CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-045262
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Heterogeneous nuclear ribonucleoprotein L 
Protein Synonyms/Alias
  
Gene Name
 HNRNPL 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
38ENYDDPHKTPASPVVubiquitination[1]
218PTRLNVFKNDQDTWDubiquitination[2, 3, 4, 5, 6]
243DPGSNPNKRQRQPPLubiquitination[1, 2, 3, 5, 6]
352CLYGNVEKVKFMKSKubiquitination[3, 5, 6]
357VEKVKFMKSKPGAAMubiquitination[6, 7]
359KVKFMKSKPGAAMVEubiquitination[3, 6, 7]
389NNFMFGQKLNVCVSKacetylation[7]
396KLNVCVSKQPAIMPGubiquitination[5, 6]
416EDGSCSYKDFSESRNacetylation[7]
416EDGSCSYKDFSESRNubiquitination[4, 5, 6]
434STPEQAAKNRIQHPSubiquitination[6, 7]
468ICDELGVKRPSSVKVubiquitination[3]
474VKRPSSVKVFSGKSEubiquitination[1, 2, 3, 5, 6]
479SVKVFSGKSERSSSGubiquitination[1, 6]
493GLLEWESKSDALETLacetylation[8]
509FLNHYQMKNPNGPYPubiquitination[1, 2, 3, 6, 7]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 530 AA 
Protein Sequence
XCCTGRLVGG HPLQGRGQDL LWCSEGSSCQ ENYDDPHKTP ASPVVHIRGL IDGVVEADLV 60
EALQEFGPIS YVVVMPKKRQ ALVEFEDVLG ACNAVNYAAD NQIYIAGHPA FVNYSTSQKI 120
SRPGDSDDSR SVNSVLLFTI LNPIYSITTD VLYTICNPCG PVQRIVIFRK NGVQAMVEFD 180
SVQSAQRAKA SLNGADIYSG CCTLKIEYAK PTRLNVFKND QDTWDYTNPN LSGQGDPGSN 240
PNKRQRQPPL LGDHPAEYGG PHGGYHSHYH DEGYGPPPPH YEGRRMGPPV GGHRRGPSRY 300
GPQYGHPPPP PPPPEYGPHA DSPVLMVYGL DQSKMNCDRV FNVFCLYGNV EKVKFMKSKP 360
GAAMVEMADG YAVDRAITHL NNNFMFGQKL NVCVSKQPAI MPGQSYGLED GSCSYKDFSE 420
SRNNRFSTPE QAAKNRIQHP SNVLHFFNAP LEVTEENFFE ICDELGVKRP SSVKVFSGKS 480
ERSSSGLLEW ESKSDALETL GFLNHYQMKN PNGPYPYTLK LCFSTAQHAS 530 
Gene Ontology
 GO:0005634; C:nucleus; IEA:InterPro.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0006397; P:mRNA processing; IEA:InterPro. 
Interpro
 IPR006536; HnRNP-L_PTB.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
  
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS