HNRDL_HUMAN
ID HNRDL_HUMAN Reviewed; 420 AA.
AC O14979; Q6SPF2; Q7KZ74; Q7KZ75; Q96IM0; Q96S43;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein D-like;
DE Short=hnRNP D-like;
DE Short=hnRNP DL;
DE AltName: Full=AU-rich element RNA-binding factor;
DE AltName: Full=JKT41-binding protein;
DE AltName: Full=Protein laAUF1;
GN Name=HNRNPDL; Synonyms=HNRPDL, JKTBP;
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] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, RNA-BINDING, AND DNA-BINDING.
RC TISSUE=Erythroleukemia, and Placenta;
RX PubMed=9538234; DOI=10.1093/oxfordjournals.jbchem.a021964;
RA Tsuchiya N., Kamei D., Takano A., Matsui T., Yamada M.;
RT "Cloning and characterization of a cDNA encoding a novel heterogeneous
RT nuclear ribonucleoprotein-like protein and its expression in myeloid
RT leukemia cells.";
RL J. Biochem. 123:499-507(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INDUCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=10072754; DOI=10.1016/s0378-1119(99)00020-7;
RA Kamei D., Tsuchiya N., Yamazaki M., Meguro H., Yamada M.;
RT "Two forms of expression and genomic structure of the human heterogeneous
RT nuclear ribonucleoprotein D-like JKTBP gene (HNRPDL).";
RL Gene 228:13-22(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, AND
RP RNA-BINDING.
RX PubMed=11705999; DOI=10.1074/jbc.m108477200;
RA Kawamura H., Tomozoe Y., Akagi T., Kamei D., Ochiai M., Yamada M.;
RT "Identification of the nucleocytoplasmic shuttling sequence of
RT heterogeneous nuclear ribonucleoprotein D-like protein JKTBP and its
RT interaction with mRNA.";
RL J. Biol. Chem. 277:2732-2739(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, Ovary, 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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 123-420.
RC TISSUE=Brain;
RX PubMed=15190078; DOI=10.1074/jbc.m403160200;
RA Boopathi E., Lenka N., Prabu S.K., Fang J.-K., Wilkinson F., Atchison M.,
RA Giallongo A., Avadhani N.G.;
RT "Regulation of murine cytochrome c oxidase Vb gene expression during
RT myogenesis: YY-1 and heterogeneous nuclear ribonucleoprotein D-like protein
RT (JKTBP1) reciprocally regulate transcription activity by physical
RT interaction with the BERF-1/ZBP-89 factor.";
RL J. Biol. Chem. 279:35242-35254(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 131-420, INTERACTION WITH TNPO1, MUTAGENESIS
RP OF GLY-404, INDUCTION, AND RNA-BINDING.
RX PubMed=9524220; DOI=10.1016/s0167-4781(97)00223-6;
RA Doi A., Shiosaka T., Takaoka Y., Yanagisawa K., Fujita S.;
RT "Molecular cloning of the cDNA encoding A + U-rich element RNA binding
RT factor.";
RL Biochim. Biophys. Acta 1396:51-56(1998).
RN [9]
RP PROTEIN SEQUENCE OF 150-180; 190-209; 234-269; 275-289 AND 406-420,
RP METHYLATION AT LYS-161 AND ARG-408, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Colon carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A.,
RA Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 235-269 AND 275-289.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP SUBCELLULAR LOCATION, AND RNA-BINDING.
RX PubMed=12406575; DOI=10.1016/s0378-1119(02)00926-5;
RA Kamei D., Yamada M.;
RT "Interactions of heterogeneous nuclear ribonucleoprotein D-like protein
RT JKTBP and its domains with high-affinity binding sites.";
RL Gene 298:49-57(2002).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, 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].
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION BY
RP 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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-216, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, 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 [20]
RP INVOLVEMENT IN LGMDD3, AND VARIANTS LGMDD3 ASN-378 AND HIS-378.
RX PubMed=24647604; DOI=10.1093/hmg/ddu127;
RA Vieira N.M., Naslavsky M.S., Licinio L., Kok F., Schlesinger D.,
RA Vainzof M., Sanchez N., Kitajima J.P., Gal L., Cavacana N., Serafini P.R.,
RA Chuartzman S., Vasquez C., Mimbacas A., Nigro V., Pavanello R.C.,
RA Schuldiner M., Kunkel L.M., Zatz M.;
RT "A defect in the RNA-processing protein HNRPDL causes limb-girdle muscular
RT dystrophy 1G (LGMD1G).";
RL Hum. Mol. Genet. 23:4103-4110(2014).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, 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 [22]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-25, AND IDENTIFICATION BY MASS
RP 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 [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-209, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Acts as a transcriptional regulator. Promotes transcription
CC repression. Promotes transcription activation in differentiated
CC myotubes (By similarity). Binds to double- and single-stranded DNA
CC sequences. Binds to the transcription suppressor CATR sequence of the
CC COX5B promoter (By similarity). Binds with high affinity to RNA
CC molecules that contain AU-rich elements (AREs) found within the 3'-UTR
CC of many proto-oncogenes and cytokine mRNAs. Binds both to nuclear and
CC cytoplasmic poly(A) mRNAs. Binds to poly(G) and poly(A), but not to
CC poly(U) or poly(C) RNA homopolymers. Binds to the 5'-ACUAGC-3' RNA
CC consensus sequence. {ECO:0000250, ECO:0000269|PubMed:9538234}.
CC -!- SUBUNIT: Interacts with ZNF148 (By similarity). Interacts with TNPO1.
CC {ECO:0000250, ECO:0000269|PubMed:9524220}.
CC -!- INTERACTION:
CC O14979; Q15637: SF1; NbExp=4; IntAct=EBI-299727, EBI-744603;
CC O14979; P09234: SNRPC; NbExp=3; IntAct=EBI-299727, EBI-766589;
CC O14979; Q13148: TARDBP; NbExp=3; IntAct=EBI-299727, EBI-372899;
CC O14979; O76024: WFS1; NbExp=3; IntAct=EBI-299727, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11705999,
CC ECO:0000269|PubMed:12406575}. Cytoplasm {ECO:0000269|PubMed:11705999,
CC ECO:0000269|PubMed:12406575}. Note=Shuttles between the nucleus and the
CC cytoplasm in a TNPO1-dependent manner. {ECO:0000269|PubMed:11705999,
CC ECO:0000269|PubMed:12406575}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=JKTBP2 {ECO:0000303|PubMed:10072754};
CC IsoId=O14979-1; Sequence=Displayed;
CC Name=2; Synonyms=JKTBP1 {ECO:0000303|PubMed:10072754};
CC IsoId=O14979-2; Sequence=VSP_025410;
CC Name=3;
CC IsoId=O14979-3; Sequence=VSP_025410, VSP_025411;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver,
CC skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis,
CC ovary, small intestine, colon and leukocytes. Expressed in myeloid
CC leukemia, gastric adenocarcinoma, cervical carcinoma, hepatoma,
CC fibrosarcoma, colon adenocarcinoma, epidermoid carcinoma, osteosarcoma
CC and urinary bladder carcinoma cells. {ECO:0000269|PubMed:10072754,
CC ECO:0000269|PubMed:9538234}.
CC -!- INDUCTION: Up-regulated by 12-O-tetradecanoylphorbol-13-acetate (TPA)
CC in macrophages and retinoic acid (RA) in granulocytes (at protein
CC level). Down-regulated by IL4/interleukin-4.
CC {ECO:0000269|PubMed:10072754, ECO:0000269|PubMed:9524220}.
CC -!- PTM: Dimethylation of Arg-408 is probably of the asymmetric type.
CC -!- DISEASE: Muscular dystrophy, limb-girdle, autosomal dominant 3 (LGMDD3)
CC [MIM:609115]: An autosomal dominant degenerative myopathy characterized
CC by slowly progressive wasting and weakness of the proximal muscles of
CC arms and legs around the pelvic or shoulder girdles, elevated creatine
CC kinase levels and dystrophic features on muscle biopsy. LGMDD3 is
CC characterized by a mild late-onset and is associated with progressive
CC fingers and toes flexion limitation. Affected individuals may also
CC develop cataracts before age 50. {ECO:0000269|PubMed:24647604}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA22860.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB017019; BAA75241.1; -; mRNA.
DR EMBL; D89092; BAA24361.1; -; mRNA.
DR EMBL; AB066484; BAB62188.1; -; mRNA.
DR EMBL; CR407623; CAG28551.1; -; mRNA.
DR EMBL; AC124016; AAY40914.1; -; Genomic_DNA.
DR EMBL; AB017018; BAA75239.1; -; Genomic_DNA.
DR EMBL; AB017018; BAA75240.1; -; Genomic_DNA.
DR EMBL; BC007392; AAH07392.2; -; mRNA.
DR EMBL; BC011714; AAH11714.1; -; mRNA.
DR EMBL; BC071944; AAH71944.1; -; mRNA.
DR EMBL; AY453824; AAR17782.1; -; mRNA.
DR EMBL; D89678; BAA22860.1; ALT_INIT; mRNA.
DR CCDS; CCDS3593.1; -. [O14979-1]
DR PIR; JW0079; JW0079.
DR RefSeq; NP_001193929.1; NM_001207000.1.
DR RefSeq; NP_112740.1; NM_031372.3. [O14979-1]
DR AlphaFoldDB; O14979; -.
DR SMR; O14979; -.
DR BioGRID; 115308; 259.
DR CORUM; O14979; -.
DR IntAct; O14979; 110.
DR MINT; O14979; -.
DR STRING; 9606.ENSP00000483254; -.
DR GlyGen; O14979; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14979; -.
DR MetOSite; O14979; -.
DR PhosphoSitePlus; O14979; -.
DR SwissPalm; O14979; -.
DR BioMuta; HNRNPDL; -.
DR EPD; O14979; -.
DR jPOST; O14979; -.
DR MassIVE; O14979; -.
DR MaxQB; O14979; -.
DR PaxDb; O14979; -.
DR PeptideAtlas; O14979; -.
DR PRIDE; O14979; -.
DR ProteomicsDB; 48353; -. [O14979-1]
DR ProteomicsDB; 48354; -. [O14979-2]
DR ProteomicsDB; 48355; -. [O14979-3]
DR Antibodypedia; 25039; 167 antibodies from 24 providers.
DR DNASU; 9987; -.
DR Ensembl; ENST00000295470.10; ENSP00000295470.5; ENSG00000152795.18. [O14979-1]
DR Ensembl; ENST00000349655.8; ENSP00000338552.5; ENSG00000152795.18. [O14979-2]
DR Ensembl; ENST00000502762.4; ENSP00000422040.1; ENSG00000152795.18. [O14979-1]
DR Ensembl; ENST00000507721.5; ENSP00000480156.1; ENSG00000152795.18. [O14979-2]
DR Ensembl; ENST00000602300.5; ENSP00000473677.1; ENSG00000152795.18. [O14979-2]
DR Ensembl; ENST00000621267.4; ENSP00000483254.1; ENSG00000152795.18. [O14979-1]
DR Ensembl; ENST00000630114.2; ENSP00000486452.1; ENSG00000152795.18. [O14979-2]
DR Ensembl; ENST00000630827.1; ENSP00000485954.1; ENSG00000152795.18. [O14979-2]
DR GeneID; 9987; -.
DR KEGG; hsa:9987; -.
DR MANE-Select; ENST00000295470.10; ENSP00000295470.5; NM_031372.4; NP_112740.1.
DR UCSC; uc003hmr.4; human. [O14979-1]
DR CTD; 9987; -.
DR DisGeNET; 9987; -.
DR GeneCards; HNRNPDL; -.
DR HGNC; HGNC:5037; HNRNPDL.
DR HPA; ENSG00000152795; Low tissue specificity.
DR MalaCards; HNRNPDL; -.
DR MIM; 607137; gene.
DR MIM; 609115; phenotype.
DR neXtProt; NX_O14979; -.
DR OpenTargets; ENSG00000152795; -.
DR Orphanet; 55596; HNRNPDL-related limb-girdle muscular dystrophy D3.
DR PharmGKB; PA29362; -.
DR VEuPathDB; HostDB:ENSG00000152795; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000154426; -.
DR HOGENOM; CLU_012062_1_1_1; -.
DR InParanoid; O14979; -.
DR OMA; RSFNDGF; -.
DR PhylomeDB; O14979; -.
DR TreeFam; TF314808; -.
DR PathwayCommons; O14979; -.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR SignaLink; O14979; -.
DR BioGRID-ORCS; 9987; 18 hits in 1036 CRISPR screens.
DR ChiTaRS; HNRNPDL; human.
DR GeneWiki; HNRPDL; -.
DR GenomeRNAi; 9987; -.
DR Pharos; O14979; Tbio.
DR PRO; PR:O14979; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O14979; protein.
DR Bgee; ENSG00000152795; Expressed in tendon of biceps brachii and 210 other tissues.
DR ExpressionAtlas; O14979; baseline and differential.
DR Genevisible; O14979; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; NAS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
DR GO; GO:0034046; F:poly(G) binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0006396; P:RNA processing; NAS:UniProtKB.
DR CDD; cd12758; RRM1_hnRPDL; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034847; hnRPDL_RRM1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Disease variant; DNA-binding; Isopeptide bond;
KW Limb-girdle muscular dystrophy; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; RNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..420
FT /note="Heterogeneous nuclear ribonucleoprotein D-like"
FT /id="PRO_0000287239"
FT DOMAIN 148..230
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 233..312
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..420
FT /note="Necessary for interaction with TNPO1"
FT /evidence="ECO:0000269|PubMed:9524220"
FT REGION 396..420
FT /note="Necessary for its nuclear import and export"
FT REGION 398..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 161
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|Ref.9"
FT MOD_RES 216
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
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 408
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|Ref.9"
FT MOD_RES 408
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z130"
FT CROSSLNK 209
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..119
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10072754,
FT ECO:0000303|PubMed:11705999, ECO:0000303|PubMed:9538234"
FT /id="VSP_025410"
FT VAR_SEQ 341..397
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11705999"
FT /id="VSP_025411"
FT VARIANT 378
FT /note="D -> H (in LGMDD3; dbSNP:rs587777669)"
FT /evidence="ECO:0000269|PubMed:24647604"
FT /id="VAR_072567"
FT VARIANT 378
FT /note="D -> N (in LGMDD3; dbSNP:rs587777669)"
FT /evidence="ECO:0000269|PubMed:24647604"
FT /id="VAR_072568"
FT MUTAGEN 404
FT /note="G->A: Reduces significantly its nuclear
FT localization."
FT /evidence="ECO:0000269|PubMed:9524220"
SQ SEQUENCE 420 AA; 46438 MW; 00F631863859D0CA CRC64;
MEVPPRLSHV PPPLFPSAPA TLASRSLSHW RPRPPRQLAP LLPSLAPSSA RQGARRAQRH
VTAQQPSRLA GGAAIKGGRR RRPDLFRRHF KSSSIQRSAA AAAATRTARQ HPPADSSVTM
EDMNEYSNIE EFAEGSKINA SKNQQDDGKM FIGGLSWDTS KKDLTEYLSR FGEVVDCTIK
TDPVTGRSRG FGFVLFKDAA SVDKVLELKE HKLDGKLIDP KRAKALKGKE PPKKVFVGGL
SPDTSEEQIK EYFGAFGEIE NIELPMDTKT NERRGFCFIT YTDEEPVKKL LESRYHQIGS
GKCEIKVAQP KEVYRQQQQQ QKGGRGAAAG GRGGTRGRGR GQGQNWNQGF NNYYDQGYGN
YNSAYGGDQN YSGYGGYDYT GYNYGNYGYG QGYADYSGQQ STYGKASRGG GNHQNNYQPY
