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Protein

Heterogeneous nuclear ribonucleoprotein L

Gene

HNRNPL

Organism
Homo sapiens (Human)
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.1 Publication

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB
  3. RNA binding Source: ProtInc
  4. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA splicing, via spliceosome Source: Reactome
  3. RNA processing Source: ProtInc
  4. RNA splicing Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Heterogeneous nuclear ribonucleoprotein L
Short name:
hnRNP L
Gene namesi
Name:HNRNPL
Synonyms:HNRPL
ORF Names:P/OKcl.14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:5045. HNRNPL.

Subcellular locationi

Nucleusnucleoplasm 1 Publication. Cytoplasm 1 Publication
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: UniProtKB
  3. membrane Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. nucleus Source: MGI
  6. pronucleus Source: Ensembl
  7. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi105 – 1051H → A: 6-fold decrease in RNA-binding affinity. 1 Publication
Mutagenesisi132 – 1321V → A: 4-fold increase in RNA-binding affinity. 1 Publication
Mutagenesisi141 – 1411L → A: 15-fold decrease in RNA-binding affinity; when associated with A-174. 1 Publication
Mutagenesisi172 – 1721N → A: 1-fold increase in RNA-binding affinity. 1 Publication
Mutagenesisi174 – 1741S → A: 15-fold decrease in RNA-binding affinity; when associated with A-174. 1 Publication
Mutagenesisi504 – 5041H → A: Significant decrease in RNA-binding affinity. 1 Publication
Mutagenesisi506 – 5061F → A: Significant decrease in RNA-binding affinity. 1 Publication

Organism-specific databases

PharmGKBiPA162391389.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 589589Heterogeneous nuclear ribonucleoprotein LPRO_0000081862Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521Phosphoserine3 Publications
Modified residuei101 – 1011Phosphoserine1 Publication
Modified residuei185 – 1851Phosphoserine2 Publications
Modified residuei269 – 2691N6-acetyllysine1 Publication
Modified residuei291 – 2911Phosphoserine1 Publication
Modified residuei298 – 2981Phosphoserine3 Publications
Modified residuei544 – 5441Phosphoserine; by CaMK41 Publication

Post-translational modificationi

Several isoelectric forms of the L protein are probably the results of post-translational modifications.
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.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP14866.
PaxDbiP14866.
PRIDEiP14866.

2D gel databases

REPRODUCTION-2DPAGEIPI00027834.
SWISS-2DPAGEP14866.

PTM databases

PhosphoSiteiP14866.

Expressioni

Gene expression databases

BgeeiP14866.
CleanExiHS_HNRNPL.
ExpressionAtlasiP14866. baseline and differential.
GenevestigatoriP14866.

Organism-specific databases

HPAiCAB016326.
HPA051748.

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 SETD2.4 Publications

Protein-protein interaction databases

BioGridi109432. 83 interactions.
DIPiDIP-36355N.
IntActiP14866. 30 interactions.
MINTiMINT-1422378.
STRINGi9606.ENSP00000221419.

Structurei

Secondary structure

1
589
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi102 – 1087Combined sources
Helixi115 – 1228Combined sources
Helixi123 – 1253Combined sources
Beta strandi128 – 1347Combined sources
Turni135 – 1384Combined sources
Beta strandi139 – 1468Combined sources
Helixi147 – 15913Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi167 – 1737Combined sources
Beta strandi382 – 3876Combined sources
Turni391 – 3933Combined sources
Helixi396 – 4038Combined sources
Turni404 – 4063Combined sources
Beta strandi409 – 4146Combined sources
Beta strandi421 – 4288Combined sources
Helixi429 – 43911Combined sources
Beta strandi450 – 4534Combined sources
Beta strandi472 – 4765Combined sources
Helixi488 – 4914Combined sources
Beta strandi501 – 5088Combined sources
Helixi514 – 52411Combined sources
Beta strandi530 – 5345Combined sources
Beta strandi543 – 5486Combined sources
Helixi552 – 56211Combined sources
Beta strandi572 – 5743Combined sources
Beta strandi579 – 5824Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3R27X-ray2.04A/B90-180[»]
3TO8X-ray1.82A380-589[»]
ProteinModelPortaliP14866.
SMRiP14866. Positions 97-290, 379-582.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini102 – 17675RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini193 – 27078RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini382 – 47897RRM 3PROSITE-ProRule annotationAdd
BLAST
Domaini495 – 58389RRM 4PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 8951Gly-richAdd
BLAST
Compositional biasi335 – 38248Pro-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 (PubMed:23782695).1 Publication

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG326285.
GeneTreeiENSGT00550000074508.
HOGENOMiHOG000293298.
HOVERGENiHBG105786.
InParanoidiP14866.
KOiK13159.
OMAiPYEGRRM.
OrthoDBiEOG7HMS2K.
PhylomeDBiP14866.
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]
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
TIGRFAMsiTIGR01649. hnRNP-L_PTB. 1 hit.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P14866-1) [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 QPDEQRRRSG AMVKMAAAGG GGGGGRYYGG
60 70 80 90 100
GSEGGRAPKR LKTDNAGDQH GGGGGGGGGA GAAGGGGGGE NYDDPHKTPA
110 120 130 140 150
SPVVHIRGLI DGVVEADLVE ALQEFGPISY VVVMPKKRQA LVEFEDVLGA
160 170 180 190 200
CNAVNYAADN QIYIAGHPAF VNYSTSQKIS RPGDSDDSRS VNSVLLFTIL
210 220 230 240 250
NPIYSITTDV LYTICNPCGP VQRIVIFRKN GVQAMVEFDS VQSAQRAKAS
260 270 280 290 300
LNGADIYSGC CTLKIEYAKP TRLNVFKNDQ DTWDYTNPNL SGQGDPGSNP
310 320 330 340 350
NKRQRQPPLL GDHPAEYGGP HGGYHSHYHD EGYGPPPPHY EGRRMGPPVG
360 370 380 390 400
GHRRGPSRYG PQYGHPPPPP PPPEYGPHAD SPVLMVYGLD QSKMNCDRVF
410 420 430 440 450
NVFCLYGNVE KVKFMKSKPG AAMVEMADGY AVDRAITHLN NNFMFGQKLN
460 470 480 490 500
VCVSKQPAIM PGQSYGLEDG SCSYKDFSES RNNRFSTPEQ AAKNRIQHPS
510 520 530 540 550
NVLHFFNAPL EVTEENFFEI CDELGVKRPS SVKVFSGKSE RSSSGLLEWE
560 570 580
SKSDALETLG FLNHYQMKNP NGPYPYTLKL CFSTAQHAS
Length:589
Mass (Da):64,133
Last modified:November 25, 2008 - v2
Checksum:i31EEB51AF1C65F83
GO
Isoform 2 (identifier: P14866-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.

Show »
Length:456
Mass (Da):50,561
Checksum:i59DD6B10F1F41E68
GO

Sequence cautioni

The sequence CAA34261.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti396 – 3961C → G in BAB18649. (PubMed:11280764)Curated
Sequence conflicti396 – 3961C → G in CAA34261. (PubMed:2687284)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 133133Missing in isoform 2. 1 PublicationVSP_044301Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB044547 mRNA. Translation: BAB18649.1.
AK292115 mRNA. Translation: BAF84804.1.
AC008982 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW56828.1.
X16135 mRNA. Translation: CAA34261.1. Different initiation.
CCDSiCCDS33015.1. [P14866-1]
CCDS33016.1. [P14866-2]
PIRiA33616.
RefSeqiNP_001005335.1. NM_001005335.1. [P14866-2]
NP_001524.2. NM_001533.2. [P14866-1]
UniGeneiHs.644906.

Genome annotation databases

EnsembliENST00000221419; ENSP00000221419; ENSG00000104824. [P14866-1]
ENST00000600873; ENSP00000470231; ENSG00000104824. [P14866-2]
GeneIDi3191.
KEGGihsa:3191.
UCSCiuc002ojk.3. human. [P14866-2]
uc021uuh.1. human. [P14866-1]

Polymorphism databases

DMDMi215274006.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB044547 mRNA. Translation: BAB18649.1.
AK292115 mRNA. Translation: BAF84804.1.
AC008982 Genomic DNA. No translation available.
CH471126 Genomic DNA. Translation: EAW56828.1.
X16135 mRNA. Translation: CAA34261.1. Different initiation.
CCDSiCCDS33015.1. [P14866-1]
CCDS33016.1. [P14866-2]
PIRiA33616.
RefSeqiNP_001005335.1. NM_001005335.1. [P14866-2]
NP_001524.2. NM_001533.2. [P14866-1]
UniGeneiHs.644906.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3R27X-ray2.04A/B90-180[»]
3TO8X-ray1.82A380-589[»]
ProteinModelPortaliP14866.
SMRiP14866. Positions 97-290, 379-582.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109432. 83 interactions.
DIPiDIP-36355N.
IntActiP14866. 30 interactions.
MINTiMINT-1422378.
STRINGi9606.ENSP00000221419.

PTM databases

PhosphoSiteiP14866.

Polymorphism databases

DMDMi215274006.

2D gel databases

REPRODUCTION-2DPAGEIPI00027834.
SWISS-2DPAGEP14866.

Proteomic databases

MaxQBiP14866.
PaxDbiP14866.
PRIDEiP14866.

Protocols and materials databases

DNASUi3191.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221419; ENSP00000221419; ENSG00000104824. [P14866-1]
ENST00000600873; ENSP00000470231; ENSG00000104824. [P14866-2]
GeneIDi3191.
KEGGihsa:3191.
UCSCiuc002ojk.3. human. [P14866-2]
uc021uuh.1. human. [P14866-1]

Organism-specific databases

CTDi3191.
GeneCardsiGC19M039327.
H-InvDBHIX0174642.
HGNCiHGNC:5045. HNRNPL.
HPAiCAB016326.
HPA051748.
MIMi164021. gene.
603083. gene.
neXtProtiNX_P14866.
PharmGKBiPA162391389.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG326285.
GeneTreeiENSGT00550000074508.
HOGENOMiHOG000293298.
HOVERGENiHBG105786.
InParanoidiP14866.
KOiK13159.
OMAiPYEGRRM.
OrthoDBiEOG7HMS2K.
PhylomeDBiP14866.
TreeFamiTF354318.

Enzyme and pathway databases

ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiHNRNPL. human.
GeneWikiiHNRNPL.
GenomeRNAii3191.
NextBioi12694.
PROiP14866.
SOURCEiSearch...

Gene expression databases

BgeeiP14866.
CleanExiHS_HNRNPL.
ExpressionAtlasiP14866. baseline and differential.
GenevestigatoriP14866.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular basis of T cell-mediated recognition of pancreatic cancer cells."
    Ito M., Shichijo S., Tsuda N., Ochi M., Harashima N., Saito N., Itoh K.
    Cancer Res. 61:2038-2046(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Pancreatic cancer.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Synovium.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "A novel heterogeneous nuclear RNP protein with a unique distribution on nascent transcripts."
    Pinol-Roma S., Swanson M.S., Gall J.G., Dreyfuss G.
    J. Cell Biol. 109:2575-2587(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-589 (ISOFORM 1).
  6. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 67-76; 199-215; 218-233; 386-403; 425-448 AND 549-558, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  7. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
    Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
    Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Keratinocyte.
  8. "Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like repressor element in the AP-endonuclease 1 promoter."
    Kuninger D.T., Izumi T., Papaconstantinou J., Mitra S.
    Nucleic Acids Res. 30:823-829(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH APEX1.
  9. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Regulation of CD45 alternative splicing by heterogeneous ribonucleoprotein, hnRNPLL."
    Oberdoerffer S., Moita L.F., Neems D., Freitas R.P., Hacohen N., Rao A.
    Science 321:686-691(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HNRNPLL.
  12. "Heterogeneous nuclear ribonucleoprotein L is a subunit of human KMT3a/Set2 complex required for H3 Lys-36 trimethylation activity in vivo."
    Yuan W., Xie J., Long C., Erdjument-Bromage H., Ding X., Zheng Y., Tempst P., Chen S., Zhu B., Reinberg D.
    J. Biol. Chem. 284:15701-15707(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SETD2.
  13. "Auto- and cross-regulation of the hnRNP L proteins by alternative splicing."
    Rossbach O., Hung L.H., Schreiner S., Grishina I., Heiner M., Hui J., Bindereif A.
    Mol. Cell. Biol. 29:1442-1451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, MISCELLANEOUS.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-185 AND SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-101; SER-185; SER-291 AND SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "A conserved serine of heterogeneous nuclear ribonucleoprotein L (hnRNP L) mediates depolarization-regulated alternative splicing of potassium channels."
    Liu G., Razanau A., Hai Y., Yu J., Sohail M., Lobo V.G., Chu J., Kung S.K., Xie J.
    J. Biol. Chem. 287:22709-22716(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-544.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Crystal structures and RNA-binding properties of the RNA recognition motifs of heterogeneous nuclear ribonucleoprotein L: insights into its roles in alternative splicing regulation."
    Zhang W., Zeng F., Liu Y., Zhao Y., Lv H., Niu L., Teng M., Li X.
    J. Biol. Chem. 288:22636-22649(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 90-180, X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 380-589, RRM DOMAINS, MUTAGENESIS OF HIS-105; VAL-132; LEU-141; ASN-172; SER-174; HIS-504 AND PHE-506.

Entry informationi

Entry nameiHNRPL_HUMAN
AccessioniPrimary (citable) accession number: P14866
Secondary accession number(s): A6ND69, A6NIT8, Q9H3P3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 25, 2008
Last modified: January 7, 2015
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Excess hnRNP L activates NMD of its own mRNA by promoting the inclusion of a 'poison exon' containing a premature stop codon and leading to nonsense-mediated decay. It also cross-regulates inclusion of an analogous 'poison exon' in the hnRNP L-like pre-mRNA (PubMed:19124611).1 Publication

Keywords - Technical termi

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

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.