HNRPU_HUMAN
ID HNRPU_HUMAN Reviewed; 825 AA.
AC Q00839; O75507; Q8N174; Q96HY9; Q9BQ09;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 6.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein U {ECO:0000303|PubMed:1628625};
DE Short=hnRNP U {ECO:0000303|PubMed:1628625};
DE AltName: Full=GRIP120 {ECO:0000303|PubMed:9353307};
DE AltName: Full=Nuclear p120 ribonucleoprotein {ECO:0000303|PubMed:7753047};
DE AltName: Full=Scaffold-attachment factor A {ECO:0000303|PubMed:1324173, ECO:0000303|Ref.3};
DE Short=SAF-A {ECO:0000303|PubMed:1324173, ECO:0000303|Ref.3};
DE AltName: Full=p120 {ECO:0000303|PubMed:7993898};
DE AltName: Full=pp120 {ECO:0000303|PubMed:7993898};
GN Name=HNRNPU {ECO:0000312|HGNC:HGNC:5048};
GN Synonyms=C1orf199 {ECO:0000312|HGNC:HGNC:5048},
GN HNRPU {ECO:0000312|HGNC:HGNC:5048}, SAFA, U21.1;
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), SINGLE-STRANDED DNA- AND
RP RNA-BINDING, RNA-BINDING REGION, AND VARIANT LEU-712.
RX PubMed=1628625; DOI=10.1002/j.1460-2075.1992.tb05331.x;
RA Kiledjian M., Dreyfuss G.;
RT "Primary structure and binding activity of the hnRNP U protein: binding RNA
RT through RGG box.";
RL EMBO J. 11:2655-2664(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=7509195; DOI=10.1016/0167-4781(94)90044-2;
RA Fackelmayer F.O., Richter A.;
RT "hnRNP-U/SAF-A is encoded by two differentially polyadenylated mRNAs in
RT human cells.";
RL Biochim. Biophys. Acta 1217:232-234(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-712.
RA Fackelmayer F.O.;
RT "A variant of human scaffold attachment factor A (SAF-A), also known as
RT heterogeneous nuclear ribonucleoprotein U (hnRNP-U).";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye, Lymph, Placenta, and Skin;
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 2-7; 256-265 AND 463-476, PHOSPHORYLATION, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=7993898; DOI=10.1021/bi00253a007;
RA Jordan P., Heid H., Kinzel V., Kubler D.;
RT "Major cell surface-located protein substrates of an ecto-protein kinase
RT are homologs of known nuclear proteins.";
RL Biochemistry 33:14696-14706(1994).
RN [7]
RP PROTEIN SEQUENCE OF 2-9; 186-194; 319-330; 399-409; 423-432; 452-461;
RP 464-475 AND 524-535, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 2-9; 13-21; 38-69; 187-204; 256-268; 306-324; 353-360;
RP 424-433; 463-484; 495-510; 525-543; 552-558; 566-572; 576-590; 592-601;
RP 627-635; 665-674 AND 734-755, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT SER-2, METHYLATION AT ARG-739, 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 [9]
RP DNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=1324173; DOI=10.1002/j.1460-2075.1992.tb05422.x;
RA Romig H., Fackelmayer F.O., Renz A., Ramsperger U., Richter A.;
RT "Characterization of SAF-A, a novel nuclear DNA binding protein from HeLa
RT cells with high affinity for nuclear matrix/scaffold attachment DNA
RT elements.";
RL EMBO J. 11:3431-3440(1992).
RN [10]
RP DNA- AND RNA-BINDING, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=8068679; DOI=10.1021/bi00200a024;
RA Fackelmayer F.O., Richter A.;
RT "Purification of two isoforms of hnRNP-U and characterization of their
RT nucleic acid binding activity.";
RL Biochemistry 33:10416-10422(1994).
RN [11]
RP FUNCTION IN CHROMATIN STRUCTURE, DNA- AND RNA-BINDING, SUBCELLULAR
RP LOCATION, AND ASSOCIATION WITH HNRNP PARTICLES.
RX PubMed=8174554; DOI=10.1111/j.1432-1033.1994.tb18788.x;
RA Fackelmayer F.O., Dahm K., Renz A., Ramsperger U., Richter A.;
RT "Nucleic-acid-binding properties of hnRNP-U/SAF-A, a nuclear-matrix protein
RT which binds DNA and RNA in vivo and in vitro.";
RL Eur. J. Biochem. 221:749-757(1994).
RN [12]
RP INTERACTION WITH CR2.
RX PubMed=7753047; DOI=10.1016/0161-5890(95)00005-y;
RA Barel M., Balbo M., Gauffre A., Frade R.;
RT "Binding sites of the Epstein-Barr virus and C3d receptor (CR2, CD21) for
RT its three intracellular ligands, the p53 anti-oncoprotein, the p68 calcium
RT binding protein and the nuclear p120 ribonucleoprotein.";
RL Mol. Immunol. 32:389-397(1995).
RN [13]
RP DNA-BINDING, CHROMATIN-BINDING, AND ASSOCIATION WITH HNRNP PARTICLES.
RX PubMed=9204873; DOI=10.1021/bi970480f;
RA Goehring F., Fackelmayer F.O.;
RT "The scaffold/matrix attachment region binding protein hnRNP-U (SAF-A) is
RT directly bound to chromosomal DNA in vivo: a chemical cross-linking
RT study.";
RL Biochemistry 36:8276-8283(1997).
RN [14]
RP INTERACTION WITH POU3F4.
RX PubMed=9105675; DOI=10.1016/s0169-328x(96)00238-0;
RA Malik K.F., Jaffe H., Brady J., Young W.S. III;
RT "The class III POU factor Brn-4 interacts with other class III POU factors
RT and the heterogeneous nuclear ribonucleoprotein U.";
RL Brain Res. Mol. Brain Res. 45:99-107(1997).
RN [15]
RP CLEAVAGE BY CASPASES, DNA-BINDING, CHROMATIN-BINDING, SUBCELLULAR LOCATION,
RP ASSOCIATION WITH HNRNP PARTICLES, AND SAP DOMAIN.
RX PubMed=9405365; DOI=10.1093/emboj/16.24.7361;
RA Goehring F., Schwab B.L., Nicotera P., Leist M., Fackelmayer F.O.;
RT "The novel SAR-binding domain of scaffold attachment factor A (SAF-A) is a
RT target in apoptotic nuclear breakdown.";
RL EMBO J. 16:7361-7371(1997).
RN [16]
RP FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH NR3C1, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=9353307; DOI=10.1074/jbc.272.45.28471;
RA Eggert M., Michel J., Schneider S., Bornfleth H., Baniahmad A.,
RA Fackelmayer F.O., Schmidt S., Renkawitz R.;
RT "The glucocorticoid receptor is associated with the RNA-binding nuclear
RT matrix protein hnRNP U.";
RL J. Biol. Chem. 272:28471-28478(1997).
RN [17]
RP FUNCTION IN MRNA TRANSCRIPTION ELONGATION INHIBITION, ASSOCIATION WITH RNA
RP POLYMERASE II HOLOENZYME, AND ASSOCIATION WITH TFIIH BASAL TRANSCRIPTION
RP FACTOR.
RX PubMed=10490622; DOI=10.1128/mcb.19.10.6833;
RA Kim M.K., Nikodem V.M.;
RT "hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and
RT represses RNA polymerase II elongation.";
RL Mol. Cell. Biol. 19:6833-6844(1999).
RN [18]
RP CLEAVAGE SITE BY CASP3, DNA-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF ASP-100.
RX PubMed=10671544; DOI=10.1074/jbc.275.7.5031;
RA Kipp M., Schwab B.L., Przybylski M., Nicotera P., Fackelmayer F.O.;
RT "Apoptotic cleavage of scaffold attachment factor A (SAF-A) by caspase-3
RT occurs at a noncanonical cleavage site.";
RL J. Biol. Chem. 275:5031-5036(2000).
RN [19]
RP DNA-BINDING, CHROMATIN-BINDING, SUBCELLULAR LOCATION, AND SAP DOMAIN.
RX PubMed=11003645; DOI=10.1128/mcb.20.20.7480-7489.2000;
RA Kipp M., Goehring F., Ostendorp T., van Drunen C.M., van Driel R.,
RA Przybylski M., Fackelmayer F.O.;
RT "SAF-Box, a conserved protein domain that specifically recognizes scaffold
RT attachment region DNA.";
RL Mol. Cell. Biol. 20:7480-7489(2000).
RN [20]
RP INTERACTION WITH EP300, ASSOCIATION WITH RNP PARTICLES, AND
RP CHROMATIN-BINDING.
RX PubMed=11909954; DOI=10.1128/mcb.22.8.2598-2606.2002;
RA Martens J.H., Verlaan M., Kalkhoven E., Dorsman J.C., Zantema A.;
RT "Scaffold/matrix attachment region elements interact with a p300-scaffold
RT attachment factor A complex and are bound by acetylated nucleosomes.";
RL Mol. Cell. Biol. 22:2598-2606(2002).
RN [21]
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 [22]
RP SUBCELLULAR LOCATION, AND RNA-BINDING RGG-BOX REGION.
RX PubMed=14608463; DOI=10.1007/s00412-003-0258-0;
RA Helbig R., Fackelmayer F.O.;
RT "Scaffold attachment factor A (SAF-A) is concentrated in inactive X
RT chromosome territories through its RGG domain.";
RL Chromosoma 112:173-182(2003).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [24]
RP SUBCELLULAR LOCATION.
RX PubMed=15563465; DOI=10.1074/jbc.c400531200;
RA Fackelmayer F.O.;
RT "A stable proteinaceous structure in the territory of inactive X
RT chromosomes.";
RL J. Biol. Chem. 280:1720-1723(2005).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [26]
RP FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH ACTIN,
RP ACTIN-BINDING REGION, AND MUTAGENESIS OF 616-ARG--LYS-620.
RX PubMed=15711563; DOI=10.1038/nsmb904;
RA Kukalev A., Nord Y., Palmberg C., Bergman T., Percipalle P.;
RT "Actin and hnRNP U cooperate for productive transcription by RNA polymerase
RT II.";
RL Nat. Struct. Mol. Biol. 12:238-244(2005).
RN [27]
RP MUTAGENESIS OF SER-59, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND
RP SER-271, AND IDENTIFICATION BY 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 [28]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=16916646; DOI=10.1016/j.molcel.2006.07.021;
RA Valente S.T., Goff S.P.;
RT "Inhibition of HIV-1 gene expression by a fragment of hnRNP U.";
RL Mol. Cell 23:597-605(2006).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, AND IDENTIFICATION BY
RP 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 [30]
RP FUNCTION IN MRNA STABILIZATION, AND MESSENGER RNA-BINDING.
RX PubMed=17174306; DOI=10.1016/s0014-5793(07)01283-5;
RA Yugami M., Kabe Y., Yamaguchi Y., Wada T., Handa H.;
RT "hnRNP-U enhances the expression of specific genes by stabilizing mRNA.";
RL FEBS Lett. 581:1-7(2007).
RN [31]
RP FUNCTION IN TELOMERE REGULATION, AND ASSOCIATION WITH TELOMERASE HOLOENZYME
RP COMPLEX.
RX PubMed=18082603; DOI=10.1016/j.molcel.2007.09.023;
RA Fu D., Collins K.;
RT "Purification of human telomerase complexes identifies factors involved in
RT telomerase biogenesis and telomere length regulation.";
RL Mol. Cell 28:773-785(2007).
RN [32]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-66, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, AND IDENTIFICATION BY
RP 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 [35]
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=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 [36]
RP FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH CBX5, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19617346; DOI=10.1074/jbc.m109.037929;
RA Ameyar-Zazoua M., Souidi M., Fritsch L., Robin P., Thomas A., Hamiche A.,
RA Percipalle P., Ait-Si-Ali S., Harel-Bellan A.;
RT "Physical and functional interaction between heterochromatin protein 1alpha
RT and the RNA-binding protein heterogeneous nuclear ribonucleoprotein U.";
RL J. Biol. Chem. 284:27974-27979(2009).
RN [37]
RP INTERACTION WITH HIV-1 VIRUS REV PROTEIN (MICROBIAL INFECTION).
RX PubMed=19808671; DOI=10.1074/jbc.m109.021659;
RA Hadian K., Vincendeau M., Maeusbacher N., Nagel D., Hauck S.M., Ueffing M.,
RA Loyter A., Werner T., Wolff H., Brack-Werner R.;
RT "Identification of a heterogeneous nuclear ribonucleoprotein-recognition
RT region in the HIV Rev protein.";
RL J. Biol. Chem. 284:33384-33391(2009).
RN [38]
RP FUNCTION IN MRNA STABILITY, COMPONENT OF THE CRD-MEDIATED MRNA
RP STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A.,
RA Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs.";
RL RNA 15:104-115(2009).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-66 AND SER-271, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [40]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265; LYS-352; LYS-516; LYS-524;
RP LYS-551; LYS-565; LYS-635 AND LYS-814, ACETYLATION [LARGE SCALE ANALYSIS]
RP AT LYS-215 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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 [41]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH ERBB4.
RX PubMed=20858735; DOI=10.1158/1541-7786.mcr-10-0042;
RA Gilmore-Hebert M., Ramabhadran R., Stern D.F.;
RT "Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage
RT response pathways.";
RL Mol. Cancer Res. 8:1388-1398(2010).
RN [42]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4; SER-59; SER-66 AND SER-271, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [43]
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 [44]
RP FUNCTION IN MITOSIS, INTERACTION WITH AURKA; NCL AND TPX2, ASSOCIATION WITH
RP MICROTUBULES, AND SUBCELLULAR LOCATION.
RX PubMed=21242313; DOI=10.1242/jcs.063347;
RA Ma N., Matsunaga S., Morimoto A., Sakashita G., Urano T., Uchiyama S.,
RA Fukui K.;
RT "The nuclear scaffold protein SAF-A is required for kinetochore-microtubule
RT attachment and contributes to the targeting of Aurora-A to mitotic
RT spindles.";
RL J. Cell Sci. 124:394-404(2011).
RN [45]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4; SER-59 AND SER-66, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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 [46]
RP FUNCTION IN PRE-MRNA ALTERNATIVE SPLICING, PRE-MRNA-BINDING, AND
RP SNRNA-BINDING.
RX PubMed=22325991; DOI=10.1016/j.molcel.2012.01.009;
RA Xiao R., Tang P., Yang B., Huang J., Zhou Y., Shao C., Li H., Sun H.,
RA Zhang Y., Fu X.D.;
RT "Nuclear matrix factor hnRNP U/SAF-A exerts a global control of alternative
RT splicing by regulating U2 snRNP maturation.";
RL Mol. Cell 45:656-668(2012).
RN [47]
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=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [48]
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 [49]
RP FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH ACTIN, H19
RP RNA-BINDING, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23811339; DOI=10.1016/j.bbagen.2013.06.026;
RA Bi H.S., Yang X.Y., Yuan J.H., Yang F., Xu D., Guo Y.J., Zhang L.,
RA Zhou C.C., Wang F., Sun S.H.;
RT "H19 inhibits RNA polymerase II-mediated transcription by disrupting the
RT hnRNP U-actin complex.";
RL Biochim. Biophys. Acta 1830:4899-4906(2013).
RN [50]
RP INTERACTION WITH IGF2BP1; IGF2BP2 AND IGF2BP3.
RX PubMed=23640942; DOI=10.1515/hsz-2013-0111;
RA Wachter K., Kohn M., Stohr N., Huttelmaier S.;
RT "Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding
RT proteins) is modulated by distinct RNA-binding domains.";
RL Biol. Chem. 394:1077-1090(2013).
RN [51]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-59; SER-66; SER-267;
RP SER-271; THR-532 AND THR-582, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [52]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-271 AND THR-286, 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 [53]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-702; ARG-733; ARG-739; ARG-755
RP AND ARG-762, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [54]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-265; LYS-609 AND LYS-670, 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 [55]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-265, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [56]
RP INTERACTION WITH GEMIN5.
RX PubMed=25911097; DOI=10.1074/jbc.m115.646257;
RA Workman E., Kalda C., Patel A., Battle D.J.;
RT "Gemin5 binds to the survival motor neuron mRNA to regulate SMN
RT expression.";
RL J. Biol. Chem. 290:15662-15669(2015).
RN [57]
RP INTERACTION WITH UBQLN2.
RX PubMed=25616961; DOI=10.1093/hmg/ddv020;
RA Gilpin K.M., Chang L., Monteiro M.J.;
RT "ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between
RT ubiquilin-2 and hnRNPA1.";
RL Hum. Mol. Genet. 24:2565-2577(2015).
RN [58]
RP FUNCTION IN MITOSIS, INTERACTION WITH AURKA; PLK1 AND TPX2, PHOSPHORYLATION
RP AT SER-59 BY PLK1, DEPHOSPHORYLATION BY PP2A, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF SER-59.
RX PubMed=25986610; DOI=10.1128/mcb.01312-14;
RA Douglas P., Ye R., Morrice N., Britton S., Trinkle-Mulcahy L.,
RA Lees-Miller S.P.;
RT "Phosphorylation of SAF-A/hnRNP-U serine 59 by polo-like kinase 1 is
RT required for mitosis.";
RL Mol. Cell. Biol. 35:2699-2713(2015).
RN [59]
RP XIST RNA-BINDING.
RX PubMed=26244333; DOI=10.1371/journal.pgen.1005430;
RA Yamada N., Hasegawa Y., Yue M., Hamada T., Nakagawa S., Ogawa Y.;
RT "Xist exon 7 contributes to the stable localization of Xist RNA on the
RT inactive X-chromosome.";
RL PLoS Genet. 11:E1005430-E1005430(2015).
RN [60]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [61]
RP FUNCTION IN CHROMATIN STRUCTURE, SUBUNIT, ATPASE DOMAIN, AND RNA-BINDING
RP RGG-BOX REGION.
RX PubMed=28622508; DOI=10.1016/j.cell.2017.05.029;
RA Nozawa R.S., Boteva L., Soares D.C., Naughton C., Dun A.R., Buckle A.,
RA Ramsahoye B., Bruton P.C., Saleeb R.S., Arnedo M., Hill B., Duncan R.R.,
RA Maciver S.K., Gilbert N.;
RT "SAF-A regulates interphase chromosome structure through oligomerization
RT with chromatin-associated RNAs.";
RL Cell 169:1214-1227(2017).
RN [62]
RP ADP-RIBOSYLATION AT SER-187.
RX PubMed=28190768; DOI=10.1016/j.molcel.2017.01.003;
RA Bonfiglio J.J., Fontana P., Zhang Q., Colby T., Gibbs-Seymour I.,
RA Atanassov I., Bartlett E., Zaja R., Ahel I., Matic I.;
RT "Serine ADP-ribosylation depends on HPF1.";
RL Mol. Cell 0:0-0(2017).
RN [63]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-265; LYS-495; LYS-516; LYS-524;
RP LYS-536; LYS-565; LYS-574; LYS-609; LYS-626; LYS-635; LYS-664; LYS-670 AND
RP LYS-814, AND IDENTIFICATION BY MASS SPECTROMETRY [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 [64]
RP STRUCTURE BY NMR OF 23-42.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SAP domain of human E1B-55kDa-associated protein
RT 5 isoform C.";
RL Submitted (JAN-2008) to the PDB data bank.
RN [65]
RP INVOLVEMENT IN DEE54, AND VARIANT DEE54 805-TRP--TYR-825 DEL.
RX PubMed=23708187; DOI=10.1038/ng.2646;
RA Carvill G.L., Heavin S.B., Yendle S.C., McMahon J.M., O'Roak B.J., Cook J.,
RA Khan A., Dorschner M.O., Weaver M., Calvert S., Malone S., Wallace G.,
RA Stanley T., Bye A.M., Bleasel A., Howell K.B., Kivity S., Mackay M.T.,
RA Rodriguez-Casero V., Webster R., Korczyn A., Afawi Z., Zelnick N.,
RA Lerman-Sagie T., Lev D., Moeller R.S., Gill D., Andrade D.M., Freeman J.L.,
RA Sadleir L.G., Shendure J., Berkovic S.F., Scheffer I.E., Mefford H.C.;
RT "Targeted resequencing in epileptic encephalopathies identifies de novo
RT mutations in CHD2 and SYNGAP1.";
RL Nat. Genet. 45:825-830(2013).
RN [66]
RP VARIANT DEE54 171-GLN--TYR-825 DEL.
RX PubMed=25356899; DOI=10.1371/journal.pgen.1004772;
RA Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C., Patry L.,
RA Massicotte C., Ambalavanan A., Spiegelman D., Diallo O., Henrion E.,
RA Dionne-Laporte A., Fougerat A., Pshezhetsky A.V., Venkateswaran S.,
RA Rouleau G.A., Michaud J.L.;
RT "De novo mutations in moderate or severe intellectual disability.";
RL PLoS Genet. 10:E1004772-E1004772(2014).
CC -!- FUNCTION: DNA- and RNA-binding protein involved in several cellular
CC processes such as nuclear chromatin organization, telomere-length
CC regulation, transcription, mRNA alternative splicing and stability,
CC Xist-mediated transcriptional silencing and mitotic cell progression
CC (PubMed:10490622, PubMed:18082603, PubMed:19029303, PubMed:22325991,
CC PubMed:25986610, PubMed:28622508). Plays a role in the regulation of
CC interphase large-scale gene-rich chromatin organization through
CC chromatin-associated RNAs (caRNAs) in a transcription-dependent manner,
CC and thereby maintains genomic stability (PubMed:1324173,
CC PubMed:8174554, PubMed:28622508). Required for the localization of the
CC long non-coding Xist RNA on the inactive chromosome X (Xi) and the
CC subsequent initiation and maintenance of X-linked transcriptional gene
CC silencing during X-inactivation (By similarity). Plays a role as a RNA
CC polymerase II (Pol II) holoenzyme transcription regulator
CC (PubMed:8174554, PubMed:9353307, PubMed:10490622, PubMed:15711563,
CC PubMed:19617346, PubMed:23811339). Promotes transcription initiation by
CC direct association with the core-TFIIH basal transcription factor
CC complex for the assembly of a functional pre-initiation complex with
CC Pol II in a actin-dependent manner (PubMed:10490622, PubMed:15711563).
CC Blocks Pol II transcription elongation activity by inhibiting the C-
CC terminal domain (CTD) phosphorylation of Pol II and dissociates from
CC Pol II pre-initiation complex prior to productive transcription
CC elongation (PubMed:10490622). Positively regulates CBX5-induced
CC transcriptional gene silencing and retention of CBX5 in the nucleus
CC (PubMed:19617346). Negatively regulates glucocorticoid-mediated
CC transcriptional activation (PubMed:9353307). Key regulator of
CC transcription initiation and elongation in embryonic stem cells upon
CC leukemia inhibitory factor (LIF) signaling (By similarity). Involved in
CC the long non-coding RNA H19-mediated Pol II transcriptional repression
CC (PubMed:23811339). Participates in the circadian regulation of the core
CC clock component ARNTL/BMAL1 transcription (By similarity). Plays a role
CC in the regulation of telomere length (PubMed:18082603). Plays a role as
CC a global pre-mRNA alternative splicing modulator by regulating U2 small
CC nuclear ribonucleoprotein (snRNP) biogenesis (PubMed:22325991). Plays a
CC role in mRNA stability (PubMed:17174306, PubMed:17289661,
CC PubMed:19029303). Component of the CRD-mediated complex that promotes
CC MYC mRNA stabilization (PubMed:19029303). Enhances the expression of
CC specific genes, such as tumor necrosis factor TNFA, by regulating mRNA
CC stability, possibly through binding to the 3'-untranslated region (UTR)
CC (PubMed:17174306). Plays a role in mitotic cell cycle regulation
CC (PubMed:21242313, PubMed:25986610). Involved in the formation of stable
CC mitotic spindle microtubules (MTs) attachment to kinetochore, spindle
CC organization and chromosome congression (PubMed:21242313).
CC Phosphorylation at Ser-59 by PLK1 is required for chromosome alignement
CC and segregation and progression through mitosis (PubMed:25986610).
CC Contributes also to the targeting of AURKA to mitotic spindle MTs
CC (PubMed:21242313). Binds to double- and single-stranded DNA and RNA,
CC poly(A), poly(C) and poly(G) oligoribonucleotides (PubMed:1628625,
CC PubMed:8068679, PubMed:8174554, PubMed:9204873, PubMed:9405365). Binds
CC to chromatin-associated RNAs (caRNAs) (PubMed:28622508). Associates
CC with chromatin to scaffold/matrix attachment region (S/MAR) elements in
CC a chromatin-associated RNAs (caRNAs)-dependent manner (PubMed:7509195,
CC PubMed:1324173, PubMed:9204873, PubMed:9405365, PubMed:10671544,
CC PubMed:11003645, PubMed:11909954, PubMed:28622508). Binds to the Xist
CC RNA (PubMed:26244333). Binds the long non-coding H19 RNA
CC (PubMed:23811339). Binds to SMN1/2 pre-mRNAs at G/U-rich regions
CC (PubMed:22325991). Binds to small nuclear RNAs (snRNAs)
CC (PubMed:22325991). Binds to the 3'-UTR of TNFA mRNA (PubMed:17174306).
CC Binds (via RNA-binding RGG-box region) to the long non-coding Xist RNA;
CC this binding is direct and bridges the Xist RNA and the inactive
CC chromosome X (Xi) (By similarity). Also negatively regulates embryonic
CC stem cell differentiation upon LIF signaling (By similarity). Required
CC for embryonic development (By similarity). Binds to brown fat long non-
CC coding RNA 1 (Blnc1); facilitates the recruitment of Blnc1 by ZBTB7B
CC required to drive brown and beige fat development and thermogenesis (By
CC similarity). {ECO:0000250|UniProtKB:Q8VEK3,
CC ECO:0000269|PubMed:10490622, ECO:0000269|PubMed:10671544,
CC ECO:0000269|PubMed:11003645, ECO:0000269|PubMed:11909954,
CC ECO:0000269|PubMed:1324173, ECO:0000269|PubMed:15711563,
CC ECO:0000269|PubMed:1628625, ECO:0000269|PubMed:17174306,
CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:18082603,
CC ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19617346,
CC ECO:0000269|PubMed:21242313, ECO:0000269|PubMed:22325991,
CC ECO:0000269|PubMed:23811339, ECO:0000269|PubMed:25986610,
CC ECO:0000269|PubMed:26244333, ECO:0000269|PubMed:28622508,
CC ECO:0000269|PubMed:7509195, ECO:0000269|PubMed:8068679,
CC ECO:0000269|PubMed:8174554, ECO:0000269|PubMed:9204873,
CC ECO:0000269|PubMed:9353307, ECO:0000269|PubMed:9405365}.
CC -!- FUNCTION: (Microbial infection) Negatively regulates immunodeficiency
CC virus type 1 (HIV-1) replication by preventing the accumulation of
CC viral mRNA transcripts in the cytoplasm. {ECO:0000269|PubMed:16916646}.
CC -!- SUBUNIT: Oligomer (via ATPase domain and RNA-binding RGG-box region);
CC oligomerization occurs upon ATP-binding in a chromatin-associated RNAs
CC (caRNAs)- and transcription-dependent manner and is required for
CC chromatin decompaction (PubMed:28622508). ATP hydrolysis is required to
CC cycle from an oligomeric to monomeric state to compact chromatin
CC (PubMed:28622508). Component of the coding region determinant (CRD)-
CC mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1
CC (PubMed:19029303). Identified in the spliceosome C complex
CC (PubMed:11991638). Identified in a IGF2BP1-dependent mRNP granule
CC complex containing untranslated mRNAs (PubMed:17289661,
CC PubMed:19029303). Associates with heterogeneous nuclear
CC ribonucleoprotein (hnRNP) particles (PubMed:8174554, PubMed:9204873,
CC PubMed:9405365, PubMed:11909954). Associates (via middle region) with
CC the C-terminal domain (CTD) RNA polymerase II (Pol II) holoenzyme; this
CC association occurs in a RNA-independent manner (PubMed:10490622).
CC Associates (via middle region) with the core-TFIIH basal transcription
CC factor complex; this association inhibits the CTD phosphorylation of
CC RNA polymerase II holoenzyme by down-regulating TFIIH kinase activity
CC (PubMed:10490622). Associates with the telomerase holoenzyme complex
CC (PubMed:18082603). Associates with spindle microtubules (MTs) in a
CC TPX2-dependent manner (PubMed:21242313). Interacts (via C-terminus)
CC with actin; this interaction is direct and mediates association with
CC the phosphorylated CTD of RNA polymerase II and is disrupted in
CC presence of the long non-coding H19 RNA (PubMed:15711563,
CC PubMed:23811339). Interacts with AURKA (PubMed:21242313,
CC PubMed:25986610). Interacts (via C-terminus) with CBX5; this
CC interaction is, at least in part, RNA-dependent (PubMed:19617346).
CC Interacts with CR2 (PubMed:7753047). Interacts with CRY1 (By
CC similarity). Interacts (via C-terminus) with EP300; this interaction
CC enhances DNA-binding to nuclear scaffold/matrix attachment region
CC (S/MAR) elements (PubMed:11909954). Interacts with ERBB4
CC (PubMed:20858735). Interacts with GEMIN5 (PubMed:25911097). Interacts
CC with IGF2BP1 (PubMed:17289661, PubMed:23640942). Interacts with IGF2BP2
CC and IGF2BP3 (PubMed:23640942). Interacts with NCL; this interaction
CC occurs during mitosis (PubMed:21242313). Interacts (via C-terminus)
CC with NR3C1 (via C-terminus) (PubMed:9353307). Interacts with PLK1; this
CC interaction induces phosphorylation of HNRNPU at Ser-59 in mitosis
CC (PubMed:25986610). Interacts with POU3F4 (PubMed:9105675). Interacts
CC with SMARCA4; this interaction occurs in embryonic stem cells and
CC stimulates global Pol II-mediated transcription. Interacts (via C-
CC terminus) with TOP2A; this interaction protects the topoisomerase TOP2A
CC from degradation and positively regulates the relaxation of supercoiled
CC DNA by TOP2A in a RNA-dependent manner (By similarity). Interacts with
CC TPX2; this interaction recruits HNRNPU to spindle microtubules (MTs)
CC (PubMed:21242313, PubMed:25986610). Interacts with UBQLN2
CC (PubMed:25616961). Interacts (via RNA-binding RGG-box region) with
CC ZBTB7B; the interaction facilitates the recruitment of long non-coding
CC RNA Blnc1 by ZBTB7B (By similarity). Interacts with ERCC6
CC (PubMed:26030138). {ECO:0000250|UniProtKB:Q6IMY8,
CC ECO:0000250|UniProtKB:Q8VEK3, ECO:0000269|PubMed:10490622,
CC ECO:0000269|PubMed:11909954, ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:15711563, ECO:0000269|PubMed:17289661,
CC ECO:0000269|PubMed:18082603, ECO:0000269|PubMed:19029303,
CC ECO:0000269|PubMed:19617346, ECO:0000269|PubMed:20858735,
CC ECO:0000269|PubMed:21242313, ECO:0000269|PubMed:23640942,
CC ECO:0000269|PubMed:23811339, ECO:0000269|PubMed:25616961,
CC ECO:0000269|PubMed:25911097, ECO:0000269|PubMed:25986610,
CC ECO:0000269|PubMed:26030138, ECO:0000269|PubMed:28622508,
CC ECO:0000269|PubMed:7753047, ECO:0000269|PubMed:8174554,
CC ECO:0000269|PubMed:9105675, ECO:0000269|PubMed:9204873,
CC ECO:0000269|PubMed:9353307, ECO:0000269|PubMed:9405365}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 protein Rev.
CC {ECO:0000269|PubMed:19808671}.
CC -!- INTERACTION:
CC Q00839; Q8TDN6: BRIX1; NbExp=2; IntAct=EBI-351126, EBI-1052326;
CC Q00839; P42771: CDKN2A; NbExp=2; IntAct=EBI-351126, EBI-375053;
CC Q00839; P09429: HMGB1; NbExp=3; IntAct=EBI-351126, EBI-389432;
CC Q00839; Q14103: HNRNPD; NbExp=3; IntAct=EBI-351126, EBI-299674;
CC Q00839; P61978: HNRNPK; NbExp=2; IntAct=EBI-351126, EBI-304185;
CC Q00839; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-351126, EBI-947187;
CC Q00839-2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-351143, EBI-1055254;
CC Q00839-2; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-351143, EBI-11987469;
CC Q00839-2; Q13148: TARDBP; NbExp=6; IntAct=EBI-351143, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10671544,
CC ECO:0000269|PubMed:11003645, ECO:0000269|PubMed:1324173,
CC ECO:0000269|PubMed:14608463, ECO:0000269|PubMed:15563465,
CC ECO:0000269|PubMed:19617346, ECO:0000269|PubMed:21242313,
CC ECO:0000269|PubMed:8174554, ECO:0000269|PubMed:9353307,
CC ECO:0000269|PubMed:9405365}. Nucleus matrix
CC {ECO:0000269|PubMed:1324173, ECO:0000269|PubMed:14608463,
CC ECO:0000269|PubMed:8174554}. Chromosome {ECO:0000269|PubMed:11003645,
CC ECO:0000269|PubMed:14608463, ECO:0000269|PubMed:15563465}. Nucleus
CC speckle {ECO:0000269|PubMed:9353307}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:25986610}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:21242313}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:21242313, ECO:0000269|PubMed:25986610}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:21242313}. Midbody
CC {ECO:0000269|PubMed:25986610}. Cytoplasm {ECO:0000269|PubMed:19029303}.
CC Cell surface {ECO:0000269|PubMed:7993898}. Cytoplasmic granule
CC {ECO:0000269|PubMed:17289661}. Note=Localizes at inactive X chromosome
CC (Xi) regions (PubMed:11003645, PubMed:14608463, PubMed:15563465).
CC Localizes in the nucleus during interphase (PubMed:21242313). At
CC metaphase, localizes with mitotic spindle microtubules (MTs)
CC (PubMed:21242313). At anaphase, localizes in the mitotic spindle
CC midzone (PubMed:21242313). Localizes in spindle MTs proximal to spindle
CC poles in a TPX2- and AURKA-dependent manner (PubMed:21242313). The Ser-
CC 59 phosphorylated form localizes to centrosomes during prophase and
CC metaphase, to mitotic spindles in anaphase and to the midbody during
CC cytokinesis (PubMed:25986610). Colocalizes with SMARCA4 in the nucleus
CC (By similarity). Colocalizes with CBX5 in the nucleus
CC (PubMed:19617346). Colocalizes with NR3C1 in nuclear speckles
CC (PubMed:9353307). Localized in cytoplasmic ribonucleoprotein (RNP)
CC granules containing untranslated mRNAs (PubMed:17289661).
CC {ECO:0000250|UniProtKB:Q8VEK3, ECO:0000269|PubMed:11003645,
CC ECO:0000269|PubMed:14608463, ECO:0000269|PubMed:15563465,
CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:19617346,
CC ECO:0000269|PubMed:21242313, ECO:0000269|PubMed:25986610,
CC ECO:0000269|PubMed:9353307}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=Q00839-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q00839-2; Sequence=VSP_005846;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:7509195}.
CC -!- DOMAIN: The SAP domain is necessary for specific binding to nuclear
CC scaffold/matrix attachment region (S/MAR) elements in DNA
CC (PubMed:9405365, PubMed:11003645). The RNA-binding RGG-box region is
CC necessary for its association with inactive X chromosome (Xi) regions
CC and to chromatin-associated RNAs (caRNAs) (PubMed:14608463,
CC PubMed:28622508). Both the DNA-binding domain SAP and the RNA-binding
CC RGG-box region are necessary for the localization of Xist RNA on the Xi
CC (By similarity). The ATPase and RNA-binding RGG-box regions are
CC necessary for oligomerization (PubMed:28622508).
CC {ECO:0000250|UniProtKB:Q8VEK3, ECO:0000269|PubMed:11003645,
CC ECO:0000269|PubMed:14608463, ECO:0000269|PubMed:28622508,
CC ECO:0000269|PubMed:9405365}.
CC -!- PTM: Cleaved at Asp-100 by CASP3 during T-cell apoptosis, resulting in
CC a loss of DNA- and chromatin-binding activities (PubMed:9405365,
CC PubMed:10671544). {ECO:0000269|PubMed:10671544,
CC ECO:0000269|PubMed:9405365}.
CC -!- PTM: Extensively phosphorylated (PubMed:7993898). Phosphorylated on
CC Ser-59 by PLK1 and dephosphorylated by protein phosphatase 2A (PP2A) in
CC mitosis (PubMed:25986610). {ECO:0000269|PubMed:25986610,
CC ECO:0000269|PubMed:7993898}.
CC -!- PTM: Arg-739 is dimethylated, probably to asymmetric dimethylarginine
CC (Ref.8). Arg-733 is dimethylated, probably to asymmetric
CC dimethylarginine (By similarity). {ECO:0000250|UniProtKB:Q8VEK3,
CC ECO:0000269|Ref.8}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q8VEK3}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 54 (DEE54)
CC [MIM:617391]: A form of epileptic encephalopathy, a heterogeneous group
CC of severe early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. {ECO:0000269|PubMed:23708187,
CC ECO:0000269|PubMed:25356899}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC19382.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; X65488; CAA46472.1; -; mRNA.
DR EMBL; AF068846; AAC19382.1; ALT_SEQ; mRNA.
DR EMBL; BX323046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003367; AAH03367.1; -; mRNA.
DR EMBL; BC003621; AAH03621.1; -; mRNA.
DR EMBL; BC007950; AAH07950.2; -; mRNA.
DR EMBL; BC024767; AAH24767.1; -; mRNA.
DR EMBL; BC034925; AAH34925.1; -; mRNA.
DR CCDS; CCDS31081.1; -. [Q00839-2]
DR CCDS; CCDS41479.1; -. [Q00839-1]
DR PIR; S22765; S22765.
DR RefSeq; NP_004492.2; NM_004501.3. [Q00839-2]
DR RefSeq; NP_114032.2; NM_031844.2. [Q00839-1]
DR RefSeq; XP_016856604.1; XM_017001115.1.
DR RefSeq; XP_016856605.1; XM_017001116.1.
DR RefSeq; XP_016856606.1; XM_017001117.1.
DR PDB; 1ZRJ; NMR; -; A=23-42.
DR PDBsum; 1ZRJ; -.
DR AlphaFoldDB; Q00839; -.
DR SMR; Q00839; -.
DR BioGRID; 109433; 793.
DR ComplexPortal; CPX-1080; CRD-mediated mRNA stability complex.
DR CORUM; Q00839; -.
DR DIP; DIP-684N; -.
DR IntAct; Q00839; 411.
DR MINT; Q00839; -.
DR STRING; 9606.ENSP00000283179; -.
DR ChEMBL; CHEMBL4296007; -.
DR GlyGen; Q00839; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q00839; -.
DR MetOSite; Q00839; -.
DR PhosphoSitePlus; Q00839; -.
DR SwissPalm; Q00839; -.
DR BioMuta; HNRNPU; -.
DR DMDM; 254763463; -.
DR EPD; Q00839; -.
DR jPOST; Q00839; -.
DR MassIVE; Q00839; -.
DR MaxQB; Q00839; -.
DR PaxDb; Q00839; -.
DR PeptideAtlas; Q00839; -.
DR PRIDE; Q00839; -.
DR ProteomicsDB; 57874; -. [Q00839-1]
DR ProteomicsDB; 57875; -. [Q00839-2]
DR Antibodypedia; 3158; 263 antibodies from 32 providers.
DR DNASU; 3192; -.
DR Ensembl; ENST00000444376.7; ENSP00000393151.2; ENSG00000153187.20. [Q00839-2]
DR Ensembl; ENST00000640218.2; ENSP00000491215.1; ENSG00000153187.20. [Q00839-1]
DR GeneID; 3192; -.
DR KEGG; hsa:3192; -.
DR MANE-Select; ENST00000640218.2; ENSP00000491215.1; NM_031844.3; NP_114032.2.
DR UCSC; uc001iaz.2; human. [Q00839-1]
DR CTD; 3192; -.
DR DisGeNET; 3192; -.
DR GeneCards; HNRNPU; -.
DR GeneReviews; HNRNPU; -.
DR HGNC; HGNC:5048; HNRNPU.
DR HPA; ENSG00000153187; Low tissue specificity.
DR MalaCards; HNRNPU; -.
DR MIM; 602869; gene.
DR MIM; 617391; phenotype.
DR neXtProt; NX_Q00839; -.
DR OpenTargets; ENSG00000153187; -.
DR Orphanet; 238769; 1q44 microdeletion syndrome.
DR PharmGKB; PA162391486; -.
DR VEuPathDB; HostDB:ENSG00000153187; -.
DR eggNOG; KOG2242; Eukaryota.
DR GeneTree; ENSGT00940000156546; -.
DR HOGENOM; CLU_012140_1_0_1; -.
DR InParanoid; Q00839; -.
DR OMA; PHQFQQR; -.
DR PhylomeDB; Q00839; -.
DR TreeFam; TF317301; -.
DR PathwayCommons; Q00839; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR SignaLink; Q00839; -.
DR SIGNOR; Q00839; -.
DR BioGRID-ORCS; 3192; 693 hits in 1090 CRISPR screens.
DR ChiTaRS; HNRNPU; human.
DR EvolutionaryTrace; Q00839; -.
DR GeneWiki; HNRPU; -.
DR GenomeRNAi; 3192; -.
DR Pharos; Q00839; Tbio.
DR PRO; PR:Q00839; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q00839; protein.
DR Bgee; ENSG00000153187; Expressed in sperm and 208 other tissues.
DR ExpressionAtlas; Q00839; baseline and differential.
DR Genevisible; Q00839; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; IDA:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:ComplexPortal.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0098577; C:inactive sex chromosome; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:UniProtKB.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:UniProtKB.
DR GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IDA:BHF-UCL.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0106222; F:lncRNA binding; IEA:Ensembl.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
DR GO; GO:0017130; F:poly(C) RNA binding; IDA:UniProtKB.
DR GO; GO:0034046; F:poly(G) binding; IDA:UniProtKB.
DR GO; GO:0036002; F:pre-mRNA binding; IDA:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0017069; F:snRNA binding; IDA:UniProtKB.
DR GO; GO:0070034; F:telomerase RNA binding; IPI:BHF-UCL.
DR GO; GO:0001097; F:TFIIH-class transcription factor complex binding; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR GO; GO:1990845; P:adaptive thermogenesis; ISS:UniProtKB.
DR GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IDA:ComplexPortal.
DR GO; GO:0098963; P:dendritic transport of messenger ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; ISS:UniProtKB.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IMP:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; IDA:UniProtKB.
DR GO; GO:0033673; P:negative regulation of kinase activity; IMP:UniProtKB.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:ComplexPortal.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IMP:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; IMP:UniProtKB.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:UniProtKB.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IDA:ComplexPortal.
DR GO; GO:2000373; P:positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity; ISS:UniProtKB.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:1902889; P:protein localization to spindle microtubule; IMP:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:1902275; P:regulation of chromatin organization; IMP:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:1990280; P:RNA localization to chromatin; ISS:UniProtKB.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR CDD; cd12884; SPRY_hnRNP; 1.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR026745; hnRNP_U.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035778; SPRY_hnRNP_U.
DR PANTHER; PTHR12381:SF11; PTHR12381:SF11; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00513; SAP; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; ADP-ribosylation;
KW Alternative splicing; ATP-binding; Biological rhythms; Cell cycle;
KW Cell division; Centromere; Chromatin regulator; Chromosome; Citrullination;
KW Cytoplasm; Cytoskeleton; Developmental protein; Differentiation;
KW Direct protein sequencing; Disease variant; DNA-binding; Epilepsy;
KW Host-virus interaction; Isopeptide bond; Kinetochore; Methylation; Mitosis;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Ribonucleoprotein;
KW RNA-binding; Spliceosome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7993898, ECO:0000269|Ref.7,
FT ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..825
FT /note="Heterogeneous nuclear ribonucleoprotein U"
FT /id="PRO_0000081872"
FT DOMAIN 8..42
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186,
FT ECO:0000269|PubMed:11003645, ECO:0000269|PubMed:9405365"
FT DOMAIN 267..464
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 41..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..672
FT /note="ATPase domain"
FT /evidence="ECO:0000269|PubMed:28622508"
FT REGION 611..626
FT /note="Actin-binding"
FT /evidence="ECO:0000269|PubMed:15711563"
FT REGION 671..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..739
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000269|PubMed:14608463,
FT ECO:0000269|PubMed:1628625"
FT REGION 769..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..99
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..154
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 504..511
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT SITE 100..101
FT /note="Cleavage; by CASP3"
FT /evidence="ECO:0000269|PubMed:10671544,
FT ECO:0000269|PubMed:9405365"
FT MOD_RES 2
FT /note="N-acetylserine; partial"
FT /evidence="ECO:0000269|Ref.7, ECO:0000269|Ref.8,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 59
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:25986610,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 186
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 187
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000269|PubMed:28190768"
FT MOD_RES 255
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 265
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 266
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 286
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 352
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 516
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 524
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 532
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 551
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 565
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 582
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 635
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 702
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 715
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 720
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 727
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 733
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 733
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VEK3"
FT MOD_RES 739
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 739
FT /note="Dimethylated arginine; in A2780 ovarian carcinoma
FT cell line"
FT /evidence="ECO:0000269|Ref.8"
FT MOD_RES 739
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 755
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 762
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 814
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 265
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 265
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733"
FT CROSSLNK 495
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 516
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 524
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 536
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 565
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 574
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 609
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 626
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 635
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 664
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 670
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 814
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 213..231
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:1628625, ECO:0000303|PubMed:7509195"
FT /id="VSP_005846"
FT VARIANT 171..825
FT /note="Missing (in DEE54)"
FT /evidence="ECO:0000269|PubMed:25356899"
FT /id="VAR_078622"
FT VARIANT 712
FT /note="F -> L (in dbSNP:rs1052660)"
FT /evidence="ECO:0000269|PubMed:1628625, ECO:0000269|Ref.3"
FT /id="VAR_014712"
FT VARIANT 805..825
FT /note="Missing (in DEE54; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23708187"
FT /id="VAR_078623"
FT MUTAGEN 59
FT /note="S->A: No change in interaction with AURKA, PLK1 and
FT TPX2. Increases mitotic chromosome misalignment and
FT chromosome segregation defects and time required to
FT progress through mitosis."
FT /evidence="ECO:0000269|PubMed:17081983"
FT MUTAGEN 59
FT /note="S->E: Increases mitotic chromosome misalignment and
FT chromosome segregation defects and decreases time required
FT to progress through mitosis."
FT /evidence="ECO:0000269|PubMed:17081983"
FT MUTAGEN 100
FT /note="D->A: No cleavage by caspases during apoptosis.
FT Inhibits CASP3-induced cleavage in vitro."
FT /evidence="ECO:0000269|PubMed:10671544"
FT MUTAGEN 616..620
FT /note="RTQKK->ATQAA: Loss of actin-binding."
FT /evidence="ECO:0000269|PubMed:15711563"
FT CONFLICT 603
FT /note="A -> V (in Ref. 5; AAH07950)"
FT /evidence="ECO:0000305"
FT MOD_RES Q00839-2:215
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
SQ SEQUENCE 825 AA; 90584 MW; 5D4EC4188436831F CRC64;
MSSSPVNVKK LKVSELKEEL KKRRLSDKGL KAELMERLQA ALDDEEAGGR PAMEPGNGSL
DLGGDSAGRS GAGLEQEAAA GGDEEEEEEE EEEEGISALD GDQMELGEEN GAAGAADSGP
MEEEEAASED ENGDDQGFQE GEDELGDEEE GAGDENGHGE QQPQPPATQQ QQPQQQRGAA
KEAAGKSSGP TSLFAVTVAP PGARQGQQQA GGKKKAEGGG GGGRPGAPAA GDGKTEQKGG
DKKRGVKRPR EDHGRGYFEY IEENKYSRAK SPQPPVEEED EHFDDTVVCL DTYNCDLHFK
ISRDRLSASS LTMESFAFLW AGGRASYGVS KGKVCFEMKV TEKIPVRHLY TKDIDIHEVR
IGWSLTTSGM LLGEEEFSYG YSLKGIKTCN CETEDYGEKF DENDVITCFA NFESDEVELS
YAKNGQDLGV AFKISKEVLA GRPLFPHVLC HNCAVEFNFG QKEKPYFPIP EEYTFIQNVP
LEDRVRGPKG PEEKKDCEVV MMIGLPGAGK TTWVTKHAAE NPGKYNILGT NTIMDKMMVA
GFKKQMADTG KLNTLLQRAP QCLGKFIEIA ARKKRNFILD QTNVSAAAQR RKMCLFAGFQ
RKAVVVCPKD EDYKQRTQKK AEVEGKDLPE HAVLKMKGNF TLPEVAECFD EITYVELQKE
EAQKLLEQYK EESKKALPPE KKQNTGSKKS NKNKSGKNQF NRGGGHRGRG GFNMRGGNFR
GGAPGNRGGY NRRGNMPQRG GGGGGSGGIG YPYPRAPVFP GRGSYSNRGN YNRGGMPNRG
NYNQNFRGRG NNRGYKNQSQ GYNQWQQGQF WGQKPWSQHY HQGYY
