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Heterogeneous nuclear ribonucleoprotein D-like (hnRNP D-like) (hnRNP DL) (AU-rich element RNA-binding factor) (JKT41-binding protein) (Protein laAUF1)

 HNRDL_HUMAN             Reviewed;         420 AA.
O14979; Q6SPF2; Q7KZ74; Q7KZ75; Q96IM0; Q96S43;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-AUG-1999, sequence version 3.
25-OCT-2017, entry version 162.
RecName: Full=Heterogeneous nuclear ribonucleoprotein D-like;
Short=hnRNP D-like;
Short=hnRNP DL;
AltName: Full=AU-rich element RNA-binding factor;
AltName: Full=JKT41-binding protein;
AltName: Full=Protein laAUF1;
Name=HNRNPDL; Synonyms=HNRPDL, JKTBP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
SPECIFICITY, RNA-BINDING, AND DNA-BINDING.
TISSUE=Erythroleukemia, and Placenta;
PubMed=9538234; DOI=10.1093/oxfordjournals.jbchem.a021964;
Tsuchiya N., Kamei D., Takano A., Matsui T., Yamada M.;
"Cloning and characterization of a cDNA encoding a novel heterogeneous
nuclear ribonucleoprotein-like protein and its expression in myeloid
leukemia cells.";
J. Biochem. 123:499-507(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INDUCTION, AND TISSUE
SPECIFICITY.
TISSUE=Placenta;
PubMed=10072754; DOI=10.1016/S0378-1119(99)00020-7;
Kamei D., Tsuchiya N., Yamazaki M., Meguro H., Yamada M.;
"Two forms of expression and genomic structure of the human
heterogeneous nuclear ribonucleoprotein D-like JKTBP gene (HNRPDL).";
Gene 228:13-22(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, AND
RNA-BINDING.
PubMed=11705999; DOI=10.1074/jbc.M108477200;
Kawamura H., Tomozoe Y., Akagi T., Kamei D., Ochiai M., Yamada M.;
"Identification of the nucleocytoplasmic shuttling sequence of
heterogeneous nuclear ribonucleoprotein D-like protein JKTBP and its
interaction with mRNA.";
J. Biol. Chem. 277:2732-2739(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, Ovary, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 123-420.
TISSUE=Brain;
PubMed=15190078; DOI=10.1074/jbc.M403160200;
Boopathi E., Lenka N., Prabu S.K., Fang J.-K., Wilkinson F.,
Atchison M., Giallongo A., Avadhani N.G.;
"Regulation of murine cytochrome c oxidase Vb gene expression during
myogenesis: YY-1 and heterogeneous nuclear ribonucleoprotein D-like
protein (JKTBP1) reciprocally regulate transcription activity by
physical interaction with the BERF-1/ZBP-89 factor.";
J. Biol. Chem. 279:35242-35254(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 131-420, INTERACTION WITH TNPO1,
MUTAGENESIS OF GLY-404, INDUCTION, AND RNA-BINDING.
PubMed=9524220; DOI=10.1016/S0167-4781(97)00223-6;
Doi A., Shiosaka T., Takaoka Y., Yanagisawa K., Fujita S.;
"Molecular cloning of the cDNA encoding A + U-rich element RNA binding
factor.";
Biochim. Biophys. Acta 1396:51-56(1998).
[9]
PROTEIN SEQUENCE OF 150-180; 190-209; 234-269; 275-289 AND 406-420,
METHYLATION AT LYS-161 AND ARG-408, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Colon carcinoma, and Ovarian carcinoma;
Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A.,
Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[10]
PROTEIN SEQUENCE OF 235-269 AND 275-289.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[11]
SUBCELLULAR LOCATION, AND RNA-BINDING.
PubMed=12406575; DOI=10.1016/S0378-1119(02)00926-5;
Kamei D., Yamada M.;
"Interactions of heterogeneous nuclear ribonucleoprotein D-like
protein JKTBP and its domains with high-affinity binding sites.";
Gene 298:49-57(2002).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-216, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
INVOLVEMENT IN LGMD1G, AND VARIANTS LGMD1G ASN-378 AND HIS-378.
PubMed=24647604; DOI=10.1093/hmg/ddu127;
Vieira N.M., Naslavsky M.S., Licinio L., Kok F., Schlesinger D.,
Vainzof M., Sanchez N., Kitajima J.P., Gal L., Cavacana N.,
Serafini P.R., Chuartzman S., Vasquez C., Mimbacas A., Nigro V.,
Pavanello R.C., Schuldiner M., Kunkel L.M., Zatz M.;
"A defect in the RNA-processing protein HNRPDL causes limb-girdle
muscular dystrophy 1G (LGMD1G).";
Hum. Mol. Genet. 23:4103-4110(2014).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-25, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-209, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Acts as a transcriptional regulator. Promotes
transcription repression. Promotes transcription activation in
differentiated myotubes (By similarity). Binds to double- and
single-stranded DNA sequences. Binds to the transcription
suppressor CATR sequence of the COX5B promoter (By similarity).
Binds with high affinity to RNA molecules that contain AU-rich
elements (AREs) found within the 3'-UTR of many proto-oncogenes
and cytokine mRNAs. Binds both to nuclear and cytoplasmic poly(A)
mRNAs. Binds to poly(G) and poly(A), but not to poly(U) or poly(C)
RNA homopolymers. Binds to the 5'-ACUAGC-3' RNA consensus
sequence. {ECO:0000250, ECO:0000269|PubMed:9538234}.
-!- SUBUNIT: Interacts with ZNF148 (By similarity). Interacts with
TNPO1. {ECO:0000250, ECO:0000269|PubMed:9524220}.
-!- INTERACTION:
Q15637:SF1; NbExp=4; IntAct=EBI-299727, EBI-744603;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11705999,
ECO:0000269|PubMed:12406575}. Cytoplasm
{ECO:0000269|PubMed:11705999, ECO:0000269|PubMed:12406575}.
Note=Shuttles between the nucleus and the cytoplasm in a TNPO1-
dependent manner. {ECO:0000269|PubMed:11705999,
ECO:0000269|PubMed:12406575}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=JKTBP1;
IsoId=O14979-1; Sequence=Displayed;
Name=2; Synonyms=JKTBP2;
IsoId=O14979-2; Sequence=VSP_025410;
Name=3;
IsoId=O14979-3; Sequence=VSP_025410, VSP_025411;
-!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung,
liver, skeletal muscle, kidney, pancreas, spleen, thymus,
prostate, testis, ovary, small intestine, colon and leukocytes.
Expressed in myeloid leukemia, gastric adenocarcinoma, cervical
carcinoma, hepatoma, fibrosarcoma, colon adenocarcinoma,
epidermoid carcinoma, osteosarcoma and urinary bladder carcinoma
cells. {ECO:0000269|PubMed:10072754, ECO:0000269|PubMed:9538234}.
-!- INDUCTION: Up-regulated by 12-O-tetradecanoylphorbol-13-acetate
(TPA) in macrophages and retinoic acid (RA) in granulocytes (at
protein level). Down-regulated by IL4/interleukin-4.
{ECO:0000269|PubMed:10072754, ECO:0000269|PubMed:9524220}.
-!- PTM: Dimethylation of Arg-408 is probably of the asymmetric type.
-!- DISEASE: Limb-girdle muscular dystrophy 1G (LGMD1G) [MIM:609115]:
An autosomal dominant degenerative myopathy characterized by
slowly progressive wasting and weakness of the proximal muscles of
arms and legs around the pelvic or shoulder girdles, elevated
creatine kinase levels and dystrophic features on muscle biopsy.
LGMD1G is characterized by a mild late-onset and is associated
with progressive fingers and toes flexion limitation. Affected
individuals may also develop cataracts before age 50.
{ECO:0000269|PubMed:24647604}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=BAA22860.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB017019; BAA75241.1; -; mRNA.
EMBL; D89092; BAA24361.1; -; mRNA.
EMBL; AB066484; BAB62188.1; -; mRNA.
EMBL; CR407623; CAG28551.1; -; mRNA.
EMBL; AC124016; AAY40914.1; -; Genomic_DNA.
EMBL; AB017018; BAA75239.1; -; Genomic_DNA.
EMBL; AB017018; BAA75240.1; -; Genomic_DNA.
EMBL; BC007392; AAH07392.2; -; mRNA.
EMBL; BC011714; AAH11714.1; -; mRNA.
EMBL; BC071944; AAH71944.1; -; mRNA.
EMBL; AY453824; AAR17782.1; -; mRNA.
EMBL; D89678; BAA22860.1; ALT_INIT; mRNA.
CCDS; CCDS3593.1; -. [O14979-1]
PIR; JW0079; JW0079.
RefSeq; NP_001193929.1; NM_001207000.1.
RefSeq; NP_112740.1; NM_031372.3. [O14979-1]
UniGene; Hs.527105; -.
UniGene; Hs.707013; -.
ProteinModelPortal; O14979; -.
SMR; O14979; -.
BioGrid; 115308; 118.
CORUM; O14979; -.
IntAct; O14979; 41.
MINT; MINT-2998491; -.
STRING; 9606.ENSP00000295470; -.
iPTMnet; O14979; -.
PhosphoSitePlus; O14979; -.
SwissPalm; O14979; -.
BioMuta; HNRNPDL; -.
EPD; O14979; -.
MaxQB; O14979; -.
PaxDb; O14979; -.
PeptideAtlas; O14979; -.
PRIDE; O14979; -.
DNASU; 9987; -.
Ensembl; ENST00000295470; ENSP00000295470; ENSG00000152795. [O14979-1]
Ensembl; ENST00000349655; ENSP00000338552; ENSG00000152795. [O14979-2]
Ensembl; ENST00000502762; ENSP00000422040; ENSG00000152795. [O14979-1]
Ensembl; ENST00000507721; ENSP00000480156; ENSG00000152795. [O14979-2]
Ensembl; ENST00000602300; ENSP00000473677; ENSG00000152795. [O14979-2]
Ensembl; ENST00000621267; ENSP00000483254; ENSG00000152795. [O14979-1]
Ensembl; ENST00000630114; ENSP00000486452; ENSG00000152795. [O14979-2]
Ensembl; ENST00000630827; ENSP00000485954; ENSG00000152795. [O14979-2]
GeneID; 9987; -.
KEGG; hsa:9987; -.
UCSC; uc003hmr.4; human. [O14979-1]
CTD; 9987; -.
DisGeNET; 9987; -.
EuPathDB; HostDB:ENSG00000152795.17; -.
GeneCards; HNRNPDL; -.
HGNC; HGNC:5037; HNRNPDL.
HPA; HPA056820; -.
HPA; HPA063147; -.
MalaCards; HNRNPDL; -.
MIM; 607137; gene.
MIM; 609115; phenotype.
neXtProt; NX_O14979; -.
OpenTargets; ENSG00000152795; -.
Orphanet; 55596; Autosomal dominant limb-girdle muscular dystrophy type 1G.
PharmGKB; PA29362; -.
eggNOG; ENOG410IQWX; Eukaryota.
eggNOG; ENOG4111SPT; LUCA.
GeneTree; ENSGT00900000140835; -.
HOGENOM; HOG000234441; -.
HOVERGEN; HBG002295; -.
InParanoid; O14979; -.
KO; K13044; -.
OMA; GPGYTDY; -.
OrthoDB; EOG091G1CPI; -.
PhylomeDB; O14979; -.
TreeFam; TF314808; -.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
GeneWiki; HNRPDL; -.
GenomeRNAi; 9987; -.
PRO; PR:O14979; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000152795; -.
CleanEx; HS_HNRPDL; -.
ExpressionAtlas; O14979; baseline and differential.
Genevisible; O14979; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005681; C:spliceosomal complex; NAS:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
GO; GO:0034046; F:poly(G) binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0010468; P:regulation of gene expression; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006396; P:RNA processing; NAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd12758; RRM1_hnRPDL; 1.
InterPro; IPR034847; hnRPDL_RRM1.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 2.
SMART; SM00360; RRM; 2.
SUPFAM; SSF54928; SSF54928; 2.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Disease mutation; DNA-binding;
Isopeptide bond; Limb-girdle muscular dystrophy; Methylation; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 420 Heterogeneous nuclear ribonucleoprotein
D-like.
/FTId=PRO_0000287239.
DOMAIN 148 230 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 233 312 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 342 420 Necessary for interaction with TNPO1.
{ECO:0000269|PubMed:9524220}.
REGION 396 420 Necessary for its nuclear import and
export.
COMPBIAS 79 82 Poly-Arg.
COMPBIAS 316 321 Poly-Gln.
COMPBIAS 323 411 Gly-rich.
COMPBIAS 353 396 Tyr-rich.
MOD_RES 25 25 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 161 161 N6-methyllysine. {ECO:0000269|Ref.9}.
MOD_RES 216 216 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 408 408 Dimethylated arginine; alternate.
{ECO:0000269|Ref.9}.
MOD_RES 408 408 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q9Z130}.
CROSSLNK 209 209 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 119 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:10072754,
ECO:0000303|PubMed:11705999,
ECO:0000303|PubMed:9538234}.
/FTId=VSP_025410.
VAR_SEQ 341 397 Missing (in isoform 3).
{ECO:0000303|PubMed:11705999}.
/FTId=VSP_025411.
VARIANT 378 378 D -> H (in LGMD1G; dbSNP:rs587777669).
{ECO:0000269|PubMed:24647604}.
/FTId=VAR_072567.
VARIANT 378 378 D -> N (in LGMD1G; dbSNP:rs587777669).
{ECO:0000269|PubMed:24647604}.
/FTId=VAR_072568.
MUTAGEN 404 404 G->A: Reduces significantly its nuclear
localization.
{ECO:0000269|PubMed:9524220}.
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


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