ENT1_YEAST - dbPTM
ENT1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ENT1_YEAST
UniProt AC Q12518
Protein Name Epsin-1
Gene Name ENT1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 454
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Localizes in a punctate pattern. Found in the actin cortical patches.
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. Negatively regulated via phosphorylation..
Protein Sequence MSKQFVRSAKNLVKGYSSTQVLVRNATSNDNHQVSKDSLIELAEKSYDSADFFEIMDMLDKRLNDKGKYWRHIAKALTVIDYLIRFGSENCVLWCRENLYIIKTLKEFRHEDDEGIDQGQIVRVKAKELTALLSDDERLNEERNMNIKGRNRKGRRRRGTGRSDENDDDLQRAISASRLTAEEDERRRKQDEDYETALQLSKEEEELKRLQDLQRMQQQQGQQQLQQPMYYDIFGNPITPEEYAQFQLQQQQQQQQQQLQQQPMYYDVFGNPITPEELAQFQQQQQLQEQQYLASMQQQQQAMSNNPFAKSEQSSSSPKRNQLVAASSPQQLQQQKQQEPLIQNRTGNQSMTDKYSKLNELLATGTGIDTFGNVGEARIPAQHTKTGTFINSQGTGYRQVSDDPNHNPFLNSQYTGLPSTSVVPTQTGYGFGNQSQQQSQNNGSNNRGYTLIDL
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
17PhosphorylationKNLVKGYSSTQVLVR
HHHHHCCCCCEEEEE
35.2622369663
18PhosphorylationNLVKGYSSTQVLVRN
HHHHCCCCCEEEEEE
17.8622369663
19PhosphorylationLVKGYSSTQVLVRNA
HHHCCCCCEEEEEEC
19.4322369663
36AcetylationNDNHQVSKDSLIELA
CCCCCCCHHHHHHHH
53.1024489116
103AcetylationRENLYIIKTLKEFRH
CCCEEEECHHHHHCC
37.9424489116
103UbiquitinationRENLYIIKTLKEFRH
CCCEEEECHHHHHCC
37.9423749301
106UbiquitinationLYIIKTLKEFRHEDD
EEEECHHHHHCCCCC
61.1022817900
148UbiquitinationEERNMNIKGRNRKGR
HHHCCCCCCCCCCCC
46.9823749301
153UbiquitinationNIKGRNRKGRRRRGT
CCCCCCCCCCCCCCC
61.3922817900
160PhosphorylationKGRRRRGTGRSDEND
CCCCCCCCCCCCCCH
27.8422369663
163PhosphorylationRRRGTGRSDENDDDL
CCCCCCCCCCCHHHH
51.0922369663
175PhosphorylationDDLQRAISASRLTAE
HHHHHHHHHHHHCHH
21.1422369663
177PhosphorylationLQRAISASRLTAEED
HHHHHHHHHHCHHHH
22.4922369663
180PhosphorylationAISASRLTAEEDERR
HHHHHHHCHHHHHHH
30.8022369663
189UbiquitinationEEDERRRKQDEDYET
HHHHHHHHHCHHHHH
61.3623749301
201PhosphorylationYETALQLSKEEEELK
HHHHHHHCHHHHHHH
25.6728889911
202UbiquitinationETALQLSKEEEELKR
HHHHHHCHHHHHHHH
77.1724961812
311PhosphorylationSNNPFAKSEQSSSSP
HCCCCCCCCCCCCCH
37.1221440633
314PhosphorylationPFAKSEQSSSSPKRN
CCCCCCCCCCCHHHH
28.3021440633
315PhosphorylationFAKSEQSSSSPKRNQ
CCCCCCCCCCHHHHH
34.2328152593
316PhosphorylationAKSEQSSSSPKRNQL
CCCCCCCCCHHHHHH
56.7728152593
317PhosphorylationKSEQSSSSPKRNQLV
CCCCCCCCHHHHHHH
36.0725752575
327PhosphorylationRNQLVAASSPQQLQQ
HHHHHHCCCHHHHHH
32.5822369663
328PhosphorylationNQLVAASSPQQLQQQ
HHHHHCCCHHHHHHH
23.2322369663
336UbiquitinationPQQLQQQKQQEPLIQ
HHHHHHHHHHCCCHH
50.0023749301
346PhosphorylationEPLIQNRTGNQSMTD
CCCHHCCCCCCCHHH
48.2925521595
350PhosphorylationQNRTGNQSMTDKYSK
HCCCCCCCHHHHHHH
27.8722369663
352PhosphorylationRTGNQSMTDKYSKLN
CCCCCCHHHHHHHHH
34.2922369663
354UbiquitinationGNQSMTDKYSKLNEL
CCCCHHHHHHHHHHH
42.1123749301
354AcetylationGNQSMTDKYSKLNEL
CCCCHHHHHHHHHHH
42.1125381059
357UbiquitinationSMTDKYSKLNELLAT
CHHHHHHHHHHHHHH
52.8523749301
364PhosphorylationKLNELLATGTGIDTF
HHHHHHHHCCCCCCC
34.9325521595
366PhosphorylationNELLATGTGIDTFGN
HHHHHHCCCCCCCCC
26.9825521595
370PhosphorylationATGTGIDTFGNVGEA
HHCCCCCCCCCCCCC
31.3625521595
384PhosphorylationARIPAQHTKTGTFIN
CCCCCEECCCCEEEC
20.4425521595
385UbiquitinationRIPAQHTKTGTFINS
CCCCEECCCCEEECC
42.7223749301
386PhosphorylationIPAQHTKTGTFINSQ
CCCEECCCCEEECCC
42.4817330950
388PhosphorylationAQHTKTGTFINSQGT
CEECCCCEEECCCCC
26.9421082442
392PhosphorylationKTGTFINSQGTGYRQ
CCCEEECCCCCCCEE
25.7722890988
395PhosphorylationTFINSQGTGYRQVSD
EEECCCCCCCEECCC
24.3317330950
397PhosphorylationINSQGTGYRQVSDDP
ECCCCCCCEECCCCC
9.5622890988
415PhosphorylationPFLNSQYTGLPSTSV
CCCCCCCCCCCCCCE
25.3028889911
427PhosphorylationTSVVPTQTGYGFGNQ
CCEECCCCCCCCCCH
34.5428889911

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
395TPhosphorylationKinasePRK1P40494
Uniprot
415TPhosphorylationKinasePRK1P40494
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ENT1_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 ENT1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CLH_YEASTCHC1physical
14704157
EDE1_YEASTEDE1physical
12529323
PAN1_YEASTPAN1physical
12529323
UBI4P_YEASTUBI4physical
12529323
CLH_YEASTCHC1physical
10449404
SLA2_YEASTSLA2genetic
14704157
ENT2_YEASTENT2genetic
10449404
RGA1_YEASTRGA1physical
16537494
RGA2_YEASTRGA2physical
16537494
BEM3_YEASTBEM3physical
16537494
CDC42_YEASTCDC42genetic
16537494
GIC1_YEASTGIC1genetic
16537494
GIC2_YEASTGIC2genetic
16537494
BEM1_YEASTBEM1genetic
16537494
ENT2_YEASTENT2genetic
20526336
EDE1_YEASTEDE1genetic
11988742
ENT2_YEASTENT2genetic
22190733
ENT2_YEASTENT2genetic
11988742
CLH_YEASTCHC1physical
12529323
GOSR1_YEASTGOS1genetic
23891562
UBI4P_YEASTUBI4physical
11988742
BOS1_YEASTBOS1genetic
27708008
PP2C3_YEASTPTC3genetic
27708008
PHB1_YEASTPHB1genetic
27708008
TNA1_YEASTTNA1genetic
27708008
RRM3_YEASTRRM3genetic
27708008
KC11_YEASTYCK1genetic
27708008
ICE2_YEASTICE2genetic
27708008
DAL81_YEASTDAL81genetic
27708008
PHO86_YEASTPHO86genetic
27708008
BFA1_YEASTBFA1genetic
27708008
SRL3_YEASTSRL3genetic
27708008
CSF1_YEASTCSF1genetic
27708008
YL278_YEASTYLR278Cgenetic
27708008
OCA1_YEASTOCA1genetic
27708008
MNE1_YEASTMNE1genetic
27708008
PRM4_YEASTPRM4genetic
27708008
STU1_YEASTSTU1genetic
27708008
SNU56_YEASTSNU56genetic
27708008
SYF1_YEASTSYF1genetic
27708008
GPI19_YEASTGPI19genetic
27708008
PSB3_YEASTPUP3genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
MPPA_YEASTMAS2genetic
27708008
CDC12_YEASTCDC12genetic
27708008
EXO70_YEASTEXO70genetic
27708008
DPB11_YEASTDPB11genetic
27708008
PRP21_YEASTPRP21genetic
27708008
HSP77_YEASTSSC1genetic
27708008
PRP19_YEASTPRP19genetic
27708008
SMC4_YEASTSMC4genetic
27708008
GAA1_YEASTGAA1genetic
27708008
TAD3_YEASTTAD3genetic
27708008
RSC9_YEASTRSC9genetic
27708008
TBF1_YEASTTBF1genetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
ICS2_YEASTICS2genetic
27708008
RS6A_YEASTRPS6Bgenetic
27708008
RS6B_YEASTRPS6Bgenetic
27708008
TYDP1_YEASTTDP1genetic
27708008
SHG1_YEASTSHG1genetic
27708008
VBA2_YEASTVBA2genetic
27708008
BUD31_YEASTBUD31genetic
27708008
ATG15_YEASTATG15genetic
27708008
RRP8_YEASTRRP8genetic
27708008
DHAS_YEASTHOM2genetic
27708008
SAC3_YEASTSAC3genetic
27708008
NBP2_YEASTNBP2genetic
27708008
H2A1_YEASTHTA1genetic
27708008
VHS1_YEASTVHS1genetic
27708008
PMP3_YEASTPMP3genetic
27708008
IPK1_YEASTIPK1genetic
27708008
YHP1_YEASTYHP1genetic
27708008
STL1_YEASTSTL1genetic
27708008
SLX8_YEASTSLX8genetic
27708008
HXKA_YEASTHXK1genetic
27708008
TFS2_YEASTDST1genetic
27708008
HUR1_YEASTHUR1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
RTG2_YEASTRTG2genetic
27708008
HXKB_YEASTHXK2genetic
27708008
SCM4_YEASTSCM4genetic
27708008
TWF1_YEASTTWF1genetic
27708008
PHB2_YEASTPHB2genetic
27708008
ETP1_YEASTETP1genetic
27708008
YHU0_YEASTYHR140Wgenetic
27708008
STB5_YEASTSTB5genetic
27708008
AIM18_YEASTAIM18genetic
27708008
RPN10_YEASTRPN10genetic
27708008
RL16A_YEASTRPL16Agenetic
27708008
VTC4_YEASTVTC4genetic
27708008
PRY3_YEASTPRY3genetic
27708008
PRM10_YEASTPRM10genetic
27708008
ASF1_YEASTASF1genetic
27708008
VPS35_YEASTVPS35genetic
27708008
YJY1_YEASTYJR011Cgenetic
27708008
MOG1_YEASTMOG1genetic
27708008
HOC1_YEASTHOC1genetic
27708008
UBL1_YEASTYUH1genetic
27708008
YJ90_YEASTYJR120Wgenetic
27708008
MRT4_YEASTMRT4genetic
27708008
IXR1_YEASTIXR1genetic
27708008
MCR1_YEASTMCR1genetic
27708008
SAC1_YEASTSAC1genetic
27708008
RL40A_YEASTRPL40Bgenetic
27708008
RL40B_YEASTRPL40Bgenetic
27708008
VBA5_YEASTVBA5genetic
27708008
RSSA2_YEASTRPS0Bgenetic
27708008
YL053_YEASTYLR053Cgenetic
27708008
ALAM_YEASTALT1genetic
27708008
PFD6_YEASTYKE2genetic
27708008
ENT2_YEASTENT2genetic
27708008
TOP3_YEASTTOP3genetic
27708008
LIPB_YEASTLIP2genetic
27708008
COQ11_YEASTYLR290Cgenetic
27708008
UBC12_YEASTUBC12genetic
27708008
VRP1_YEASTVRP1genetic
27708008
VID22_YEASTVID22genetic
27708008
ERG6_YEASTERG6genetic
27708008
FKBP3_YEASTFPR3genetic
27708008
STB4_YEASTSTB4genetic
27708008
PKR1_YEASTPKR1genetic
27708008
CTL1_YEASTCTL1genetic
27708008
LCF4_YEASTFAA4genetic
27708008
CBPY_YEASTPRC1genetic
27708008
PET8_YEASTPET8genetic
27708008
IDH1_YEASTIDH1genetic
27708008
AQR1_YEASTAQR1genetic
27708008
PMS1_YEASTPMS1genetic
27708008
MKT1_YEASTMKT1genetic
27708008
LSM7_YEASTLSM7genetic
27708008
PFD4_YEASTGIM3genetic
27708008
TOP1_YEASTTOP1genetic
27708008
MDM12_YEASTMDM12genetic
27708008
VPS68_YEASTVPS68genetic
27708008
TIR2_YEASTTIR2genetic
27708008
YAP4_YEASTCIN5genetic
27708008
CSK2C_YEASTCKB2genetic
27708008
DIA2_YEASTDIA2genetic
27708008
WHI5_YEASTWHI5genetic
27708008
CAF20_YEASTCAF20genetic
27708008
TRM44_YEASTTRM44genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
COX10_YEASTCOX10genetic
27708008
RU2A_YEASTLEA1genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ENT1_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-18; THR-160; SER-163;THR-180; SER-327; SER-328; THR-346; SER-350; THR-364; THR-366;THR-384; THR-386; THR-388 AND THR-395, 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 THR-160; SER-163; THR-346;THR-384; THR-386 AND THR-395, 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 SER-328 AND THR-395, ANDMASS 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-346, AND MASSSPECTROMETRY.
"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-366 AND THR-384, ANDMASS SPECTROMETRY.

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