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Q8R081 (HNRPL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Heterogeneous nuclear ribonucleoprotein L

Short name=hnRNP L
Gene names
Name:Hnrnpl
Synonyms:Hnrpl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length586 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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.

Subunit structure

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.

Subcellular location

Nucleusnucleoplasm By similarity. Cytoplasm By similarity. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

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 By similarity.

Post-translational modification

Phosphorylation at Ser-541 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.

Sequence similarities

Contains 4 RRM (RNA recognition motif) domains.

Sequence caution

The sequence AAH27206.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 586586Heterogeneous nuclear ribonucleoprotein L
PRO_0000081863

Regions

Domain99 – 17375RRM 1
Domain190 – 26778RRM 2
Domain379 – 47698RRM 3
Domain492 – 58089RRM 4
Compositional bias39 – 8648Gly-rich
Compositional bias332 – 37948Pro-rich

Amino acid modifications

Modified residue981Phosphoserine By similarity
Modified residue1821Phosphoserine By similarity
Modified residue2661N6-acetyllysine By similarity
Modified residue2881Phosphoserine By similarity
Modified residue2951Phosphoserine By similarity
Modified residue5411Phosphoserine; by CaMK4 By similarity

Experimental info

Sequence conflict3881Q → E in BAA24237. Ref.2

Secondary structure

................................... 586
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8R081 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: BB56D3D6A8553F7E

FASTA58663,964
        10         20         30         40         50         60 
MSRRLLPRAE KRRRRLEQRQ QPDEQLRRAG AMVKMAAAGG GGGGGRYYGG GNEGGRAPKR 

        70         80         90        100        110        120 
LKTENAGDQH GGGGGGGSGA AGGGGGENYD DPHKTPASPV VHIRGLIDGV VEADLVEALQ 

       130        140        150        160        170        180 
EFGPISYVVV MPKKRQALVE FEDVLGACNA VNYAADNQIY IAGHPAFVNY STSQKISRPG 

       190        200        210        220        230        240 
DSDDSRSVNS VLLFTILNPI YSITTDVLYT ICNPCGPVQR IVIFRKNGVQ AMVEFDSVQS 

       250        260        270        280        290        300 
AQRAKASLNG ADIYSGCCTL KIEYAKPTRL NVFKNDQDTW DYTNPNLSGQ GDPGSNPNKR 

       310        320        330        340        350        360 
QRQPPLLGDH PAEYGGPHGG YHSHYHDEGY GPPPPHYEGR RMGPPVGGHR RGPSRYGPQY 

       370        380        390        400        410        420 
GHPPPPPPPP DYGPHADSPV LMVYGLDQSK MNCDRVFNVF CLYGNVEKVK FMKSKPGAAM 

       430        440        450        460        470        480 
VEMADGYAVD RAITHLNNNF MFGQKMNVCV SKQPAIMPGQ SYGLEDGSCS YKDFSESRNN 

       490        500        510        520        530        540 
RFSTPEQAAK NRIQHPSNVL HFFNAPLEVT EENFFEICDE LGVKRPTSVK VFSGKSERSS 

       550        560        570        580 
SGLLEWDSKS DALETLGFLN HYQMKNPNGP YPYTLKLCFS TAQHAS 

« Hide

References

« Hide 'large scale' references
[1]"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].
Strain: FVB/N.
Tissue: Colon and Salivary gland.
[2]"Mouse ribonucleoprotein."
Sakai N., Saitou Y., Toyota T.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 388-586.
[3]Lubec G., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 396-408 AND 566-576.
Tissue: Brain.
[4]"Crystal structure of a heterogeneous nuclear ribonucleoprotein l (hnrpl) from Mus musculus at 1.60 a resolution."
Joint center for structural genomics (JCSG)
Submitted (NOV-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 376-579.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC027206 mRNA. Translation: AAH27206.1. Different initiation.
BC030461 mRNA. Translation: AAH30461.1.
BC099683 mRNA. Translation: AAH99683.1.
AB009392 mRNA. Translation: BAA24237.1.
CCDSCCDS39864.2.
RefSeqNP_796275.3. NM_177301.5.
XP_006539621.1. XM_006539558.1.
UniGeneMm.9043.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3S01X-ray2.15A376-586[»]
3TYTX-ray1.60A376-579[»]
ProteinModelPortalQ8R081.
SMRQ8R081. Positions 94-287, 376-579.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200360. 4 interactions.
IntActQ8R081. 6 interactions.
MINTMINT-4097731.

PTM databases

PhosphoSiteQ8R081.

2D gel databases

REPRODUCTION-2DPAGEQ8R081.

Proteomic databases

MaxQBQ8R081.
PaxDbQ8R081.
PRIDEQ8R081.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000038572; ENSMUSP00000049407; ENSMUSG00000015165.
ENSMUST00000174548; ENSMUSP00000133728; ENSMUSG00000015165.
GeneID15388.
KEGGmmu:15388.
UCSCuc009fzz.2. mouse.

Organism-specific databases

CTD3191.
MGIMGI:104816. Hnrnpl.

Phylogenomic databases

eggNOGNOG326285.
GeneTreeENSGT00550000074508.
HOGENOMHOG000293298.
HOVERGENHBG105786.
KOK13159.
OrthoDBEOG7HMS2K.
PhylomeDBQ8R081.

Gene expression databases

ArrayExpressQ8R081.
BgeeQ8R081.
CleanExMM_HNRNPL.
GenevestigatorQ8R081.

Family and domain databases

Gene3D3.30.70.330. 4 hits.
InterProIPR006536. HnRNP-L_PTB.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
SMARTSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsTIGR01649. hnRNP-L_PTB. 1 hit.
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHNRNPL. mouse.
NextBio288066.
PROQ8R081.
SOURCESearch...

Entry information

Entry nameHNRPL_MOUSE
AccessionPrimary (citable) accession number: Q8R081
Secondary accession number(s): O54789, Q499X2, Q8K0S7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot