CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002257
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lupus La protein 
Protein Synonyms/Alias
 La autoantigen; La ribonucleoprotein; Sjoegren syndrome type B antigen; SS-B 
Gene Name
 SSB 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9AENGDNEKMAALEAKubiquitination[1, 2, 3]
37LPRDKFLKEQIKLDEubiquitination[1, 3]
41KFLKEQIKLDEGWVPsumoylation[4]
76VEALSKSKAELMEISubiquitination[1, 2, 3, 5]
95KIRRSPSKPLPEVTDubiquitination[1, 3]
116KNRSVYIKGFPTDATacetylation[6]
116KNRSVYIKGFPTDATubiquitination[1, 3, 5]
128DATLDDIKEWLEDKGacetylation[6]
134IKEWLEDKGQVLNIQubiquitination[5]
165FDSIESAKKFVETPGubiquitination[3, 7]
176ETPGQKYKETDLLILubiquitination[1, 3]
191FKDDYFAKKNEERKQubiquitination[5]
216QEQEAKQKLEEDAEMacetylation[8]
216QEQEAKQKLEEDAEMubiquitination[2, 5, 8]
224LEEDAEMKSLEEKIGubiquitination[1, 3]
229EMKSLEEKIGCLLKFubiquitination[1, 2, 3, 8]
287KEALGKAKDANNGNLubiquitination[1, 2, 3, 8]
312VLEGEVEKEALKKIIubiquitination[1, 3]
317VEKEALKKIIEDQQEubiquitination[9]
328DQQESLNKWKSKGRRacetylation[6, 10]
328DQQESLNKWKSKGRRubiquitination[1, 2, 3, 5, 8, 9, 11]
354QPGSGKGKVQFQGKKacetylation[8, 10]
360GKVQFQGKKTKFASDacetylation[6, 8]
391RAREETDKEEPASKQacetylation[8]
397DKEEPASKQQKTENGubiquitination[5]
Reference
 [1] 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]
 [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] 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] Sumoylation in axons triggers retrograde transport of the RNA-binding protein La.
 van Niekerk EA, Willis DE, Chang JH, Reumann K, Heise T, Twiss JL.
 Proc Natl Acad Sci U S A. 2007 Jul 31;104(31):12913-8. [PMID: 17646655]
 [5] 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]
 [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]
 [7] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [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] 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]
 [10] 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]
 [11] 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] 
Functional Description
 Binds to the 3' poly(U) terminii of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation. 
Sequence Annotation
 DOMAIN 7 99 HTH La-type RNA-binding.
 DOMAIN 111 187 RRM.
 MOD_RES 116 116 N6-acetyllysine.
 MOD_RES 128 128 N6-acetyllysine.
 MOD_RES 328 328 N6-acetyllysine.
 MOD_RES 360 360 N6-acetyllysine.
 MOD_RES 366 366 Phosphoserine; by CK2.  
Keyword
 3D-structure; Acetylation; Complete proteome; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; RNA-binding; Systemic lupus erythematosus. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 408 AA 
Protein Sequence
MAENGDNEKM AALEAKICHQ IEYYFGDFNL PRDKFLKEQI KLDEGWVPLE IMIKFNRLNR 60
LTTDFNVIVE ALSKSKAELM EISEDKTKIR RSPSKPLPEV TDEYKNDVKN RSVYIKGFPT 120
DATLDDIKEW LEDKGQVLNI QMRRTLHKAF KGSIFVVFDS IESAKKFVET PGQKYKETDL 180
LILFKDDYFA KKNEERKQNK VEAKLRAKQE QEAKQKLEED AEMKSLEEKI GCLLKFSGDL 240
DDQTCREDLH ILFSNHGEIK WIDFVRGAKE GIILFKEKAK EALGKAKDAN NGNLQLRNKE 300
VTWEVLEGEV EKEALKKIIE DQQESLNKWK SKGRRFKGKG KGNKAAQPGS GKGKVQFQGK 360
KTKFASDDEH DEHDENGATG PVKRAREETD KEEPASKQQK TENGAGDQ 408 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0030529; C:ribonucleoprotein complex; TAS:ProtInc.
 GO:0003729; F:mRNA binding; TAS:ProtInc.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0000049; F:tRNA binding; TAS:ProtInc.
 GO:0008334; P:histone mRNA metabolic process; TAS:ProtInc.
 GO:0006400; P:tRNA modification; TAS:ProtInc. 
Interpro
 IPR002344; Lupus_La.
 IPR006630; Lupus_La_RNA-bd.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR014886; RRM_3.
 IPR000504; RRM_dom.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF05383; La
 PF00076; RRM_1
 PF08777; RRM_3 
SMART
 SM00715; LA
 SM00360; RRM 
PROSITE
 PS50961; HTH_LA
 PS50102; RRM 
PRINTS
 PR00302; LUPUSLA.