HNRNPL
entrez
3191
canonical
uniprot
P14866
canonical
ensembl
ENSG00000104824
resolver
ensembl
ENSG00000282947
resolver
ensp
ENSP00000221419
resolver
ensp
ENSP00000469349
resolver
ensp
ENSP00000470231
resolver
ensp
ENSP00000497920
resolver
ensp
ENSP00000586414
resolver
ensp
ENSP00000725417
resolver
enst
ENST00000647557
resolver
genesymbol
HNRNPL
resolver
genesymbol_syn
HNRPL
resolver
hgnc
HGNC:5045
resolver
uniprot
A0A3B3ITJ4
resolver
uniprot
A6ND69
resolver
uniprot
A6NIT8
resolver
uniprot
Q6NTA2
resolver
uniprot
Q9H3P3
resolver
uniprot_entry
A0A3B3ITJ4_HUMAN
resolver
uniprot_entry
HNRPL_HUMAN
resolver
uniprot_entry
Q6NTA2_HUMAN
resolver
uniprot_sec
A6ND69
resolver
uniprot_sec
A6NIT8
resolver
uniprot_sec
Q9H3P3
resolver
amino_acid_sequence
MSRRLLPRAEKRRRRLEQRQQPDEQRRRSGAMVKMAAAGGGGGGGRYYGGGSEGGRAPKRLKTDNAGDQHGGGGGGGGGAGAAGGGGGGENYDDPHKTPASPVVHIRGLIDGVVEADLVEALQEFGPISYVVVMPKKRQALVEFEDVLGACNAVNYAADNQIYIAGHPAFVNYSTSQKISRPGDSDDSRSVNSVLLFTILNPIYSITTDVLYTICNPCGPVQRIVIFRKNGVQAMVEFDSVQSAQRAKASLNGADIYSGCCTLKIEYAKPTRLNVFKNDQDTWDYTNPNLSGQGDPGSNPNKRQRQPPLLGDHPAEYGGPHGGYHSHYHDEGYGPPPPHYEGRRMGPPVGGHRRGPSRYGPQYGHPPPPPPPPEYGPHADSPVLMVYGLDQSKMNCDRVFNVFCLYGNVEKVKFMKSKPGAAMVEMADGYAVDRAITHLNNNFMFGQKLNVCVSKQPAIMPGQSYGLEDGSCSYKDFSESRNNRFSTPEQAAKNRIQHPSNVLHFFNAPLEVTEENFFEICDELGVKRPSSVKVFSGKSERSSSGLLEWESKSDALETLGFLNHYQMKNPNGPYPYTLKLCFSTAQHAS
uniprot
proteins
function
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). As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPK and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (PubMed:33174841). Regulates alternative splicing of a core group of genes involved in neuronal differentiation, likely by mediating H3K36me3-coupled transcription elongation and co-transcriptional RNA processing via interaction with CHD8. {ECO:0000269|PubMed:11809897, ECO:0000269|PubMed:22570490, ECO:0000269|PubMed:25623890, ECO:0000269|PubMed:26051023, ECO:0000269|PubMed:2687284, ECO:0000269|PubMed:33174841, ECO:0000269|PubMed:36537238}.
uniprot
proteins
mass_dalton
64133
uniprot
proteins
mutagenesis
MUTAGEN 105; /note="H->A: 6-fold decrease in RNA-binding affinity."; /evidence="ECO:0000269|PubMed:23782695"; MUTAGEN 132; /note="V->A: 4-fold increase in RNA-binding affinity."; /evidence="ECO:0000269|PubMed:23782695"; MUTAGEN 141; /note="L->A: 15-fold decrease in RNA-binding affinity; when associated with A-174."; /evidence="ECO:0000269|PubMed:23782695"; MUTAGEN 172; /note="N->A: 1-fold increase in RNA-binding affinity."; /evidence="ECO:0000269|PubMed:23782695"; MUTAGEN 174; /note="S->A: 15-fold decrease in RNA-binding affinity; when associated with A-174."; /evidence="ECO:0000269|PubMed:23782695"; MUTAGEN 504; /note="H->A: Significant decrease in RNA-binding affinity."; /evidence="ECO:0000269|PubMed:23782695"; MUTAGEN 506; /note="F->A: Significant decrease in RNA-binding affinity."; /evidence="ECO:0000269|PubMed:23782695
uniprot
proteins
post_translational_modification
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}.; PTM: Ubiquitinated by the SCF-FBXO16 E3 ubiquitin ligase, leading to proteasomal degradation. {ECO:0000269|PubMed:34333526}.
uniprot
proteins
pubmed
11280764
uniprot
proteins
pubmed
11809897
uniprot
proteins
pubmed
1286667
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
17289661
uniprot
proteins
pubmed
18161049
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18669861
uniprot
proteins
pubmed
19124611
uniprot
proteins
pubmed
19332550
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22570490
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23782695
uniprot
proteins
pubmed
24164894
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25623890
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26051023
uniprot
proteins
pubmed
2687284
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
33174841
uniprot
proteins
pubmed
34333526
uniprot
proteins
pubmed
36537238
uniprot
proteins
sequence_length
589
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:2687284, ECO:0000305|PubMed:26051023, ECO:0000305|PubMed:36537238}. 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}.
uniprot
proteins