CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002713
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 40S ribosomal protein SA 
Protein Synonyms/Alias
 37 kDa laminin receptor precursor; 37LRP; 37/67 kDa laminin receptor; LRP/LR; 67 kDa laminin receptor; 67LR; Colon carcinoma laminin-binding protein; Laminin receptor 1; LamR; Laminin-binding protein precursor p40; LBP/p40; Multidrug resistance-associated protein MGr1-Ag; NEM/1CHD4 
Gene Name
 RPSA 
Gene Synonyms/Alias
 LAMBR; LAMR1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11ALDVLQMKEEDVLKFubiquitination[1, 2]
40QMEQYIYKRKSDGIYubiquitination[2, 3]
42EQYIYKRKSDGIYIIubiquitination[2]
52GIYIINLKRTWEKLLacetylation[4]
52GIYIINLKRTWEKLLubiquitination[2, 5, 6]
57NLKRTWEKLLLAARAubiquitination[2, 5]
89TGQRAVLKFAAATGAubiquitination[2, 3, 6]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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
Functional Description
 Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA- precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Acts as a PPP1R16B-dependent substrate of PPP1CA. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. 
Sequence Annotation
 REPEAT 230 232 [DE]-W-[ST] 1.
 REPEAT 247 249 [DE]-W-[ST] 2.
 REPEAT 266 268 [DE]-W-[ST] 3.
 REPEAT 275 277 [DE]-W-[ST] 4.
 REPEAT 293 295 [DE]-W-[ST] 5.
 REGION 54 113 Interaction with PPP1R16B.
 REGION 161 180 Laminin-binding.
 REGION 205 229 Laminin-binding.
 REGION 242 295 Laminin-binding.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 43 43 Phosphoserine (By similarity).
 MOD_RES 52 52 N6-acetyllysine.
 MOD_RES 139 139 Phosphotyrosine.
 MOD_RES 241 241 Phosphothreonine.  
Keyword
 3D-structure; Acetylation; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Membrane; Nucleus; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 295 AA 
Protein Sequence
MSGALDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYIYK RKSDGIYIIN LKRTWEKLLL 60
AARAIVAIEN PADVSVISSR NTGQRAVLKF AAATGATPIA GRFTPGTFTN QIQAAFREPR 120
LLVVTDPRAD HQPLTEASYV NLPTIALCNT DSPLRYVDIA IPCNNKGAHS VGLMWWMLAR 180
EVLRMRGTIS REHPWEVMPD LYFYRDPEEI EKEEQAAAEK AVTKEEFQGE WTAPAPEFTA 240
TQPEVADWSE GVQVPSVPIQ QFPTEDWSAQ PATEDWSAAP TAQATEWVGA TTDWS 295 
Gene Ontology
 GO:0030686; C:90S preribosome; IBA:RefGenome.
 GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
 GO:0005634; C:nucleus; TAS:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0005055; F:laminin receptor activity; IEA:HAMAP.
 GO:0043022; F:ribosome binding; IPI:UniProtKB.
 GO:0003735; F:structural constituent of ribosome; IBA:RefGenome.
 GO:0007155; P:cell adhesion; NAS:ProtInc.
 GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:RefGenome.
 GO:0000461; P:endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:RefGenome.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
 GO:0000028; P:ribosomal small subunit assembly; IBA:RefGenome.
 GO:0006407; P:rRNA export from nucleus; IBA:RefGenome.
 GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
 GO:0006414; P:translational elongation; TAS:Reactome.
 GO:0006413; P:translational initiation; TAS:Reactome.
 GO:0006415; P:translational termination; TAS:Reactome.
 GO:0019083; P:viral transcription; TAS:Reactome. 
Interpro
 IPR027504; 40S_ribosomal_SA.
 IPR001865; Ribosomal_S2.
 IPR018130; Ribosomal_S2_CS.
 IPR027498; Ribosomal_S2_euk.
 IPR005707; Ribosomal_S2_euk/arc.
 IPR023591; Ribosomal_S2_flav_dom. 
Pfam
 PF00318; Ribosomal_S2 
SMART
  
PROSITE
 PS00962; RIBOSOMAL_S2_1
 PS00963; RIBOSOMAL_S2_2 
PRINTS
 PR00395; RIBOSOMALS2.