CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018775
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 La-related protein 4B 
Protein Synonyms/Alias
 La ribonucleoprotein domain family member 4B; La ribonucleoprotein domain family member 5; La-related protein 5 
Gene Name
 LARP4B 
Gene Synonyms/Alias
 KIAA0217; LARP5 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
162DPREVLKKTLEFCLSubiquitination[1]
201VANLDHIKKLSTDVDubiquitination[2]
257EEVEALFKGDNLPKFubiquitination[1, 2]
311IKARIKAKAIAINTFubiquitination[2, 3, 4]
321AINTFLPKNGFRPLDubiquitination[1, 3, 4, 5]
472QNPSAYAKREAGPGRubiquitination[1]
563SLIIGPSKERTLSADubiquitination[1]
724PSPSAMGKRLSREQSacetylation[6]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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
Functional Description
 Stimulates mRNA translation. 
Sequence Annotation
 DOMAIN 150 239 HTH La-type RNA-binding.
 DOMAIN 240 307 RRM.
 MOD_RES 424 424 Phosphoserine.
 MOD_RES 434 434 Phosphoserine.
 MOD_RES 451 451 Phosphoserine.
 MOD_RES 498 498 Phosphoserine (By similarity).
 MOD_RES 518 518 Phosphothreonine.
 MOD_RES 524 524 Phosphoserine.
 MOD_RES 566 566 Phosphothreonine.
 MOD_RES 718 718 Phosphoserine (By similarity).
 MOD_RES 724 724 N6-acetyllysine.
 MOD_RES 727 727 Phosphoserine.
 MOD_RES 736 736 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome; RNA-binding; Translation regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 738 AA 
Protein Sequence
MTSDQDAKVV AEPQTQRVQE GKDSAHLMNG PISQTTSQTS SIPPLSQVPA TKVSELNPNA 60
EVWGAPVLHL EASSAADGVS AAWEEVAGHH ADRGPQGSDA NGDGDQGHEN AALPDPQESD 120
PADMNALALG PSEYDSLPEN SETGGNESQP DSQEDPREVL KKTLEFCLSR ENLASDMYLI 180
SQMDSDQYVP ITTVANLDHI KKLSTDVDLI VEVLRSLPLV QVDEKGEKVR PNQNRCIVIL 240
REISESTPVE EVEALFKGDN LPKFINCEFA YNDNWFITFE TEADAQQAYK YLREEVKTFQ 300
GKPIKARIKA KAIAINTFLP KNGFRPLDVS LYAQQRYATS FYFPPMYSPQ QQFPLYSLIT 360
PQTWSATHSY LDPPLVTPFP NTGFINGFTS PAFKPAASPL TSLRQYPPRS RNPSKSHLRH 420
AIPSAERGPG LLESPSIFNF TADRLINGVR SPQTRQAGQT RTRIQNPSAY AKREAGPGRV 480
EPGSLESSPG LGRGRKNSFG YRKKREEKFT SSQTQSPTPP KPPSPSFELG LSSFPPLPGA 540
AGNLKTEDLF ENRLSSLIIG PSKERTLSAD ASVNTLPVVV SREPSVPASC AVSATYERSP 600
SPAHLPDDPK VAEKQRETHS VDRLPSALTA TACKSVQVNG AATELRKPSY AEICQRTSKE 660
PPSSPLQPQK EQKPNTVGCG KEEKKLAEPA ERYREPPALK STPGAPRDQR RPAGGRPSPS 720
AMGKRLSREQ STPPKSPQ 738 
Gene Ontology
 GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0045727; P:positive regulation of translation; IMP:UniProtKB. 
Interpro
 IPR006630; Lupus_La_RNA-bd.
 IPR000504; RRM_dom.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF05383; La 
SMART
 SM00715; LA
 SM00360; RRM 
PROSITE
 PS50961; HTH_LA
 PS50102; RRM 
PRINTS