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Heterogeneous nuclear ribonucleoprotein L (hnRNP L)

 HNRPL_HUMAN             Reviewed;         589 AA.
P14866; A6ND69; A6NIT8; Q9H3P3;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 2.
23-MAY-2018, entry version 196.
RecName: Full=Heterogeneous nuclear ribonucleoprotein L;
Short=hnRNP L;
Name=HNRNPL; Synonyms=HNRPL; ORFNames=P/OKcl.14;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Pancreatic cancer;
PubMed=11280764;
Ito M., Shichijo S., Tsuda N., Ochi M., Harashima N., Saito N.,
Itoh K.;
"Molecular basis of T cell-mediated recognition of pancreatic cancer
cells.";
Cancer Res. 61:2038-2046(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 23-589 (ISOFORM 1), FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=2687284; DOI=10.1083/jcb.109.6.2575;
Pinol-Roma S., Swanson M.S., Gall J.G., Dreyfuss G.;
"A novel heterogeneous nuclear RNP protein with a unique distribution
on nascent transcripts.";
J. Cell Biol. 109:2575-2587(1989).
[6]
PROTEIN SEQUENCE OF 67-76; 199-215; 218-233; 386-403; 425-448 AND
549-558, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[7]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[8]
FUNCTION, AND INTERACTION WITH APEX1.
PubMed=11809897; DOI=10.1093/nar/30.3.823;
Kuninger D.T., Izumi T., Papaconstantinou J., Mitra S.;
"Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like
repressor element in the AP-endonuclease 1 promoter.";
Nucleic Acids Res. 30:823-829(2002).
[9]
IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
Johnsen A.H., Christiansen J., Nielsen F.C.;
"Molecular composition of IMP1 ribonucleoprotein granules.";
Mol. Cell. Proteomics 6:798-811(2007).
[10]
INTERACTION WITH ELAVL1.
PubMed=18161049; DOI=10.1002/hep.22036;
Matsui K., Nishizawa M., Ozaki T., Kimura T., Hashimoto I., Yamada M.,
Kaibori M., Kamiyama Y., Ito S., Okumura T.;
"Natural antisense transcript stabilizes inducible nitric oxide
synthase messenger RNA in rat hepatocytes.";
Hepatology 47:686-697(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-298, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
INTERACTION WITH HNRNPLL.
PubMed=18669861; DOI=10.1126/science.1157610;
Oberdoerffer S., Moita L.F., Neems D., Freitas R.P., Hacohen N.,
Rao A.;
"Regulation of CD45 alternative splicing by heterogeneous
ribonucleoprotein, hnRNPLL.";
Science 321:686-691(2008).
[13]
INTERACTION WITH SETD2.
PubMed=19332550; DOI=10.1074/jbc.M808431200;
Yuan W., Xie J., Long C., Erdjument-Bromage H., Ding X., Zheng Y.,
Tempst P., Chen S., Zhu B., Reinberg D.;
"Heterogeneous nuclear ribonucleoprotein L is a subunit of human
KMT3a/Set2 complex required for H3 Lys-36 trimethylation activity in
vivo.";
J. Biol. Chem. 284:15701-15707(2009).
[14]
ALTERNATIVE SPLICING, AND MISCELLANEOUS.
PubMed=19124611; DOI=10.1128/MCB.01689-08;
Rossbach O., Hung L.H., Schreiner S., Grishina I., Heiner M., Hui J.,
Bindereif A.;
"Auto- and cross-regulation of the hnRNP L proteins by alternative
splicing.";
Mol. Cell. Biol. 29:1442-1451(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-269, 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-52; SER-185 AND SER-298,
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-52; SER-101; SER-185;
SER-291 AND SER-298, 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 AT SER-544, AND FUNCTION.
PubMed=22570490; DOI=10.1074/jbc.M112.357343;
Liu G., Razanau A., Hai Y., Yu J., Sohail M., Lobo V.G., Chu J.,
Kung S.K., Xie J.;
"A conserved serine of heterogeneous nuclear ribonucleoprotein L
(hnRNP L) mediates depolarization-regulated alternative splicing of
potassium channels.";
J. Biol. Chem. 287:22709-22716(2012).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-101; SER-185 AND
SER-298, 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).
[22]
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).
[23]
FUNCTION.
PubMed=24164894; DOI=10.1128/MCB.00740-13;
Shankarling G., Cole B.S., Mallory M.J., Lynch K.W.;
"Transcriptome-wide RNA interaction profiling reveals physical and
functional targets of hnRNP L in human T cells.";
Mol. Cell. Biol. 34:71-83(2014).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-62, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[25]
FUNCTION.
PubMed=25623890; DOI=10.1016/j.bbagrm.2015.01.004;
Loh T.J., Cho S., Moon H., Jang H.N., Williams D.R., Jung D.W.,
Kim I.C., Ghigna C., Biamonti G., Zheng X., Shen H.;
"hnRNP L inhibits CD44 V10 exon splicing through interacting with its
upstream intron.";
Biochim. Biophys. Acta 1849:743-750(2015).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-136, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[27]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=26051023; DOI=10.1016/j.jmb.2015.05.020;
Blatter M., Dunin-Horkawicz S., Grishina I., Maris C., Thore S.,
Maier T., Bindereif A., Bujnicki J.M., Allain F.H.;
"The signature of the five-stranded vRRM fold defined by functional,
structural and computational analysis of the hnRNP L protein.";
J. Mol. Biol. 427:3001-3022(2015).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-62, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[30]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-62; LYS-136; LYS-302
AND LYS-568, 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).
[31]
X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 90-180, X-RAY
CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 380-589, RNA-BINDING, RRM DOMAINS,
AND MUTAGENESIS OF HIS-105; VAL-132; LEU-141; ASN-172; SER-174;
HIS-504 AND PHE-506.
PubMed=23782695; DOI=10.1074/jbc.M113.463901;
Zhang W., Zeng F., Liu Y., Zhao Y., Lv H., Niu L., Teng M., Li X.;
"Crystal structures and RNA-binding properties of the RNA recognition
motifs of heterogeneous nuclear ribonucleoprotein L: insights into its
roles in alternative splicing regulation.";
J. Biol. Chem. 288:22636-22649(2013).
-!- FUNCTION: Splicing factor binding to exonic or intronic sites and
acting as either an activator or repressor of exon inclusion.
Exhibits a binding preference for CA-rich elements
(PubMed:11809897, PubMed:22570490, PubMed:24164894,
PubMed:25623890, PubMed:26051023). Component of the heterogeneous
nuclear ribonucleoprotein (hnRNP) complexes and associated with
most nascent transcripts (PubMed:2687284). Associates, together
with APEX1, to the negative calcium responsive element (nCaRE) B2
of the APEX2 promoter (PubMed:11809897).
{ECO:0000269|PubMed:11809897, ECO:0000269|PubMed:22570490,
ECO:0000269|PubMed:25623890, ECO:0000269|PubMed:26051023,
ECO:0000269|PubMed:2687284}.
-!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
containing untranslated mRNAs (PubMed:17289661). Interacts with
HNRNPLL (PubMed:18669861). Interacts with APEX1; the interaction
is DNA-dependent (PubMed:11809897). Component of a complex with
SETD2 (PubMed:19332550). Interacts with ELAVL1 (PubMed:18161049).
{ECO:0000269|PubMed:11809897, ECO:0000269|PubMed:17289661,
ECO:0000269|PubMed:18161049, ECO:0000269|PubMed:18669861,
ECO:0000269|PubMed:19332550}.
-!- INTERACTION:
P22626:HNRNPA2B1; NbExp=4; IntAct=EBI-16071645, EBI-299649;
Q12906:ILF3; NbExp=2; IntAct=EBI-16071645, EBI-78756;
P40337:VHL; NbExp=2; IntAct=EBI-719024, EBI-301246;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:2687284,
ECO:0000305|PubMed:26051023}. Cytoplasm
{ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP
granules containing untranslated mRNAs. These granules are not
identical with P bodies or stress granules.
{ECO:0000269|PubMed:17289661}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P14866-1; Sequence=Displayed;
Name=2;
IsoId=P14866-2; Sequence=VSP_044301;
-!- DOMAIN: RRM domain 2 has moderate RNA-binding affinity. RRM
domains 3 and 4 may facilitate RNA looping when binding to two
appropriately separated binding sites within the same target pre-
mRNA (PubMed:23782695). {ECO:0000269|PubMed:23782695}.
-!- PTM: Several isoelectric forms of the L protein are probably the
results of post-translational modifications.
-!- PTM: Phosphorylation at Ser-544 by CaMK4 enhances interaction with
a CaMK4-responsive RNA element (CaRRE1), and prevents inclusion of
the stress axis-regulated exon (STREX) of the KCNMA1 potassium
channel transcripts upon membrane depolarization.
{ECO:0000269|PubMed:22570490}.
-!- MISCELLANEOUS: Excess hnRNP L activates NMD of its own mRNA by
promoting the inclusion of a 'poison exon' containing a premature
stop codon and leading to nonsense-mediated decay. It also cross-
regulates inclusion of an analogous 'poison exon' in the hnRNP L-
like pre-mRNA (PubMed:19124611). {ECO:0000305|PubMed:19124611}.
-!- SEQUENCE CAUTION:
Sequence=CAA34261.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB044547; BAB18649.1; -; mRNA.
EMBL; AK292115; BAF84804.1; -; mRNA.
EMBL; AC008982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471126; EAW56828.1; -; Genomic_DNA.
EMBL; X16135; CAA34261.1; ALT_INIT; mRNA.
CCDS; CCDS33015.1; -. [P14866-1]
CCDS; CCDS33016.1; -. [P14866-2]
PIR; A33616; A33616.
RefSeq; NP_001005335.1; NM_001005335.1. [P14866-2]
RefSeq; NP_001524.2; NM_001533.2. [P14866-1]
RefSeq; XP_011525191.1; XM_011526889.1. [P14866-2]
UniGene; Hs.644906; -.
PDB; 3R27; X-ray; 2.04 A; A/B=90-180.
PDB; 3TO8; X-ray; 1.82 A; A=380-589.
PDBsum; 3R27; -.
PDBsum; 3TO8; -.
ProteinModelPortal; P14866; -.
SMR; P14866; -.
BioGrid; 109432; 119.
CORUM; P14866; -.
DIP; DIP-36355N; -.
IntAct; P14866; 45.
MINT; P14866; -.
STRING; 9606.ENSP00000221419; -.
iPTMnet; P14866; -.
PhosphoSitePlus; P14866; -.
SwissPalm; P14866; -.
BioMuta; HNRNPL; -.
DMDM; 215274006; -.
REPRODUCTION-2DPAGE; IPI00027834; -.
SWISS-2DPAGE; P14866; -.
EPD; P14866; -.
MaxQB; P14866; -.
PaxDb; P14866; -.
PeptideAtlas; P14866; -.
PRIDE; P14866; -.
DNASU; 3191; -.
Ensembl; ENST00000221419; ENSP00000221419; ENSG00000104824. [P14866-1]
Ensembl; ENST00000600873; ENSP00000470231; ENSG00000104824. [P14866-2]
Ensembl; ENST00000634237; ENSP00000489244; ENSG00000282947. [P14866-2]
Ensembl; ENST00000634753; ENSP00000489021; ENSG00000282947. [P14866-1]
GeneID; 3191; -.
KEGG; hsa:3191; -.
UCSC; uc060yfy.1; human. [P14866-1]
CTD; 3191; -.
DisGeNET; 3191; -.
EuPathDB; HostDB:ENSG00000104824.16; -.
GeneCards; HNRNPL; -.
H-InvDB; HIX0174642; -.
HGNC; HGNC:5045; HNRNPL.
HPA; CAB016326; -.
HPA; HPA051748; -.
HPA; HPA052661; -.
MIM; 164021; gene.
MIM; 603083; gene.
neXtProt; NX_P14866; -.
OpenTargets; ENSG00000104824; -.
PharmGKB; PA162391389; -.
eggNOG; KOG1456; Eukaryota.
eggNOG; ENOG410XQHN; LUCA.
GeneTree; ENSGT00550000074508; -.
HOGENOM; HOG000293298; -.
HOVERGEN; HBG105786; -.
InParanoid; P14866; -.
KO; K13159; -.
OMA; RAGAMVK; -.
OrthoDB; EOG091G0PR3; -.
PhylomeDB; P14866; -.
TreeFam; TF354318; -.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
SIGNOR; P14866; -.
ChiTaRS; HNRNPL; human.
GeneWiki; HNRNPL; -.
GenomeRNAi; 3191; -.
PRO; PR:P14866; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000104824; -.
CleanEx; HS_HNRNPL; -.
ExpressionAtlas; P14866; baseline and differential.
Genevisible; P14866; HS.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0045120; C:pronucleus; IEA:Ensembl.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0035770; C:ribonucleoprotein granule; IDA:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl.
GO; GO:1990715; F:mRNA CDS binding; IEA:Ensembl.
GO; GO:0097157; F:pre-mRNA intronic binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0034198; P:cellular response to amino acid starvation; IEA:Ensembl.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
GO; GO:1902416; P:positive regulation of mRNA binding; IEA:Ensembl.
GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:UniProtKB.
GO; GO:1901652; P:response to peptide; IEA:Ensembl.
GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
GO; GO:0006396; P:RNA processing; TAS:ProtInc.
CDD; cd12780; RRM1_hnRNPL; 1.
CDD; cd12785; RRM2_hnRNPL; 1.
CDD; cd12699; RRM3_hnRNPL; 1.
CDD; cd12704; RRM4_hnRNPL; 1.
Gene3D; 3.30.70.330; -; 4.
InterPro; IPR006536; HnRNP-L/PTB.
InterPro; IPR034816; hnRNP-L_RRM3.
InterPro; IPR035005; hnRNPL_RRM1.
InterPro; IPR035008; hnRNPL_RRM2.
InterPro; IPR034817; hnRNPL_RRM4.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 2.
SMART; SM00360; RRM; 3.
SUPFAM; SSF54928; SSF54928; 3.
TIGRFAMs; TIGR01649; hnRNP-L_PTB; 1.
PROSITE; PS50102; RRM; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Isopeptide bond; Methylation;
Nucleus; Phosphoprotein; Reference proteome; Repeat;
Ribonucleoprotein; RNA-binding; Ubl conjugation.
CHAIN 1 589 Heterogeneous nuclear ribonucleoprotein
L.
/FTId=PRO_0000081862.
DOMAIN 102 176 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 193 270 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 382 478 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 495 583 RRM 4. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COMPBIAS 39 89 Gly-rich.
COMPBIAS 335 382 Pro-rich.
MOD_RES 52 52 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 101 101 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 269 269 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 298 298 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 354 354 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q8R081}.
MOD_RES 358 358 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q8R081}.
MOD_RES 381 381 Phosphoserine.
{ECO:0000250|UniProtKB:Q8R081}.
MOD_RES 544 544 Phosphoserine; by CaMK4.
{ECO:0000269|PubMed:22570490}.
CROSSLNK 59 59 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 62 62 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 136 136 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 302 302 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 568 568 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 133 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044301.
MUTAGEN 105 105 H->A: 6-fold decrease in RNA-binding
affinity. {ECO:0000269|PubMed:23782695}.
MUTAGEN 132 132 V->A: 4-fold increase in RNA-binding
affinity. {ECO:0000269|PubMed:23782695}.
MUTAGEN 141 141 L->A: 15-fold decrease in RNA-binding
affinity; when associated with A-174.
{ECO:0000269|PubMed:23782695}.
MUTAGEN 172 172 N->A: 1-fold increase in RNA-binding
affinity. {ECO:0000269|PubMed:23782695}.
MUTAGEN 174 174 S->A: 15-fold decrease in RNA-binding
affinity; when associated with A-174.
{ECO:0000269|PubMed:23782695}.
MUTAGEN 504 504 H->A: Significant decrease in RNA-binding
affinity. {ECO:0000269|PubMed:23782695}.
MUTAGEN 506 506 F->A: Significant decrease in RNA-binding
affinity. {ECO:0000269|PubMed:23782695}.
CONFLICT 396 396 C -> G (in Ref. 1; BAB18649 and 5;
CAA34261). {ECO:0000305}.
STRAND 102 108 {ECO:0000244|PDB:3R27}.
HELIX 115 122 {ECO:0000244|PDB:3R27}.
HELIX 123 125 {ECO:0000244|PDB:3R27}.
STRAND 128 134 {ECO:0000244|PDB:3R27}.
TURN 135 138 {ECO:0000244|PDB:3R27}.
STRAND 139 146 {ECO:0000244|PDB:3R27}.
HELIX 147 159 {ECO:0000244|PDB:3R27}.
STRAND 162 164 {ECO:0000244|PDB:3R27}.
STRAND 167 173 {ECO:0000244|PDB:3R27}.
STRAND 382 387 {ECO:0000244|PDB:3TO8}.
TURN 391 393 {ECO:0000244|PDB:3TO8}.
HELIX 396 403 {ECO:0000244|PDB:3TO8}.
TURN 404 406 {ECO:0000244|PDB:3TO8}.
STRAND 409 414 {ECO:0000244|PDB:3TO8}.
STRAND 421 428 {ECO:0000244|PDB:3TO8}.
HELIX 429 439 {ECO:0000244|PDB:3TO8}.
STRAND 450 453 {ECO:0000244|PDB:3TO8}.
STRAND 472 476 {ECO:0000244|PDB:3TO8}.
HELIX 488 491 {ECO:0000244|PDB:3TO8}.
STRAND 501 508 {ECO:0000244|PDB:3TO8}.
HELIX 514 524 {ECO:0000244|PDB:3TO8}.
STRAND 530 534 {ECO:0000244|PDB:3TO8}.
STRAND 543 548 {ECO:0000244|PDB:3TO8}.
HELIX 552 562 {ECO:0000244|PDB:3TO8}.
STRAND 572 574 {ECO:0000244|PDB:3TO8}.
STRAND 579 582 {ECO:0000244|PDB:3TO8}.
SEQUENCE 589 AA; 64133 MW; 31EEB51AF1C65F83 CRC64;
MSRRLLPRAE KRRRRLEQRQ QPDEQRRRSG AMVKMAAAGG GGGGGRYYGG GSEGGRAPKR
LKTDNAGDQH GGGGGGGGGA GAAGGGGGGE NYDDPHKTPA SPVVHIRGLI DGVVEADLVE
ALQEFGPISY VVVMPKKRQA LVEFEDVLGA CNAVNYAADN QIYIAGHPAF VNYSTSQKIS
RPGDSDDSRS VNSVLLFTIL NPIYSITTDV LYTICNPCGP VQRIVIFRKN GVQAMVEFDS
VQSAQRAKAS LNGADIYSGC CTLKIEYAKP TRLNVFKNDQ DTWDYTNPNL SGQGDPGSNP
NKRQRQPPLL GDHPAEYGGP HGGYHSHYHD EGYGPPPPHY EGRRMGPPVG GHRRGPSRYG
PQYGHPPPPP PPPEYGPHAD SPVLMVYGLD QSKMNCDRVF NVFCLYGNVE KVKFMKSKPG
AAMVEMADGY AVDRAITHLN NNFMFGQKLN VCVSKQPAIM PGQSYGLEDG SCSYKDFSES
RNNRFSTPEQ AAKNRIQHPS NVLHFFNAPL EVTEENFFEI CDELGVKRPS SVKVFSGKSE
RSSSGLLEWE SKSDALETLG FLNHYQMKNP NGPYPYTLKL CFSTAQHAS


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