.1096/fj.10-178715;
Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J.,
Chung S.J., Senju S., Nishimura Y., Kim K.T.;
"Modulation of exosome-mediated mRNA turnover by interaction of GTP-
binding protein 1 (GTPBP1) with its target mRNAs.";
FASEB J. 25:2757-2769(2011).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-171 AND LYS-359, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[20]
STRUCTURE BY NMR OF 333-416.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RRM domain in heterogeneous nuclear
ribonucleoprotein R (HNRNP R).";
Submitted (OCT-2006) to the PDB data bank.
-!- FUNCTION: Component of ribonucleosomes, which are complexes of at
least 20 other different heterogenious nuclear ribonucleoproteins
(hnRNP). hnRNP play an important role in processing of precursor
mRNA in the nucleus.
-!- SUBUNIT: Identified in the spliceosome C complex. Identified in a
IGF2BP1-dependent mRNP granule complex containing untranslated
mRNAs. Interacts with GTPBP1. {ECO:0000269|PubMed:11991638,
ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:21515746}.
-!- INTERACTION:
Q5VWX1:KHDRBS2; NbExp=3; IntAct=EBI-713419, EBI-742808;
P16333:NCK1; NbExp=2; IntAct=EBI-713419, EBI-389883;
Q99873:PRMT1; NbExp=4; IntAct=EBI-713419, EBI-78738;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7TMK9}.
Microsome {ECO:0000250|UniProtKB:Q7TMK9}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:17289661}. Cytoplasm
{ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP
granules containing untranslated mRNAs. The tyrosine
phosphorylated form bound to RNA is found in microsomes (By
similarity). {ECO:0000250|UniProtKB:Q7TMK9,
ECO:0000269|PubMed:17289661}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O43390-1; Sequence=Displayed;
Name=2;
IsoId=O43390-2; Sequence=VSP_038360;
Name=3; Synonyms=hnRNP-R2;
IsoId=O43390-3; Sequence=VSP_047647;
Note=Expression is low and neural-specific.;
Name=4;
IsoId=O43390-4; Sequence=VSP_054703, VSP_038360;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
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EMBL; AF000364; AAC39540.1; -; mRNA.
EMBL; DQ351905; ABC73063.1; -; mRNA.
EMBL; AL109936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001449; AAH01449.1; -; mRNA.
CCDS; CCDS232.1; -. [O43390-1]
CCDS; CCDS44085.1; -. [O43390-2]
CCDS; CCDS60020.1; -. [O43390-4]
CCDS; CCDS72727.1; -. [O43390-3]
PIR; T02673; T02673.
RefSeq; NP_001095868.1; NM_001102398.2. [O43390-2]
RefSeq; NP_001284549.1; NM_001297620.1. [O43390-3]
RefSeq; NP_005817.1; NM_005826.4. [O43390-1]
RefSeq; XP_005245768.1; XM_005245711.4. [O43390-1]
RefSeq; XP_011538773.1; XM_011540471.2. [O43390-2]
RefSeq; XP_016855497.1; XM_017000008.1. [O43390-3]
UniGene; Hs.373763; -.
PDB; 2DK2; NMR; -; A=333-416.
PDBsum; 2DK2; -.
ProteinModelPortal; O43390; -.
SMR; O43390; -.
BioGrid; 115530; 290.
CORUM; O43390; -.
IntAct; O43390; 63.
MINT; O43390; -.
STRING; 9606.ENSP00000363745; -.
iPTMnet; O43390; -.
PhosphoSitePlus; O43390; -.
SwissPalm; O43390; -.
BioMuta; HNRNPR; -.
EPD; O43390; -.
MaxQB; O43390; -.
PaxDb; O43390; -.
PeptideAtlas; O43390; -.
PRIDE; O43390; -.
ProteomicsDB; 48919; -.
ProteomicsDB; 48920; -. [O43390-2]
TopDownProteomics; O43390-1; -. [O43390-1]
DNASU; 10236; -.
Ensembl; ENST00000302271; ENSP00000304405; ENSG00000125944. [O43390-1]
Ensembl; ENST00000374612; ENSP00000363741; ENSG00000125944. [O43390-1]
Ensembl; ENST00000374616; ENSP00000363745; ENSG00000125944. [O43390-2]
Ensembl; ENST00000427764; ENSP00000392799; ENSG00000125944. [O43390-3]
Ensembl; ENST00000478691; ENSP00000474437; ENSG00000125944. [O43390-4]
Ensembl; ENST00000634263; ENSP00000489371; ENSG00000282958. [O43390-1]
Ensembl; ENST00000634634; ENSP00000488941; ENSG00000282958. [O43390-3]
Ensembl; ENST00000634713; ENSP00000488945; ENSG00000282958. [O43390-2]
Ensembl; ENST00000634766; ENSP00000489252; ENSG00000282958. [O43390-1]
Ensembl; ENST00000635150; ENSP00000489275; ENSG00000282958. [O43390-4]
GeneID; 10236; -.
KEGG; hsa:10236; -.
UCSC; uc001bgp.5; human. [O43390-1]
CTD; 10236; -.
DisGeNET; 10236; -.
EuPathDB; HostDB:ENSG00000125944.18; -.
GeneCards; HNRNPR; -.
HGNC; HGNC:5047; HNRNPR.
HPA; CAB011687; -.
HPA; HPA026092; -.
MIM; 607201; gene.
neXtProt; NX_O43390; -.
OpenTargets; ENSG00000125944; -.
PharmGKB; PA162391459; -.
eggNOG; KOG0117; Eukaryota.
eggNOG; ENOG410XTJ5; LUCA.
GeneTree; ENSGT00550000074366; -.
HOGENOM; HOG000186082; -.
HOVERGEN; HBG051917; -.
InParanoid; O43390; -.
KO; K13161; -.
OMA; YYPPPRM; -.
OrthoDB; EOG091G0EUB; -.
PhylomeDB; O43390; -.
TreeFam; TF314932; -.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
ChiTaRS; HNRNPR; human.
EvolutionaryTrace; O43390; -.
GeneWiki; HNRNPR; -.
GenomeRNAi; 10236; -.
PMAP-CutDB; O43390; -.
PRO; PR:O43390; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000125944; Expressed in 241 organ(s), highest expression level in female gonad.
CleanEx; HS_HNRNPR; -.
ExpressionAtlas; O43390; baseline and differential.
Genevisible; O43390; HS.
GO; GO:0043679; C:axon terminus; IEA:Ensembl.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
GO; GO:0030426; C:growth cone; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0005681; C:spliceosomal complex; NAS:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0061157; P:mRNA destabilization; IEA:Ensembl.
GO; GO:0006397; P:mRNA processing; NAS:UniProtKB.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0043086; P:negative regulation of catalytic activity; IEA:Ensembl.
GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
CDD; cd12482; RRM1_hnRNPR; 1.
CDD; cd12488; RRM2_hnRNPR; 1.
Gene3D; 3.30.70.330; -; 3.
InterPro; IPR006535; HnRNP_R/Q_splicing_fac.
InterPro; IPR034410; hnRNPR_RRM1.
InterPro; IPR034411; hnRNPR_RRM2.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 3.
SMART; SM00360; RRM; 3.
SUPFAM; SSF54928; SSF54928; 3.
TIGRFAMs; TIGR01648; hnRNP-R-Q; 1.
PROSITE; PS50102; RRM; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Endoplasmic reticulum;
Isopeptide bond; Microsome; mRNA processing; mRNA splicing; Nucleus;
Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
Spliceosome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.5}.
CHAIN 2 633 Heterogeneous nuclear ribonucleoprotein
R.
/FTId=PRO_0000081870.
DOMAIN 165 244 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 246 328 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 341 411 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REPEAT 462 471 1; approximate.
REPEAT 472 482 2.
REPEAT 488 497 3; approximate.
REGION 447 567 RNA-binding RGG-box.
REGION 462 497 3 X 11 AA approximate repeats of D-D-Y-Y-
G-Y-D-Y-H-D-Y.
MOTIF 412 418 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 2 153 Asp/Glu-rich (acidic).
COMPBIAS 579 633 Asn/Gln-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.5}.
MOD_RES 366 366 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 13 13 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 171 171 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 359 359 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 101 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_054703.
VAR_SEQ 129 166 Missing (in isoform 3).
{ECO:0000303|PubMed:15858414}.
/FTId=VSP_047647.
VAR_SEQ 269 269 V -> VTGL (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_038360.
HELIX 334 338 {ECO:0000244|PDB:2DK2}.
STRAND 342 347 {ECO:0000244|PDB:2DK2}.
HELIX 354 362 {ECO:0000244|PDB:2DK2}.
STRAND 367 373 {ECO:0000244|PDB:2DK2}.
STRAND 376 383 {ECO:0000244|PDB:2DK2}.
HELIX 384 394 {ECO:0000244|PDB:2DK2}.
STRAND 405 408 {ECO:0000244|PDB:2DK2}.
SEQUENCE 633 AA; 70943 MW; 088341F6465ED46F CRC64;
MANQVNGNAV QLKEEEEPMD TSSVTHTEHY KTLIEAGLPQ KVAERLDEIF QTGLVAYVDL
DERAIDALRE FNEEGALSVL QQFKESDLSH VQNKSAFLCG VMKTYRQREK QGSKVQESTK
GPDEAKIKAL LERTGYTLDV TTGQRKYGGP PPDSVYSGVQ PGIGTEVFVG KIPRDLYEDE
LVPLFEKAGP IWDLRLMMDP LSGQNRGYAF ITFCGKEAAQ EAVKLCDSYE IRPGKHLGVC
ISVANNRLFV GSIPKNKTKE NILEEFSKVT EGLVDVILYH QPDDKKKNRG FCFLEYEDHK
SAAQARRRLM SGKVKVWGNV VTVEWADPVE EPDPEVMAKV KVLFVRNLAT TVTEEILEKS
FSEFGKLERV KKLKDYAFVH FEDRGAAVKA MDEMNGKEIE GEEIEIVLAK PPDKKRKERQ
AARQASRSTA YEDYYYHPPP RMPPPIRGRG RGGGRGGYGY PPDYYGYEDY YDDYYGYDYH
DYRGGYEDPY YGYDDGYAVR GRGGGRGGRG APPPPRGRGA PPPRGRAGYS QRGAPLGPPR
GSRGGRGGPA QQQRGRGSRG SRGNRGGNVG GKRKADGYNQ PDSKRRQTNN QQNWGSQPIA
QQPLQQGGDY SGNYGYNNDN QEFYQDTYGQ QWK


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29-275 Heterogeneous nuclear RNAs (hnRNAs) which include mRNA precursors and mature mRNAs are associated with specific proteins to form heterogenous ribonucleoprotein (hnRNP) complexes. Heterogeneous nuclear 0.05 mg
29-230 Heterogeneous nuclear RNAs (hnRNAs) which include mRNA precursors and mature mRNAs are associated with specific proteins to form heterogenous ribonucleoprotein (hnRNP) complexes. Heterogeneous nuclear 0.1 mg
29-274 Heterogeneous nuclear RNAs (hnRNAs) which include mRNA precursors and mature mRNAs are associated with specific proteins to form heterogenous ribonucleoprotein (hnRNP) complexes. Heterogeneous nuclear 0.1 mg
18-003-43633 Heterogeneous nuclear ribonucleoprotein H3 - hnRNP H3; hnRNP 2H9 Polyclonal 0.1 mg Protein A
EIAAB33407 Heterogeneous nuclear ribonucleoprotein A1-like 2,hnRNP A1-like 2,hnRNP core protein A1-like 2,HNRNPA1L,HNRNPA1L2,Homo sapiens,Human
18-003-43580 Heterogeneous nuclear ribonucleoprotein K - hnRNP K; Transformation up-regulated nuclear protein; TUNP Polyclonal 0.05 mg Aff Pur
18-003-43579 Heterogeneous nuclear ribonucleoprotein K - hnRNP K; Transformation up-regulated nuclear protein; TUNP Polyclonal 0.1 mg Protein A
20-373-85048 Heterogeneous nuclear ribonucleoprotein L - hnRNP L Monoclonal 0.05 ml
E02H0091 Rat Heterogeneous Nuclear Ribonucleoprotein A1 ELISA , hnRNP
18-003-43575 Heterogeneous nuclear ribonucleoprotein L - hnRNP L Polyclonal 0.05 mg Aff Pur
E02H0092 Rat Heterogeneous Nuclear Ribonucleoprotein L ELISA, HnRNP L 96 Tests/kit
E02H0091 Rat Heterogeneous Nuclear Ribonucleoprotein A1 ELISA , hnRNP 96 Tests/kit
18-003-43553 Heterogeneous nuclear ribonucleoprotein L - hnRNP L Polyclonal 0.1 mg Protein A
18-003-43574 Heterogeneous nuclear ribonucleoprotein L - hnRNP L Polyclonal 0.1 mg Protein A
RH003* Rat heterogeneous nuclear ribonucleoprotein E,hnRNP E ELISA Kit 96T
RH004* Rat heterogeneous nuclear ribonucleoprotein P2,hnRNP P2 ELISA Kit 96T
E02H0092 Rat Heterogeneous Nuclear Ribonucleoprotein L ELISA, HnRNP L
18-003-43624 Heterogeneous nuclear ribonucleoprotein A0 - hnRNP A0 Polyclonal 0.1 mg Protein A
20-373-85016 Heterogeneous nuclear ribonucleoprotein H - hnRNP H Monoclonal 0.1 ml
E02H0260 Rat Heterogeneous nuclear ribonucleoprotein A2 ELISA, hnRNP A2 96 Tests/kit
18-003-43678 Heterogeneous nuclear ribonucleoprotein A3 - hnRNP A3 Polyclonal 0.1 mg Protein A
18-003-43679 Heterogeneous nuclear ribonucleoprotein A3 - hnRNP A3 Polyclonal 0.1 mg Protein A
20-373-85019 Heterogeneous nuclear ribonucleoprotein L - hnRNP L Monoclonal 0.1 ml
20-373-85045 Heterogeneous nuclear ribonucleoprotein H - hnRNP H Monoclonal 0.05 ml
E02H0260 Rat Heterogeneous nuclear ribonucleoprotein A2 ELISA, hnRNP A2


 

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