CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001608
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Sphingosine-1-phosphate lyase 1 
Protein Synonyms/Alias
 S1PL; SP-lyase 1; SPL 1; hSPL; Sphingosine-1-phosphate aldolase 
Gene Name
 SGPL1 
Gene Synonyms/Alias
 KIAA1252 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
25ILEVYSTKAKNYVNGubiquitination[1]
114KVDKEYVKALPSQGLubiquitination[2, 3, 4, 5]
129SSSAVLEKLKEYSSMubiquitination[2, 5]
131SAVLEKLKEYSSMDAubiquitination[1, 2, 3, 4, 5, 6, 7]
155TVYSGEEKLTELLVKubiquitination[1, 3, 7]
228YRDLAFEKGIKTPEIubiquitination[1, 4, 7]
247SAHAAFNKAASYFGMubiquitination[4]
263IVRVPLTKMMEVDVRubiquitination[2, 5, 8]
342HPFDFRVKGVTSISAubiquitination[1]
353SISADTHKYGYAPKGacetylation[9, 10]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [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] 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]
 [7] 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]
 [8] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [9] 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]
 [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] 
Functional Description
 Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis. 
Sequence Annotation
 MOD_RES 353 353 N6-(pyridoxal phosphate)lysine; alternate
 MOD_RES 353 353 N6-acetyllysine; alternate.
 MOD_RES 356 356 Nitrated tyrosine.
 MOD_RES 366 366 Nitrated tyrosine.
 MOD_RES 564 564 Phosphoserine.  
Keyword
 Acetylation; Apoptosis; Complete proteome; Endoplasmic reticulum; Lipid metabolism; Lyase; Membrane; Nitration; Phosphoprotein; Polymorphism; Pyridoxal phosphate; Reference proteome; Signal-anchor; Sphingolipid metabolism; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 568 AA 
Protein Sequence
MPSTDLLMLK AFEPYLEILE VYSTKAKNYV NGHCTKYEPW QLIAWSVVWT LLIVWGYEFV 60
FQPESLWSRF KKKCFKLTRK MPIIGRKIQD KLNKTKDDIS KNMSFLKVDK EYVKALPSQG 120
LSSSAVLEKL KEYSSMDAFW QEGRASGTVY SGEEKLTELL VKAYGDFAWS NPLHPDIFPG 180
LRKIEAEIVR IACSLFNGGP DSCGCVTSGG TESILMACKA YRDLAFEKGI KTPEIVAPQS 240
AHAAFNKAAS YFGMKIVRVP LTKMMEVDVR AMRRAISRNT AMLVCSTPQF PHGVIDPVPE 300
VAKLAVKYKI PLHVDACLGG FLIVFMEKAG YPLEHPFDFR VKGVTSISAD THKYGYAPKG 360
SSLVLYSDKK YRNYQFFVDT DWQGGIYASP TIAGSRPGGI SAACWAALMH FGENGYVEAT 420
KQIIKTARFL KSELENIKGI FVFGNPQLSV IALGSRDFDI YRLSNLMTAK GWNLNQLQFP 480
PSIHFCITLL HARKRVAIQF LKDIRESVTQ IMKNPKAKTT GMGAIYGMAQ TTVDRNMVAE 540
LSSVFLDSLY STDTVTQGSQ MNGSPKPH 568 
Gene Ontology
 GO:0030176; C:integral to endoplasmic reticulum membrane; NAS:UniProtKB.
 GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0008117; F:sphinganine-1-phosphate aldolase activity; IDA:UniProtKB.
 GO:0008209; P:androgen metabolic process; IEA:Compara.
 GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
 GO:0006672; P:ceramide metabolic process; IDA:UniProtKB.
 GO:0008210; P:estrogen metabolic process; IEA:Compara.
 GO:0097194; P:execution phase of apoptosis; IDA:UniProtKB.
 GO:0060325; P:face morphogenesis; IEA:Compara.
 GO:0010761; P:fibroblast migration; IEA:Compara.
 GO:0030097; P:hemopoiesis; IEA:Compara.
 GO:0001822; P:kidney development; IEA:Compara.
 GO:0033327; P:Leydig cell differentiation; IEA:Compara.
 GO:0001553; P:luteinization; IEA:Compara.
 GO:0060021; P:palate development; IEA:Compara.
 GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Compara.
 GO:0009791; P:post-embryonic development; IEA:Compara.
 GO:0040014; P:regulation of multicellular organism growth; IEA:Compara.
 GO:0048705; P:skeletal system morphogenesis; IEA:Compara.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0007283; P:spermatogenesis; IEA:Compara.
 GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
 GO:0030149; P:sphingolipid catabolic process; NAS:UniProtKB.
 GO:0001570; P:vasculogenesis; IEA:Compara. 
Interpro
 IPR002129; PyrdxlP-dep_de-COase.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1. 
Pfam
 PF00282; Pyridoxal_deC 
SMART
  
PROSITE
 PS00392; DDC_GAD_HDC_YDC 
PRINTS