SNF7_YEAST - dbPTM
SNF7_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNF7_YEAST
UniProt AC P39929
Protein Name Vacuolar-sorting protein SNF7 {ECO:0000305}
Gene Name SNF7 {ECO:0000303|PubMed:1752413}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 240
Subcellular Localization Cytoplasm . Endosome membrane
Peripheral membrane protein . Nucleus envelope .
Protein Description Acts a component of the ESCRT-III complex required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). [PubMed: 11559748]
Protein Sequence MWSSLFGWTSSNAKNKESPTKAIVRLREHINLLSKKQSHLRTQITNQENEARIFLTKGNKVMAKNALKKKKTIEQLLSKVEGTMESMEQQLFSIESANLNLETMRAMQEGAKAMKTIHSGLDIDKVDETMDEIREQVELGDEISDAISRPLITGANEVDEDELDEELDMLAQENANQETSKIVNNNVNAAPISENKVSLPSVPSNKIKQSENSVKDGEEEEDEEDEDEKALRELQAEMGL
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
3Phosphorylation-----MWSSLFGWTS
-----CCCCCCCCCC		18.8330377154
18PhosphorylationSNAKNKESPTKAIVR
CCCCCCCCCCHHHHH		39.2121440633
71AcetylationKNALKKKKTIEQLLS
HHHHHCCHHHHHHHH		64.7124489116
72PhosphorylationNALKKKKTIEQLLSK
HHHHCCHHHHHHHHH		38.3322369663
78PhosphorylationKTIEQLLSKVEGTME
HHHHHHHHHHHHHHH		43.1622369663
112AcetylationRAMQEGAKAMKTIHS
HHHHHHHHHHHHHHC		60.9325381059
112UbiquitinationRAMQEGAKAMKTIHS
HHHHHHHHHHHHHHC		60.9323749301
115AcetylationQEGAKAMKTIHSGLD
HHHHHHHHHHHCCCC		49.5424489116
116PhosphorylationEGAKAMKTIHSGLDI
HHHHHHHHHHCCCCH		15.7322369663
119PhosphorylationKAMKTIHSGLDIDKV
HHHHHHHCCCCHHHH		36.8822369663
144PhosphorylationVELGDEISDAISRPL
HHHCHHHHHHHHCCC		20.9528889911
193PhosphorylationNVNAAPISENKVSLP
CCCCCCCCCCCCCCC		33.7722369663
196UbiquitinationAAPISENKVSLPSVP
CCCCCCCCCCCCCCC		29.2023749301
198PhosphorylationPISENKVSLPSVPSN
CCCCCCCCCCCCCCC		35.8528889911
201PhosphorylationENKVSLPSVPSNKIK
CCCCCCCCCCCCCCC		52.5328889911
204PhosphorylationVSLPSVPSNKIKQSE
CCCCCCCCCCCCCCC		48.9122369663
210PhosphorylationPSNKIKQSENSVKDG
CCCCCCCCCCCCCCC		33.4729136822
213PhosphorylationKIKQSENSVKDGEEE
CCCCCCCCCCCCCCC		26.8821551504
229UbiquitinationDEEDEDEKALRELQA
CCCHHHHHHHHHHHH		66.1123749301
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 SNF7_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNF7_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 SNF7_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRO1_YEASTBRO1physical
15086794
SNF7_YEASTSNF7physical
15086794
PALA_YEASTRIM20physical
15086794
CYC8_YEASTCYC8genetic
8224817
PACC_YEASTRIM101genetic
16024810
BRO1_YEASTBRO1physical
17446860
SNF7_YEASTSNF7physical
18467557
VTA1_YEASTVTA1physical
18467557
VPS20_YEASTVPS20physical
19591838
RIM13_YEASTRIM13physical
19725809
PALA_YEASTRIM20physical
19725809
VPS20_YEASTVPS20physical
19725809
VPS24_YEASTVPS24physical
19725809
BRO1_YEASTBRO1physical
19725809
VPS4_YEASTVPS4physical
19725809
TIR1_YEASTTIR1genetic
20402793
DAN1_YEASTDAN1genetic
20402793
IF5A2_YEASTANB1genetic
20402793
PACC_YEASTRIM101genetic
20402793
SMF1_YEASTSMF1genetic
15166140
SNF7_YEASTSNF7physical
18854142
VPS24_YEASTVPS24physical
18854142
SNX41_YEASTSNX41genetic
20134403
CARP_YEASTPEP4genetic
18794364
CLA4_YEASTCLA4genetic
21824003
ELM1_YEASTELM1genetic
21824003
ATN1_YEASTENA1genetic
18395523
SNF7_YEASTSNF7physical
22615397
YET3_YEASTYET3physical
22875988
VPS60_YEASTVPS60physical
22875988
VAB2_YEASTVAB2physical
22875988
LAM4_YEASTYHR080Cphysical
22875988
MPS3_YEASTMPS3physical
22875988
GON7_YEASTGON7physical
22875988
RE107_YEASTREC107physical
22875988
NNF1_YEASTNNF1physical
22875988
HSK3_YEASTHSK3physical
22875988
DYHC_YEASTDYN1physical
22875988
SED5_YEASTSED5physical
22875988
RCF1_YEASTRCF1physical
22875988
MDM1_YEASTMDM1physical
22875988
VPS20_YEASTVPS20physical
22875988
END3_YEASTEND3physical
22875988
AF9_YEASTYAF9physical
22875988
NUF2_YEASTNUF2physical
22875988
YO223_YEASTDSC3physical
22875988
CTF19_YEASTCTF19physical
22875988
TUP1_YEASTTUP1physical
22875988
MED3_YEASTPGD1physical
22875988
YJE9_YEASTYJL049Wphysical
22875988
BUL2_YEASTBUL2physical
22875988
NOT3_YEASTNOT3physical
22875988
TYE7_YEASTTYE7physical
22875988
SNF7_YEASTSNF7physical
23063125
NRG1_YEASTNRG1genetic
25239548
PACC_YEASTRIM101genetic
25239548
DID4_YEASTDID4genetic
24711499
NYV1_YEASTNYV1genetic
25017437
ATC2_YEASTPMC1genetic
25017437
MIG1_YEASTMIG1genetic
25017437
NRG1_YEASTNRG1genetic
25017437
CANB_YEASTCNB1genetic
23933635
ATC1_YEASTPMR1genetic
23933635
PACC_YEASTRIM101genetic
23933635
NRG1_YEASTNRG1genetic
23933635
VPS20_YEASTVPS20physical
24058170
VPS24_YEASTVPS24physical
24058170
VPS4_YEASTVPS4physical
24058170
VTA1_YEASTVTA1physical
24058170
BRO1_YEASTBRO1physical
24058170
RIM13_YEASTRIM13physical
24058170
PALA_YEASTRIM20physical
24058170
YG34_YEASTYGR122Wphysical
24058170
WDR6_YEASTRTT10genetic
21880895
DPH7_YEASTRRT2genetic
21880895
SNX41_YEASTSNX41genetic
21880895
YJE9_YEASTYJL049Wphysical
26510789
CWC16_YEASTYJU2genetic
27708008
SEC65_YEASTSEC65genetic
27708008
TF2B_YEASTSUA7genetic
27708008
PGTB2_YEASTBET2genetic
27708008
HEH2_YEASTHEH2physical
27733427
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNF7_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-72; THR-116; SER-119;SER-193 AND SER-204, 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 SER-213, AND MASSSPECTROMETRY.
"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-72 AND SER-119, 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-72, AND MASSSPECTROMETRY.

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