RALY_HUMAN
ID RALY_HUMAN Reviewed; 306 AA.
AC Q9UKM9; Q14621; Q2M365; Q5QPL8; Q9BQX6; Q9UJE3;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=RNA-binding protein Raly;
DE AltName: Full=Autoantigen p542;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein C-like 2;
DE Short=hnRNP core protein C-like 2;
DE AltName: Full=hnRNP associated with lethal yellow protein homolog;
GN Name=RALY; Synonyms=HNRPCL2, P542;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10500250; DOI=10.1016/s0167-4781(99)00126-8;
RA Khrebtukova I., Kuklin A., Woychik R.P., Michaud E.J.;
RT "Alternative processing of the human and mouse raly genes.";
RL Biochim. Biophys. Acta 1447:107-112(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN AUTOIMMUNE DISEASE,
RP AND FUNCTION.
RC TISSUE=Lymphocyte;
RX PubMed=9376072; DOI=10.1006/jaut.1997.9996;
RA Rhodes G.H., Valbracht J.R., Nguyen M.-D., Vaughan J.H.;
RT "The p542 gene encodes an autoantigen that cross-reacts with EBNA-1 of the
RT Epstein Barr virus and which may be a heterogeneous nuclear
RT ribonucleoprotein.";
RL J. Autoimmun. 10:447-454(1997).
RN [3]
RP SEQUENCE REVISION.
RA Vaughan J.H.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 23-44; 56-66; 79-99; 121-126; 132-141 AND 184-216,
RP PHOSPHORYLATION AT SER-135, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 227-253, AND AUTOANTIGENIC EPITOPE MAPPING.
RX PubMed=7533788; DOI=10.1172/jci117781;
RA Vaughan J.H., Valbracht J.R., Nguyen M.-D., Handley H.H., Smith R.S.,
RA Patrick K., Rhodes G.H.;
RT "Epstein-Barr virus-induced autoimmune responses. I. Immunoglobulin M
RT autoantibodies to proteins mimicking and not mimicking Epstein-Barr virus
RT nuclear antigen-1.";
RL J. Clin. Invest. 95:1306-1315(1995).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND THR-298, AND
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, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286; SER-288; SER-295 AND
RP THR-298, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-286; SER-288;
RP SER-295 AND THR-298, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
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-165, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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-135, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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-135, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-106 (ISOFORM 1), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-135, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; THR-286; SER-288 AND
RP THR-298, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 (ISOFORM 1), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-159 AND LYS-165, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4 AND LYS-159, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-94; LYS-99; LYS-159;
RP LYS-165; LYS-179 AND LYS-191, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [27]
RP INTERACTION WITH FUS.
RX PubMed=30354839; DOI=10.1091/mbc.e18-02-0108;
RA Gasperini L., Rossi A., Cornella N., Peroni D., Zuccotti P., Potrich V.,
RA Quattrone A., Macchi P.;
RT "The hnRNP raly regulates PRMT1 expression and interacts with the ALS-
RT linked protein FUS: implication for reciprocal cellular localization.";
RL Mol. Biol. Cell 2018:MBCE18020108-MBCE18020108(2018).
RN [28]
RP STRUCTURE BY NMR OF 1-97.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domain in RNA-binding protein NP_057951.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: RNA-binding protein that acts as a transcriptional cofactor
CC for cholesterol biosynthetic genes in the liver. Binds the lipid-
CC responsive non-coding RNA LeXis and is required for LeXis-mediated
CC effect on cholesterogenesis (By similarity). May be a heterogeneous
CC nuclear ribonucleoprotein (hnRNP) (PubMed:9376072).
CC {ECO:0000250|UniProtKB:Q64012, ECO:0000269|PubMed:9376072}.
CC -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:11991638).
CC Interacts (through its RNA-binding domain) with FUS (through its RNA-
CC binding domain); both are components of the same RNPs
CC (PubMed:30354839). {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:30354839}.
CC -!- INTERACTION:
CC Q9UKM9; P35637: FUS; NbExp=5; IntAct=EBI-714796, EBI-400434;
CC Q9UKM9; P07910: HNRNPC; NbExp=2; IntAct=EBI-714796, EBI-357966;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q64012}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q9UKM9-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9UKM9-2; Sequence=VSP_005804;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, lung, liver, skeletal
CC muscle, kidney and pancreas. Weakly expressed in placenta.
CC {ECO:0000269|PubMed:10500250}.
CC -!- MISCELLANEOUS: Autoantigen found in infectious mononucleosis caused by
CC Epstein-Barr virus. An epitope recognized by B-cells, which cross-react
CC with the BKRF1 protein (EBNA-1 nuclear protein) of Epstein-Barr virus
CC has been identified. {ECO:0000269|PubMed:9376072}.
CC -!- SIMILARITY: Belongs to the RRM HNRPC family. RALY subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF148457; AAF04487.1; -; mRNA.
DR EMBL; L38696; AAC28898.1; -; mRNA.
DR EMBL; AL031668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC105018; AAI05019.1; -; mRNA.
DR CCDS; CCDS13229.1; -. [Q9UKM9-2]
DR CCDS; CCDS13230.1; -. [Q9UKM9-1]
DR RefSeq; NP_031393.2; NM_007367.3. [Q9UKM9-2]
DR RefSeq; NP_057951.1; NM_016732.2. [Q9UKM9-1]
DR RefSeq; XP_005260391.1; XM_005260334.4. [Q9UKM9-1]
DR RefSeq; XP_005260393.1; XM_005260336.4. [Q9UKM9-2]
DR RefSeq; XP_011526996.1; XM_011528694.2. [Q9UKM9-1]
DR RefSeq; XP_011526997.1; XM_011528695.2. [Q9UKM9-1]
DR RefSeq; XP_016883220.1; XM_017027731.1. [Q9UKM9-1]
DR PDB; 1WF1; NMR; -; A=1-97.
DR PDBsum; 1WF1; -.
DR AlphaFoldDB; Q9UKM9; -.
DR BMRB; Q9UKM9; -.
DR SMR; Q9UKM9; -.
DR BioGRID; 116575; 302.
DR CORUM; Q9UKM9; -.
DR IntAct; Q9UKM9; 114.
DR MINT; Q9UKM9; -.
DR STRING; 9606.ENSP00000246194; -.
DR iPTMnet; Q9UKM9; -.
DR PhosphoSitePlus; Q9UKM9; -.
DR SwissPalm; Q9UKM9; -.
DR BioMuta; RALY; -.
DR DMDM; 25091115; -.
DR CPTAC; CPTAC-264; -.
DR CPTAC; CPTAC-265; -.
DR EPD; Q9UKM9; -.
DR jPOST; Q9UKM9; -.
DR MassIVE; Q9UKM9; -.
DR MaxQB; Q9UKM9; -.
DR PaxDb; Q9UKM9; -.
DR PeptideAtlas; Q9UKM9; -.
DR PRIDE; Q9UKM9; -.
DR ProteomicsDB; 84821; -. [Q9UKM9-1]
DR ProteomicsDB; 84822; -. [Q9UKM9-2]
DR Antibodypedia; 10794; 252 antibodies from 30 providers.
DR DNASU; 22913; -.
DR Ensembl; ENST00000246194.8; ENSP00000246194.3; ENSG00000125970.12. [Q9UKM9-1]
DR Ensembl; ENST00000375114.7; ENSP00000364255.3; ENSG00000125970.12. [Q9UKM9-2]
DR GeneID; 22913; -.
DR KEGG; hsa:22913; -.
DR MANE-Select; ENST00000246194.8; ENSP00000246194.3; NM_016732.3; NP_057951.1.
DR UCSC; uc002xab.4; human. [Q9UKM9-1]
DR CTD; 22913; -.
DR DisGeNET; 22913; -.
DR GeneCards; RALY; -.
DR HGNC; HGNC:15921; RALY.
DR HPA; ENSG00000125970; Low tissue specificity.
DR MIM; 614663; gene.
DR neXtProt; NX_Q9UKM9; -.
DR OpenTargets; ENSG00000125970; -.
DR PharmGKB; PA34201; -.
DR VEuPathDB; HostDB:ENSG00000125970; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000157601; -.
DR InParanoid; Q9UKM9; -.
DR OMA; HYYRNEL; -.
DR OrthoDB; 1182824at2759; -.
DR PhylomeDB; Q9UKM9; -.
DR TreeFam; TF330974; -.
DR PathwayCommons; Q9UKM9; -.
DR SignaLink; Q9UKM9; -.
DR SIGNOR; Q9UKM9; -.
DR BioGRID-ORCS; 22913; 7 hits in 1080 CRISPR screens.
DR ChiTaRS; RALY; human.
DR EvolutionaryTrace; Q9UKM9; -.
DR GeneWiki; RALY; -.
DR GenomeRNAi; 22913; -.
DR Pharos; Q9UKM9; Tbio.
DR PRO; PR:Q9UKM9; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9UKM9; protein.
DR Bgee; ENSG00000125970; Expressed in ganglionic eminence and 208 other tissues.
DR ExpressionAtlas; Q9UKM9; baseline and differential.
DR Genevisible; Q9UKM9; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:1903506; P:regulation of nucleic acid-templated transcription; ISS:UniProtKB.
DR CDD; cd12604; RRM_RALY; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR017347; hnRNP_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034502; RALY_RRM.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF037992; hnRNP-C_Raly; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW Direct protein sequencing; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW RNA-binding; Spliceosome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..306
FT /note="RNA-binding protein Raly"
FT /id="PRO_0000081746"
FT DOMAIN 21..92
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 215..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..253
FT /note="Epitope (recognized by BKRF1 antibodies)"
FT COILED 183..216
FT /evidence="ECO:0000255"
FT COMPBIAS 255..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64012"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 165
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 262
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q64012"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64012"
FT MOD_RES 286
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807684,
FT ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 94
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 159
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 165
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 110..125
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9376072"
FT /id="VSP_005804"
FT VARIANT 139
FT /note="V -> M (in dbSNP:rs35191085)"
FT /id="VAR_052215"
FT VARIANT 215
FT /note="Q -> R (in dbSNP:rs3180568)"
FT /id="VAR_015223"
FT VARIANT 251
FT /note="G -> S (in dbSNP:rs2281209)"
FT /id="VAR_015224"
FT CONFLICT 214..215
FT /note="EQ -> DE (in Ref. 2; AAC28898)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="A -> AS (in Ref. 2; AAC28898)"
FT /evidence="ECO:0000305"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:1WF1"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:1WF1"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1WF1"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1WF1"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:1WF1"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1WF1"
FT HELIX 66..75
FT /evidence="ECO:0007829|PDB:1WF1"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1WF1"
FT MOD_RES Q9UKM9-2:106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
SQ 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
