ENT2_YEAST - dbPTM
ENT2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ENT2_YEAST
UniProt AC Q05785
Protein Name Epsin-2
Gene Name ENT2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 613
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Localizes in a punctate pattern. Found in the actin cortical patches, although the majority is located at the cell periphery.
Protein Description Binds to membranes enriched in phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin..
Protein Sequence MSKQFVRSAKNMMKGYSSTQVLVRDATANDSRTPSIDTLDDLAQRSYDSVDFFEIMDMLDKRLNDKGKYWRHVAKSLTVLDYLVRFGSENCVLWCRENFYVIKTLREFRHENESGFDEGQIIRVKAKELVSLLNDEERLREERSMNTRNRRANRAARPRPRRQRTRSNPHDSSPSYQDDLEKALEESRITAQEDEQRRRELAQYDDEDPDFQAALQLSKEEEELKQLQELQRLQKQQQSLSQFQAPLQQQQPQQQPAYYDIFGNPISQDEYLQYQYQQDQEQAMAQQRWLDQQQEQQQLAEQQYFQQQQQAAAAASALQQQQTAANMQQQQQQPADFQQPLPTGSNNPFSMDNLERQKQEQQHAQLQRQQEEARQQQEQLKLQQLQRQQQEEAQLHQKRQEEAQLQQQQAQLLQQQAQFQQQQPLKQTRTGNQSISDKYSDLNTLLATGTGIDTFGNTGEARIPAQHTKTGTFINSQGTGYKQVTNEPKNNPFLSNQYTGLPSTNIVPTQTGYGFGNQPQSPPTNSPQQNPTGISYSQPQQQQQPQQQPQYMQNFQQQQPQYAQNFQQQPQYTQNYQQQPQYIQPHQQQQQQQQQQQQQQGYTPDQGVSLIDL
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
10UbiquitinationKQFVRSAKNMMKGYS
HHHHHHHHHHHHCCC		46.7722817900
14UbiquitinationRSAKNMMKGYSSTQV
HHHHHHHHCCCCCEE		43.8823749301
17PhosphorylationKNMMKGYSSTQVLVR
HHHHHCCCCCEEEEE		35.2622369663
18PhosphorylationNMMKGYSSTQVLVRD
HHHHCCCCCEEEEEE		17.8622369663
19PhosphorylationMMKGYSSTQVLVRDA
HHHCCCCCEEEEEEC		19.4319779198
103AcetylationRENFYVIKTLREFRH
CCCEEEECHHHHHHC		31.3124489116
127AcetylationQIIRVKAKELVSLLN
CEEEEEHHHHHHHCC		45.9524489116
165PhosphorylationPRPRRQRTRSNPHDS
CCCCCCCCCCCCCCC		30.0622369663
167PhosphorylationPRRQRTRSNPHDSSP
CCCCCCCCCCCCCCC		54.8422369663
172PhosphorylationTRSNPHDSSPSYQDD
CCCCCCCCCCCHHHH		40.9122369663
173PhosphorylationRSNPHDSSPSYQDDL
CCCCCCCCCCHHHHH		24.7522369663
175PhosphorylationNPHDSSPSYQDDLEK
CCCCCCCCHHHHHHH		37.0622890988
176PhosphorylationPHDSSPSYQDDLEKA
CCCCCCCHHHHHHHH		21.2422890988
182UbiquitinationSYQDDLEKALEESRI
CHHHHHHHHHHHHCC		66.6223749301
187PhosphorylationLEKALEESRITAQED
HHHHHHHHCCCHHHH		21.4323749301
190PhosphorylationALEESRITAQEDEQR
HHHHHCCCHHHHHHH		22.6028889911
225UbiquitinationSKEEEELKQLQELQR
CHHHHHHHHHHHHHH		52.8522106047
381AcetylationRQQQEQLKLQQLQRQ
HHHHHHHHHHHHHHH		43.9024489116
381UbiquitinationRQQQEQLKLQQLQRQ
HHHHHHHHHHHHHHH		43.9023749301
426UbiquitinationFQQQQPLKQTRTGNQ
HHHHCCCHHCCCCCC		57.2024961812
428PhosphorylationQQQPLKQTRTGNQSI
HHCCCHHCCCCCCCH		28.7225521595
430PhosphorylationQPLKQTRTGNQSISD
CCCHHCCCCCCCHHH		43.8222369663
434PhosphorylationQTRTGNQSISDKYSD
HCCCCCCCHHHHHHC		28.2322369663
436PhosphorylationRTGNQSISDKYSDLN
CCCCCCHHHHHHCHH		33.0422369663
439PhosphorylationNQSISDKYSDLNTLL
CCCHHHHHHCHHHHH		16.6522369663
440PhosphorylationQSISDKYSDLNTLLA
CCHHHHHHCHHHHHH		41.1722369663
444PhosphorylationDKYSDLNTLLATGTG
HHHHCHHHHHHCCCC		30.3722369663
448PhosphorylationDLNTLLATGTGIDTF
CHHHHHHCCCCCCCC		34.9320377248
450PhosphorylationNTLLATGTGIDTFGN
HHHHHCCCCCCCCCC		26.9825521595
454PhosphorylationATGTGIDTFGNTGEA
HCCCCCCCCCCCCCC		31.3624909858
458PhosphorylationGIDTFGNTGEARIPA
CCCCCCCCCCCCCCC		36.4622369663
468PhosphorylationARIPAQHTKTGTFIN
CCCCCEECCCCEEEC		20.4425521595
469UbiquitinationRIPAQHTKTGTFINS
CCCCEECCCCEEECC		42.7224961812
469AcetylationRIPAQHTKTGTFINS
CCCCEECCCCEEECC		42.7224489116
470PhosphorylationIPAQHTKTGTFINSQ
CCCEECCCCEEECCC		42.4822369663
472PhosphorylationAQHTKTGTFINSQGT
CEECCCCEEECCCCC		26.9422369663
476PhosphorylationKTGTFINSQGTGYKQ
CCCEEECCCCCCCEE		25.7722369663
479PhosphorylationTFINSQGTGYKQVTN
EEECCCCCCCEECCC		29.6922369663
481PhosphorylationINSQGTGYKQVTNEP
ECCCCCCCEECCCCC		9.7022369663
482UbiquitinationNSQGTGYKQVTNEPK
CCCCCCCEECCCCCC		39.3723749301
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
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ENT2_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 ENT2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CLH_YEASTCHC1physical
14704157
SLA2_YEASTSLA2genetic
14704157
BEM3_YEASTBEM3physical
19531587
RGA2_YEASTRGA2physical
19531587
EDE1_YEASTEDE1genetic
19903324
RIC1_YEASTRIC1genetic
20526336
SMD1_YEASTSMD1genetic
27708008
MRM2_YEASTMRM2genetic
27708008
DGK1_YEASTDGK1genetic
27708008
CDC37_YEASTCDC37genetic
27708008
PSB3_YEASTPUP3genetic
27708008
RSP5_YEASTRSP5genetic
27708008
MOB2_YEASTMOB2genetic
27708008
BRL1_YEASTBRL1genetic
27708008
ORC6_YEASTORC6genetic
27708008
DNA2_YEASTDNA2genetic
27708008
PAN1_YEASTPAN1genetic
27708008
CDC11_YEASTCDC11genetic
27708008
NTR2_YEASTNTR2genetic
27708008
RPF2_YEASTRPF2genetic
27708008
TAD3_YEASTTAD3genetic
27708008
ORC1_YEASTORC1genetic
27708008
GPI12_YEASTGPI12genetic
27708008
MED10_YEASTNUT2genetic
27708008
EDE1_YEASTEDE1genetic
27708008
ICS2_YEASTICS2genetic
27708008
SWC5_YEASTSWC5genetic
27708008
ENT1_YEASTENT1genetic
27708008
BAP3_YEASTBAP3genetic
27708008
VPS41_YEASTVPS41genetic
27708008
MNN10_YEASTMNN10genetic
27708008
CEM1_YEASTCEM1genetic
27708008
TFS2_YEASTDST1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
DBF2_YEASTDBF2genetic
27708008
ASK10_YEASTASK10genetic
27708008
OPI1_YEASTOPI1genetic
27708008
HTD2_YEASTHTD2genetic
27708008
VPS53_YEASTVPS53genetic
27708008
LPLA_YEASTAIM22genetic
27708008
YJY1_YEASTYJR011Cgenetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
YJ90_YEASTYJR120Wgenetic
27708008
ELM1_YEASTELM1genetic
27708008
MDM35_YEASTMDM35genetic
27708008
FABG_YEASTOAR1genetic
27708008
STB4_YEASTSTB4genetic
27708008
MRE11_YEASTMRE11genetic
27708008
HDA1_YEASTHDA1genetic
27708008
INO4_YEASTINO4genetic
27708008
CY1_YEASTCYT1genetic
27708008
DIA2_YEASTDIA2genetic
27708008
LIPA_YEASTLIP5genetic
27708008
FABD_YEASTMCT1genetic
27708008
SUR1_YEASTSUR1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ENT2_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-165; SER-167; SER-172;SER-173; THR-430; THR-450; THR-468; THR-470; THR-479 AND TYR-481, ANDMASS 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 THR-165; SER-167; SER-173;SER-436; THR-468; THR-470 AND SER-476, AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-430 AND SER-434, ANDMASS 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-165; SER-167 ANDTHR-468, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, AND MASSSPECTROMETRY.

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