SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8R081

- HNRPL_MOUSE

UniProt

Q8R081 - HNRPL_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Heterogeneous nuclear ribonucleoprotein L
Gene
Hnrnpl, Hnrpl
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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.

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW
  2. nucleotide binding Source: InterPro
  3. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. mRNA processing Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein L
Short name:
hnRNP L
Gene namesi
Name:Hnrnpl
Synonyms:Hnrpl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:104816. Hnrnpl.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleoplasm Source: UniProtKB-SubCell
  3. nucleus Source: MGI
  4. pronucleus Source: MGI
  5. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 586586Heterogeneous nuclear ribonucleoprotein L
PRO_0000081863Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei98 – 981Phosphoserine By similarity
Modified residuei182 – 1821Phosphoserine By similarity
Modified residuei266 – 2661N6-acetyllysine By similarity
Modified residuei288 – 2881Phosphoserine By similarity
Modified residuei295 – 2951Phosphoserine By similarity
Modified residuei541 – 5411Phosphoserine; by CaMK4 By similarity

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8R081.
PaxDbiQ8R081.
PRIDEiQ8R081.

2D gel databases

REPRODUCTION-2DPAGEQ8R081.

PTM databases

PhosphoSiteiQ8R081.

Expressioni

Gene expression databases

ArrayExpressiQ8R081.
BgeeiQ8R081.
CleanExiMM_HNRNPL.
GenevestigatoriQ8R081.

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.

Protein-protein interaction databases

BioGridi200360. 4 interactions.
IntActiQ8R081. 6 interactions.
MINTiMINT-4097731.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi379 – 3846
Turni388 – 3903
Helixi393 – 4008
Turni401 – 4033
Beta strandi406 – 4116
Beta strandi419 – 4257
Helixi426 – 43611
Beta strandi447 – 4504
Beta strandi452 – 4554
Beta strandi469 – 4735
Helixi485 – 4884
Beta strandi498 – 5058
Helixi511 – 52111
Beta strandi527 – 5315
Beta strandi536 – 54510
Helixi549 – 55911
Beta strandi567 – 5715
Beta strandi576 – 5783

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S01X-ray2.15A376-586[»]
3TYTX-ray1.60A376-579[»]
ProteinModelPortaliQ8R081.
SMRiQ8R081. Positions 94-287, 376-579.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini99 – 17375RRM 1
Add
BLAST
Domaini190 – 26778RRM 2
Add
BLAST
Domaini379 – 47698RRM 3
Add
BLAST
Domaini492 – 58089RRM 4
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 8648Gly-rich
Add
BLAST
Compositional biasi332 – 37948Pro-rich
Add
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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG326285.
GeneTreeiENSGT00550000074508.
HOGENOMiHOG000293298.
HOVERGENiHBG105786.
KOiK13159.
OrthoDBiEOG7HMS2K.
PhylomeDBiQ8R081.

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]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsiTIGR01649. hnRNP-L_PTB. 1 hit.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R081-1 [UniParc]FASTAAdd to Basket

« Hide

MSRRLLPRAE KRRRRLEQRQ QPDEQLRRAG AMVKMAAAGG GGGGGRYYGG    50
GNEGGRAPKR LKTENAGDQH GGGGGGGSGA AGGGGGENYD DPHKTPASPV 100
VHIRGLIDGV VEADLVEALQ EFGPISYVVV MPKKRQALVE FEDVLGACNA 150
VNYAADNQIY IAGHPAFVNY STSQKISRPG DSDDSRSVNS VLLFTILNPI 200
YSITTDVLYT ICNPCGPVQR IVIFRKNGVQ AMVEFDSVQS AQRAKASLNG 250
ADIYSGCCTL KIEYAKPTRL NVFKNDQDTW DYTNPNLSGQ GDPGSNPNKR 300
QRQPPLLGDH PAEYGGPHGG YHSHYHDEGY GPPPPHYEGR RMGPPVGGHR 350
RGPSRYGPQY GHPPPPPPPP DYGPHADSPV LMVYGLDQSK MNCDRVFNVF 400
CLYGNVEKVK FMKSKPGAAM VEMADGYAVD RAITHLNNNF MFGQKMNVCV 450
SKQPAIMPGQ SYGLEDGSCS YKDFSESRNN RFSTPEQAAK NRIQHPSNVL 500
HFFNAPLEVT EENFFEICDE LGVKRPTSVK VFSGKSERSS SGLLEWDSKS 550
DALETLGFLN HYQMKNPNGP YPYTLKLCFS TAQHAS 586
Length:586
Mass (Da):63,964
Last modified:November 25, 2008 - v2
Checksum:iBB56D3D6A8553F7E
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti388 – 3881Q → E in BAA24237. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC027206 mRNA. Translation: AAH27206.1. Different initiation.
BC030461 mRNA. Translation: AAH30461.1.
BC099683 mRNA. Translation: AAH99683.1.
AB009392 mRNA. Translation: BAA24237.1.
CCDSiCCDS39864.2.
RefSeqiNP_796275.3. NM_177301.5.
XP_006539621.1. XM_006539558.1.
UniGeneiMm.9043.

Genome annotation databases

EnsembliENSMUST00000038572; ENSMUSP00000049407; ENSMUSG00000015165.
ENSMUST00000174548; ENSMUSP00000133728; ENSMUSG00000015165.
GeneIDi15388.
KEGGimmu:15388.
UCSCiuc009fzz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC027206 mRNA. Translation: AAH27206.1 . Different initiation.
BC030461 mRNA. Translation: AAH30461.1 .
BC099683 mRNA. Translation: AAH99683.1 .
AB009392 mRNA. Translation: BAA24237.1 .
CCDSi CCDS39864.2.
RefSeqi NP_796275.3. NM_177301.5.
XP_006539621.1. XM_006539558.1.
UniGenei Mm.9043.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3S01 X-ray 2.15 A 376-586 [» ]
3TYT X-ray 1.60 A 376-579 [» ]
ProteinModelPortali Q8R081.
SMRi Q8R081. Positions 94-287, 376-579.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200360. 4 interactions.
IntActi Q8R081. 6 interactions.
MINTi MINT-4097731.

PTM databases

PhosphoSitei Q8R081.

2D gel databases

REPRODUCTION-2DPAGE Q8R081.

Proteomic databases

MaxQBi Q8R081.
PaxDbi Q8R081.
PRIDEi Q8R081.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000038572 ; ENSMUSP00000049407 ; ENSMUSG00000015165 .
ENSMUST00000174548 ; ENSMUSP00000133728 ; ENSMUSG00000015165 .
GeneIDi 15388.
KEGGi mmu:15388.
UCSCi uc009fzz.2. mouse.

Organism-specific databases

CTDi 3191.
MGIi MGI:104816. Hnrnpl.

Phylogenomic databases

eggNOGi NOG326285.
GeneTreei ENSGT00550000074508.
HOGENOMi HOG000293298.
HOVERGENi HBG105786.
KOi K13159.
OrthoDBi EOG7HMS2K.
PhylomeDBi Q8R081.

Miscellaneous databases

ChiTaRSi HNRNPL. mouse.
NextBioi 288066.
PROi Q8R081.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8R081.
Bgeei Q8R081.
CleanExi MM_HNRNPL.
Genevestigatori Q8R081.

Family and domain databases

Gene3Di 3.30.70.330. 4 hits.
InterProi IPR006536. HnRNP-L_PTB.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
SMARTi SM00360. RRM. 3 hits.
[Graphical view ]
TIGRFAMsi TIGR01649. hnRNP-L_PTB. 1 hit.
PROSITEi PS50102. RRM. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiHNRPL_MOUSE
AccessioniPrimary (citable) accession number: Q8R081
Secondary accession number(s): O54789, Q499X2, Q8K0S7
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi