GVP36_YEAST - dbPTM
GVP36_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GVP36_YEAST
UniProt AC P40531
Protein Name Protein GVP36
Gene Name GVP36
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 326
Subcellular Localization Golgi apparatus membrane
Peripheral membrane protein .
Protein Description
Protein Sequence MSFNAFASSLSKKLQEISTSVSEKTQELPSLAQSTQRMVQERLGQVTDISQLPREYTELEDKVDTIKLIYNHFLGVTAIYENGSYDYPKYINESVNEFSRSVASKLTELTHATSASEAQNILVAPGPIKEPKTLNYALSKVALNSSECLNKMFPTEEQPLASALLQFSDVQAKIAQARIQQDTLIQTKFNKNLRERLSFEIGKADKCRKDVHSMRLRYDVARTNLANNKKPEKEASLRVQMETLEDQFAQVTEDATVCLQEVISHANFSEDLKELAKAQAEYFETSAGLMKEFLSNSFAEEPEAKPEVAEEEKPQTAISMNDEDDA
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
2Acetylation------MSFNAFASS
------CCHHHHHHH
27.4915665377
2Phosphorylation------MSFNAFASS
------CCHHHHHHH
27.4922369663
8PhosphorylationMSFNAFASSLSKKLQ
CCHHHHHHHHHHHHH
25.9222369663
9PhosphorylationSFNAFASSLSKKLQE
CHHHHHHHHHHHHHH
32.9822369663
11PhosphorylationNAFASSLSKKLQEIS
HHHHHHHHHHHHHHH
29.6822369663
12UbiquitinationAFASSLSKKLQEIST
HHHHHHHHHHHHHHH
63.9022817900
12SuccinylationAFASSLSKKLQEIST
HHHHHHHHHHHHHHH
63.9023954790
13UbiquitinationFASSLSKKLQEISTS
HHHHHHHHHHHHHHC
52.6123749301
18PhosphorylationSKKLQEISTSVSEKT
HHHHHHHHHCCCHHH
17.5528889911
19PhosphorylationKKLQEISTSVSEKTQ
HHHHHHHHCCCHHHH
38.5228889911
20PhosphorylationKLQEISTSVSEKTQE
HHHHHHHCCCHHHHH
19.4920377248
22PhosphorylationQEISTSVSEKTQELP
HHHHHCCCHHHHHCH
32.8922369663
24AcetylationISTSVSEKTQELPSL
HHHCCCHHHHHCHHH
48.2624489116
24UbiquitinationISTSVSEKTQELPSL
HHHCCCHHHHHCHHH
48.2623749301
25PhosphorylationSTSVSEKTQELPSLA
HHCCCHHHHHCHHHH
24.1921126336
30PhosphorylationEKTQELPSLAQSTQR
HHHHHCHHHHHHHHH
49.3022369663
34PhosphorylationELPSLAQSTQRMVQE
HCHHHHHHHHHHHHH
22.3922369663
35PhosphorylationLPSLAQSTQRMVQER
CHHHHHHHHHHHHHH
14.2323749301
62AcetylationEYTELEDKVDTIKLI
HHHHHHHHHHHHHHH
32.4124489116
62UbiquitinationEYTELEDKVDTIKLI
HHHHHHHHHHHHHHH
32.4123749301
622-HydroxyisobutyrylationEYTELEDKVDTIKLI
HHHHHHHHHHHHHHH
32.41-
67UbiquitinationEDKVDTIKLIYNHFL
HHHHHHHHHHHHHHH
30.8122817900
94PhosphorylationYPKYINESVNEFSRS
CHHHHCHHHHHHHHH
26.2521440633
99PhosphorylationNESVNEFSRSVASKL
CHHHHHHHHHHHHHH
19.9121440633
101PhosphorylationSVNEFSRSVASKLTE
HHHHHHHHHHHHHHH
22.3421440633
104PhosphorylationEFSRSVASKLTELTH
HHHHHHHHHHHHHHH
26.4924961812
107PhosphorylationRSVASKLTELTHATS
HHHHHHHHHHHHCCC
32.4622369663
110PhosphorylationASKLTELTHATSASE
HHHHHHHHHCCCHHH
11.8422369663
113PhosphorylationLTELTHATSASEAQN
HHHHHHCCCHHHHCC
19.7422369663
114PhosphorylationTELTHATSASEAQNI
HHHHHCCCHHHHCCE
30.4922369663
116PhosphorylationLTHATSASEAQNILV
HHHCCCHHHHCCEEE
32.9820377248
129AcetylationLVAPGPIKEPKTLNY
EECCCCCCCCCHHHH
71.7124489116
132AcetylationPGPIKEPKTLNYALS
CCCCCCCCHHHHHHH
67.7324489116
139PhosphorylationKTLNYALSKVALNSS
CHHHHHHHHHHCCCH
19.5322369663
140UbiquitinationTLNYALSKVALNSSE
HHHHHHHHHHCCCHH
32.1723749301
145PhosphorylationLSKVALNSSECLNKM
HHHHHCCCHHHHHHH
28.5022369663
146PhosphorylationSKVALNSSECLNKMF
HHHHCCCHHHHHHHC
31.1224909858
151AcetylationNSSECLNKMFPTEEQ
CCHHHHHHHCCCCCC
29.0425381059
173UbiquitinationQFSDVQAKIAQARIQ
HHHHHHHHHHHHHHH
22.8323749301
188AcetylationQDTLIQTKFNKNLRE
HCHHHHHHCCHHHHH
30.4824489116
198PhosphorylationKNLRERLSFEIGKAD
HHHHHHHHHEECCHH
27.3622369663
203AcetylationRLSFEIGKADKCRKD
HHHHEECCHHHHCCH
60.1024489116
213PhosphorylationKCRKDVHSMRLRYDV
HHCCHHHHHHHHHHH
12.8724961812
295PhosphorylationGLMKEFLSNSFAEEP
HHHHHHHCCHHCCCC
35.4322369663
297PhosphorylationMKEFLSNSFAEEPEA
HHHHHCCHHCCCCCC
23.5820377248
305UbiquitinationFAEEPEAKPEVAEEE
HCCCCCCCCCCCCCC
39.8023749301
313UbiquitinationPEVAEEEKPQTAISM
CCCCCCCCCCCCCCC
45.7823749301
316PhosphorylationAEEEKPQTAISMNDE
CCCCCCCCCCCCCCC
34.1922369663
319PhosphorylationEKPQTAISMNDEDDA
CCCCCCCCCCCCCCC
14.7422369663

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 GVP36_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GVP36_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 GVP36_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SSB1_YEASTSSB1physical
19536198
DHE5_YEASTGDH3genetic
20093466
RBG1_YEASTRBG1genetic
20093466
ACH1_YEASTACH1genetic
20093466
CSG2_YEASTCSG2genetic
20093466
ARF1_YEASTARF1genetic
20093466
RPN4_YEASTRPN4genetic
20093466
VPS41_YEASTVPS41genetic
20093466
TRS85_YEASTTRS85genetic
20093466
BCS1_YEASTBCS1genetic
20093466
RV167_YEASTRVS167genetic
20093466
DOT1_YEASTDOT1genetic
20093466
GET2_YEASTGET2genetic
20093466
SLX8_YEASTSLX8genetic
20093466
UBP5_YEASTUBP5genetic
20093466
PT122_YEASTPET122genetic
20093466
SA155_YEASTSAP155genetic
20093466
VAM7_YEASTVAM7genetic
20093466
CWH41_YEASTCWH41genetic
20093466
HSE1_YEASTHSE1genetic
20093466
PTH_YEASTPTH1genetic
20093466
AIM18_YEASTAIM18genetic
20093466
HAP4_YEASTHAP4genetic
20093466
VPS51_YEASTVPS51genetic
20093466
DBP7_YEASTDBP7genetic
20093466
TRK2_YEASTTRK2genetic
20093466
UBI4P_YEASTUBI4genetic
20093466
SRN2_YEASTSRN2genetic
20093466
STM1_YEASTSTM1genetic
20093466
SRR1L_YEASTBER1genetic
20093466
AMPD_YEASTAMD1genetic
20093466
YPT7_YEASTYPT7genetic
20093466
UBX4_YEASTUBX4genetic
20093466
SCS7_YEASTSCS7genetic
20093466
TCB2_YEASTTCB2genetic
20093466
TLG2_YEASTTLG2genetic
20093466
MDM12_YEASTMDM12genetic
20093466
GYP1_YEASTGYP1genetic
20093466
PALA_YEASTRIM20genetic
20093466
ACM1_YEASTACM1genetic
20093466
MRX11_YEASTYPL041Cgenetic
20093466
ATG13_YEASTATG13genetic
20093466
RCR1_YEASTRCR1genetic
27708008
RV167_YEASTRVS167genetic
27708008
VPS9_YEASTVPS9genetic
27708008
RBG1_YEASTRBG1genetic
27708008
ACH1_YEASTACH1genetic
27708008
YBI1_YEASTYBL081Wgenetic
27708008
CHK1_YEASTCHK1genetic
27708008
APE3_YEASTAPE3genetic
27708008
MTU1_YEASTSLM3genetic
27708008
TRS85_YEASTTRS85genetic
27708008
RPA14_YEASTRPA14genetic
27708008
OMS1_YEASTOMS1genetic
27708008
LSM6_YEASTLSM6genetic
27708008
DOT1_YEASTDOT1genetic
27708008
GET2_YEASTGET2genetic
27708008
PT122_YEASTPET122genetic
27708008
HSE1_YEASTHSE1genetic
27708008
PTH_YEASTPTH1genetic
27708008
VPS53_YEASTVPS53genetic
27708008
CYP7_YEASTCPR7genetic
27708008
HOC1_YEASTHOC1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
HAP4_YEASTHAP4genetic
27708008
VPS51_YEASTVPS51genetic
27708008
DBP7_YEASTDBP7genetic
27708008
UBI4P_YEASTUBI4genetic
27708008
HOG1_YEASTHOG1genetic
27708008
STM1_YEASTSTM1genetic
27708008
COA4_YEASTCOA4genetic
27708008
YPT7_YEASTYPT7genetic
27708008
MSC1_YEASTMSC1genetic
27708008
AIM34_YEASTAIM34genetic
27708008
MAC1_YEASTMAC1genetic
27708008
UBX4_YEASTUBX4genetic
27708008
MRE11_YEASTMRE11genetic
27708008
SCS7_YEASTSCS7genetic
27708008
TCB2_YEASTTCB2genetic
27708008
MDM12_YEASTMDM12genetic
27708008
CY1_YEASTCYT1genetic
27708008
GYP1_YEASTGYP1genetic
27708008
PALA_YEASTRIM20genetic
27708008
MRX11_YEASTYPL041Cgenetic
27708008
COX10_YEASTCOX10genetic
27708008
ATG13_YEASTATG13genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GVP36_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-20; SER-30; THR-110;SER-114; SER-145; SER-297 AND SER-319, 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-113 AND SER-114, 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 SER-319, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-305 AND LYS-313, AND MASSSPECTROMETRY.

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