HNRL1_HUMAN
ID HNRL1_HUMAN Reviewed; 856 AA.
AC Q9BUJ2; B3KMW7; O76022; Q6ZSZ0; Q7L8P4; Q8N6Z4; Q96G37; Q9HAL3; Q9UG75;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein U-like protein 1;
DE AltName: Full=Adenovirus early region 1B-associated protein 5;
DE AltName: Full=E1B-55 kDa-associated protein 5;
DE Short=E1B-AP5;
GN Name=HNRNPUL1; Synonyms=E1BAP5, HNRPUL1;
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 1), FUNCTION IN MRNA PROCESSING,
RP INTERACTION WITH ADENOVIRUS 5 E1B-55 KDA, RNA-BINDING, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=9733834; DOI=10.1128/jvi.72.10.7960-7971.1998;
RA Gabler S., Schuett H., Groitl P., Wolf H., Shenk T., Dobner T.;
RT "E1B-55kilodalton-associated protein: a cellular protein with RNA-binding
RT activity implicated in nucleocytoplasmic transport of adenovirus and
RT cellular mRNAs.";
RL J. Virol. 72:7960-7971(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 5).
RC TISSUE=Brain, and Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), AND VARIANT
RP CYS-91.
RC TISSUE=Brain, Eye, Muscle, and Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 355-856.
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP INTERACTION WITH NXF1.
RX PubMed=10668806; DOI=10.1017/s1355838200991994;
RA Bachi A., Braun I.C., Rodrigues J.P., Pante N., Ribbeck K., von Kobbe C.,
RA Kutay U., Wilm M., Goerlich D., Carmo-Fonseca M., Izaurralde E.;
RT "The C-terminal domain of TAP interacts with the nuclear pore complex and
RT promotes export of specific CTE-bearing RNA substrates.";
RL RNA 6:136-158(2000).
RN [8]
RP METHYLATION, INTERACTION WITH PRMT2, AND SUBCELLULAR LOCATION.
RX PubMed=11513728; DOI=10.1042/0264-6021:3580305;
RA Kzhyshkowska J., Schuett H., Liss M., Kremmer E., Stauber R., Wolf H.,
RA Dobner T.;
RT "Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-
RT Gly-Gly (RGG) box and interacts with human arginine methyltransferase
RT HRMT1L1.";
RL Biochem. J. 358:305-314(2001).
RN [9]
RP FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH BRD7, ASSOCIATION
RP WITH HISTONES AND BRD7, AND SUBCELLULAR LOCATION.
RX PubMed=12489984; DOI=10.1042/bj20021281;
RA Kzhyshkowska J.G., Rusch A., Wolf H., Dobner T.;
RT "Regulation of transcription by the heterogeneous nuclear ribonucleoprotein
RT E1B-AP5 is mediated by complex formation with the novel bromodomain-
RT containing protein BRD7.";
RL Biochem. J. 371:385-393(2003).
RN [10]
RP METHYLATION DURING ADENOVIRAL INFECTION.
RX PubMed=15242333; DOI=10.1042/bj20040210;
RA Kzhyshkowska J., Kremmer E., Hofmann M., Wolf H., Dobner T.;
RT "Protein arginine methylation during lytic adenovirus infection.";
RL Biochem. J. 383:259-265(2004).
RN [11]
RP INTERACTION WITH TP53.
RX PubMed=15907477; DOI=10.1016/j.febslet.2005.03.095;
RA Barral P.M., Rusch A., Turnell A.S., Gallimore P.H., Byrd P.J., Dobner T.,
RA Grand R.J.;
RT "The interaction of the hnRNP family member E1B-AP5 with p53.";
RL FEBS Lett. 579:2752-2758(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-718, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-512, 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP 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 [25]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-639; ARG-645; ARG-656 AND
RP ARG-671, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-117 AND LYS-142, 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 [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-117 AND LYS-142, AND
RP IDENTIFICATION BY MASS 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 [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-117 AND LYS-142, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [30]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-117; LYS-142; LYS-146; LYS-162;
RP LYS-270; LYS-449 AND LYS-539, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Acts as a basic transcriptional regulator. Represses basic
CC transcription driven by several virus and cellular promoters. When
CC associated with BRD7, activates transcription of glucocorticoid-
CC responsive promoter in the absence of ligand-stimulation. Also plays a
CC role in mRNA processing and transport. Binds avidly to poly(G) and
CC poly(C) RNA homopolymers in vitro. {ECO:0000269|PubMed:12489984,
CC ECO:0000269|PubMed:9733834}.
CC -!- SUBUNIT: Interacts with the adenovirus type 5 (Ad5) E1B-55 kDa, BRD7,
CC PRMT2, TP53 and NXF1. Associates with histones and BRD7.
CC {ECO:0000269|PubMed:10668806, ECO:0000269|PubMed:11513728,
CC ECO:0000269|PubMed:12489984, ECO:0000269|PubMed:15907477,
CC ECO:0000269|PubMed:9733834}.
CC -!- INTERACTION:
CC Q9BUJ2; Q9NPI1: BRD7; NbExp=5; IntAct=EBI-1018153, EBI-711221;
CC Q9BUJ2; Q86Y13: DZIP3; NbExp=7; IntAct=EBI-1018153, EBI-948630;
CC Q9BUJ2; P52597: HNRNPF; NbExp=5; IntAct=EBI-1018153, EBI-352986;
CC Q9BUJ2; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-1018153, EBI-9478422;
CC Q9BUJ2; Q8NDC0: MAPK1IP1L; NbExp=5; IntAct=EBI-1018153, EBI-741424;
CC Q9BUJ2; O75928-2: PIAS2; NbExp=3; IntAct=EBI-1018153, EBI-348567;
CC Q9BUJ2; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-1018153, EBI-1105153;
CC Q9BUJ2; Q9BQ04: RBM4B; NbExp=3; IntAct=EBI-1018153, EBI-715531;
CC Q9BUJ2; Q15427: SF3B4; NbExp=4; IntAct=EBI-1018153, EBI-348469;
CC Q9BUJ2; Q16637: SMN2; NbExp=4; IntAct=EBI-1018153, EBI-395421;
CC Q9BUJ2; O60504: SORBS3; NbExp=3; IntAct=EBI-1018153, EBI-741237;
CC Q9BUJ2; Q13148: TARDBP; NbExp=3; IntAct=EBI-1018153, EBI-372899;
CC Q9BUJ2; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-1018153, EBI-10175039;
CC Q9BUJ2; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-1018153, EBI-2559305;
CC Q9BUJ2; O00308: WWP2; NbExp=9; IntAct=EBI-1018153, EBI-743923;
CC Q9BUJ2; Q82506: NS; Xeno; NbExp=3; IntAct=EBI-1018153, EBI-6149498;
CC Q9BUJ2-2; Q13148: TARDBP; NbExp=3; IntAct=EBI-11018029, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11513728,
CC ECO:0000269|PubMed:12489984, ECO:0000269|PubMed:9733834}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Isoform a;
CC IsoId=Q9BUJ2-1; Sequence=Displayed;
CC Name=2; Synonyms=Isoform b;
CC IsoId=Q9BUJ2-2; Sequence=VSP_017552;
CC Name=3;
CC IsoId=Q9BUJ2-3; Sequence=VSP_017548, VSP_017549, VSP_017551;
CC Name=4;
CC IsoId=Q9BUJ2-4; Sequence=VSP_017547;
CC Name=5;
CC IsoId=Q9BUJ2-5; Sequence=VSP_017546, VSP_017550, VSP_017551;
CC -!- DOMAIN: The RGG-box domain is methylated.
CC -!- PTM: Methylated. {ECO:0000269|PubMed:11513728,
CC ECO:0000269|PubMed:15242333}.
CC -!- MISCELLANEOUS: Its methylation is enhanced in the late phase of
CC adenoviral infection.
CC -!- MISCELLANEOUS: [Isoform 5]: May be due to intron retention.
CC {ECO:0000305}.
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DR EMBL; AJ007509; CAA07548.1; -; mRNA.
DR EMBL; AK021455; BAB13831.1; -; mRNA.
DR EMBL; AK022863; BAG51129.1; -; mRNA.
DR EMBL; AK127057; BAC86806.1; -; mRNA.
DR EMBL; AC011462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471126; EAW57025.1; -; Genomic_DNA.
DR EMBL; BC002564; AAH02564.1; -; mRNA.
DR EMBL; BC009988; AAH09988.2; -; mRNA.
DR EMBL; BC014232; AAH14232.1; -; mRNA.
DR EMBL; BC027713; AAH27713.1; -; mRNA.
DR EMBL; AL050146; CAB43291.1; -; mRNA.
DR CCDS; CCDS12576.1; -. [Q9BUJ2-1]
DR CCDS; CCDS12577.1; -. [Q9BUJ2-4]
DR PIR; T08776; T08776.
DR PIR; T13159; T13159.
DR RefSeq; NP_001308137.1; NM_001321208.1. [Q9BUJ2-4]
DR RefSeq; NP_001308140.1; NM_001321211.1. [Q9BUJ2-4]
DR RefSeq; NP_008971.2; NM_007040.5. [Q9BUJ2-1]
DR RefSeq; NP_653333.1; NM_144732.4. [Q9BUJ2-4]
DR AlphaFoldDB; Q9BUJ2; -.
DR SMR; Q9BUJ2; -.
DR BioGRID; 116281; 274.
DR CORUM; Q9BUJ2; -.
DR DIP; DIP-39419N; -.
DR IntAct; Q9BUJ2; 121.
DR MINT; Q9BUJ2; -.
DR STRING; 9606.ENSP00000375863; -.
DR GlyGen; Q9BUJ2; 12 sites, 2 O-linked glycans (12 sites).
DR iPTMnet; Q9BUJ2; -.
DR PhosphoSitePlus; Q9BUJ2; -.
DR SwissPalm; Q9BUJ2; -.
DR BioMuta; HNRNPUL1; -.
DR DMDM; 90101344; -.
DR EPD; Q9BUJ2; -.
DR jPOST; Q9BUJ2; -.
DR MassIVE; Q9BUJ2; -.
DR MaxQB; Q9BUJ2; -.
DR PaxDb; Q9BUJ2; -.
DR PeptideAtlas; Q9BUJ2; -.
DR PRIDE; Q9BUJ2; -.
DR ProteomicsDB; 79090; -. [Q9BUJ2-1]
DR ProteomicsDB; 79091; -. [Q9BUJ2-2]
DR ProteomicsDB; 79092; -. [Q9BUJ2-3]
DR ProteomicsDB; 79093; -. [Q9BUJ2-4]
DR ProteomicsDB; 79094; -. [Q9BUJ2-5]
DR TopDownProteomics; Q9BUJ2-2; -. [Q9BUJ2-2]
DR Antibodypedia; 17170; 184 antibodies from 27 providers.
DR DNASU; 11100; -.
DR Ensembl; ENST00000378215.8; ENSP00000367460.3; ENSG00000105323.18. [Q9BUJ2-3]
DR Ensembl; ENST00000392006.8; ENSP00000375863.2; ENSG00000105323.18. [Q9BUJ2-1]
DR Ensembl; ENST00000593587.5; ENSP00000472629.1; ENSG00000105323.18. [Q9BUJ2-4]
DR Ensembl; ENST00000595018.5; ENSP00000473132.1; ENSG00000105323.18. [Q9BUJ2-4]
DR Ensembl; ENST00000602130.5; ENSP00000470687.1; ENSG00000105323.18. [Q9BUJ2-2]
DR GeneID; 11100; -.
DR KEGG; hsa:11100; -.
DR MANE-Select; ENST00000392006.8; ENSP00000375863.2; NM_007040.6; NP_008971.2.
DR UCSC; uc002opz.5; human. [Q9BUJ2-1]
DR CTD; 11100; -.
DR DisGeNET; 11100; -.
DR GeneCards; HNRNPUL1; -.
DR HGNC; HGNC:17011; HNRNPUL1.
DR HPA; ENSG00000105323; Low tissue specificity.
DR MIM; 605800; gene.
DR neXtProt; NX_Q9BUJ2; -.
DR OpenTargets; ENSG00000105323; -.
DR PharmGKB; PA162391519; -.
DR VEuPathDB; HostDB:ENSG00000105323; -.
DR eggNOG; KOG2242; Eukaryota.
DR GeneTree; ENSGT00940000157823; -.
DR HOGENOM; CLU_012140_0_1_1; -.
DR InParanoid; Q9BUJ2; -.
DR OMA; TGVWQTQ; -.
DR OrthoDB; 778148at2759; -.
DR PhylomeDB; Q9BUJ2; -.
DR TreeFam; TF317301; -.
DR PathwayCommons; Q9BUJ2; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q9BUJ2; -.
DR BioGRID-ORCS; 11100; 18 hits in 1085 CRISPR screens.
DR ChiTaRS; HNRNPUL1; human.
DR GeneWiki; HNRPUL1; -.
DR GenomeRNAi; 11100; -.
DR Pharos; Q9BUJ2; Tbio.
DR PRO; PR:Q9BUJ2; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BUJ2; protein.
DR Bgee; ENSG00000105323; Expressed in ventricular zone and 205 other tissues.
DR ExpressionAtlas; Q9BUJ2; baseline and differential.
DR Genevisible; Q9BUJ2; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; TAS:ProtInc.
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; IPR027025; hnRNP_U-like_1.
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:SF41; PTHR12381:SF41; 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 Activator; Alternative splicing; Isopeptide bond; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Ribonucleoprotein;
KW RNA-binding; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..856
FT /note="Heterogeneous nuclear ribonucleoprotein U-like
FT protein 1"
FT /id="PRO_0000227555"
FT DOMAIN 3..37
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 191..388
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REPEAT 612..614
FT /note="1-1"
FT REPEAT 620..622
FT /note="1-2"
FT REPEAT 639..641
FT /note="1-3"
FT REPEAT 645..647
FT /note="1-4"
FT REPEAT 656..658
FT /note="1-5"
FT REGION 1..103
FT /note="Necessary for interaction with HRMT1L1"
FT REGION 35..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..856
FT /note="Necessary for interaction with TP53"
FT /evidence="ECO:0000269|PubMed:15907477"
FT REGION 456..594
FT /note="Necessary for interaction with BRD7 and
FT transcriptional activation"
FT /evidence="ECO:0000269|PubMed:12489984"
FT REGION 595..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..658
FT /note="5 X 3 AA repeats of R-G-G"
FT REGION 612..658
FT /note="Necessary for transcription repression"
FT COMPBIAS 51..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..721
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..785
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..808
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 209
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDM6"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 639
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 645
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 645
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VDM6"
FT MOD_RES 656
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 656
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8VDM6"
FT MOD_RES 661
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDM6"
FT MOD_RES 671
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 117
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:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 162
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 270
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 449
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 539
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..460
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017546"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017547"
FT VAR_SEQ 35..77
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017548"
FT VAR_SEQ 263..333
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017549"
FT VAR_SEQ 461..562
FT /note="KMRVMGLRRQRNYAGRWDVLIQQATQCLNRLIQIAARKKRNYILDQTNVYGS
FT AQRRKMRPFEGFQRKAIVICPTDEDLKDRTIKRTDEEGKDVPDHAVLEMK -> MGFCH
FT VGQAGLELLTSGDPPASASQSAGITGVSHRARPSVFVFLIHYSSFLHLLPSGRPLFWVE
FT GTRLQKVLTSSSCSLWGTSFLL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017550"
FT VAR_SEQ 754
FT /note="Q -> QSFGFFPSTFQ (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017551"
FT VAR_SEQ 755..806
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017552"
FT VARIANT 91
FT /note="G -> C (in dbSNP:rs17849624)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025606"
FT CONFLICT 27
FT /note="A -> T (in Ref. 1; CAA07548)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="N -> S (in Ref. 2; BAC86806)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="G -> A (in Ref. 1; CAA07548)"
FT /evidence="ECO:0000305"
FT CONFLICT 625
FT /note="G -> A (in Ref. 1; CAA07548)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="S -> N (in Ref. 1; CAA07548)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="A -> S (in Ref. 2; BAC86806)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="A -> G (in Ref. 1; CAA07548)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 856 AA; 95739 MW; 6E57C0271E5F3A77 CRC64;
MDVRRLKVNE LREELQRRGL DTRGLKAELA ERLQAALEAE EPDDERELDA DDEPGRPGHI
NEEVETEGGS ELEGTAQPPP PGLQPHAEPG GYSGPDGHYA MDNITRQNQF YDTQVIKQEN
ESGYERRPLE MEQQQAYRPE MKTEMKQGAP TSFLPPEASQ LKPDRQQFQS RKRPYEENRG
RGYFEHREDR RGRSPQPPAE EDEDDFDDTL VAIDTYNCDL HFKVARDRSS GYPLTIEGFA
YLWSGARASY GVRRGRVCFE MKINEEISVK HLPSTEPDPH VVRIGWSLDS CSTQLGEEPF
SYGYGGTGKK STNSRFENYG DKFAENDVIG CFADFECGND VELSFTKNGK WMGIAFRIQK
EALGGQALYP HVLVKNCAVE FNFGQRAEPY CSVLPGFTFI QHLPLSERIR GTVGPKSKAE
CEILMMVGLP AAGKTTWAIK HAASNPSKKY NILGTNAIMD KMRVMGLRRQ RNYAGRWDVL
IQQATQCLNR LIQIAARKKR NYILDQTNVY GSAQRRKMRP FEGFQRKAIV ICPTDEDLKD
RTIKRTDEEG KDVPDHAVLE MKANFTLPDV GDFLDEVLFI ELQREEADKL VRQYNEEGRK
AGPPPEKRFD NRGGGGFRGR GGGGGFQRYE NRGPPGGNRG GFQNRGGGSG GGGNYRGGFN
RSGGGGYSQN RWGNNNRDNN NSNNRGSYNR APQQQPPPQQ PPPPQPPPQQ PPPPPSYSPA
RNPPGASTYN KNSNIPGSSA NTSTPTVSSY SPPQPSYSQP PYNQGGYSQG YTAPPPPPPP
PPAYNYGSYG GYNPAPYTPP PPPTAQTYPQ PSYNQYQQYA QQWNQYYQNQ GQWPPYYGNY
DYGSYSGNTQ GGTSTQ
