LCB4_YEAST - dbPTM
LCB4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LCB4_YEAST
UniProt AC Q12246
Protein Name Sphingoid long chain base kinase 4 {ECO:0000303|PubMed:9677363}
Gene Name LCB4 {ECO:0000303|PubMed:9677363}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 624
Subcellular Localization Cell membrane
Peripheral membrane protein . Endoplasmic reticulum membrane
Peripheral membrane protein . Late endosome membrane
Peripheral membrane protein . Golgi apparatus membrane
Peripheral membrane protein .
Protein Description Catalyzes the phosphorylation of the sphingoid long chain bases dihydrosphingosine (DHS or sphinganine) and phytosphingosine (PHS) to form dihydrosphingosine 1-phosphate (DHS-1P) and phytosphingosine 1-phosphate (PHS-1P) respectively. [PubMed: 9677363]
Protein Sequence MVVQKKLRAILTDEGVLIKSQSHHMFNKHGQLRSGDSLSLLSCLSCLDDGTLSSDGGSFDEDDSLELLPLNTTIPFNRILNAKYVNVGQKGFNNGKISSNPFQTENLSSSSENDDVENHSLSNDKAPVSESQSFPKKDKWDTKTNTVKVSPDDSQDNSPSLGIKDNQQLIELTFAVPKGHDVIPQKLTLLIDHVSRKSRANTGEENISSGTVEEILEKSYENSKRNRSILVIINPHGGKGTAKNLFLTKARPILVESGCKIEIAYTKYARHAIDIAKDLDISKYDTIACASGDGIPYEVINGLYRRPDRVDAFNKLAVTQLPCGSGNAMSISCHWTNNPSYAALCLVKSIETRIDLMCCSQPSYMNEWPRLSFLSQTYGVIAESDINTEFIRWMGPVRFNLGVAFNIIQGKKYPCEVFVKYAAKSKKELKVHFLENKDKNKGCLTFEPNPSPNSSPDLLSKNNINNSTKDELSPNFLNEDNFKLKYPMTEPVPRDWEKMDSELTDNLTIFYTGKMPYIAKDTKFFPAALPADGTIDLVITDARIPVTRMTPILLSLDKGSHVLEPEVIHSKILAYKIIPKVESGLFSVDGEKFPLEPLQVEIMPMLCKTLLRNGRYIDTEFESM
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
43S-palmitoylationDSLSLLSCLSCLDDG
CCHHHHHHHHHCCCC		3.06-
43S-palmitoylationDSLSLLSCLSCLDDG
CCHHHHHHHHHCCCC		3.0616227572
46S-palmitoylationSLLSCLSCLDDGTLS
HHHHHHHHCCCCCCC		2.89-
46S-palmitoylationSLLSCLSCLDDGTLS
HHHHHHHHCCCCCCC		2.8916227572
84PhosphorylationNRILNAKYVNVGQKG
HHHCCCEEEECCCCC		8.5427214570
90UbiquitinationKYVNVGQKGFNNGKI
EEEECCCCCCCCCCC		60.5923749301
98PhosphorylationGFNNGKISSNPFQTE
CCCCCCCCCCCCCCC		27.7822369663
99PhosphorylationFNNGKISSNPFQTEN
CCCCCCCCCCCCCCC		52.5822369663
104PhosphorylationISSNPFQTENLSSSS
CCCCCCCCCCCCCCC		27.5022369663
108PhosphorylationPFQTENLSSSSENDD
CCCCCCCCCCCCCCC		39.4920377248
109PhosphorylationFQTENLSSSSENDDV
CCCCCCCCCCCCCCC		40.8420377248
110PhosphorylationQTENLSSSSENDDVE
CCCCCCCCCCCCCCC		37.9920377248
111PhosphorylationTENLSSSSENDDVEN
CCCCCCCCCCCCCCC		42.2220377248
120PhosphorylationNDDVENHSLSNDKAP
CCCCCCCCCCCCCCC		45.1122369663
122PhosphorylationDVENHSLSNDKAPVS
CCCCCCCCCCCCCCC		46.1022369663
125UbiquitinationNHSLSNDKAPVSESQ
CCCCCCCCCCCCCCC		59.8623749301
129PhosphorylationSNDKAPVSESQSFPK
CCCCCCCCCCCCCCC		30.3921551504
131PhosphorylationDKAPVSESQSFPKKD
CCCCCCCCCCCCCCC		24.5024909858
133PhosphorylationAPVSESQSFPKKDKW
CCCCCCCCCCCCCCC		53.4424909858
143UbiquitinationKKDKWDTKTNTVKVS
CCCCCCCCCCEEEEC		36.9923749301
148UbiquitinationDTKTNTVKVSPDDSQ
CCCCCEEEECCCCCC		34.6523749301
150PhosphorylationKTNTVKVSPDDSQDN
CCCEEEECCCCCCCC		19.5228889911
154PhosphorylationVKVSPDDSQDNSPSL
EEECCCCCCCCCCCC		46.9822369663
158PhosphorylationPDDSQDNSPSLGIKD
CCCCCCCCCCCCCCC		24.9322369663
160PhosphorylationDSQDNSPSLGIKDNQ
CCCCCCCCCCCCCCC		38.7622369663
164UbiquitinationNSPSLGIKDNQQLIE
CCCCCCCCCCCEEEE		49.1523749301
186UbiquitinationGHDVIPQKLTLLIDH
CCCCCCHHHHHHHHH		37.7817644757
197UbiquitinationLIDHVSRKSRANTGE
HHHHHCHHHHCCCCC		36.4717644757
198PhosphorylationIDHVSRKSRANTGEE
HHHHCHHHHCCCCCC		35.2023749301
202PhosphorylationSRKSRANTGEENISS
CHHHHCCCCCCCCCC		45.0123749301
208PhosphorylationNTGEENISSGTVEEI
CCCCCCCCCCCHHHH		34.0119823750
209PhosphorylationTGEENISSGTVEEIL
CCCCCCCCCCHHHHH		34.3919823750
211PhosphorylationEENISSGTVEEILEK
CCCCCCCCHHHHHHH		27.0519823750
249UbiquitinationAKNLFLTKARPILVE
HHHHHEECCCEEEEE		44.5417644757
260UbiquitinationILVESGCKIEIAYTK
EEEECCCEEEEEECH		47.0717644757
267AcetylationKIEIAYTKYARHAID
EEEEEECHHHHHHHH		25.0024489116
340PhosphorylationCHWTNNPSYAALCLV
EECCCCCCHHHHHHH		29.5328889911
439UbiquitinationHFLENKDKNKGCLTF
EEEECCCCCCCCEEE		63.2717644757
441UbiquitinationLENKDKNKGCLTFEP
EECCCCCCCCEEECC		57.6623749301
445PhosphorylationDKNKGCLTFEPNPSP
CCCCCCEEECCCCCC		29.9923749301
451PhosphorylationLTFEPNPSPNSSPDL
EEECCCCCCCCCCCH		43.2722369663
454PhosphorylationEPNPSPNSSPDLLSK
CCCCCCCCCCCHHHC		46.7822369663
455PhosphorylationPNPSPNSSPDLLSKN
CCCCCCCCCCHHHCC		29.1322369663
460PhosphorylationNSSPDLLSKNNINNS
CCCCCHHHCCCCCCC		40.4022890988
461UbiquitinationSSPDLLSKNNINNST
CCCCHHHCCCCCCCC		54.7217644757
467PhosphorylationSKNNINNSTKDELSP
HCCCCCCCCCCCCCC		32.1422369663
468PhosphorylationKNNINNSTKDELSPN
CCCCCCCCCCCCCCC		44.6422369663
469UbiquitinationNNINNSTKDELSPNF
CCCCCCCCCCCCCCC		49.3723749301
469AcetylationNNINNSTKDELSPNF
CCCCCCCCCCCCCCC		49.3724489116
473PhosphorylationNSTKDELSPNFLNED
CCCCCCCCCCCCCCC		18.7523749301
485AcetylationNEDNFKLKYPMTEPV
CCCCCCEECCCCCCC		48.1524489116
486PhosphorylationEDNFKLKYPMTEPVP
CCCCCEECCCCCCCC		14.5224930733
550PhosphorylationRIPVTRMTPILLSLD
CCCCCCCCCEEEEEC		12.1428889911
558UbiquitinationPILLSLDKGSHVLEP
CEEEEECCCCCCCCH		68.5523749301
571UbiquitinationEPEVIHSKILAYKII
CHHHHCCHHHHHCCC		27.8117644757
583PhosphorylationKIIPKVESGLFSVDG
CCCCCCCCCCEEECC		43.7328889911
623PhosphorylationYIDTEFESM------
EECCCCCCC------		34.8021440633
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
451SPhosphorylationKinasePHO85P17157
Uniprot
455SPhosphorylationKinasePHO85P17157
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LCB4_YEAST !!
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 LCB4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LCB5_YEASTLCB5genetic
11056159
SUR2_YEASTSUR2genetic
16269340
GET1_YEASTGET1genetic
16269340
UBC6_YEASTUBC6genetic
16269340
COPB2_YEASTSEC27genetic
16269340
PMA1_YEASTPMA1genetic
16269340
SCS7_YEASTSCS7genetic
16269340
AKR2_YEASTAKR2physical
11283351
LCB5_YEASTLCB5genetic
18408719
UBP13_YEASTUBP13genetic
20093466
PEX32_YEASTPEX32genetic
20093466
STE50_YEASTSTE50genetic
20093466
LSM6_YEASTLSM6genetic
20093466
HXKA_YEASTHXK1genetic
20093466
ITC1_YEASTITC1genetic
20093466
AAKG_YEASTSNF4genetic
20093466
TPC1_YEASTTPC1genetic
20093466
BNS1_YEASTBNS1genetic
20093466
PAU13_YEASTPAU13genetic
20093466
RL8A_YEASTRPL8Agenetic
20093466
NDT80_YEASTNDT80genetic
20093466
CRP1_YEASTCRP1genetic
20093466
CTF8_YEASTCTF8genetic
20093466
IMPX_YEASTIMP2genetic
20093466
YII9_YEASTYIL089Wgenetic
20093466
FIS1_YEASTFIS1genetic
20093466
DCG1_YEASTDCG1genetic
20093466
VPS55_YEASTVPS55genetic
20093466
CYT2_YEASTCYT2genetic
20093466
RL14A_YEASTRPL14Agenetic
20093466
RSSA2_YEASTRPS0Bgenetic
20093466
BUD8_YEASTBUD8genetic
20093466
YM8M_YEASTYMR279Cgenetic
20093466
LSM7_YEASTLSM7genetic
20093466
SWS2_YEASTSWS2genetic
20093466
IRA2_YEASTIRA2genetic
20093466
AIM39_YEASTAIM39genetic
20093466
YAR1_YEASTYAR1genetic
20093466
NCBP2_YEASTCBC2genetic
20093466
CARP_YEASTPEP4genetic
20093466
ELP3_YEASTELP3genetic
20093466
PRPD_YEASTPDH1genetic
20093466
YME1_YEASTYME1genetic
20093466
UBA3_YEASTUBA3genetic
20093466
SCS7_YEASTSCS7genetic
20526336
SUR2_YEASTSUR2genetic
20526336
PP2C1_YEASTPTC1genetic
21127252
FUS3_YEASTFUS3genetic
21127252
REI1_YEASTREI1genetic
21127252
PP2A4_YEASTPPG1genetic
21127252
KCS1_YEASTKCS1genetic
21127252
SSK2_YEASTSSK2genetic
21127252
PBS2_YEASTPBS2genetic
21127252
SUM1_YEASTSUM1genetic
21127252
YAK1_YEASTYAK1genetic
21127252
AFT1_YEASTAFT1genetic
21127252
SWR1_YEASTSWR1genetic
21127252
GLN3_YEASTGLN3genetic
21127252
CTK1_YEASTCTK1genetic
21127252
BUB1_YEASTBUB1genetic
21127252
RTG3_YEASTRTG3genetic
21127252
SET2_YEASTSET2genetic
21127252
CSG2_YEASTCSG2genetic
21987634
DOP1_YEASTDOP1genetic
21987634
SUR2_YEASTSUR2genetic
21987634
ILM1_YEASTILM1genetic
21987634
SCS7_YEASTSCS7genetic
21987634
BNI4_YEASTBNI4genetic
21987634
PSD1_YEASTPSD1genetic
23891562
SRO7_YEASTSRO7genetic
23891562
ELO3_YEASTELO3genetic
23891562
CSG2_YEASTCSG2genetic
23891562
AIM18_YEASTAIM18genetic
27708008
RS28B_YEASTRPS28Bgenetic
27708008
RS30A_YEASTRPS30Agenetic
27708008
RS30B_YEASTRPS30Agenetic
27708008
CCZ1_YEASTCCZ1genetic
27708008
RS6A_YEASTRPS6Bgenetic
27708008
RS6B_YEASTRPS6Bgenetic
27708008
STE50_YEASTSTE50genetic
27708008
RV161_YEASTRVS161genetic
27708008
MAF1_YEASTMAF1genetic
27708008
SWF1_YEASTSWF1genetic
27708008
EF2_YEASTEFT2genetic
27708008
HXKA_YEASTHXK1genetic
27708008
RL24A_YEASTRPL24Agenetic
27708008
AAKG_YEASTSNF4genetic
27708008
ITC1_YEASTITC1genetic
27708008
RTF1_YEASTRTF1genetic
27708008
TPC1_YEASTTPC1genetic
27708008
BNS1_YEASTBNS1genetic
27708008
RL8A_YEASTRPL8Agenetic
27708008
PAU13_YEASTPAU13genetic
27708008
NDT80_YEASTNDT80genetic
27708008
URM1_YEASTURM1genetic
27708008
YKE4_YEASTYKE4genetic
27708008
FIS1_YEASTFIS1genetic
27708008
YII9_YEASTYIL089Wgenetic
27708008
IMPX_YEASTIMP2genetic
27708008
DCG1_YEASTDCG1genetic
27708008
SDHX_YEASTYJL045Wgenetic
27708008
GSH1_YEASTGSH1genetic
27708008
UBP12_YEASTUBP12genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
FEN1_YEASTRAD27genetic
27708008
RT109_YEASTRTT109genetic
27708008
RL8B_YEASTRPL8Bgenetic
27708008
BRE2_YEASTBRE2genetic
27708008
AVL9_YEASTAVL9genetic
27708008
BUD8_YEASTBUD8genetic
27708008
VPS9_YEASTVPS9genetic
27708008
YM8M_YEASTYMR279Cgenetic
27708008
SWS2_YEASTSWS2genetic
27708008
DUS2_YEASTSMM1genetic
27708008
BRE5_YEASTBRE5genetic
27708008
YO13A_YEASTYOL013W-Agenetic
27708008
AIM39_YEASTAIM39genetic
27708008
IRA2_YEASTIRA2genetic
27708008
RRP6_YEASTRRP6genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LCB4_YEAST

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"Long-chain base kinase Lcb4 Is anchored to the membrane through itspalmitoylation by Akr1.";
Kihara A., Kurotsu F., Sano T., Iwaki S., Igarashi Y.;
Mol. Cell. Biol. 25:9189-9197(2005).
Cited for: PALMITOYLATION AT CYS-43 AND CYS-46.
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-158; SER-160;SER-454 AND SER-455, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-454 ANDSER-455, AND MASS SPECTROMETRY.
"Phosphorylation by Pho85 cyclin-dependent kinase acts as a signal forthe down-regulation of the yeast sphingoid long-chain base kinase Lcb4during the stationary phase.";
Iwaki S., Kihara A., Sano T., Igarashi Y.;
J. Biol. Chem. 280:6520-6527(2005).
Cited for: PHOSPHORYLATION AT SER-451 AND SER-455, AND UBIQUITINATION.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-468, AND MASSSPECTROMETRY.

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