PHO88_YEAST - dbPTM
PHO88_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHO88_YEAST
UniProt AC P38264
Protein Name SRP-independent targeting protein 3 {ECO:0000303|PubMed:27905431}
Gene Name PHO88 {ECO:0000303|PubMed:8709965}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 188
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein . Mitochondrion .
Protein Description Functions in the SND pathway, a SRP (signal recognition particle) and GET (guided entry of tail-anchored proteins) independent pathway for targeting a broad range of substrate proteins to the endoplasmic reticulum. SND functions in parallel to GET in targeting proteins with downstream hydrophobic motifs. [PubMed: 27905431 Involved in inorganic phosphate uptake]
Protein Sequence MNPQVSNIIIMLVMMQLSRRIDMEDPTIIMYIRILYCSSIGISWIIYQMARKRIVAKNDMTTMKYVEPGNAMSGEGEKLQVTTVRDYDLKEIDSAIKSIYTGMAMMGFMHLYLKYTNPLFMQSISPVKSALEHNEVKIHLFGKPATGDLKRPFKAPSLFGGMGQTGPKTDKKSIEEAERAGNAGVKAE
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
6Phosphorylation--MNPQVSNIIIMLV
--CCHHHHHHHHHHH
19.6428889911
18PhosphorylationMLVMMQLSRRIDMED
HHHHHHHHHCCCCCC
11.5628889911
57UbiquitinationARKRIVAKNDMTTMK
HHHCCEECCCCCCCE
42.4523749301
61PhosphorylationIVAKNDMTTMKYVEP
CEECCCCCCCEEECC
26.9727017623
64AcetylationKNDMTTMKYVEPGNA
CCCCCCCEEECCCCC
44.0124489116
64UbiquitinationKNDMTTMKYVEPGNA
CCCCCCCEEECCCCC
44.0123749301
73PhosphorylationVEPGNAMSGEGEKLQ
ECCCCCCCCCCCEEE
31.1423749301
78AcetylationAMSGEGEKLQVTTVR
CCCCCCCEEEEEEEE
55.8924489116
78UbiquitinationAMSGEGEKLQVTTVR
CCCCCCCEEEEEEEE
55.8923749301
902-HydroxyisobutyrylationTVRDYDLKEIDSAIK
EEECCCHHHHHHHHH
50.12-
90SuccinylationTVRDYDLKEIDSAIK
EEECCCHHHHHHHHH
50.1223954790
90AcetylationTVRDYDLKEIDSAIK
EEECCCHHHHHHHHH
50.1224489116
90UbiquitinationTVRDYDLKEIDSAIK
EEECCCHHHHHHHHH
50.1223749301
114UbiquitinationGFMHLYLKYTNPLFM
HHHHHHHHCCCHHHH
36.1517644757
123PhosphorylationTNPLFMQSISPVKSA
CCHHHHHCCCCHHHH
17.1624961812
125PhosphorylationPLFMQSISPVKSALE
HHHHHCCCCHHHHHH
28.9628152593
128AcetylationMQSISPVKSALEHNE
HHCCCCHHHHHHCCC
33.1424489116
128UbiquitinationMQSISPVKSALEHNE
HHCCCCHHHHHHCCC
33.1424961812
137UbiquitinationALEHNEVKIHLFGKP
HHHCCCEEEEECCCC
20.4517644757
137AcetylationALEHNEVKIHLFGKP
HHHCCCEEEEECCCC
20.4524489116
143UbiquitinationVKIHLFGKPATGDLK
EEEEECCCCCCCCCC
24.9323749301
143AcetylationVKIHLFGKPATGDLK
EEEEECCCCCCCCCC
24.9324489116
150UbiquitinationKPATGDLKRPFKAPS
CCCCCCCCCCCCCCH
63.8717644757
154UbiquitinationGDLKRPFKAPSLFGG
CCCCCCCCCCHHCCC
63.1717644757
154AcetylationGDLKRPFKAPSLFGG
CCCCCCCCCCHHCCC
63.1724489116
157PhosphorylationKRPFKAPSLFGGMGQ
CCCCCCCHHCCCCCC
40.9922369663
165PhosphorylationLFGGMGQTGPKTDKK
HCCCCCCCCCCCCHH
50.1222369663
168SuccinylationGMGQTGPKTDKKSIE
CCCCCCCCCCHHHHH
71.3623954790
168UbiquitinationGMGQTGPKTDKKSIE
CCCCCCCCCCHHHHH
71.3617644757
168AcetylationGMGQTGPKTDKKSIE
CCCCCCCCCCHHHHH
71.3624489116
172UbiquitinationTGPKTDKKSIEEAER
CCCCCCHHHHHHHHH
60.5217644757
172AcetylationTGPKTDKKSIEEAER
CCCCCCHHHHHHHHH
60.5224489116
173PhosphorylationGPKTDKKSIEEAERA
CCCCCHHHHHHHHHH
40.7627717283
186UbiquitinationRAGNAGVKAE-----
HHHHCCCCCC-----
45.9717644757

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 PHO88_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHO88_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 PHO88_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PHO86_YEASTPHO86genetic
8709965
HAC1_YEASTHAC1genetic
16269340
MGA2_YEASTMGA2genetic
16269340
DGK1_YEASTDGK1genetic
16269340
ACO1_YEASTOLE1genetic
16269340
YNS1_YEASTYNL181Wgenetic
16269340
SEC18_YEASTSEC18genetic
16269340
UPPS_YEASTNUS1genetic
16269340
GUP1_YEASTGUP1genetic
16269340
ILM1_YEASTILM1genetic
16269340
OSTB_YEASTWBP1genetic
16269340
OSTD_YEASTSWP1physical
18467557
EMC5_YEASTEMC5physical
18467557
COS1_YEASTCOS1physical
18467557
PIS_YEASTPIS1physical
18467557
CAB3_YEASTCAB3physical
18467557
PHO88_YEASTPHO88physical
18467557
MSMO_YEASTERG25physical
18467557
FCY2_YEASTFCY2physical
18467557
HXT1_YEASTHXT1physical
18467557
TMEDA_YEASTERV25physical
18467557
GOT1_YEASTGOT1physical
18467557
LAC1_YEASTLAC1physical
18467557
SUR2_YEASTSUR2physical
18467557
ACO1_YEASTOLE1physical
18467557
TPO3_YEASTTPO3physical
18467557
SSH1_YEASTSSH1physical
18467557
SPC1_YEASTSPC1physical
18467557
SOP4_YEASTSOP4physical
18467557
ORM2_YEASTORM2physical
18467557
SCS7_YEASTSCS7physical
18467557
SPC2_YEASTSPC2physical
18467557
SHR3_YEASTSHR3physical
18467557
CP51_YEASTERG11physical
18467557
COS4_YEASTCOS4physical
18467557
SEC62_YEASTSEC62physical
18467557
SEY1_YEASTSEY1physical
18467557
VHS3_YEASTVHS3physical
18467557
ILM1_YEASTILM1physical
18467557
STE24_YEASTSTE24physical
18467557
TPO2_YEASTTPO2physical
18467557
DAL5_YEASTDAL5physical
18467557
PHO23_YEASTPHO23genetic
19547744
EMC1_YEASTEMC1genetic
23891562
EMC6_YEASTEMC6genetic
23891562
EMC2_YEASTEMC2genetic
23891562
PCY1_YEASTPCT1genetic
23891562
DGK1_YEASTDGK1genetic
23891562
VPS64_YEASTVPS64genetic
23891562
PFD4_YEASTGIM3genetic
23891562
SCS2_YEASTSCS2genetic
23891562
ERG4_YEASTERG4genetic
23891562
RPN12_YEASTRPN12genetic
23891562
PSA3_YEASTPRE9genetic
23891562
PRS6B_YEASTRPT3genetic
23891562
PSB1_YEASTPRE3genetic
23891562
PSB5_YEASTPRE2genetic
23891562
PSA4_YEASTPRE6genetic
23891562
PSA7_YEASTPRE10genetic
23891562

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PHO88_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-157, AND MASSSPECTROMETRY.

TOP