CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015336
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 La-related protein 1 
Protein Synonyms/Alias
 La ribonucleoprotein domain family member 1 
Gene Name
 LARP1 
Gene Synonyms/Alias
 KIAA0731; LARP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
367DYQFGYRKFDGVEGPubiquitination[1, 2]
462SLIFAALKDSKVVEIubiquitination[3]
473VVEIVDEKVRRREEPubiquitination[2, 3]
539TEEVSNLKTLPKGLSubiquitination[4, 5]
753PTDALANKLFGAPEPubiquitination[1, 2, 3, 4, 5, 6]
792TPRTPQLKDSSQTSRubiquitination[2]
805SRFYPVVKEGRTLDAubiquitination[1, 2, 4, 5]
813EGRTLDAKMPRKRKTubiquitination[2]
871CTPQSLPKFQHPSHEubiquitination[4, 5]
881HPSHELLKENGFTQHubiquitination[4, 5]
892FTQHVYHKYRRRCLNacetylation[7, 8]
936KKMYEEFKQLALEDAubiquitination[3]
944QLALEDAKEGYRYGLubiquitination[4, 5]
972KFRLDIFKDFQEETVubiquitination[4, 5]
1003FLKYSKAKNLDIDPKubiquitination[2]
1017KLQEYLGKFRRLEDFacetylation[7]
1017KLQEYLGKFRRLEDFubiquitination[1, 2, 3, 4, 5]
1083QPVREDAKWTSQHSNphosphoglycerylation[9]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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]
 [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] 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]
 [8] 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]
 [9] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237] 
Functional Description
  
Sequence Annotation
 DOMAIN 397 487 HTH La-type RNA-binding.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 75 75 Phosphoserine.
 MOD_RES 90 90 Phosphoserine.
 MOD_RES 143 143 Phosphoserine.
 MOD_RES 165 165 Phosphoserine.
 MOD_RES 215 215 Phosphoserine.
 MOD_RES 220 220 Phosphoserine.
 MOD_RES 228 228 Phosphoserine (By similarity).
 MOD_RES 324 324 Phosphoserine (By similarity).
 MOD_RES 327 327 Phosphoserine (By similarity).
 MOD_RES 376 376 Phosphothreonine.
 MOD_RES 517 517 Phosphoserine.
 MOD_RES 521 521 Phosphoserine.
 MOD_RES 526 526 Phosphothreonine.
 MOD_RES 548 548 Phosphoserine.
 MOD_RES 627 627 Phosphoserine.
 MOD_RES 631 631 Phosphoserine.
 MOD_RES 649 649 Phosphothreonine.
 MOD_RES 724 724 Phosphothreonine.
 MOD_RES 766 766 Phosphoserine.
 MOD_RES 774 774 Phosphoserine.
 MOD_RES 777 777 Phosphotyrosine.
 MOD_RES 824 824 Phosphoserine.
 MOD_RES 845 845 Phosphothreonine.
 MOD_RES 851 851 Phosphoserine.
 MOD_RES 865 865 Phosphothreonine.
 MOD_RES 868 868 Phosphoserine.
 MOD_RES 892 892 N6-acetyllysine.
 MOD_RES 1017 1017 N6-acetyllysine.
 MOD_RES 1056 1056 Phosphoserine (By similarity).  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Phosphoprotein; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1096 AA 
Protein Sequence
MATQVEPLLP GGATLLQAEE HGGLVRKKPP PAPEGKGEPG PNDVRGGEPD GSARRPRPPC 60
AKPHKEGTGQ QERESPRPLQ LPGAEGPAIS DGEEGGGEPG AGGGAAGAAG AGRRDFVEAP 120
PPKVNPWTKN ALPPVLTTVN GQSPPEHSAP AKVVRAAVPK QRKGSKVGDF GDAINWPTPG 180
EIAHKSVQPQ SHKPQPTRKL PPKKDMKEQE KGEGSDSKES PKTKSDESGE EKNGDEDCQR 240
GGQKKKGNKH KWVPLQIDMK PEVPREKLAS RPTRPPEPRH IPANRGEIKG SESATYVPVA 300
PPTPAWQPEI KPEPAWHDQD ETSSVKSDGA GGARASFRGR GRGRGRGRGR GRGGTRTHFD 360
YQFGYRKFDG VEGPRTPKYM NNITYYFDNV SSTELYSVDQ ELLKDYIKRQ IEYYFSVDNL 420
ERDFFLRRKM DADGFLPITL IASFHRVQAL TTDISLIFAA LKDSKVVEIV DEKVRRREEP 480
EKWPLPPIVD YSQTDFSQLL NCPEFVPRQH YQKETESAPG SPRAVTPVPT KTEEVSNLKT 540
LPKGLSASLP DLDSENWIEV KKRPRPSPAR PKKSEESRFS HLTSLPQQLP SQQLMSKDQD 600
EQEELDFLFD EEMEQMDGRK NTFTAWSDEE SDYEIDDRDV NKILIVTQTP HYMRRHPGGD 660
RTGNHTSRAK MSAELAKVIN DGLFYYEQDL WAEKFEPEYS QIKQEVENFK KVNMISREQF 720
DTLTPEPPVD PNQEVPPGPP RFQQVPTDAL ANKLFGAPEP STIARSLPTT VPESPNYRNT 780
RTPRTPRTPQ LKDSSQTSRF YPVVKEGRTL DAKMPRKRKT RHSSNPPLES HVGWVMDSRE 840
HRPRTASISS SPSEGTPTVG SYGCTPQSLP KFQHPSHELL KENGFTQHVY HKYRRRCLNE 900
RKRLGIGQSQ EMNTLFRFWS FFLRDHFNKK MYEEFKQLAL EDAKEGYRYG LECLFRYYSY 960
GLEKKFRLDI FKDFQEETVK DYEAGQLYGL EKFWAFLKYS KAKNLDIDPK LQEYLGKFRR 1020
LEDFRVDPPM GEEGNHKRHS VVAGGGGGEG RKRCPSQSSS RPAAMISQPP TPPTGQPVRE 1080
DAKWTSQHSN TQTLGK 1096 
Gene Ontology
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0016239; P:positive regulation of macroautophagy; IMP:BHF-UCL. 
Interpro
 IPR006607; DM15.
 IPR006630; Lupus_La_RNA-bd.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF05383; La 
SMART
 SM00684; DM15
 SM00715; LA 
PROSITE
 PS50961; HTH_LA 
PRINTS