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Protein

Heterogeneous nuclear ribonucleoprotein L

Gene

Hnrnpl

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter.By similarity

GO - Molecular functioni

  • mRNA 3'-UTR binding Source: RGD
  • mRNA CDS binding Source: RGD
  • nucleotide binding Source: InterPro
  • pre-mRNA intronic binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  • cellular response to amino acid starvation Source: RGD
  • circadian rhythm Source: RGD
  • mRNA processing Source: InterPro
  • negative regulation of mRNA splicing, via spliceosome Source: RGD
  • positive regulation of mRNA binding Source: RGD
  • positive regulation of translation Source: RGD
  • regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
  • response to peptide Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-RNO-72163. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein L
Short name:
hnRNP L
Gene namesi
Name:HnrnplImported
Synonyms:Fblim1Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi71059. Hnrnpl.

Subcellular locationi

  • Nucleusnucleoplasm By similarity
  • Cytoplasm 1 Publication

  • Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. These granules are not identical with P bodies or stress granules.By similarity

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • ribonucleoprotein granule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 623623Heterogeneous nuclear ribonucleoprotein LPRO_0000436064Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki62 – 62Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei98 – 981PhosphoserineBy similarity
Cross-linki133 – 133Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei182 – 1821PhosphoserineBy similarity
Modified residuei266 – 2661N6-acetyllysineBy similarity
Modified residuei288 – 2881PhosphoserineBy similarity
Modified residuei295 – 2951PhosphoserineBy similarity
Modified residuei415 – 4151PhosphoserineBy similarity
Modified residuei578 – 5781Phosphoserine; by CaMK4By similarity

Post-translational modificationi

Several isoelectric forms of the L protein are probably the results of post-translational modifications.By similarity
Phosphorylation at Ser-578 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.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiF1LQ48.
PeptideAtlasiF1LQ48.
PRIDEiF1LQ48.

PTM databases

iPTMnetiF1LQ48.

Expressioni

Gene expression databases

ExpressionAtlasiF1LQ48. baseline and differential.

Interactioni

Subunit structurei

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with HNRNPLL. Interacts with APEX1; the interaction is DNA-dependent. Component of a complex with SETD2 (By similarity). Interacts with ELAVL1 (PubMed:18161049).By similarity1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027425.

Structurei

Secondary structure

1
623
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi99 – 1046Combined sources
Helixi112 – 1198Combined sources
Helixi120 – 1223Combined sources
Beta strandi125 – 1317Combined sources
Turni132 – 1354Combined sources
Beta strandi136 – 1438Combined sources
Helixi144 – 1485Combined sources
Helixi151 – 1544Combined sources
Beta strandi159 – 17012Combined sources
Beta strandi172 – 1743Combined sources
Turni179 – 1813Combined sources
Helixi182 – 1854Combined sources
Beta strandi186 – 1883Combined sources
Beta strandi190 – 1989Combined sources
Helixi205 – 2128Combined sources
Helixi213 – 2153Combined sources
Beta strandi218 – 2247Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi230 – 2378Combined sources
Helixi238 – 24811Combined sources
Beta strandi253 – 2586Combined sources
Beta strandi260 – 2645Combined sources
Beta strandi266 – 2683Combined sources
Beta strandi276 – 2849Combined sources
Helixi285 – 2895Combined sources
Beta strandi411 – 42111Combined sources
Turni425 – 4273Combined sources
Helixi430 – 4378Combined sources
Turni438 – 4403Combined sources
Beta strandi443 – 4486Combined sources
Beta strandi450 – 4523Combined sources
Beta strandi456 – 4627Combined sources
Helixi463 – 47311Combined sources
Beta strandi476 – 4783Combined sources
Beta strandi484 – 4874Combined sources
Beta strandi502 – 5054Combined sources
Beta strandi506 – 5105Combined sources
Helixi522 – 5254Combined sources
Beta strandi535 – 5428Combined sources
Helixi548 – 55811Combined sources
Beta strandi564 – 5685Combined sources
Beta strandi575 – 5828Combined sources
Helixi586 – 59611Combined sources
Beta strandi606 – 6083Combined sources
Beta strandi613 – 6164Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MQLNMR-A86-190[»]
2MQMNMR-A174-291[»]
2MQNNMR-A408-623[»]
2MQONMR-A86-190[»]
2MQPNMR-A174-291[»]
2MQQNMR-A409-623[»]
4QPTX-ray1.35A409-623[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini99 – 17375RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini190 – 26778RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini416 – 49075RRM 3PROSITE-ProRule annotationAdd
BLAST
Domaini498 – 58689RRM 41 PublicationAdd
BLAST

Domaini

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.By similarity

Sequence similaritiesi

Contains 4 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation1 Publication

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1456. Eukaryota.
ENOG410XQHN. LUCA.
GeneTreeiENSGT00550000074508.
HOGENOMiHOG000293298.
HOVERGENiHBG058843.
InParanoidiF1LQ48.
KOiK13159.
OMAiPYEGRRM.
OrthoDBiEOG7HMS2K.
TreeFamiTF354318.

Family and domain databases

Gene3Di3.30.70.330. 4 hits.
InterProiIPR006536. HnRNP-L/PTB.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 3 hits.
TIGRFAMsiTIGR01649. hnRNP-L_PTB. 2 hits.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: F1LQ48-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSRRLLPRAE KRRRRLEQRQ QPDEQLRRAG AMVKMAAAGG GGGGGRYYGG
60 70 80 90 100
GNEGGRAPKR LKTENAGDQH GGGGGGGSGA AGGGGGENYD DPHKTPASPV
110 120 130 140 150
VHIRGLIDGV VEADLVEALQ EFGPISYVVV MPKKRQALVE FEDVLGACNA
160 170 180 190 200
VNYAADNQIY IAGHPAFVNY STSQKISRPG DSDDSRSVNS VLLFTILNPI
210 220 230 240 250
YSITTDVLYT ICNPCGPVQR IVIFRKNGVQ AMVEFDSVQS AQRAKASLNG
260 270 280 290 300
ADIYSGCCTL KIEYAKPTRL NVFKNDQDTW DYTNPNLSGQ GDPGSNPNKR
310 320 330 340 350
QRQPPLLGDH PAEYGEGRGF PSVDSRGSCA PARRPPRKFS PVLPLFPSHP
360 370 380 390 400
PGGPHGGYHS HYHDEGYGPP PPHYEGRRMG PPVGGHRRGP SRYGPQYGHP
410 420 430 440 450
PPPPPPPDYG PHADSPVLMV YGLDQSKMNC DRVFNVFCLY GNVEKVKFMK
460 470 480 490 500
SKPGAAMVEM ADGYAVDRAI THLNNNFMFG QKMNVCVSKQ PAIMPGQSYG
510 520 530 540 550
LEDGSCSYKD FSESRNNRFS TPEQAAKNRI QHPSNVLHFF NAPLEVTEEN
560 570 580 590 600
FFEICDELGV KRPTSVKVFS GKSERSSSGL LEWDSKSDAL ETLGFLNHYQ
610 620
MKNPNGPYPY TLKLCFSTAQ HAS
Length:623
Mass (Da):67,903
Last modified:April 3, 2013 - v2
Checksum:i0DEB312EC2B896AF
GO
Isoform 2 (identifier: F1LQ48-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-378: Missing.

Show »
Length:245
Mass (Da):27,251
Checksum:i4F814C3211650207
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 378378Missing in isoform 2. VSP_058247Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB260892 mRNA. Translation: BAG72209.1.
AABR07002851 Genomic DNA. No translation available.
BC086392 mRNA. Translation: AAH86392.1.
RefSeqiNP_001128232.1. NM_001134760.1. [F1LQ48-1]
UniGeneiRn.33873.

Genome annotation databases

EnsembliENSRNOT00000027425; ENSRNOP00000027425; ENSRNOG00000020235. [F1LQ48-1]
ENSRNOT00000057034; ENSRNOP00000053867; ENSRNOG00000020235. [F1LQ48-2]
GeneIDi80846.
KEGGirno:80846.
UCSCiRGD:1359551. rat.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB260892 mRNA. Translation: BAG72209.1.
AABR07002851 Genomic DNA. No translation available.
BC086392 mRNA. Translation: AAH86392.1.
RefSeqiNP_001128232.1. NM_001134760.1. [F1LQ48-1]
UniGeneiRn.33873.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MQLNMR-A86-190[»]
2MQMNMR-A174-291[»]
2MQNNMR-A408-623[»]
2MQONMR-A86-190[»]
2MQPNMR-A174-291[»]
2MQQNMR-A409-623[»]
4QPTX-ray1.35A409-623[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027425.

PTM databases

iPTMnetiF1LQ48.

Proteomic databases

PaxDbiF1LQ48.
PeptideAtlasiF1LQ48.
PRIDEiF1LQ48.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027425; ENSRNOP00000027425; ENSRNOG00000020235. [F1LQ48-1]
ENSRNOT00000057034; ENSRNOP00000053867; ENSRNOG00000020235. [F1LQ48-2]
GeneIDi80846.
KEGGirno:80846.
UCSCiRGD:1359551. rat.

Organism-specific databases

CTDi3191.
RGDi71059. Hnrnpl.

Phylogenomic databases

eggNOGiKOG1456. Eukaryota.
ENOG410XQHN. LUCA.
GeneTreeiENSGT00550000074508.
HOGENOMiHOG000293298.
HOVERGENiHBG058843.
InParanoidiF1LQ48.
KOiK13159.
OMAiPYEGRRM.
OrthoDBiEOG7HMS2K.
TreeFamiTF354318.

Enzyme and pathway databases

ReactomeiR-RNO-72163. mRNA Splicing - Major Pathway.

Gene expression databases

ExpressionAtlasiF1LQ48. baseline and differential.

Family and domain databases

Gene3Di3.30.70.330. 4 hits.
InterProiIPR006536. HnRNP-L/PTB.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 3 hits.
TIGRFAMsiTIGR01649. hnRNP-L_PTB. 2 hits.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Natural antisense transcript stabilizes inducible nitric oxide synthase messenger RNA in rat hepatocytes."
    Matsui K., Nishizawa M., Ozaki T., Kimura T., Hashimoto I., Yamada M., Kaibori M., Kamiyama Y., Ito S., Okumura T.
    Hepatology 47:686-697(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, INTERACTION WITH ELAVL1.
    Strain: WistarImported.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: OvaryImported.
  4. "The signature of the five-stranded vRRM fold defined by functional, structural and computational analysis of the hnRNP L protein."
    Blatter M., Dunin-Horkawicz S., Grishina I., Maris C., Thore S., Maier T., Bindereif A., Bujnicki J.M., Allain F.H.
    J. Mol. Biol. 427:3001-3022(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 408-623, X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 31-245, DOMAIN, RNA-BINDING.

Entry informationi

Entry nameiHNRPL_RAT
AccessioniPrimary (citable) accession number: F1LQ48
Secondary accession number(s): F1LPP9, Q5U1Y5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 11, 2016
Last sequence update: April 3, 2013
Last modified: July 6, 2016
This is version 44 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.