YEL1_YEAST - dbPTM
YEL1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YEL1_YEAST
UniProt AC P34225
Protein Name Guanine-nucleotide exchange factor YEL1
Gene Name YEL1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 687
Subcellular Localization Cytoplasm. Cell membrane
Peripheral membrane protein. Bud neck. Bud tip. Localizes at the cell membrane only at the bud neck and bud tip and this localization is ARF3-dependent.
Protein Description Guanine-nucleotide exchange factor for ARF3 required for localization of ARF3 to the bud neck and tip and involved in actin patch polarization..
Protein Sequence MCASLNEVKKNDTYGVSQKGYNDNFSESEGVLHGSKSMPTSMKNMLQSPTMVNMCDILQNKEAANDEKPVIPTTDTATAGTGTEDISSTQSEETDQNSHLIASEILEGTFKDVSYKEYANFLGNDNNNQVLTEFVKLLSPLPSSLLETLFNLSKSIYFIAEAQNIDRILECLSIEWIACHPNTHWKSGYKSCHIVLFSLLILNSDLHNNFQVDHKKIKFSMVAFINNTLRALREENEYEELKIYSREHLIIEELSEYYKTLNETPLPLCTESRTSINISDNQSSLKRFSTLGSREFSTSNLRSVNSNSTTLYSRDGQVSVREMSAKSNKNFHNNHPMDALYLKESFDDGLITENGSSWFMDDLILISKKSLPRKYSKRDKDQVAAPKMTSKRNKSFFGWLKPSKTTTLIEHTSRRTSLSYLNKDSEWERVKIQVKEGRIFIFKIKPDVKDIIQSSETDSATIDYFKDISSSYFAYSLLEAEAHVVQDNIIIGSGAMKSNVCNKNTKRKSGNFTVSFPENINGPKLVLEFQTRSVEEAHKFMDCINFWAGRISPVPLTQFEAVSNAEYGWSDKILTEHASLNLKNIVVSEWKPLLGLELLYEDAKDVEMVELKERLKELMNFTRQLGIWIDKHNEIKDKLVEIWSFDDNYFEAVMNNWNSRYLYMNNQYKKRLSYLKALQKAMGSVQF
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
26PhosphorylationKGYNDNFSESEGVLH
CCCCCCCCCCCCCCC		46.6022369663
28PhosphorylationYNDNFSESEGVLHGS
CCCCCCCCCCCCCCC		38.1522369663
35PhosphorylationSEGVLHGSKSMPTSM
CCCCCCCCCCCCCHH		15.7123749301
36UbiquitinationEGVLHGSKSMPTSMK
CCCCCCCCCCCCHHH		56.2023749301
37PhosphorylationGVLHGSKSMPTSMKN
CCCCCCCCCCCHHHH		31.5223749301
40PhosphorylationHGSKSMPTSMKNMLQ
CCCCCCCCHHHHHHC		32.5821440633
41PhosphorylationGSKSMPTSMKNMLQS
CCCCCCCHHHHHHCC		23.1421440633
50PhosphorylationKNMLQSPTMVNMCDI
HHHHCCCCHHHHHHH		38.7121551504
88PhosphorylationTGTEDISSTQSEETD
CCCCCCCCCCCCCCC		30.6921551504
91PhosphorylationEDISSTQSEETDQNS
CCCCCCCCCCCCCCC		37.1721551504
242UbiquitinationENEYEELKIYSREHL
HCCCHHHHCCCCHHH		42.7624961812
272PhosphorylationPLPLCTESRTSINIS
CCCCCCCCCCEEECC		23.7821551504
274PhosphorylationPLCTESRTSINISDN
CCCCCCCCEEECCCC		43.1523749301
275PhosphorylationLCTESRTSINISDNQ
CCCCCCCEEECCCCH		16.7219795423
279PhosphorylationSRTSINISDNQSSLK
CCCEEECCCCHHHHH		26.4821440633
283PhosphorylationINISDNQSSLKRFST
EECCCCHHHHHHHHH		43.8428152593
284PhosphorylationNISDNQSSLKRFSTL
ECCCCHHHHHHHHHC		28.3121440633
286UbiquitinationSDNQSSLKRFSTLGS
CCCHHHHHHHHHCCC		54.0323749301
289PhosphorylationQSSLKRFSTLGSREF
HHHHHHHHHCCCCCC		27.1022369663
290PhosphorylationSSLKRFSTLGSREFS
HHHHHHHHCCCCCCC		32.2122369663
293PhosphorylationKRFSTLGSREFSTSN
HHHHHCCCCCCCCCC		31.5822369663
297PhosphorylationTLGSREFSTSNLRSV
HCCCCCCCCCCCEEC		26.6022369663
298PhosphorylationLGSREFSTSNLRSVN
CCCCCCCCCCCEECC		27.2722369663
299PhosphorylationGSREFSTSNLRSVNS
CCCCCCCCCCEECCC		32.4422369663
303PhosphorylationFSTSNLRSVNSNSTT
CCCCCCEECCCCCCE		28.9022369663
306PhosphorylationSNLRSVNSNSTTLYS
CCCEECCCCCCEEEC		29.9622369663
308PhosphorylationLRSVNSNSTTLYSRD
CEECCCCCCEEECCC		23.6922369663
309PhosphorylationRSVNSNSTTLYSRDG
EECCCCCCEEECCCC		25.6819779198
310PhosphorylationSVNSNSTTLYSRDGQ
ECCCCCCEEECCCCE		24.4222369663
312PhosphorylationNSNSTTLYSRDGQVS
CCCCCEEECCCCEEE		10.2822369663
313PhosphorylationSNSTTLYSRDGQVSV
CCCCEEECCCCEEEE		27.3222369663
319PhosphorylationYSRDGQVSVREMSAK
ECCCCEEEEEEECCC		13.9427214570
324PhosphorylationQVSVREMSAKSNKNF
EEEEEEECCCCCCCC		28.0027017623
395PhosphorylationMTSKRNKSFFGWLKP
CCCCCCCCCCCCCCC		29.3821440633
416PhosphorylationIEHTSRRTSLSYLNK
EEECCCCCCCHHHCC		32.6730377154
417PhosphorylationEHTSRRTSLSYLNKD
EECCCCCCCHHHCCC		17.3228889911
498PhosphorylationIGSGAMKSNVCNKNT
ECCCCHHCCCCCCCC		22.7821126336
674PhosphorylationQYKKRLSYLKALQKA
HHHHHHHHHHHHHHH		19.4728889911
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 YEL1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YEL1_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 YEL1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARF3_YEASTARF3physical
17786213
YD090_YEASTYDR090Cgenetic
27708008
OMS1_YEASTOMS1genetic
27708008
ASK10_YEASTASK10genetic
27708008
RS27B_YEASTRPS27Bgenetic
27708008
URA8_YEASTURA8genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
SECU_YEASTPDS1genetic
29674565
FCF1_YEASTFCF1genetic
29674565
SEM1_YEASTSEM1genetic
29674565
EMP47_YEASTEMP47genetic
29674565
MMS2_YEASTMMS2genetic
29674565
SIC1_YEASTSIC1genetic
29674565
BRR1_YEASTBRR1genetic
29674565
RS26B_YEASTRPS26Bgenetic
29674565
GSH1_YEASTGSH1genetic
29674565
RL14A_YEASTRPL14Agenetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YEL1_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-284; THR-290; SER-293;SER-297; SER-303 AND SER-306, AND MASS SPECTROMETRY.
"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-26 AND THR-290, AND MASSSPECTROMETRY.

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