LDB19_YEAST - dbPTM
LDB19_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LDB19_YEAST
UniProt AC Q12502
Protein Name Protein LDB19
Gene Name LDB19
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 818
Subcellular Localization Cytoplasm . Golgi apparatus .
Protein Description May be involved in protein-linked oligosaccharide phosphorylation since the deletion reduces the negative charge of the cell surface. Involved in the resistance to EDTA, cadmium chloride, cycloheximide, 6-dimethylaminopurine, methyl caffeate, beta-chloro-L-alanine, caffeine and cerulenin..
Protein Sequence MAFSRLTSTHQSNHNGYSNSNKKGQSLPLTLSIDVESPPCVLYGSAMESSGAVLSGLFTVTVVDPYSSAEDKSLKNTESNVSTTSKSLKRKSTFGSALSSRLSSLSASTSNISPSTSSTSISHSPTPANLRIMAGYTKITITSVTLSLVQKIHFHKPFVPNISSMQTCMNCKTKITNMKSWEIQSNTQDLSVGSHSYPFSYLIPGSVPCSSSLGATAETQVKYELIAVVTYIDPHRNSFSSGHSTPRKEGSSSKKRLLQLAMPIAVTRSIPRGPDKNSLRVFPPTELTAAAVLPNVVYPKSTFPLEMKLDGVSSGDRRWRMRKLSWRIEETTRVKAHACPVHKHELRQLEEQVKIKESEKSKKPRSHIKRYGELGPQIRVAVNSLENMPSQRLPGEPGREQAPNSSGPASTGNVGLDDENPVNEDEEDQPGSEFIHPSDDALRQELLMQQQRARQQQLQQELKNNSSLFTEEVRIISKGEMKSGWKTDFDNNGKIELVTEIDCMGLNSGVSNPVMHASTLQTPSTGNKKPSINVACDIQDPNLGLYVSHILAVEIVVAEETLQYANGQPIRKPNSKNKKETNNNTMNVHNPDQRLAELSPIFANRNTPKVRRMGPEDITPVNSNKSNHSTNKEKASNGASNSNIVSVPTGAARVLRMQFRLTVTERSGLGISWDEEVPPIYQDVELLSPPCYELSINNGIKNKLYSTMSTPVRSEDDFVGGSDEDIGNYESQGLEPGPNVQEVTITQNKLTIPPTAHHYQPASSSQRSLTTVQSPPLESVVSVQGSVPFRGHVLTPHSTRDIRIQNFSDFLDSNRITQ
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
75UbiquitinationSAEDKSLKNTESNVS
CCCCCCCCCCCCCCC		69.7623749301
77PhosphorylationEDKSLKNTESNVSTT
CCCCCCCCCCCCCCC		38.9221082442
79PhosphorylationKSLKNTESNVSTTSK
CCCCCCCCCCCCCCH		40.2619684113
82PhosphorylationKNTESNVSTTSKSLK
CCCCCCCCCCCHHHC		30.1619684113
83PhosphorylationNTESNVSTTSKSLKR
CCCCCCCCCCHHHCC		30.7023749301
84PhosphorylationTESNVSTTSKSLKRK
CCCCCCCCCHHHCCH		27.0119684113
85PhosphorylationESNVSTTSKSLKRKS
CCCCCCCCHHHCCHH		21.9728889911
87PhosphorylationNVSTTSKSLKRKSTF
CCCCCCHHHCCHHHH		38.6023749301
91UbiquitinationTSKSLKRKSTFGSAL
CCHHHCCHHHHHHHH		52.8717644757
92PhosphorylationSKSLKRKSTFGSALS
CHHHCCHHHHHHHHH		32.7628889911
93PhosphorylationKSLKRKSTFGSALSS
HHHCCHHHHHHHHHH		34.7417330950
96PhosphorylationKRKSTFGSALSSRLS
CCHHHHHHHHHHHHH		23.1122369663
99PhosphorylationSTFGSALSSRLSSLS
HHHHHHHHHHHHHHC		17.0922369663
100PhosphorylationTFGSALSSRLSSLSA
HHHHHHHHHHHHHCC		37.7822369663
103PhosphorylationSALSSRLSSLSASTS
HHHHHHHHHHCCCCC		28.2922369663
104PhosphorylationALSSRLSSLSASTSN
HHHHHHHHHCCCCCC		30.8223749301
106PhosphorylationSSRLSSLSASTSNIS
HHHHHHHCCCCCCCC		23.3222369663
108PhosphorylationRLSSLSASTSNISPS
HHHHHCCCCCCCCCC		29.0622369663
109PhosphorylationLSSLSASTSNISPST
HHHHCCCCCCCCCCC		26.0522369663
110PhosphorylationSSLSASTSNISPSTS
HHHCCCCCCCCCCCC		29.6622369663
113PhosphorylationSASTSNISPSTSSTS
CCCCCCCCCCCCCCC		19.6322369663
115PhosphorylationSTSNISPSTSSTSIS
CCCCCCCCCCCCCCC		33.8422369663
116PhosphorylationTSNISPSTSSTSISH
CCCCCCCCCCCCCCC		30.0422369663
117PhosphorylationSNISPSTSSTSISHS
CCCCCCCCCCCCCCC		35.6422369663
118PhosphorylationNISPSTSSTSISHSP
CCCCCCCCCCCCCCC		26.6822369663
119PhosphorylationISPSTSSTSISHSPT
CCCCCCCCCCCCCCC		29.8222369663
120PhosphorylationSPSTSSTSISHSPTP
CCCCCCCCCCCCCCC		24.8421440633
122PhosphorylationSTSSTSISHSPTPAN
CCCCCCCCCCCCCCC		20.0622369663
124PhosphorylationSSTSISHSPTPANLR
CCCCCCCCCCCCCEE		24.5522369663
126PhosphorylationTSISHSPTPANLRIM
CCCCCCCCCCCEEEE		37.7422369663
136PhosphorylationNLRIMAGYTKITITS
CEEEEECCEEEEEEE		8.7028889911
137PhosphorylationLRIMAGYTKITITSV
EEEEECCEEEEEEEE		18.3028889911
140PhosphorylationMAGYTKITITSVTLS
EECCEEEEEEEEHHH		21.5428889911
142PhosphorylationGYTKITITSVTLSLV
CCEEEEEEEEHHHHH		14.4328889911
143PhosphorylationYTKITITSVTLSLVQ
CEEEEEEEEHHHHHH		14.8428889911
145PhosphorylationKITITSVTLSLVQKI
EEEEEEEHHHHHHHH		15.4728889911
173PhosphorylationQTCMNCKTKITNMKS
HHHHHCCCEEECCCC		29.8528889911
176PhosphorylationMNCKTKITNMKSWEI
HHCCCEEECCCCEEE		30.7128889911
238PhosphorylationYIDPHRNSFSSGHST
EECCCCCCCCCCCCC		26.8522369663
240PhosphorylationDPHRNSFSSGHSTPR
CCCCCCCCCCCCCCC		34.9222369663
241PhosphorylationPHRNSFSSGHSTPRK
CCCCCCCCCCCCCCC		38.2222369663
244PhosphorylationNSFSSGHSTPRKEGS
CCCCCCCCCCCCCCC		43.5622369663
245PhosphorylationSFSSGHSTPRKEGSS
CCCCCCCCCCCCCCC		22.8022369663
300UbiquitinationLPNVVYPKSTFPLEM
CCCCCCCCCCCCEEE		44.4317644757
369UbiquitinationKKPRSHIKRYGELGP
CCCHHHHHHHHHCHH		33.8617644757
384PhosphorylationQIRVAVNSLENMPSQ
HHHHHHHHHHCCCCC		30.3828889911
463UbiquitinationQQLQQELKNNSSLFT
HHHHHHHHHCCCCCE		54.0223749301
482UbiquitinationIISKGEMKSGWKTDF
EEECCCCCCCCEECC		41.3322817900
486UbiquitinationGEMKSGWKTDFDNNG
CCCCCCCEECCCCCC		41.5623749301
599PhosphorylationDQRLAELSPIFANRN
HHHHHHHCHHHCCCC		13.8828152593
607PhosphorylationPIFANRNTPKVRRMG
HHHCCCCCCCHHHCC		22.6523749301
619PhosphorylationRMGPEDITPVNSNKS
HCCCCCCCCCCCCCC		33.2422369663
623PhosphorylationEDITPVNSNKSNHST
CCCCCCCCCCCCCCC		45.9622369663
625UbiquitinationITPVNSNKSNHSTNK
CCCCCCCCCCCCCCH		53.0817644757
626PhosphorylationTPVNSNKSNHSTNKE
CCCCCCCCCCCCCHH		43.9828889911
629PhosphorylationNSNKSNHSTNKEKAS
CCCCCCCCCCHHHHC		37.6221551504
630PhosphorylationSNKSNHSTNKEKASN
CCCCCCCCCHHHHCC		42.6424961812
634UbiquitinationNHSTNKEKASNGASN
CCCCCHHHHCCCCCC		59.7423749301
703UbiquitinationINNGIKNKLYSTMST
ECCCCCCHHCCCCCC		43.7423749301
705PhosphorylationNGIKNKLYSTMSTPV
CCCCCHHCCCCCCCC		12.0527017623
706PhosphorylationGIKNKLYSTMSTPVR
CCCCHHCCCCCCCCC		28.2427017623
709PhosphorylationNKLYSTMSTPVRSED
CHHCCCCCCCCCCCC		29.6428889911
710PhosphorylationKLYSTMSTPVRSEDD
HHCCCCCCCCCCCCC		18.2527017623
714PhosphorylationTMSTPVRSEDDFVGG
CCCCCCCCCCCCCCC		45.6823749301
722PhosphorylationEDDFVGGSDEDIGNY
CCCCCCCCCCCCCCC		31.7223749301
729PhosphorylationSDEDIGNYESQGLEP
CCCCCCCCHHCCCCC		16.2523749301
731PhosphorylationEDIGNYESQGLEPGP
CCCCCCHHCCCCCCC		21.1330377154
774PhosphorylationRSLTTVQSPPLESVV
CCEEEECCCCCCCEE		24.9319684113
779PhosphorylationVQSPPLESVVSVQGS
ECCCCCCCEEEEECC		35.1928889911
782PhosphorylationPPLESVVSVQGSVPF
CCCCCEEEEECCCCC		13.4319684113
795PhosphorylationPFRGHVLTPHSTRDI
CCCCEEECCCCCCCE		20.1928132839
798PhosphorylationGHVLTPHSTRDIRIQ
CEEECCCCCCCEEEC		26.7529136822
799PhosphorylationHVLTPHSTRDIRIQN
EEECCCCCCCEEECC		29.3529136822
808PhosphorylationDIRIQNFSDFLDSNR
CEEECCHHHHHHHCC		34.6928889911
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 LDB19_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LDB19_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 LDB19_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RSP5_YEASTRSP5physical
16554755
RSP5_YEASTRSP5physical
18719252
PMA1_YEASTPMA1genetic
23891562
ATC6_YEASTSPF1genetic
23891562
MNN11_YEASTMNN11genetic
23891562
RGP1_YEASTRGP1genetic
23891562
RIC1_YEASTRIC1genetic
23891562
YPT6_YEASTYPT6genetic
23891562
GET3_YEASTGET3genetic
23891562
VPS17_YEASTVPS17genetic
23891562
ERG26_YEASTERG26genetic
23891562
MSMO_YEASTERG25genetic
23891562
ERG5_YEASTERG5genetic
23891562
PACC_YEASTRIM101genetic
23891562
PALF_YEASTRIM8genetic
23891562
PALH_YEASTRIM21genetic
23891562
CSG2_YEASTCSG2genetic
23891562
TPM1_YEASTTPM1genetic
23891562
PEX18_YEASTPEX18genetic
23891562
BAR1_YEASTBAR1genetic
24820415
ROG3_YEASTROG3genetic
24820415
ROD1_YEASTROD1genetic
24820415
SST2_YEASTSST2genetic
24820415
RSP5_YEASTRSP5physical
24820415
RHO1_YEASTRHO1physical
26459639
SCC1_YEASTMCD1genetic
27708008
CCZ1_YEASTCCZ1genetic
27708008
CDC24_YEASTCDC24genetic
27708008
TCPD_YEASTCCT4genetic
27708008
PSB7_YEASTPRE4genetic
27708008
RNA15_YEASTRNA15genetic
27708008
PSF2_YEASTPSF2genetic
27708008
FIP1_YEASTFIP1genetic
27708008
NOP56_YEASTNOP56genetic
27708008
GPI12_YEASTGPI12genetic
27708008
LIP1_YEASTLIP1genetic
27708008
LST8_YEASTLST8genetic
27708008
SEC12_YEASTSEC12genetic
27708008
MVD1_YEASTMVD1genetic
27708008
GPI2_YEASTGPI2genetic
27708008
BUR1_YEASTSGV1genetic
27708008
ATC3_YEASTDRS2genetic
27708008
SEA4_YEASTSEA4genetic
27708008
SWC5_YEASTSWC5genetic
27708008
RV161_YEASTRVS161genetic
27708008
BRE1_YEASTBRE1genetic
27708008
TPS2_YEASTTPS2genetic
27708008
SPO71_YEASTSPO71genetic
27708008
INO2_YEASTINO2genetic
27708008
H2A1_YEASTHTA1genetic
27708008
MET32_YEASTMET32genetic
27708008
LSM6_YEASTLSM6genetic
27708008
RAD4_YEASTRAD4genetic
27708008
FMP32_YEASTFMP32genetic
27708008
PIB2_YEASTPIB2genetic
27708008
PALF_YEASTRIM8genetic
27708008
RTG2_YEASTRTG2genetic
27708008
ASK10_YEASTASK10genetic
27708008
ELP2_YEASTELP2genetic
27708008
UBA4_YEASTUBA4genetic
27708008
ICE2_YEASTICE2genetic
27708008
FMC1_YEASTFMC1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
YET1_YEASTYET1genetic
27708008
KTI12_YEASTKTI12genetic
27708008
SSH4_YEASTSSH4genetic
27708008
CBT1_YEASTCBT1genetic
27708008
MEH1_YEASTMEH1genetic
27708008
IRS4_YEASTIRS4genetic
27708008
PUF3_YEASTPUF3genetic
27708008
CDC73_YEASTCDC73genetic
27708008
GTR1_YEASTGTR1genetic
27708008
ZDS1_YEASTZDS1genetic
27708008
LSM7_YEASTLSM7genetic
27708008
ERFD_YEASTSHR5genetic
27708008
LGE1_YEASTLGE1genetic
27708008
BUL2_YEASTBUL2genetic
28814503
BUL1_YEASTBUL1genetic
28814503
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LDB19_YEAST

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Related Literatures of Post-Translational Modification
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 THR-93; SER-384 AND THR-619,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 THR-93, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery.";
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-486, AND MASSSPECTROMETRY.

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