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 09-DEC-2015, entry version 179. DE RecName: Full=Heterogeneous nuclear ribonucleoprotein U; DE Short=hnRNP U; DE AltName: Full=Scaffold attachment factor A; DE Short=SAF-A; DE AltName: Full=p120; DE AltName: Full=pp120; GN Name=HNRNPU; Synonyms=HNRPU, SAFA, U21.1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), RNA-BINDING DOMAIN, AND RP VARIANT LEU-712. RX PubMed=1628625; RA Kiledjian M., Dreyfuss G.; RT "Primary structure and binding activity of the hnRNP U protein: RT binding RNA through RGG box."; RL EMBO J. 11:2655-2664(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT). 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 RT in human cells."; RL Biochim. Biophys. Acta 1217:232-234(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT LEU-712. RA Fackelmayer F.O.; RT "A variant of human scaffold attachment factor A (SAF-A), also known RT as 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., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA 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., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA 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., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA 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 SHORT). 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 RT project: 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, AND RP SUBCELLULAR LOCATION. 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 RT kinase 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; RP 353-360; 424-433; 463-484; 495-510; 525-543; 552-558; 566-572; RP 576-590; 592-601; 627-635; 665-674 AND 734-755, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT SER-2, METHYLATION AT ARG-739, AND RP 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 CHARACTERIZATION. 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 [10] 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) RT for its three intracellular ligands, the p53 anti-oncoprotein, the p68 RT calcium binding protein and the nuclear p120 ribonucleoprotein."; RL Mol. Immunol. 32:389-397(1995). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE RP SPLICEOSOMAL 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 [12] 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 RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-271, AND RP 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, AND IDENTIFICATION RP 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 RT cancer cells: identification of phosphoproteins in the LNCaP cell RT line."; RL Electrophoresis 28:2027-2034(2007). RN [15] 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 [16] 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., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, AND IDENTIFICATION RP 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 [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [19] RP FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX, RP IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=19029303; DOI=10.1261/rna.1175909; RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., RA Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.; RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RT RNPs."; RL RNA 15:104-115(2009). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-66 AND SER-271, RP AND 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 [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265; LYS-352; LYS-516; RP LYS-524; LYS-551; LYS-565; LYS-635 AND LYS-814, ACETYLATION [LARGE RP SCALE ANALYSIS] AT LYS-215 (ISOFORM SHORT), 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., RA Walther T.C., 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 [22] RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, AND RP SUBCELLULAR LOCATION. 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 RT damage response pathways."; RL Mol. Cancer Res. 8:1388-1398(2010). RN [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-4; SER-59; SER-66 AND SER-271, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [24] 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., RA Buerckstuemmer T., 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 [25] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-4; SER-59 AND SER-66, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], 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., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [26] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., 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 [27] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [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., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [28] 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- RT binding proteins) is modulated by distinct RNA-binding domains."; RL Biol. Chem. 394:1077-1090(2013). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-271 AND THR-286, RP AND 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [30] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-265; LYS-609 AND LYS-670, RP AND 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 [31] 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 RT protein 5 isoform C."; RL Submitted (JAN-2008) to the PDB data bank. RN [32] 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 RT between ubiquilin-2 and hnRNPA1."; RL Hum. Mol. Genet. 24:2565-2577(2015). CC -!- FUNCTION: Component of the CRD-mediated complex that promotes MYC CC mRNA stabilization. Binds to pre-mRNA. Has high affinity for CC scaffold-attached region (SAR) DNA. Binds to double- and single- CC stranded DNA and RNA. Plays a role in the circadian regulation of CC the core clock component ARNTL/BMAL1 transcription (By CC similarity). {ECO:0000250|UniProtKB:Q8VEK3, CC ECO:0000269|PubMed:19029303}. CC -!- SUBUNIT: Identified in the spliceosome C complex. Component of the CC coding region determinant (CRD)-mediated complex, composed of CC DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in a IGF2BP1- CC dependent mRNP granule complex containing untranslated mRNAs. CC Interacts with IGF2BP1, IGF2BP2, IGF2BP3 and ERBB4. Ligand for CC CR2. Interacts with CRY1 (By similarity). Interacts with UBQLN2 CC (PubMed:25616961). {ECO:0000250|UniProtKB:Q8VEK3, CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:17289661, CC ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:20858735, CC ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:25616961, CC ECO:0000269|PubMed:7753047}. CC -!- INTERACTION: CC P42771:CDKN2A; NbExp=2; IntAct=EBI-351126, EBI-375053; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20858735}. CC Cytoplasm {ECO:0000269|PubMed:19029303}. Cell surface CC {ECO:0000269|PubMed:7993898}. Note=Localized in cytoplasmic mRNP CC granules containing untranslated mRNAs. Component of CC ribonucleosomes. {ECO:0000269|PubMed:17289661}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q00839-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q00839-2; Sequence=VSP_005846; CC Note=Contains a N6-acetyllysine at position 215. CC {ECO:0000244|PubMed:19608861}; CC -!- PTM: Extensively phosphorylated. {ECO:0000269|PubMed:7993898}. CC -!- PTM: Arg-739 is dimethylated, probably to asymmetric CC dimethylarginine. {ECO:0000269|Ref.8}. CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q8VEK3}. CC -!- SIMILARITY: Contains 1 B30.2/SPRY domain. {ECO:0000255|PROSITE- CC ProRule:PRU00548}. CC -!- SIMILARITY: Contains 1 SAP domain. {ECO:0000255|PROSITE- CC ProRule:PRU00186}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC19382.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={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; X65488; CAA46472.1; -; mRNA. DR EMBL; AF068846; AAC19382.1; ALT_SEQ; mRNA. DR EMBL; BX323046; CAI11058.1; -; 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 UniGene; Hs.106212; -. DR PDB; 1ZRJ; NMR; -; A=23-42. DR PDBsum; 1ZRJ; -. DR ProteinModelPortal; Q00839; -. DR SMR; Q00839; 3-48, 298-470. DR BioGrid; 109433; 315. DR DIP; DIP-684N; -. DR IntAct; Q00839; 299. DR MINT; MINT-1654412; -. DR STRING; 9606.ENSP00000283179; -. DR PhosphoSite; Q00839; -. DR BioMuta; HNRNPU; -. DR DMDM; 254763463; -. DR MaxQB; Q00839; -. DR PaxDb; Q00839; -. DR PRIDE; Q00839; -. DR DNASU; 3192; -. DR Ensembl; ENST00000283179; ENSP00000283179; ENSG00000153187. [Q00839-1] DR Ensembl; ENST00000444376; ENSP00000393151; ENSG00000153187. [Q00839-2] DR GeneID; 3192; -. DR KEGG; hsa:3192; -. DR UCSC; uc001iaz.1; human. [Q00839-1] DR UCSC; uc001iba.1; human. [Q00839-2] DR CTD; 3192; -. DR GeneCards; HNRNPU; -. DR HGNC; HGNC:5048; HNRNPU. DR HPA; CAB011532; -. DR HPA; HPA058707; -. DR MIM; 602869; gene. DR neXtProt; NX_Q00839; -. DR PharmGKB; PA162391486; -. DR eggNOG; ENOG410IR1W; Eukaryota. DR eggNOG; ENOG410Y1WQ; LUCA. DR GeneTree; ENSGT00390000020210; -. DR HOGENOM; HOG000253920; -. DR HOVERGEN; HBG061101; -. DR InParanoid; Q00839; -. DR KO; K12888; -. DR OMA; FKRQMAD; -. DR OrthoDB; EOG79CZ07; -. DR PhylomeDB; Q00839; -. DR TreeFam; TF317301; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA. DR ChiTaRS; HNRNPU; human. DR EvolutionaryTrace; Q00839; -. DR GeneWiki; HNRPU; -. DR GenomeRNAi; 3192; -. DR NextBio; 12700; -. DR PRO; PR:Q00839; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; Q00839; -. DR CleanEx; HS_HNRNPU; -. 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; IEA:UniProtKB-SubCell. 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:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0001047; F:core promoter binding; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; TAS:ProtInc. DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB. DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IMP:UniProtKB. DR GO; GO:0010467; P:gene expression; TAS:Reactome. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB. DR GO; GO:0001649; P:osteoblast differentiation; IDA:UniProtKB. DR GO; GO:0006396; P:RNA processing; TAS:ProtInc. DR GO; GO:0008380; P:RNA splicing; TAS:Reactome. DR Gene3D; 1.10.720.30; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR001870; B30.2/SPRY. DR InterPro; IPR013320; ConA-like_dom. DR InterPro; IPR026745; hnRNP_U. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003034; SAP_dom. DR InterPro; IPR003877; SPRY_dom. DR PANTHER; PTHR12381:SF11; PTHR12381:SF11; 3. 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 PROSITE; PS50188; B302_SPRY; 1. DR PROSITE; PS50800; SAP; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Biological rhythms; Citrullination; Complete proteome; Cytoplasm; KW Direct protein sequencing; DNA-binding; Isopeptide bond; Methylation; KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus; KW Phosphoprotein; Polymorphism; Reference proteome; Ribonucleoprotein; KW RNA-binding; Spliceosome; Ubl conjugation. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:22223895, FT ECO:0000244|PubMed:22814378, FT ECO:0000269|PubMed:7993898, FT ECO:0000269|Ref.7, ECO:0000269|Ref.8}. FT CHAIN 2 825 Heterogeneous nuclear ribonucleoprotein FT U. FT /FTId=PRO_0000081872. FT DOMAIN 8 42 SAP. {ECO:0000255|PROSITE- FT ProRule:PRU00186}. FT DOMAIN 267 464 B30.2/SPRY. {ECO:0000255|PROSITE- FT ProRule:PRU00548}. FT NP_BIND 504 511 ATP. {ECO:0000255}. FT REGION 714 739 RNA-binding RGG-box. FT {ECO:0000269|PubMed:1628625}. FT COMPBIAS 2 160 Asp/Glu-rich (acidic). FT COMPBIAS 84 94 Poly-Glu. FT COMPBIAS 161 209 Gln-rich. FT COMPBIAS 703 825 Gly-rich. FT COMPBIAS 740 750 Poly-Gly. FT MOD_RES 2 2 N-acetylserine; partial. FT {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:22223895, FT ECO:0000244|PubMed:22814378, FT ECO:0000269|Ref.7, ECO:0000269|Ref.8}. FT MOD_RES 4 4 Phosphoserine. FT {ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 59 59 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18220336, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 66 66 Phosphoserine. FT {ECO:0000244|PubMed:18220336, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 255 255 Citrulline. FT {ECO:0000250|UniProtKB:Q8VEK3}. FT MOD_RES 265 265 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 271 271 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:17487921, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 286 286 Phosphothreonine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 352 352 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 516 516 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 524 524 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 551 551 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 565 565 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 635 635 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 739 739 Dimethylated arginine; in A2780 ovarian FT carcinoma cell line. {ECO:0000269|Ref.8}. FT MOD_RES 814 814 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT CROSSLNK 265 265 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2); FT alternate. {ECO:0000244|PubMed:25218447}. FT CROSSLNK 609 609 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 670 670 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT VAR_SEQ 213 231 Missing (in isoform Short). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:1628625, FT ECO:0000303|PubMed:7509195}. FT /FTId=VSP_005846. FT VARIANT 712 712 F -> L (in dbSNP:rs1052660). FT {ECO:0000269|PubMed:1628625, FT ECO:0000269|Ref.3}. FT /FTId=VAR_014712. FT CONFLICT 603 603 A -> V (in Ref. 5; AAH07950). FT {ECO:0000305}. FT TURN 24 25 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 //