UniProt Accession

 HNRPL_HUMAN; P14866; A6ND69; A6NIT8; Q9H3P3 

Genbank Protein ID

 AB044547; AK292115; AC008982; CH471126; X16135 

Genbank Nucleotide ID

 BAB18649.1; BAF84804.1; EAW56828.1; CAA34261.1 

Protein Name

 Heterogeneous nuclear ribonucleoprotein L 

Protein Synonyms/Alias

 hnRNP L 

Gene Name

 HNRNPL 

Gene Synonyms/Alias

 HNRPL; P/OKcl.14 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
59	SEGGRAPKRLKTDNA	ubiquitination	[1, 2]
62	GRAPKRLKTDNAGDQ	ubiquitination	[2, 3, 4, 5, 6, 7]
97	ENYDDPHKTPASPVV	ubiquitination	[2, 4, 5, 8, 9]
229	QRIVIFRKNGVQAMV	ubiquitination	[1, 2, 4, 7]
248	VQSAQRAKASLNGAD	ubiquitination	[1, 7]
264	YSGCCTLKIEYAKPT	ubiquitination	[1]
269	TLKIEYAKPTRLNVF	acetylation	[10]
269	TLKIEYAKPTRLNVF	ubiquitination	[1, 4, 7, 8, 9, 11]
277	PTRLNVFKNDQDTWD	ubiquitination	[1, 2, 4, 8, 9, 11]
302	DPGSNPNKRQRQPPL	ubiquitination	[1, 2, 4, 7, 8, 9, 11]
411	CLYGNVEKVKFMKSK	ubiquitination	[1, 4, 11]
416	VEKVKFMKSKPGAAM	ubiquitination	[1]
418	KVKFMKSKPGAAMVE	ubiquitination	[1, 4]
455	KLNVCVSKQPAIMPG	ubiquitination	[1, 7, 11]
475	EDGSCSYKDFSESRN	acetylation	[10]
475	EDGSCSYKDFSESRN	ubiquitination	[1, 11]
493	STPEQAAKNRIQHPS	ubiquitination	[1]
527	ICDELGVKRPSSVKV	ubiquitination	[4]
533	VKRPSSVKVFSGKSE	ubiquitination	[1, 2, 4, 7, 8, 9, 11]
538	SVKVFSGKSERSSSG	ubiquitination	[1, 2]
552	GLLEWESKSDALETL	acetylation	[10]
568	FLNHYQMKNPNGPYP	ubiquitination	[1, 2, 4, 7, 8, 9]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [8] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [9] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [10] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [11] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 102 176 RRM 1.
 DOMAIN 193 270 RRM 2.
 DOMAIN 382 456 RRM 3.
 MOD_RES 52 52 Phosphoserine.
 MOD_RES 101 101 Phosphoserine.
 MOD_RES 185 185 Phosphoserine.
 MOD_RES 269 269 N6-acetyllysine.
 MOD_RES 291 291 Phosphoserine.
 MOD_RES 298 298 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 589 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0045120; C:pronucleus; IEA:Compara.
 GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
 GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome. 

Interpro

 IPR006536; HnRNP-L_PTB.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 

Pfam

  

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS