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Q8R081

- HNRPL_MOUSE

UniProt

Q8R081 - HNRPL_MOUSE

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Protein

Heterogeneous nuclear ribonucleoprotein L

Gene

Hnrnpl

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. nucleotide binding Source: InterPro
  2. RNA binding Source: UniProtKB-KW
  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-KW
  2. nucleus Source: MGI
  3. pronucleus Source: MGI
  4. 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 LPRO_0000081863Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei98 – 981PhosphoserineBy similarity
Modified residuei182 – 1821PhosphoserineBy similarity
Modified residuei266 – 2661N6-acetyllysineBy similarity
Modified residuei288 – 2881PhosphoserineBy similarity
Modified residuei295 – 2951PhosphoserineBy similarity
Modified residuei541 – 5411Phosphoserine; by CaMK4By 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

BgeeiQ8R081.
CleanExiMM_HNRNPL.
ExpressionAtlasiQ8R081. baseline and differential.
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).By similarity

Protein-protein interaction databases

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

Structurei

Secondary structure

1
586
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.
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
Domaini379 – 47698RRM 3PROSITE-ProRule annotationAdd
BLAST
Domaini492 – 58089RRM 4PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 8648Gly-richAdd
BLAST
Compositional biasi332 – 37948Pro-richAdd
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).By similarity

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG326285.
GeneTreeiENSGT00550000074508.
HOGENOMiHOG000293298.
HOVERGENiHBG105786.
InParanoidiQ8R081.
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

        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 PAEYGGPHGG YHSHYHDEGY GPPPPHYEGR RMGPPVGGHR
360 370 380 390 400
RGPSRYGPQY GHPPPPPPPP DYGPHADSPV LMVYGLDQSK MNCDRVFNVF
410 420 430 440 450
CLYGNVEKVK FMKSKPGAAM VEMADGYAVD RAITHLNNNF MFGQKMNVCV
460 470 480 490 500
SKQPAIMPGQ SYGLEDGSCS YKDFSESRNN RFSTPEQAAK NRIQHPSNVL
510 520 530 540 550
HFFNAPLEVT EENFFEICDE LGVKRPTSVK VFSGKSERSS SGLLEWDSKS
560 570 580
DALETLGFLN HYQMKNPNGP YPYTLKLCFS TAQHAS
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.

Experimental Info

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

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.
InParanoidi Q8R081.
KOi K13159.
OrthoDBi EOG7HMS2K.
PhylomeDBi Q8R081.

Miscellaneous databases

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

Gene expression databases

Bgeei Q8R081.
CleanExi MM_HNRNPL.
ExpressionAtlasi Q8R081. baseline and differential.
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: October 29, 2014
This is version 109 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