ECM22_YEAST - dbPTM
ECM22_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ECM22_YEAST
UniProt AC Q05958
Protein Name Sterol regulatory element-binding protein ECM22
Gene Name ECM22
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 814
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Transcription factor involved in sterol uptake and regulation of sterol biosynthesis. Binds to sterol regulatory elements (SRE) with the consensus sequence 5'-TCGTATA-3' present in ERG2 and ERG3 promoters and regulates transcription of ERG2 and ERG3 in response to sterol levels. Seems to be involved in activation of DAN2 and DAN3 cell wall mannoproteins..
Protein Sequence MTSDDGNAGQEREKDAELIEVGGKKVSKTSTGKRKFHNKSKTGCDNCKRRRVKCDEGKPFCKKCTNMKLDCVYSPIQPRRRKDSSSSKFASAVHDRVGKKNLSDNAIMLQQQQQQLHHQQEQQFRQQQQVQLQQQLLPHVGTDEQSNSPNSVPPSVSNNMENLLLPHLLASLVNNTSNSTNSSANGAEAHNNITQTAPSSMINNNHPNMALPGNSPLSIPITPSFQSTAMNLSSSLNGLLSPGRLNSVTNGLQQPQLQQQNQQIPQQQGTQSPFSNIPFDQLAQLNKMGLNFNMKSFNTLFPYGAANGMASEFQELFGLGKFATSNNRAIKVSTAEEALANMQQEQEDKNKQFTKNPLDNTKTDAVNSGNNPLNGNENKVTASDILSHNKNLIIDNTGLTISPPHTLSKPSIDQNIASPSTGVSNVTSTKSLLSIPDNRTALGNSPTLKTSPMGDLLSNSEALSPRSSNSHTQQQSSPHSNASSASRLVPELVGLSRKSNLNLIDLKLFHHYCTDVWHTITEAGISGPEVWSTYIPDLAFHFPFLMHTILAFSATHLSRTEAGLDNYVSSHRLEALRLLREAVLEISDDNTDALVASALILILDSLANASSSSPTAWIFHVKGAVTILTAVWPLSETSKFYNLISVDLSDLGEAVINQSNHNNDNDNSNNGDGNNNNTISELVCFDESIADLYPVEIDSPYLITLAYLDKLHREKNQLDFMLRVFSFPALLDRTFLALLMTGDLGAMRIMRSYYTLLRGYTTEIKDKVWFLDSVSQVLPQDVDEYSGGGGMHMMLDFLGGGLPSMTTTNFSAFM
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
2Phosphorylation------MTSDDGNAG
------CCCCCCCCC		40.6428889911
3Phosphorylation-----MTSDDGNAGQ
-----CCCCCCCCCC		32.1923749301
24AcetylationELIEVGGKKVSKTST
HEEEECCEEEEECCC		44.0324489116
74PhosphorylationMKLDCVYSPIQPRRR
CEECEEECCCCCCCC		8.6428889911
86PhosphorylationRRRKDSSSSKFASAV
CCCCCCCCHHHHHHH		41.3127214570
87PhosphorylationRRKDSSSSKFASAVH
CCCCCCCHHHHHHHH		33.4728889911
88UbiquitinationRKDSSSSKFASAVHD
CCCCCCHHHHHHHHH		47.0722817900
88AcetylationRKDSSSSKFASAVHD
CCCCCCHHHHHHHHH		47.0722865919
400PhosphorylationIIDNTGLTISPPHTL
EECCCCCCCCCCCCC		22.2829734811
402PhosphorylationDNTGLTISPPHTLSK
CCCCCCCCCCCCCCC		27.4321440633
406PhosphorylationLTISPPHTLSKPSID
CCCCCCCCCCCCCCC		38.2024961812
411PhosphorylationPHTLSKPSIDQNIAS
CCCCCCCCCCCCCCC		42.4021440633
418PhosphorylationSIDQNIASPSTGVSN
CCCCCCCCCCCCCCC		18.6524909858
420PhosphorylationDQNIASPSTGVSNVT
CCCCCCCCCCCCCCC		34.9921440633
431PhosphorylationSNVTSTKSLLSIPDN
CCCCCCCHHHCCCCC		34.3321551504
434PhosphorylationTSTKSLLSIPDNRTA
CCCCHHHCCCCCCCC		37.0528889911
440PhosphorylationLSIPDNRTALGNSPT
HCCCCCCCCCCCCCC		32.2728889911
445PhosphorylationNRTALGNSPTLKTSP
CCCCCCCCCCCCCCC		19.9122369663
447PhosphorylationTALGNSPTLKTSPMG
CCCCCCCCCCCCCCH		40.4822369663
450PhosphorylationGNSPTLKTSPMGDLL
CCCCCCCCCCCHHHC		40.9727017623
451PhosphorylationNSPTLKTSPMGDLLS
CCCCCCCCCCHHHCC		15.9922890988
460PhosphorylationMGDLLSNSEALSPRS
CHHHCCCCCCCCCCC		22.3722890988
464PhosphorylationLSNSEALSPRSSNSH
CCCCCCCCCCCCCCC		25.8911208779
476PhosphorylationNSHTQQQSSPHSNAS
CCCCCCCCCCCCCHH		41.3128889911
477PhosphorylationSHTQQQSSPHSNASS
CCCCCCCCCCCCHHH		23.4623749301
480PhosphorylationQQQSSPHSNASSASR
CCCCCCCCCHHHHHH		37.1630377154
498AcetylationELVGLSRKSNLNLID
HHHCCCCCCCCCHHH		40.0824489116
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 ECM22_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ECM22_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 ECM22_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UPC2_YEASTUPC2genetic
11533229
ERG2_YEASTERG2genetic
16702413
ERG6_YEASTERG6genetic
16702413
ERG28_YEASTERG28genetic
16702413
MOT3_YEASTMOT3physical
16783004
ELO3_YEASTELO3genetic
15638242
YAP5_YEASTYAP5genetic
20831804
SWI5_YEASTSWI5genetic
20831804
URE2_YEASTURE2genetic
20959818
YP022_YEASTYPR022Cgenetic
20959818
ARP8_YEASTARP8genetic
20959818
SIN3_YEASTSIN3genetic
20959818
UPC2_YEASTUPC2genetic
20959818
VPS71_YEASTVPS71genetic
20959818
TOD6_YEASTTOD6genetic
20959818
HMO1_YEASTHMO1genetic
20959818
MGA2_YEASTMGA2genetic
20959818
SODC_YEASTSOD1genetic
20959818
AF9_YEASTYAF9genetic
20959818
HAP5_YEASTHAP5genetic
20959818
KCS1_YEASTKCS1genetic
21127252
UPC2_YEASTUPC2genetic
21127252
MET18_YEASTMET18genetic
21127252
CHA4_YEASTCHA4genetic
21127252
PRR2_YEASTPRR2genetic
21127252
CTK1_YEASTCTK1genetic
21127252
VMS1_YEASTVMS1genetic
21127252
ASH1_YEASTASH1genetic
21127252
UPC2_YEASTUPC2genetic
26448198
STE12_YEASTSTE12genetic
26448198
GPR1_YEASTGPR1genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
ATC3_YEASTDRS2genetic
27708008
ELO2_YEASTELO2genetic
27708008
ODO2_YEASTKGD2genetic
27708008
UPC2_YEASTUPC2genetic
27708008
ODPA_YEASTPDA1genetic
27708008
YG036_YEASTYGL036Wgenetic
27708008
SPO74_YEASTSPO74genetic
27708008
SLX9_YEASTSLX9genetic
27708008
SNF6_YEASTSNF6genetic
27708008
INM1_YEASTINM1genetic
27708008
ATG32_YEASTATG32genetic
27708008
VPS53_YEASTVPS53genetic
27708008
IME1_YEASTIME1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
UPC2_YEASTUPC2genetic
28986257
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ECM22_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 SER-74; SER-431; SER-434;SER-445 AND SER-464, AND MASS SPECTROMETRY.

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