SGPL1_HUMAN - dbPTM
SGPL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SGPL1_HUMAN
UniProt AC O95470
Protein Name Sphingosine-1-phosphate lyase 1 {ECO:0000305}
Gene Name SGPL1 {ECO:0000312|HGNC:HGNC:10817}
Organism Homo sapiens (Human).
Sequence Length 568
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type III membrane protein .
Protein Description Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis..
Protein Sequence MPSTDLLMLKAFEPYLEILEVYSTKAKNYVNGHCTKYEPWQLIAWSVVWTLLIVWGYEFVFQPESLWSRFKKKCFKLTRKMPIIGRKIQDKLNKTKDDISKNMSFLKVDKEYVKALPSQGLSSSAVLEKLKEYSSMDAFWQEGRASGTVYSGEEKLTELLVKAYGDFAWSNPLHPDIFPGLRKIEAEIVRIACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFEKGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYPLEHPFDFRVKGVTSISADTHKYGYAPKGSSLVLYSDKKYRNYQFFVDTDWQGGIYASPTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKGIFVFGNPQLSVIALGSRDFDIYRLSNLMTAKGWNLNQLQFPPSIHFCITLLHARKRVAIQFLKDIRESVTQIMKNPKAKTTGMGAIYGMAQTTVDRNMVAELSSVFLDSLYSTDTVTQGSQMNGSPKPH
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
3Phosphorylation-----MPSTDLLMLK
-----CCCHHHHHHH		33.0021406692
4Phosphorylation----MPSTDLLMLKA
----CCCHHHHHHHH		25.4620068231
8SulfoxidationMPSTDLLMLKAFEPY
CCCHHHHHHHHHHHH		4.7321406390
25UbiquitinationILEVYSTKAKNYVNG
HHHHHCCCCHHCCCC		51.9621906983
30UbiquitinationSTKAKNYVNGHCTKY
CCCCHHCCCCCCCCC		10.9323000965
34UbiquitinationKNYVNGHCTKYEPWQ
HHCCCCCCCCCCHHH		3.5821890473
49UbiquitinationLIAWSVVWTLLIVWG
HHHHHHHHHHHHHHC		4.5221890473
51UbiquitinationAWSVVWTLLIVWGYE
HHHHHHHHHHHHCCH		1.4821890473
75UbiquitinationSRFKKKCFKLTRKMP
HHHHHHHHHHHHHCC		11.3123000965
80UbiquitinationKCFKLTRKMPIIGRK
HHHHHHHHCCCCCHH		43.74-
91UbiquitinationIGRKIQDKLNKTKDD
CCHHHHHHHHCCHHH		37.27-
912-HydroxyisobutyrylationIGRKIQDKLNKTKDD
CCHHHHHHHHCCHHH		37.27-
101UbiquitinationKTKDDISKNMSFLKV
CCHHHHHHCCCEEEC		57.9329967540
104PhosphorylationDDISKNMSFLKVDKE
HHHHHCCCEEECCHH		36.5024719451
107UbiquitinationSKNMSFLKVDKEYVK
HHCCCEEECCHHHHH		46.5133845483
110UbiquitinationMSFLKVDKEYVKALP
CCEEECCHHHHHHCC		54.6623000965
114UbiquitinationKVDKEYVKALPSQGL
ECCHHHHHHCCCCCC		43.2223000965
118PhosphorylationEYVKALPSQGLSSSA
HHHHHCCCCCCCHHH		37.4230266825
122PhosphorylationALPSQGLSSSAVLEK
HCCCCCCCHHHHHHH		29.1330266825
123PhosphorylationLPSQGLSSSAVLEKL
CCCCCCCHHHHHHHH		27.6230266825
124PhosphorylationPSQGLSSSAVLEKLK
CCCCCCHHHHHHHHH		21.0130266825
129UbiquitinationSSSAVLEKLKEYSSM
CHHHHHHHHHHHCCC		61.7823000965
131UbiquitinationSAVLEKLKEYSSMDA
HHHHHHHHHHCCCHH		66.7223000965
133PhosphorylationVLEKLKEYSSMDAFW
HHHHHHHHCCCHHHH		12.4030624053
134PhosphorylationLEKLKEYSSMDAFWQ
HHHHHHHCCCHHHHH		21.9330624053
135PhosphorylationEKLKEYSSMDAFWQE
HHHHHHCCCHHHHHC		21.5630624053
148UbiquitinationQEGRASGTVYSGEEK
HCCCCCCCEECCHHH		17.4927667366
151UbiquitinationRASGTVYSGEEKLTE
CCCCCEECCHHHHHH		35.0823503661
155UbiquitinationTVYSGEEKLTELLVK
CEECCHHHHHHHHHH		57.3023000965
155AcetylationTVYSGEEKLTELLVK
CEECCHHHHHHHHHH		57.3023236377
167UbiquitinationLVKAYGDFAWSNPLH
HHHHHCCCCCCCCCC		6.9623503661
183UbiquitinationDIFPGLRKIEAEIVR
CCCCCHHHHHHHHHH		50.3621890473
228UbiquitinationYRDLAFEKGIKTPEI
HHHHHHHCCCCCCCC		60.5321906983
231UbiquitinationLAFEKGIKTPEIVAP
HHHHCCCCCCCCCCC		67.6923503661
240PhosphorylationPEIVAPQSAHAAFNK
CCCCCCHHHHHHHHH		22.44-
247UbiquitinationSAHAAFNKAASYFGM
HHHHHHHHHHHHHCC		38.5923503661
247MethylationSAHAAFNKAASYFGM
HHHHHHHHHHHHHCC		38.59115981337
263UbiquitinationIVRVPLTKMMEVDVR
EEEEECCCHHHHHHH		43.8821890473
342UbiquitinationHPFDFRVKGVTSISA
CCCCEEEECEEEEEC		43.332190698
345UbiquitinationDFRVKGVTSISADTH
CEEEECEEEEECCCC		29.0727667366
353UbiquitinationSISADTHKYGYAPKG
EEECCCCCCEECCCC		42.3229901268
353OtherSISADTHKYGYAPKG
EEECCCCCCEECCCC		42.32-
353AcetylationSISADTHKYGYAPKG
EEECCCCCCEECCCC		42.3225825284
353N6-(pyridoxal phosphate)lysineSISADTHKYGYAPKG
EEECCCCCCEECCCC		42.32-
354PhosphorylationISADTHKYGYAPKGS
EECCCCCCEECCCCC		14.0423898821
356Nitrated tyrosineADTHKYGYAPKGSSL
CCCCCCEECCCCCEE		19.35-
356PhosphorylationADTHKYGYAPKGSSL
CCCCCCEECCCCCEE		19.3523898821
356NitrationADTHKYGYAPKGSSL
CCCCCCEECCCCCEE		19.3516777052
356NitrationADTHKYGYAPKGSSL
CCCCCCEECCCCCEE		19.3516777052
359UbiquitinationHKYGYAPKGSSLVLY
CCCEECCCCCEEEEE		64.3529967540
366Nitrated tyrosineKGSSLVLYSDKKYRN
CCCEEEEECCCCCCC		13.82-
366NitrationKGSSLVLYSDKKYRN
CCCEEEEECCCCCCC		13.8216777052
366NitrationKGSSLVLYSDKKYRN
CCCEEEEECCCCCCC		13.8216777052
3692-HydroxyisobutyrylationSLVLYSDKKYRNYQF
EEEEECCCCCCCEEE		45.85-
401PhosphorylationGSRPGGISAACWAAL
CCCCCHHHHHHHHHH		17.06-
425UbiquitinationEATKQIIKTARFLKS
HHHHHHHHHHHHHHH		37.4527667366
449PhosphorylationVFGNPQLSVIALGSR
EECCCCEEEEEECCC		13.26-
455PhosphorylationLSVIALGSRDFDIYR
EEEEEECCCCCEEHH		29.53-
468PhosphorylationYRLSNLMTAKGWNLN
HHHHHCCCCCCCCCH		28.5217192257
507PhosphorylationFLKDIRESVTQIMKN
HHHHHHHHHHHHHHC		22.18-
509PhosphorylationKDIRESVTQIMKNPK
HHHHHHHHHHHHCCC		22.96-
542PhosphorylationRNMVAELSSVFLDSL
HHHHHHHHHHHHHHC		18.8920068231
543PhosphorylationNMVAELSSVFLDSLY
HHHHHHHHHHHHHCC		29.5229496963
548PhosphorylationLSSVFLDSLYSTDTV
HHHHHHHHCCCCCCC		31.2127174698
550PhosphorylationSVFLDSLYSTDTVTQ
HHHHHHCCCCCCCCC		17.3027174698
551PhosphorylationVFLDSLYSTDTVTQG
HHHHHCCCCCCCCCC		25.7126074081
552PhosphorylationFLDSLYSTDTVTQGS
HHHHCCCCCCCCCCC		23.3318691976
554PhosphorylationDSLYSTDTVTQGSQM
HHCCCCCCCCCCCCC		26.0720068231
556PhosphorylationLYSTDTVTQGSQMNG
CCCCCCCCCCCCCCC		29.3420068231
559PhosphorylationTDTVTQGSQMNGSPK
CCCCCCCCCCCCCCC		19.2125159151
564PhosphorylationQGSQMNGSPKPH---
CCCCCCCCCCCC---		25.4225159151
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SGPL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SGPL1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SGPL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATP5L_HUMANATP5Lphysical
26344197
TM9S4_HUMANTM9SF4physical
26344197
TRIM9_HUMANTRIM9physical
28514442
AIFM1_HUMANAIFM1physical
28514442
MO4L1_HUMANMORF4L1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SGPL1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-353, AND MASS SPECTROMETRY.
Nitration
ReferencePubMed
"Nitroproteins from a human pituitary adenoma tissue discovered with anitrotyrosine affinity column and tandem mass spectrometry.";
Zhan X., Desiderio D.M.;
Anal. Biochem. 354:279-289(2006).
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-356 AND TYR-366, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-468, AND MASSSPECTROMETRY.

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