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P14866

- HNRPL_HUMAN

UniProt

P14866 - HNRPL_HUMAN

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Protein
Heterogeneous nuclear ribonucleoprotein L
Gene
HNRNPL, HNRPL, P/OKcl.14
Organism
Homo sapiens (Human)
Status
Reviewed - 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. RNA binding Source: ProtInc
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. RNA processing Source: ProtInc
  2. RNA splicing Source: Reactome
  3. gene expression Source: Reactome
  4. mRNA splicing, via spliceosome 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. Cytoplasm
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: UniProt
  3. nucleoplasm Source: Reactome
  4. nucleus Source: MGI
  5. 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 L
PRO_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.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP14866.
PaxDbiP14866.
PRIDEiP14866.

2D gel databases

REPRODUCTION-2DPAGEIPI00027834.
SWISS-2DPAGEP14866.

PTM databases

PhosphoSiteiP14866.

Expressioni

Gene expression databases

ArrayExpressiP14866.
BgeeiP14866.
CleanExiHS_HNRNPL.
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. 78 interactions.
DIPiDIP-36355N.
IntActiP14866. 30 interactions.
MINTiMINT-1422378.
STRINGi9606.ENSP00000221419.

Structurei

Secondary structure

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

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 8951Gly-rich
Add
BLAST
Compositional biasi335 – 38248Pro-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 (1 Publication).1 Publication

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG326285.
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

MSRRLLPRAE KRRRRLEQRQ QPDEQRRRSG AMVKMAAAGG GGGGGRYYGG    50
GSEGGRAPKR LKTDNAGDQH GGGGGGGGGA GAAGGGGGGE NYDDPHKTPA 100
SPVVHIRGLI DGVVEADLVE ALQEFGPISY VVVMPKKRQA LVEFEDVLGA 150
CNAVNYAADN QIYIAGHPAF VNYSTSQKIS RPGDSDDSRS VNSVLLFTIL 200
NPIYSITTDV LYTICNPCGP VQRIVIFRKN GVQAMVEFDS VQSAQRAKAS 250
LNGADIYSGC CTLKIEYAKP TRLNVFKNDQ DTWDYTNPNL SGQGDPGSNP 300
NKRQRQPPLL GDHPAEYGGP HGGYHSHYHD EGYGPPPPHY EGRRMGPPVG 350
GHRRGPSRYG PQYGHPPPPP PPPEYGPHAD SPVLMVYGLD QSKMNCDRVF 400
NVFCLYGNVE KVKFMKSKPG AAMVEMADGY AVDRAITHLN NNFMFGQKLN 450
VCVSKQPAIM PGQSYGLEDG SCSYKDFSES RNNRFSTPEQ AAKNRIQHPS 500
NVLHFFNAPL EVTEENFFEI CDELGVKRPS SVKVFSGKSE RSSSGLLEWE 550
SKSDALETLG FLNHYQMKNP NGPYPYTLKL CFSTAQHAS 589
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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 133133Missing in isoform 2.
VSP_044301Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti396 – 3961C → G in BAB18649. 1 Publication
Sequence conflicti396 – 3961C → G in CAA34261. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS33015.1. [P14866-1 ]
CCDS33016.1. [P14866-2 ]
PIRi A33616.
RefSeqi NP_001005335.1. NM_001005335.1. [P14866-2 ]
NP_001524.2. NM_001533.2. [P14866-1 ]
UniGenei Hs.644906.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3R27 X-ray 2.04 A/B 90-180 [» ]
3TO8 X-ray 1.82 A 380-589 [» ]
ProteinModelPortali P14866.
SMRi P14866. Positions 97-290, 379-582.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109432. 78 interactions.
DIPi DIP-36355N.
IntActi P14866. 30 interactions.
MINTi MINT-1422378.
STRINGi 9606.ENSP00000221419.

PTM databases

PhosphoSitei P14866.

Polymorphism databases

DMDMi 215274006.

2D gel databases

REPRODUCTION-2DPAGE IPI00027834.
SWISS-2DPAGE P14866.

Proteomic databases

MaxQBi P14866.
PaxDbi P14866.
PRIDEi P14866.

Protocols and materials databases

DNASUi 3191.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000221419 ; ENSP00000221419 ; ENSG00000104824 . [P14866-1 ]
ENST00000600873 ; ENSP00000470231 ; ENSG00000104824 . [P14866-2 ]
GeneIDi 3191.
KEGGi hsa:3191.
UCSCi uc002ojk.3. human. [P14866-2 ]
uc021uuh.1. human. [P14866-1 ]

Organism-specific databases

CTDi 3191.
GeneCardsi GC19M039327.
H-InvDB HIX0174642.
HGNCi HGNC:5045. HNRNPL.
HPAi CAB016326.
HPA051748.
MIMi 164021. gene.
603083. gene.
neXtProti NX_P14866.
PharmGKBi PA162391389.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG326285.
HOGENOMi HOG000293298.
HOVERGENi HBG105786.
InParanoidi P14866.
KOi K13159.
OMAi PYEGRRM.
OrthoDBi EOG7HMS2K.
PhylomeDBi P14866.
TreeFami TF354318.

Enzyme and pathway databases

Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi HNRNPL. human.
GeneWikii HNRNPL.
GenomeRNAii 3191.
NextBioi 12694.
PROi P14866.
SOURCEi Search...

Gene expression databases

ArrayExpressi P14866.
Bgeei P14866.
CleanExi HS_HNRNPL.
Genevestigatori P14866.

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. "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: September 3, 2014
This is version 157 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 (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

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