CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001310
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribosomal L1 domain-containing protein 1 
Protein Synonyms/Alias
 CATX-11; Cellular senescence-inhibited gene protein; Protein PBK1 
Gene Name
 RSL1D1 
Gene Synonyms/Alias
 CATX11; CSIG; PBK1; L12 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
48DALLTHCKSRKNNYGubiquitination[1]
188VSVNLLSKNLSREINubiquitination[1, 2, 3]
435PEKKPKIKEEAVKEKsumoylation[4]
468KFFTTPSKSVRKASHacetylation[5]
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] 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] 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]
 [4] Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions.
 Lamoliatte F, Bonneil E, Durette C, Caron-Lizotte O, Wildemann D, Zerweck J, Wenschuh H, Thibault P.
 Mol Cell Proteomics. 2013 Jun 7;. [PMID: 23750026]
 [5] 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
  
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 340 340 Phosphothreonine.
 MOD_RES 358 358 Phosphothreonine.
 MOD_RES 361 361 Phosphoserine.
 MOD_RES 375 375 Phosphothreonine.
 MOD_RES 392 392 Phosphoserine.
 MOD_RES 396 396 Phosphoserine.
 MOD_RES 415 415 Phosphothreonine.
 MOD_RES 423 423 Phosphothreonine.
 MOD_RES 427 427 Phosphoserine.
 MOD_RES 443 443 Phosphoserine.
 MOD_RES 465 465 Phosphothreonine.
 MOD_RES 468 468 N6-acetyllysine.
 MOD_RES 469 469 Phosphoserine.  
Keyword
 Acetylation; Coiled coil; Complete proteome; Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 490 AA 
Protein Sequence
MEDSASASLS SAAATGTSTS TPAAPTARKQ LDKEQVRKAV DALLTHCKSR KNNYGLLLNE 60
NESLFLMVVL WKIPSKELRV RLTLPHSIRS DSEDICLFTK DEPNSTPEKT EQFYRKLLNK 120
HGIKTVSQII SLQTLKKEYK SYEAKLRLLS SFDFFLTDAR IRRLLPSLIG RHFYQRKKVP 180
VSVNLLSKNL SREINDCIGG TVLNISKSGS CSAIRIGHVG MQIEHIIENI VAVTKGLSEK 240
LPEKWESVKL LFVKTEKSAA LPIFSSFVSN WDEATKRSLL NKKKKEARRK RRERNFEKQK 300
ERKKKRQQAR KTASVLSKDD VAPESGDTTV KKPESKKEQT PEHGKKKRGR GKAQVKATNE 360
SEDEIPQLVP IGKKTPANEK VEIQKHATGK KSPAKSPNPS TPRGKKRKAL PASETPKAAE 420
SETPGKSPEK KPKIKEEAVK EKSPSLGKKD ARQTPKKPEA KFFTTPSKSV RKASHTPKKW 480
PKKPKVPQST 490 
Gene Ontology
 GO:0015934; C:large ribosomal subunit; IEA:InterPro.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 GO:0032880; P:regulation of protein localization; IMP:MGI.
 GO:0006412; P:translation; IEA:InterPro. 
Interpro
 IPR002143; Ribosomal_L1.
 IPR016094; Ribosomal_L1_2-a/b-sand.
 IPR023674; Ribosomal_L1_SF. 
Pfam
 PF00687; Ribosomal_L1 
SMART
  
PROSITE
  
PRINTS