P14866 (HNRPL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heterogeneous nuclear ribonucleoprotein L
Short name=hnRNP L

Gene names

Name:	HNRNPL
Synonyms:	HNRPL
ORF Names:	P/OKcl.14

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	589 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Is associated with most nascent transcripts including those of the landmark giant loops of amphibian lampbrush chromosomes. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter. Ref.8
Subunit structure	Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with HNRPLL. Interacts with APEX1; the interaction is DNA-dependent. Ref.8 Ref.9 Ref.11
Subcellular location	Nucleus › nucleoplasm. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.9
Post-translational modification	Several isoelectric forms of the L protein are probably the results of post-translational modifications.
Sequence similarities	Contains 3 RRM (RNA recognition motif) domains.
Sequence caution	The sequence CAA34261.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA splicing, via spliceosome Traceable author statement. Source: Reactome
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome ribonucleoprotein complex Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	RNA binding Traceable author statement Ref.5. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro transcription regulatory region DNA binding Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P14866-1)

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.

Isoform 2 (identifier: P14866-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 589

589

Heterogeneous nuclear ribonucleoprotein L

PRO_0000081862

Regions

Domain

102 – 176

75

RRM 1

Domain

193 – 270

78

RRM 2

Domain

382 – 456

75

RRM 3

Compositional bias

39 – 89

51

Gly-rich

Compositional bias

335 – 382

48

Pro-rich

Amino acid modifications

Modified residue

52

1

Phosphoserine Ref.10 Ref.13 Ref.15

Modified residue

101

1

Phosphoserine Ref.15

Modified residue

185

1

Phosphoserine Ref.13 Ref.15

Modified residue

269

1

N6-acetyllysine Ref.12

Modified residue

291

1

Phosphoserine Ref.15

Modified residue

298

1

Phosphoserine Ref.10 Ref.13 Ref.15

Modified residue

475

1

N6-acetyllysine Ref.12

Modified residue

552

1

N6-acetyllysine Ref.12

Natural variations

Alternative sequence

1 – 133

133

Missing in isoform 2.

VSP_044301

Experimental info

Sequence conflict

396

1

C → G in BAB18649. Ref.1

Sequence conflict

396

1

C → G in CAA34261. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

589

Helix Strand Turn

Details...

Beta strand

102 – 108

7

Helix

115 – 122

8

Helix

123 – 125

3

Beta strand

128 – 134

7

Turn

135 – 138

4

Beta strand

139 – 146

8

Helix

147 – 159

13

Beta strand

162 – 164

3

Beta strand

167 – 173

7

Beta strand

382 – 387

6

Turn

391 – 393

3

Helix

396 – 403

8

Turn

404 – 406

3

Beta strand

409 – 414

6

Beta strand

421 – 428

8

Helix

429 – 439

11

Beta strand

450 – 453

4

Beta strand

472 – 476

5

Helix

488 – 491

4

Beta strand

501 – 508

8

Helix

514 – 524

11

Beta strand

530 – 534

5

Beta strand

543 – 548

6

Helix

552 – 562

11

Beta strand

572 – 574

3

Beta strand

579 – 582

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 31EEB51AF1C65F83	FASTA	589	64,133
	10 20 30 40 50 60 MSRRLLPRAE KRRRRLEQRQ QPDEQRRRSG AMVKMAAAGG GGGGGRYYGG GSEGGRAPKR 70 80 90 100 110 120 LKTDNAGDQH GGGGGGGGGA GAAGGGGGGE NYDDPHKTPA SPVVHIRGLI DGVVEADLVE 130 140 150 160 170 180 ALQEFGPISY VVVMPKKRQA LVEFEDVLGA CNAVNYAADN QIYIAGHPAF VNYSTSQKIS 190 200 210 220 230 240 RPGDSDDSRS VNSVLLFTIL NPIYSITTDV LYTICNPCGP VQRIVIFRKN GVQAMVEFDS 250 260 270 280 290 300 VQSAQRAKAS LNGADIYSGC CTLKIEYAKP TRLNVFKNDQ DTWDYTNPNL SGQGDPGSNP 310 320 330 340 350 360 NKRQRQPPLL GDHPAEYGGP HGGYHSHYHD EGYGPPPPHY EGRRMGPPVG GHRRGPSRYG 370 380 390 400 410 420 PQYGHPPPPP PPPEYGPHAD SPVLMVYGLD QSKMNCDRVF NVFCLYGNVE KVKFMKSKPG 430 440 450 460 470 480 AAMVEMADGY AVDRAITHLN NNFMFGQKLN VCVSKQPAIM PGQSYGLEDG SCSYKDFSES 490 500 510 520 530 540 RNNRFSTPEQ AAKNRIQHPS NVLHFFNAPL EVTEENFFEI CDELGVKRPS SVKVFSGKSE 550 560 570 580 RSSSGLLEWE SKSDALETLG FLNHYQMKNP NGPYPYTLKL CFSTAQHAS
	Isoform 2 [UniParc]. Checksum: 59DD6B10F1F41E68	FASTA	456	50,561
	10 20 30 40 50 60 MPKKRQALVE FEDVLGACNA VNYAADNQIY IAGHPAFVNY STSQKISRPG DSDDSRSVNS 70 80 90 100 110 120 VLLFTILNPI YSITTDVLYT ICNPCGPVQR IVIFRKNGVQ AMVEFDSVQS AQRAKASLNG 130 140 150 160 170 180 ADIYSGCCTL KIEYAKPTRL NVFKNDQDTW DYTNPNLSGQ GDPGSNPNKR QRQPPLLGDH 190 200 210 220 230 240 PAEYGGPHGG YHSHYHDEGY GPPPPHYEGR RMGPPVGGHR RGPSRYGPQY GHPPPPPPPP 250 260 270 280 290 300 EYGPHADSPV LMVYGLDQSK MNCDRVFNVF CLYGNVEKVK FMKSKPGAAM VEMADGYAVD 310 320 330 340 350 360 RAITHLNNNF MFGQKLNVCV SKQPAIMPGQ SYGLEDGSCS YKDFSESRNN RFSTPEQAAK 370 380 390 400 410 420 NRIQHPSNVL HFFNAPLEVT EENFFEICDE LGVKRPSSVK VFSGKSERSS SGLLEWESKS 430 440 450 DALETLGFLN HYQMKNPNGP YPYTLKLCFS TAQHAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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, 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]	"Molecular composition of IMP1 ribonucleoprotein granules." Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C. Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-298, MASS SPECTROMETRY. 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 HNRPLL.
[12]	"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; LYS-475 AND LYS-552, MASS SPECTROMETRY.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00027834.

PIR

A33616.

RefSeq

NP_001005335.1. NM_001005335.1.
NP_001524.2. NM_001533.2.

UniGene

Hs.644906.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3R27	X-ray	2.04	A/B	90-180	[»]
3TO8	X-ray	1.82	A	380-589	[»]

ProteinModelPortal

P14866.

ModBase

Search...

Protein-protein interaction databases

IntAct

P14866. 28 interactions.

MINT

MINT-1422378.

STRING

9606.ENSP00000221419.

PTM databases

PhosphoSite

P14866.

Polymorphism databases

DMDM

215274006.

2D gel databases

REPRODUCTION-2DPAGE

IPI00027834.

SWISS-2DPAGE

P14866.

Proteomic databases

PaxDb

P14866.

PRIDE

P14866.

Protocols and materials databases

DNASU

3191.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000221419; ENSP00000221419; ENSG00000104824.
ENST00000388750; ENSP00000373402; ENSG00000104824.
ENST00000600873; ENSP00000470231; ENSG00000104824.

GeneID

3191.

KEGG

hsa:3191.

UCSC

uc021uuh.1. human.

Organism-specific databases

CTD

3191.

GeneCards

GC19M039327.

H-InvDB

HIX0174642.

HGNC

HGNC:5045. HNRNPL.

HPA

CAB016326.

MIM

164021. gene.
603083. gene.

neXtProt

NX_P14866.

PharmGKB

PA162391389.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG326285.

HOGENOM

HOG000293298.

HOVERGEN

HBG105786.

InParanoid

P14866.

KO

K13159.

OMA

RPTSVKV.

OrthoDB

EOG4RFKSD.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P14866.

Bgee

P14866.

CleanEx

HS_HNRNPL.

Genevestigator

P14866.

GermOnline

ENSG00000104824. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 4 hits.

InterPro

IPR006536. HnRNP-L_PTB.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

SMART

SM00360. RRM. 3 hits.
[Graphical view]

TIGRFAMs

TIGR01649. hnRNP-L_PTB. 1 hit.

PROSITE

PS50102. RRM. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HNRNPL. human.

GenomeRNAi

3191.

NextBio

12694.

SOURCE

Search...

Entry information

Entry name

HNRPL_HUMAN

Accession

Primary (citable) accession number: P14866
Secondary accession number(s): A6ND69, A6NIT8, Q9H3P3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 142 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.