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

RNA-binding protein Raly (Autoantigen p542) (Heterogeneous nuclear ribonucleoprotein C-like 2) (hnRNP core protein C-like 2) (hnRNP associated with lethal yellow protein homolog)

 RALY_HUMAN              Reviewed;         306 AA.
Q9UKM9; Q14621; Q2M365; Q5QPL8; Q9BQX6; Q9UJE3;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
12-SEP-2018, entry version 172.
RecName: Full=RNA-binding protein Raly;
AltName: Full=Autoantigen p542;
AltName: Full=Heterogeneous nuclear ribonucleoprotein C-like 2;
Short=hnRNP core protein C-like 2;
AltName: Full=hnRNP associated with lethal yellow protein homolog;
Name=RALY; Synonyms=HNRPCL2, P542;
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 2), AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=10500250; DOI=10.1016/S0167-4781(99)00126-8;
Khrebtukova I., Kuklin A., Woychik R.P., Michaud E.J.;
"Alternative processing of the human and mouse raly genes.";
Biochim. Biophys. Acta 1447:107-112(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN AUTOIMMUNE
DISEASE, AND FUNCTION.
TISSUE=Lymphocyte;
PubMed=9376072; DOI=10.1006/jaut.1997.9996;
Rhodes G.H., Valbracht J.R., Nguyen M.-D., Vaughan J.H.;
"The p542 gene encodes an autoantigen that cross-reacts with EBNA-1 of
the Epstein Barr virus and which may be a heterogeneous nuclear
ribonucleoprotein.";
J. Autoimmun. 10:447-454(1997).
[3]
SEQUENCE REVISION.
Vaughan J.H.;
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[6]
PROTEIN SEQUENCE OF 23-44; 56-66; 79-99; 121-126; 132-141 AND 184-216,
PHOSPHORYLATION AT SER-135, 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.
[7]
PROTEIN SEQUENCE OF 227-253, AND AUTOANTIGENIC EPITOPE MAPPING.
PubMed=7533788; DOI=10.1172/JCI117781;
Vaughan J.H., Valbracht J.R., Nguyen M.-D., Handley H.H., Smith R.S.,
Patrick K., Rhodes G.H.;
"Epstein-Barr virus-induced autoimmune responses. I. Immunoglobulin M
autoantibodies to proteins mimicking and not mimicking Epstein-Barr
virus nuclear antigen-1.";
J. Clin. Invest. 95:1306-1315(1995).
[8]
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pituitary;
PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
"Phosphoproteomic analysis of the human pituitary.";
Pituitary 9:109-120(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND THR-298, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
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 SER-135, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286; SER-288; SER-295
AND THR-298, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-286; SER-288;
SER-295 AND THR-298, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165, 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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-106 (ISOFORM 1), AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-135, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; THR-286; SER-288
AND THR-298, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106
(ISOFORM 1), AND 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).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-159 AND LYS-165, 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).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4 AND LYS-159, 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).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-94; LYS-99; LYS-159;
LYS-165; LYS-179 AND LYS-191, 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).
[27]
STRUCTURE BY NMR OF 1-97.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RRM domain in RNA-binding protein NP_057951.";
Submitted (NOV-2004) to the PDB data bank.
-!- FUNCTION: RNA-binding protein that acts as a transcriptional
cofactor for cholesterol biosynthetic genes in the liver. Binds
the lipid-responsive non-coding RNA LeXis and is required for
LeXis-mediated effect on cholesterogenesis (By similarity). May be
a heterogeneous nuclear ribonucleoprotein (hnRNP)
(PubMed:9376072). {ECO:0000250|UniProtKB:Q64012,
ECO:0000269|PubMed:9376072}.
-!- SUBUNIT: Identified in the spliceosome C complex.
{ECO:0000269|PubMed:11991638}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q64012}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2;
IsoId=Q9UKM9-1; Sequence=Displayed;
Name=1;
IsoId=Q9UKM9-2; Sequence=VSP_005804;
Note=Contains a phosphoserine at position 106.
{ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:24275569};
-!- TISSUE SPECIFICITY: Expressed in heart, brain, lung, liver,
skeletal muscle, kidney and pancreas. Weakly expressed in
placenta. {ECO:0000269|PubMed:10500250}.
-!- MISCELLANEOUS: Autoantigen found in infectious mononucleosis
caused by Epstein-Barr virus. An epitope recognized by B-cells,
which cross-react with the BKRF1 protein (EBNA-1 nuclear protein)
of Epstein-Barr virus has been identified.
{ECO:0000269|PubMed:9376072}.
-!- SIMILARITY: Belongs to the RRM HNRPC family. RALY subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF148457; AAF04487.1; -; mRNA.
EMBL; L38696; AAC28898.1; -; mRNA.
EMBL; AL031668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC105018; AAI05019.1; -; mRNA.
CCDS; CCDS13229.1; -. [Q9UKM9-2]
CCDS; CCDS13230.1; -. [Q9UKM9-1]
RefSeq; NP_031393.2; NM_007367.3. [Q9UKM9-2]
RefSeq; NP_057951.1; NM_016732.2. [Q9UKM9-1]
RefSeq; XP_005260391.1; XM_005260334.4. [Q9UKM9-1]
RefSeq; XP_005260393.1; XM_005260336.4. [Q9UKM9-2]
RefSeq; XP_011526996.1; XM_011528694.2. [Q9UKM9-1]
RefSeq; XP_011526997.1; XM_011528695.2. [Q9UKM9-1]
RefSeq; XP_016883220.1; XM_017027731.1. [Q9UKM9-1]
UniGene; Hs.136947; -.
PDB; 1WF1; NMR; -; A=1-97.
PDBsum; 1WF1; -.
ProteinModelPortal; Q9UKM9; -.
SMR; Q9UKM9; -.
BioGrid; 116575; 132.
CORUM; Q9UKM9; -.
IntAct; Q9UKM9; 50.
MINT; Q9UKM9; -.
STRING; 9606.ENSP00000246194; -.
iPTMnet; Q9UKM9; -.
PhosphoSitePlus; Q9UKM9; -.
SwissPalm; Q9UKM9; -.
BioMuta; RALY; -.
DMDM; 25091115; -.
EPD; Q9UKM9; -.
PaxDb; Q9UKM9; -.
PeptideAtlas; Q9UKM9; -.
PRIDE; Q9UKM9; -.
ProteomicsDB; 84821; -.
ProteomicsDB; 84822; -. [Q9UKM9-2]
Ensembl; ENST00000246194; ENSP00000246194; ENSG00000125970. [Q9UKM9-1]
Ensembl; ENST00000375114; ENSP00000364255; ENSG00000125970. [Q9UKM9-2]
GeneID; 22913; -.
KEGG; hsa:22913; -.
UCSC; uc002xab.4; human. [Q9UKM9-1]
CTD; 22913; -.
DisGeNET; 22913; -.
EuPathDB; HostDB:ENSG00000125970.11; -.
GeneCards; RALY; -.
HGNC; HGNC:15921; RALY.
HPA; HPA040971; -.
HPA; HPA043614; -.
MIM; 614663; gene.
neXtProt; NX_Q9UKM9; -.
OpenTargets; ENSG00000125970; -.
PharmGKB; PA34201; -.
eggNOG; KOG0118; Eukaryota.
eggNOG; COG0724; LUCA.
GeneTree; ENSGT00390000006718; -.
HOVERGEN; HBG002302; -.
InParanoid; Q9UKM9; -.
KO; K12895; -.
OMA; XLFDYRG; -.
OrthoDB; EOG091G0O1Q; -.
PhylomeDB; Q9UKM9; -.
TreeFam; TF330974; -.
ChiTaRS; RALY; human.
EvolutionaryTrace; Q9UKM9; -.
GeneWiki; RALY; -.
GenomeRNAi; 22913; -.
PRO; PR:Q9UKM9; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000125970; Expressed in 224 organ(s), highest expression level in right testis.
CleanEx; HS_RALY; -.
ExpressionAtlas; Q9UKM9; baseline and differential.
Genevisible; Q9UKM9; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
GO; GO:1903506; P:regulation of nucleic acid-templated transcription; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd12604; RRM_RALY; 1.
Gene3D; 3.30.70.330; -; 1.
InterPro; IPR017347; hnRNP_C.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR034502; RALY_RRM.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 1.
PIRSF; PIRSF037992; hnRNP-C_Raly; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Direct protein sequencing; Isopeptide bond;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome;
Transcription; Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 306 RNA-binding protein Raly.
/FTId=PRO_0000081746.
DOMAIN 21 92 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 227 253 Epitope (recognized by BKRF1 antibodies).
COILED 183 216 {ECO:0000255}.
COMPBIAS 225 251 Poly-Gly.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 44 44 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q64012}.
MOD_RES 63 63 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 135 135 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|Ref.6}.
MOD_RES 165 165 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 262 262 Phosphothreonine.
{ECO:0000250|UniProtKB:Q64012}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000250|UniProtKB:Q64012}.
MOD_RES 286 286 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 288 288 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 295 295 Phosphoserine.
{ECO:0000244|PubMed:16807684,
ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 298 298 Phosphothreonine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 94 94 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 99 99 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 159 159 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 165 165 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 179 179 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 191 191 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 110 125 Missing (in isoform 1).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9376072}.
/FTId=VSP_005804.
VARIANT 139 139 V -> M (in dbSNP:rs35191085).
/FTId=VAR_052215.
VARIANT 215 215 Q -> R (in dbSNP:rs3180568).
/FTId=VAR_015223.
VARIANT 251 251 G -> S (in dbSNP:rs2281209).
/FTId=VAR_015224.
CONFLICT 214 215 EQ -> DE (in Ref. 2; AAC28898).
{ECO:0000305}.
CONFLICT 230 230 A -> AS (in Ref. 2; AAC28898).
{ECO:0000305}.
STRAND 20 25 {ECO:0000244|PDB:1WF1}.
HELIX 35 42 {ECO:0000244|PDB:1WF1}.
HELIX 43 45 {ECO:0000244|PDB:1WF1}.
STRAND 49 54 {ECO:0000244|PDB:1WF1}.
STRAND 57 61 {ECO:0000244|PDB:1WF1}.
STRAND 63 65 {ECO:0000244|PDB:1WF1}.
HELIX 66 75 {ECO:0000244|PDB:1WF1}.
STRAND 87 90 {ECO:0000244|PDB:1WF1}.
SEQUENCE 306 AA; 32463 MW; 7F4376D3BD8E4728 CRC64;
MSLKLQASNV TNKNDPKSIN SRVFIGNLNT ALVKKSDVET IFSKYGRVAG CSVHKGYAFV
QYSNERHARA AVLGENGRVL AGQTLDINMA GEPKPDRPKG LKRAASAIYS GYIFDYDYYR
DDFYDRLFDY RGRLSPVPVP RAVPVKRPRV TVPLVRRVKT NVPVKLFARS TAVTTSSAKI
KLKSSELQAI KTELTQIKSN IDALLSRLEQ IAAEQKANPD GKKKGDGGGA GGGGGGGGSG
GGGSGGGGGG GSSRPPAPQE NTTSEAGLPQ GEARTRDDGD EEGLLTHSEE ELEHSQDTDA
DDGALQ


Related products :

Catalog number Product name Quantity
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
EIAAB33721 hnRNP associated with lethal yellow protein,Maternally-expressed hnRNP C-related protein,Merc,Mouse,Mus musculus,Raly,RNA-binding protein Raly
EIAAB33724 Heterogeneous nuclear ribonucleoprotein C-like 3,hnRNP core protein C-like 3,HNRPCL3,Homo sapiens,hRALYL,Human,RALYL,RNA-binding Raly-like protein
EIAAB35658 Bos taurus,Bovine,Helix-destabilizing protein,Heterogeneous nuclear ribonucleoprotein A1,hnRNP A1,hnRNP core protein A1,HNRNPA1,HNRPA1,Single-strand RNA-binding protein,Unwinding protein 1,UP1
EIAAB35657 HDP,Helix-destabilizing protein,Heterogeneous nuclear ribonucleoprotein A1,hnRNP A1,hnRNP core protein A1,Hnrnpa1,Hnrpa1,Rat,Rattus norvegicus,Single-strand RNA-binding protein
EIAAB35655 Helix-destabilizing protein,Heterogeneous nuclear ribonucleoprotein A1,hnRNP A1,hnRNP core protein A1,HNRNPA1,HNRPA1,Homo sapiens,Human,Single-strand RNA-binding protein
EIAAB35656 Fli-2,HDP-1,Helix-destabilizing protein,Heterogeneous nuclear ribonucleoprotein A1,hnRNP A1,hnRNP core protein A1,Hnrnpa1,Hnrpa1,Mouse,Mus musculus,Single-strand-binding protein,Tis,Topoisomerase-inhi
RALY RALY Gene RNA binding protein, autoantigenic (hnRNP-associated with lethal yellow homolog (mouse))
EIAAB33407 Heterogeneous nuclear ribonucleoprotein A1-like 2,hnRNP A1-like 2,hnRNP core protein A1-like 2,HNRNPA1L,HNRNPA1L2,Homo sapiens,Human
18-003-43577 Heterogeneous nuclear ribonucleoprotein A1 - Helix-destabilizing protein; Single-strand RNA-binding protein; hnRNP core protein A1 Polyclonal 0.1 mg Protein A
18-003-43578 Heterogeneous nuclear ribonucleoprotein A1 - Helix-destabilizing protein; Single-strand RNA-binding protein; hnRNP core protein A1 Polyclonal 0.1 mg Protein A
18-003-44203 Heterogeneous nuclear ribonucleoprotein Q - hnRNP Q; hnRNP-Q; Synaptotagmin-binding. cytoplasmic RNA-interacting protein; Glycine- and tyrosine-rich RNA-binding protein; GRY-RBP; NS1-associated protei 0.1 mg Protein A
18-003-44204 Heterogeneous nuclear ribonucleoprotein Q - hnRNP Q; hnRNP-Q; Synaptotagmin-binding. cytoplasmic RNA-interacting protein; Glycine- and tyrosine-rich RNA-binding protein; GRY-RBP; NS1-associated protei 0.1 mg Protein A
20-373-85047 Heterogeneous nuclear ribonucleoprotein Q - hnRNP Q; hnRNP-Q; Synaptotagmin-binding. cytoplasmic RNA-interacting protein; Glycine- and tyrosine-rich RNA-binding protein; GRY-RBP; NS1-associated protei 0.05 ml
20-373-85018 Heterogeneous nuclear ribonucleoprotein Q - hnRNP Q; hnRNP-Q; Synaptotagmin-binding. cytoplasmic RNA-interacting protein; Glycine- and tyrosine-rich RNA-binding protein; GRY-RBP; NS1-associated protei 0.1 ml
CSB-EL019302HU Human RNA binding protein, autoantigenic (hnRNP-associated with lethal yellow homolog (mouse)) (RALY) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL019302MO Mouse RNA binding protein, autoantigenic (hnRNP-associated with lethal yellow homolog (mouse)) (RALY) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
29-401 HNRPUL1 is a nuclear RNA-binding protein of the heterogeneous nuclear ribonucleoprotein (hnRNP) family. This protein binds specifically to adenovirus E1B-55kDa oncoprotein. It may play an important ro 0.1 mg
29-500 HNRPUL1 is a nuclear RNA-binding protein of the heterogeneous nuclear ribonucleoprotein (hnRNP) family. This protein binds specifically to adenovirus E1B-55kDa oncoprotein. It may play an important ro 0.05 mg
18-003-44183 Polypyrimidine tract-binding protein 1 - PTB; Heterogeneous nuclear ribonucleoprotein I; hnRNP I; 57 kDa RNA-binding protein PPTB-1 Polyclonal 0.05 mg Aff Pur
EIAAB32931 57 kDa RNA-binding protein PPTB-1,Heterogeneous nuclear ribonucleoprotein I,hnRNP I,Homo sapiens,Human,Polypyrimidine tract-binding protein 1,PTB,PTB,PTBP1
EIAAB30032 Alpha-CP1,Heterogeneous nuclear ribonucleoprotein E1,hnRNP E1,Homo sapiens,Human,Nucleic acid-binding protein SUB2.3,PCBP1,Poly(rC)-binding protein 1
EIAAB32932 Heterogeneous nuclear ribonucleoprotein I,hnRNP I,Pig,Polypyrimidine tract-binding protein 1,PTB,PTB,PTBP1,Sus scrofa
18-003-42470 RNA binding protein (Autoantigenic. hnRNP-associated with lethal yellow) long isoform variant - RNA binding protein (Autoantigenic. hnRNP-associated with lethal yellow). long isoform Polyclonal 0.05 mg Aff Pur
EIAAB32929 Heterogeneous nuclear ribonucleoprotein I,hnRNP I,Mouse,Mus musculus,Polypyrimidine tract-binding protein 1,PTB,Ptb,Ptbp1


 

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