SCD5_YEAST - dbPTM
SCD5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCD5_YEAST
UniProt AC P34758
Protein Name Protein SCD5
Gene Name SCD5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 872
Subcellular Localization Membrane
Peripheral membrane protein.
Protein Description Involved in vesicular transport at a late stage of the secretory pathway..
Protein Sequence MSFDWLNVPGLDLSSGDQAEKRPSNGLGPPSVSFDFGINTAAPHDSSFWDQGSRSHSDTTLSYRNNHSNTAADNATNVSSPQKDNPPNGEVRTLSGGDVYAESPEDMQVPLSLSQNQLTHEEIRTYLRWYHYICLRTHGKLVRLNDVFRFLTNFNLSQKVKDRIVEIFRSCKNALNIGQFFAVLRLVSRAIIYGILPLRRMILEKAPVPKPRPILSSENHEEVYEEVEDDDSSAKTGDQKVDFDSFASLLLTGKTTRKRVRRRIKNLNFKSKKVRFSEHITFQDPPNLNQESSNNSEARKQDPDAEDEDQDSNNDSPLDFTLPMDQLLKRLYKRRKNSGLVSSLPSEQQETEEEKKVLEDMKDSLSHFKQIQTVDSASLPISSVFLQNGNTLPTSNVNNTTVPQQLPLEPLKPTATGSANHLVREEYNQGLHPSNGAIQTGLQPLKPTATGSANYLMRSHMEQPQSIKPSSTPETVTNSGGLQPLKPTATGSANYLMKQHISPSVNNPVSSMFQAQFTNQSSSPQSTGPAFLNSPNITLPQSNQQQPYQEVNPTQAKIEPSNISPQHTYSNNVRINNGNIVSMPKVEITGAFPPQNTLPQHQQSHLLSPQNTIPQHQRSQLISPQNTFTQNQPILSPQHTYSNNQATMISPQNTYTNNQQQPQHLPPPPPPRAQQQQQGAIVPPQHMYSNVQKQNNLVPTQPSYTNSPSIQSPNFLSPQNAANSYFQSLLSSSPSPNPTPSNASTVNGNNASNGISSFQNTSAAMNNTQSHQTYIQQQQQQQTQQRIYGGQLSQMQQHPGQLHLNNSDIHSQPNKPNYGMLGQQVHQQQQQQQQQFPFTADVNRSNSSDILGNLQSLQQQVDALQIQYNRRP
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
24PhosphorylationDQAEKRPSNGLGPPS
CCCCCCCCCCCCCCC		47.7921440633
31PhosphorylationSNGLGPPSVSFDFGI
CCCCCCCCEEEECCC		33.2621440633
55PhosphorylationFWDQGSRSHSDTTLS
CCCCCCCCCCCCEEE		29.1022369663
57PhosphorylationDQGSRSHSDTTLSYR
CCCCCCCCCCEEECC		37.5922369663
59PhosphorylationGSRSHSDTTLSYRNN
CCCCCCCCEEECCCC		32.4322369663
60PhosphorylationSRSHSDTTLSYRNNH
CCCCCCCEEECCCCC		20.7822369663
62PhosphorylationSHSDTTLSYRNNHSN
CCCCCEEECCCCCCC		21.6922369663
63PhosphorylationHSDTTLSYRNNHSNT
CCCCEEECCCCCCCC		22.0722369663
76PhosphorylationNTAADNATNVSSPQK
CCCCCCCCCCCCCCC		42.2728132839
79PhosphorylationADNATNVSSPQKDNP
CCCCCCCCCCCCCCC		38.0724909858
80PhosphorylationDNATNVSSPQKDNPP
CCCCCCCCCCCCCCC		27.3725533186
292PhosphorylationPPNLNQESSNNSEAR
CCCCCCCCCCCHHHH		28.7119779198
312PhosphorylationAEDEDQDSNNDSPLD
CCCCCCCCCCCCCCC		31.7219779198
416PhosphorylationEPLKPTATGSANHLV
CCCCCCCCCCHHHHH		33.8628889911
448PhosphorylationGLQPLKPTATGSANY
CCCCCCCCCCCCHHH		34.9528889911
450PhosphorylationQPLKPTATGSANYLM
CCCCCCCCCCHHHHH		33.8628889911
488PhosphorylationGLQPLKPTATGSANY
CCCCCCCCCCCCHHH		34.9528889911
490PhosphorylationQPLKPTATGSANYLM
CCCCCCCCCCHHHHH		33.8628889911
492PhosphorylationLKPTATGSANYLMKQ
CCCCCCCCHHHHHHH		14.6921440633
495PhosphorylationTATGSANYLMKQHIS
CCCCCHHHHHHHCCC		14.1121440633
561PhosphorylationTQAKIEPSNISPQHT
CCCCCCCCCCCCCCC		33.7222369663
564PhosphorylationKIEPSNISPQHTYSN
CCCCCCCCCCCCCCC		23.8222369663
568PhosphorylationSNISPQHTYSNNVRI
CCCCCCCCCCCCEEE		24.3322369663
569PhosphorylationNISPQHTYSNNVRIN
CCCCCCCCCCCEEEE		13.7922369663
570PhosphorylationISPQHTYSNNVRINN
CCCCCCCCCCEEEEC		24.0822369663
604PhosphorylationTLPQHQQSHLLSPQN
CCCHHHHHHCCCCCC		14.9928889911
608PhosphorylationHQQSHLLSPQNTIPQ
HHHHHCCCCCCCCCH		30.6921082442
845PhosphorylationFTADVNRSNSSDILG
CCCCCCCCCHHHHHH		35.5430377154
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
416TPhosphorylationKinasePRK1P40494
Uniprot
450TPhosphorylationKinasePRK1P40494
Uniprot
490TPhosphorylationKinasePRK1P40494
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
416TPhosphorylation

13679512
450TPhosphorylation

13679512
490TPhosphorylation

13679512
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 SCD5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP12_YEASTGLC7physical
12356757
PP12_YEASTGLC7genetic
12356757
ABP1_YEASTABP1genetic
12181333
RV161_YEASTRVS161genetic
12181333
RV167_YEASTRVS167genetic
12181333
FIMB_YEASTSAC6genetic
12181333
CLH_YEASTCHC1genetic
12181333
END3_YEASTEND3genetic
12181333
PAN1_YEASTPAN1genetic
12181333
SLA2_YEASTSLA2genetic
12181333
AKL1_YEASTAKL1genetic
12956961
PRK1_YEASTPRK1genetic
13679512
PRK1_YEASTPRK1genetic
12956961
ARK1_YEASTARK1genetic
12956961
PAN1_YEASTPAN1physical
17898076
END3_YEASTEND3physical
17898076
PAN1_YEASTPAN1genetic
17898076
END3_YEASTEND3genetic
17898076
PP12_YEASTGLC7physical
17898076
SCD5_YEASTSCD5physical
19345193
LDS1_YEASTLDS1genetic
20093466
AVT5_YEASTAVT5genetic
20093466
EDE1_YEASTEDE1genetic
20093466
RIM1_YEASTRIM1genetic
20093466
BCS1_YEASTBCS1genetic
20093466
RTF1_YEASTRTF1genetic
20093466
HUR1_YEASTHUR1genetic
20093466
ATC1_YEASTPMR1genetic
20093466
RL8A_YEASTRPL8Agenetic
20093466
HAP4_YEASTHAP4genetic
20093466
CCW12_YEASTCCW12genetic
20093466
STM1_YEASTSTM1genetic
20093466
SST2_YEASTSST2genetic
20093466
SIN3_YEASTSIN3genetic
20093466
DFG16_YEASTDFG16genetic
20093466
SLA1_YEASTSLA1genetic
22825870
SHE9_YEASTSHE9physical
22875988
END3_YEASTEND3physical
22875988
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SCD5_YEAST

loading...

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 SER-57 AND SER-564, AND MASSSPECTROMETRY.
"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 SER-57 AND SER-564, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory