SIP5_YEAST - dbPTM
SIP5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIP5_YEAST
UniProt AC P40210
Protein Name Protein SIP5
Gene Name SIP5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 489
Subcellular Localization Cytoplasm .
Protein Description May negatively regulate the SNF1 kinase by promoting the interaction of the REG1/GLC7 phosphatase complex with the kinase. Deletion of SIP5 promotes resistance to artimisin, which is probably an indirect effect of an action on the electron transport chain..
Protein Sequence MGNVPGKIDQEDSFNDVRPDSSYNTTSSNSVIKQYDEEASSRVRTRRTTSLVNNILNGNNARTKTGSHLSSTSRRKTSREKELAKEAHAKQLVVRCSETVDGGFLAPFGCYSFEKLDYDATVVKNLIIKRKLAPFYTPLQDFDESWTRDELIKIVDGLPLHDTFDENLEEFEDVPIGNLRKSTFNELIDKSLSKKEQRRMHAKIFRARLYKKRILWQENENETFLERKLEMKRIGSKSSNVEDNTSSQPRKNYHLPSDDLKYTLYKNGSECPICFLYFPGPFNYSKCCQQPICTECFVQIKRADPHFPHDEVDPTEPQTNDSEKDPNLLTSEPANCPYCATASFSITYQPPTNRETGIGGMPADSYVYKDAAISRADGGQPNISAITSDTIRPDWEIKLNKERARLMRRSANATAIHISNRLIDPSHSRRRNTSHSITPIHDESTSASRSPEPTINELEDQMVREAIRLSLEDQDNRKKSKNRNTSLRP
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
13PhosphorylationGKIDQEDSFNDVRPD
CCCCCCCCCCCCCCC		25.7923749301
21PhosphorylationFNDVRPDSSYNTTSS
CCCCCCCCCCCCCCC		37.0927214570
22PhosphorylationNDVRPDSSYNTTSSN
CCCCCCCCCCCCCCC		29.7727214570
25PhosphorylationRPDSSYNTTSSNSVI
CCCCCCCCCCCCCHH		21.5927017623
26PhosphorylationPDSSYNTTSSNSVIK
CCCCCCCCCCCCHHH		26.9027017623
27PhosphorylationDSSYNTTSSNSVIKQ
CCCCCCCCCCCHHHH		26.0328889911
28PhosphorylationSSYNTTSSNSVIKQY
CCCCCCCCCCHHHHH		30.9121551504
30PhosphorylationYNTTSSNSVIKQYDE
CCCCCCCCHHHHHCH		27.4527017623
33UbiquitinationTSSNSVIKQYDEEAS
CCCCCHHHHHCHHHH		40.4223749301
45PhosphorylationEASSRVRTRRTTSLV
HHHHHHHHHHHHHHH		22.9630377154
48PhosphorylationSRVRTRRTTSLVNNI
HHHHHHHHHHHHHHH		19.9022369663
49PhosphorylationRVRTRRTTSLVNNIL
HHHHHHHHHHHHHHH		20.4622369663
50PhosphorylationVRTRRTTSLVNNILN
HHHHHHHHHHHHHHC		29.7022369663
64UbiquitinationNGNNARTKTGSHLSS
CCCCCCCCCCCCCCC		45.3923749301
70PhosphorylationTKTGSHLSSTSRRKT
CCCCCCCCCCCCCCC		26.5828889911
71PhosphorylationKTGSHLSSTSRRKTS
CCCCCCCCCCCCCCH		36.4428889911
72PhosphorylationTGSHLSSTSRRKTSR
CCCCCCCCCCCCCHH		23.9128889911
73PhosphorylationGSHLSSTSRRKTSRE
CCCCCCCCCCCCHHH		31.8428889911
124UbiquitinationDYDATVVKNLIIKRK
CCCCHHHHHHHHHCC		41.5224961812
145PhosphorylationPLQDFDESWTRDELI
CHHHCCCCCCHHHHH		35.2821440633
182PhosphorylationPIGNLRKSTFNELID
CCCCCCHHHHHHHHH		31.6222369663
183PhosphorylationIGNLRKSTFNELIDK
CCCCCHHHHHHHHHH		33.2522369663
232UbiquitinationLERKLEMKRIGSKSS
HHHHHHHHHCCCCCC		31.3322817900
236PhosphorylationLEMKRIGSKSSNVED
HHHHHCCCCCCCCCC		27.3017563356
237UbiquitinationEMKRIGSKSSNVEDN
HHHHCCCCCCCCCCC		53.3323749301
238PhosphorylationMKRIGSKSSNVEDNT
HHHCCCCCCCCCCCC		28.9217563356
239PhosphorylationKRIGSKSSNVEDNTS
HHCCCCCCCCCCCCC		48.9417563356
246PhosphorylationSNVEDNTSSQPRKNY
CCCCCCCCCCCCCCC		32.9823749301
369UbiquitinationPADSYVYKDAAISRA
CCCCEEEECHHHHHC		30.7423749301
410PhosphorylationRARLMRRSANATAIH
HHHHHHHHHCCCEEE		18.6025521595
426PhosphorylationSNRLIDPSHSRRRNT
ECCCCCCCCCCCCCC		30.2830377154
428PhosphorylationRLIDPSHSRRRNTSH
CCCCCCCCCCCCCCC		31.6423749301
433PhosphorylationSHSRRRNTSHSITPI
CCCCCCCCCCCCEEC		26.4617330950
434PhosphorylationHSRRRNTSHSITPIH
CCCCCCCCCCCEECC		20.8417330950
436PhosphorylationRRRNTSHSITPIHDE
CCCCCCCCCEECCCC		28.1117330950
438PhosphorylationRNTSHSITPIHDEST
CCCCCCCEECCCCCC		21.1427214570
444PhosphorylationITPIHDESTSASRSP
CEECCCCCCCCCCCC		33.4519779198
446PhosphorylationPIHDESTSASRSPEP
ECCCCCCCCCCCCCC		33.2619779198
448PhosphorylationHDESTSASRSPEPTI
CCCCCCCCCCCCCCH		32.8119779198
450PhosphorylationESTSASRSPEPTINE
CCCCCCCCCCCCHHH		30.9928889911
454PhosphorylationASRSPEPTINELEDQ
CCCCCCCCHHHHHHH		34.4729688323
470PhosphorylationVREAIRLSLEDQDNR
HHHHHHHCHHCHHHH		21.6223749301
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 ligaseRSP5P39940
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SIP5_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 SIP5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HMO1_YEASTHMO1physical
16554755
NACA_YEASTEGD2physical
16554755
NACB1_YEASTEGD1physical
16554755
SEC7_YEASTSEC7genetic
27708008
CDC12_YEASTCDC12genetic
27708008
CDC23_YEASTCDC23genetic
27708008
YKT6_YEASTYKT6genetic
27708008
SEC12_YEASTSEC12genetic
27708008
ORC4_YEASTORC4genetic
27708008
SEC17_YEASTSEC17genetic
27708008
CDC27_YEASTCDC27genetic
27708008
APC11_YEASTAPC11genetic
27708008
DPOD_YEASTPOL3genetic
27708008
NSE4_YEASTNSE4genetic
27708008
TCPZ_YEASTCCT6genetic
27708008
GPI17_YEASTGPI17genetic
27708008
GNA1_YEASTGNA1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
PRS8_YEASTRPT6genetic
27708008
DAM1_YEASTDAM1genetic
27708008
MPPA_YEASTMAS2genetic
27708008
MET30_YEASTMET30genetic
27708008
PRP19_YEASTPRP19genetic
27708008
SYFB_YEASTFRS1genetic
27708008
UTP13_YEASTUTP13genetic
27708008
SEC22_YEASTSEC22genetic
27708008
TAF13_YEASTTAF13genetic
27708008
NOG2_YEASTNOG2genetic
27708008
RFC4_YEASTRFC4genetic
27708008
PROF_YEASTPFY1genetic
27708008
GPN2_YEASTGPN2genetic
27708008
ULP1_YEASTULP1genetic
27708008
NAB3_YEASTNAB3genetic
27708008
SLA1_YEASTSLA1genetic
27708008
AIM4_YEASTAIM4genetic
27708008
SWC5_YEASTSWC5genetic
27708008
AGP1_YEASTAGP1genetic
27708008
BUD31_YEASTBUD31genetic
27708008
IPT1_YEASTIPT1genetic
27708008
TBP7_YEASTYTA7genetic
27708008
ORM2_YEASTORM2genetic
27708008
NAA30_YEASTMAK3genetic
27708008
IES5_YEASTIES5genetic
29674565
ICE2_YEASTICE2genetic
29674565
RPA34_YEASTRPA34genetic
29674565
ATP18_YEASTATP18genetic
29674565
YNF8_YEASTYNL058Cgenetic
29674565
ASE1_YEASTASE1genetic
29674565
RU2A_YEASTLEA1genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SIP5_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-50; THR-183 AND SER-246,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-183; SER-236 ANDSER-239, AND MASS 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 THR-183 AND THR-433, ANDMASS SPECTROMETRY.

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