YAT2_YEAST - dbPTM
YAT2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YAT2_YEAST
UniProt AC P40017
Protein Name Carnitine O-acetyltransferase YAT2
Gene Name YAT2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 923
Subcellular Localization Cytoplasm .
Protein Description Involved in the shutteling of acetyl-CoA in the cell..
Protein Sequence MSSGSTIVSSDKSGRTFKHEEELPKLPLPKLCDTLQRLKESLEPLYYADGYYQHPLDPEQIEKLSSIIRDFEENPVSEKLQSKLQSYHDTRDCYLDELHLDINNQTSTREIQDDVLPRNPFLVLADDALPNITQADRSAVLVHSAARFISALKQDLLPPDINATNGKPLSMAPFLNLFGTTRSPVFQRGEVENFDLNKPYTASDLEDPDYSSDEDDNDEPTQKDFDDRKRKHEEDIFTGNGITIKRHPDSKHILIISRGQYYTLEVLDSTNKIIYTAAELTTIFNHIIKDSSGIEKSTALGSLTSHSFRNWKYARKRLQKRYPNELHRIDSALFVLVLDESQEETTNDGDDTADISQMFNRTITERDKKCTSANCKRVFYGTSIINSKGHQVGSCVSRWYDKLQLVVTADAKATVIWDSFTCDGSVVLRFTSEIYTESVLRLARDVNAGDPQFSLWPNVTQMDPETKKLMTATISADGGGPSEIDPKLVVNKIDWSFSNILNTHVHLSETKLADLISKYDIVRASIPLGRRSAQRLGVKPDSMVQVALQIAHYALYGRMVFGLEPVSTRGFKNSRSSFINIQSQALLELCQLFISSSIDGTDKLDKFIQTCETHNNMVKHAKSGVGYEKHFNALKYLFKFHDHFGIHLSGDESSAAKDLFENPLVLPFSQPELIVANCGNAATTTFGITPAVPHGFGIGYIIKDDQVDLTVTSQFRQGDRLMFMLSWVLGEIRSYWRMSRGTSHNKTGVKISPVVDKLYEMDNAVNNPPKRNGHTVNGSRKTSSSSQVNLNRYGGFFDLEGHIDSRNISKTPSMKNLQKTFNGLTMSADNDHSSSAVSVPTEKEKLNTGHEILQIQPREVASNGLEADDETDIEIVAGNADGTSSSASSATSLNSKKRNVINSRFDIDFDRSRVGRKVATLDQ
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------MSSGSTIVS
------CCCCCEEEC
43.3222814378
2Phosphorylation------MSSGSTIVS
------CCCCCEEEC
43.3230377154
5Phosphorylation---MSSGSTIVSSDK
---CCCCCEEECCCC
19.5330377154
9PhosphorylationSSGSTIVSSDKSGRT
CCCCEEECCCCCCCC
29.0328889911
200PhosphorylationNFDLNKPYTASDLED
CCCCCCCCCHHHCCC
19.2922369663
201PhosphorylationFDLNKPYTASDLEDP
CCCCCCCCHHHCCCC
28.3622369663
203PhosphorylationLNKPYTASDLEDPDY
CCCCCCHHHCCCCCC
34.6222369663
210PhosphorylationSDLEDPDYSSDEDDN
HHCCCCCCCCCCCCC
18.5722369663
211PhosphorylationDLEDPDYSSDEDDND
HCCCCCCCCCCCCCC
38.4022369663
212PhosphorylationLEDPDYSSDEDDNDE
CCCCCCCCCCCCCCC
38.5022369663
221PhosphorylationEDDNDEPTQKDFDDR
CCCCCCCCCCCCHHH
46.3222369663
2512-HydroxyisobutyrylationIKRHPDSKHILIISR
EEECCCCCEEEEEEC
41.88-
368AcetylationRTITERDKKCTSANC
HHCCHHHHCCCCCCC
56.8425381059
747PhosphorylationRGTSHNKTGVKISPV
CCCCCCCCCCEECCH
53.1528889911
752PhosphorylationNKTGVKISPVVDKLY
CCCCCEECCHHHHHH
13.1122369663
779PhosphorylationNGHTVNGSRKTSSSS
CCCCCCCCCCCCCCC
25.9630377154
782PhosphorylationTVNGSRKTSSSSQVN
CCCCCCCCCCCCCEE
32.5022369663
783PhosphorylationVNGSRKTSSSSQVNL
CCCCCCCCCCCCEEE
31.1222369663
784PhosphorylationNGSRKTSSSSQVNLN
CCCCCCCCCCCEEEE
38.9622369663
785PhosphorylationGSRKTSSSSQVNLNR
CCCCCCCCCCEEEEC
25.2622369663
786PhosphorylationSRKTSSSSQVNLNRY
CCCCCCCCCEEEECC
39.8422369663
805PhosphorylationDLEGHIDSRNISKTP
ECCCCCCCCCCCCCC
26.9927214570
809PhosphorylationHIDSRNISKTPSMKN
CCCCCCCCCCCCHHH
33.7422369663
811PhosphorylationDSRNISKTPSMKNLQ
CCCCCCCCCCHHHHH
17.5022369663
813PhosphorylationRNISKTPSMKNLQKT
CCCCCCCCHHHHHHH
47.8522369663
820PhosphorylationSMKNLQKTFNGLTMS
CHHHHHHHHCCEEEC
14.9022369663
825PhosphorylationQKTFNGLTMSADNDH
HHHHCCEEECCCCCC
15.5229734811
827PhosphorylationTFNGLTMSADNDHSS
HHCCEEECCCCCCCC
27.5122369663
833PhosphorylationMSADNDHSSSAVSVP
ECCCCCCCCCCCCCC
28.9322369663
834PhosphorylationSADNDHSSSAVSVPT
CCCCCCCCCCCCCCC
20.9222369663
835PhosphorylationADNDHSSSAVSVPTE
CCCCCCCCCCCCCCH
35.3922369663
838PhosphorylationDHSSSAVSVPTEKEK
CCCCCCCCCCCHHHH
23.3022369663
841PhosphorylationSSAVSVPTEKEKLNT
CCCCCCCCHHHHCCC
58.4929734811
903PhosphorylationKKRNVINSRFDIDFD
CCCCCHHCCCCCCCC
24.1727214570
920PhosphorylationRVGRKVATLDQ----
HCCCEEEECCC----
33.5830377154

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 YAT2_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YAT2_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 YAT2_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CACM_YEASTYAT1physical
18719252
SWC5_YEASTSWC5genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
NU133_YEASTNUP133genetic
27708008
SEI1_YEASTFLD1genetic
27708008
RL6B_YEASTRPL6Bgenetic
27708008
DHE5_YEASTGDH3genetic
27708008
PFF1_YEASTPFF1genetic
27708008
SNF5_YEASTSNF5genetic
27708008
THRC_YEASTTHR4genetic
27708008
YCY0_YEASTYCR090Cgenetic
27708008
RL13A_YEASTRPL13Agenetic
27708008
XRS2_YEASTXRS2genetic
27708008
RLA4_YEASTRPP2Bgenetic
27708008
ATG1_YEASTATG1genetic
27708008
ORM1_YEASTORM1genetic
27708008
VMA21_YEASTVMA21genetic
27708008
RTS3_YEASTRTS3genetic
27708008
ELP2_YEASTELP2genetic
27708008
LRP1_YEASTLRP1genetic
27708008
DHOM_YEASTHOM6genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
IXR1_YEASTIXR1genetic
27708008
EF1G2_YEASTTEF4genetic
27708008
FEN1_YEASTRAD27genetic
27708008
BAS1_YEASTBAS1genetic
27708008
RT109_YEASTRTT109genetic
27708008
UBI4P_YEASTUBI4genetic
27708008
RL8B_YEASTRPL8Bgenetic
27708008
TSR2_YEASTTSR2genetic
27708008
SST2_YEASTSST2genetic
27708008
YPT7_YEASTYPT7genetic
27708008
VPS9_YEASTVPS9genetic
27708008
IMP2_YEASTIMP2genetic
27708008
LGE1_YEASTLGE1genetic
27708008
YP260_YEASTYPL260Wgenetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YAT2_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-784; SER-786 ANDSER-833, 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-782 AND SER-786, ANDMASS SPECTROMETRY.

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