PEP12_YEAST - dbPTM
PEP12_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PEP12_YEAST
UniProt AC P32854
Protein Name Syntaxin PEP12
Gene Name PEP12
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 288
Subcellular Localization Membrane
Single-pass type IV membrane protein .
Protein Description Plays a role in the sorting and targeting of vacuolar proteases..
Protein Sequence MSEDEFFGGDNEAVWNGSRFSDSPEFQTLKEEVAAELFEINGQISTLQQFTATLKSFIDRGDVSAKVVERINKRSVAKIEEIGGLIKKVNTSVKKMDAIEEASLDKTQIIAREKLVRDVSYSFQEFQGIQRQFTQVMKQVNERAKESLEASEMANDAALLDEEQRQNSSKSTRIPGSQIVIERDPINNEEFAYQQNLIEQRDQEISNIERGITELNEVFKDLGSVVQQQGVLVDNIEANIYTTSDNTQLASDELRKAMRYQKRTSRWRVYLLIVLLVMLLFIFLIMKL
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------MSEDEFFGG
------CCCCCCCCC		54.4722369663
18PhosphorylationNEAVWNGSRFSDSPE
CCCCCCCCCCCCCHH		27.2630377154
21PhosphorylationVWNGSRFSDSPEFQT
CCCCCCCCCCHHHHH		35.7529734811
23PhosphorylationNGSRFSDSPEFQTLK
CCCCCCCCHHHHHHH		25.7325752575
45PhosphorylationFEINGQISTLQQFTA
HHHCCEEHHHHHHHH		18.3829688323
46PhosphorylationEINGQISTLQQFTAT
HHCCEEHHHHHHHHH		30.1629688323
51PhosphorylationISTLQQFTATLKSFI
EHHHHHHHHHHHHHH		17.8829688323
53PhosphorylationTLQQFTATLKSFIDR
HHHHHHHHHHHHHHH		31.4929688323
95AcetylationKVNTSVKKMDAIEEA
HHCCCCHHCHHHHHH		39.6025381059
103PhosphorylationMDAIEEASLDKTQII
CHHHHHHCCCHHHHH		40.1424961812
106AcetylationIEEASLDKTQIIARE
HHHHCCCHHHHHHHH		47.8525381059
145UbiquitinationKQVNERAKESLEASE
HHHHHHHHHHHHHHH		54.8023749301
220UbiquitinationTELNEVFKDLGSVVQ
HHHHHHHHHHHHHHH		58.1619722269
241PhosphorylationDNIEANIYTTSDNTQ
CEEEEEEEECCCCCC		12.0827017623
242PhosphorylationNIEANIYTTSDNTQL
EEEEEEEECCCCCCC		18.9427017623
243PhosphorylationIEANIYTTSDNTQLA
EEEEEEECCCCCCCC		19.6727017623
244PhosphorylationEANIYTTSDNTQLAS
EEEEEECCCCCCCCC		22.5127017623
247PhosphorylationIYTTSDNTQLASDEL
EEECCCCCCCCCHHH		29.9227017623
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 ligaseTUL1P36096
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PEP12_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 PEP12_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SEC18_YEASTSEC18physical
9201718
PEP7_YEASTPEP7physical
9201718
VPS45_YEASTVPS45physical
9201718
YKT6_YEASTYKT6physical
12453154
VPS45_YEASTVPS45physical
10545112
VTI1_YEASTVTI1physical
9199167
SPO20_YEASTSPO20physical
10924463
TLG1_YEASTTLG1physical
14981247
VTI1_YEASTVTI1physical
14981247
VAM3_YEASTVAM3genetic
9245783
VAM3_YEASTVAM3genetic
9722605
VAM3_YEASTVAM3genetic
9247140
PEP7_YEASTPEP7genetic
9201718
VPS45_YEASTVPS45genetic
9201718
VAM3_YEASTVAM3genetic
9475723
SEC13_YEASTSEC13genetic
9199164
PPB_YEASTPHO8genetic
9184222
VAM3_YEASTVAM3genetic
14583628
VAM3_YEASTVAM3genetic
15047864
SFT2_YEASTSFT2physical
11283351
ARL1_YEASTARL1genetic
20093466
MTC4_YEASTMTC4genetic
20093466
AP3M_YEASTAPM3genetic
20093466
VAC17_YEASTVAC17genetic
20093466
URC2_YEASTURC2genetic
20093466
ERV14_YEASTERV14genetic
20093466
UBA4_YEASTUBA4genetic
20093466
SKN7_YEASTSKN7genetic
20093466
URM1_YEASTURM1genetic
20093466
BCK1_YEASTBCK1genetic
20093466
GPI7_YEASTLAS21genetic
20093466
SYS1_YEASTSYS1genetic
20093466
CBF1_YEASTCBF1genetic
20093466
UBR2_YEASTUBR2genetic
20093466
PKR1_YEASTPKR1genetic
20093466
RIM13_YEASTRIM13genetic
20093466
AF9_YEASTYAF9genetic
20093466
ARL3_YEASTARL3genetic
20093466
YP153_YEASTYPR153Wgenetic
20093466
ENT3_YEASTENT3physical
20658963
PLB3_YEASTPLB3genetic
20526336
PIL1_YEASTPIL1genetic
20526336
THRC_YEASTTHR4genetic
20526336
SYSC_YEASTSES1genetic
20526336
GSH1_YEASTGSH1genetic
21601516
VPS33_YEASTVPS33physical
23051737
PFD2_YEASTGIM4genetic
23891562
PFD4_YEASTGIM3genetic
23891562
BCK1_YEASTBCK1genetic
22282571
VTI1_YEASTVTI1physical
23776654
STX8_YEASTSYN8physical
23776654
ARL1_YEASTARL1genetic
27708008
MTC4_YEASTMTC4genetic
27708008
AP3M_YEASTAPM3genetic
27708008
URC2_YEASTURC2genetic
27708008
ERV14_YEASTERV14genetic
27708008
MDM34_YEASTMDM34genetic
27708008
CBP4_YEASTCBP4genetic
27708008
UBA4_YEASTUBA4genetic
27708008
SKN7_YEASTSKN7genetic
27708008
URM1_YEASTURM1genetic
27708008
SYS1_YEASTSYS1genetic
27708008
GPI7_YEASTLAS21genetic
27708008
BCK1_YEASTBCK1genetic
27708008
ELM1_YEASTELM1genetic
27708008
CSF1_YEASTCSF1genetic
27708008
COG8_YEASTCOG8genetic
27708008
PKR1_YEASTPKR1genetic
27708008
RIM13_YEASTRIM13genetic
27708008
COG6_YEASTCOG6genetic
27708008
AF9_YEASTYAF9genetic
27708008
TBCA_YEASTRBL2genetic
27708008
ARL3_YEASTARL3genetic
27708008
YP153_YEASTYPR153Wgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PEP12_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-2 AND SER-23, 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 SER-2, AND MASSSPECTROMETRY.

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