PEX30_YEAST - dbPTM
PEX30_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PEX30_YEAST
UniProt AC Q06169
Protein Name Peroxisomal membrane protein PEX30
Gene Name PEX30
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 523
Subcellular Localization Peroxisome membrane
Multi-pass membrane protein.
Protein Description
Protein Sequence MSGNTTNVHETRAKFAETLQPRIGGNTTKVIRAALEKNEAESGVSEDNDNGSLEKVNVATSPLLTSTPPTISKALVKLYPYLILIDEFLNVVTWTGKNIWSSVLMLCLFITTVEYFETLVKYFGHLAIIAILWGYSLLDNYIEGTLSSSPTLEDIALLMNRVSLKSDILLSPMVNLGTQDIQRLLYTTVILSPIYVMITWLLLPPRSLMLMVGMFLLTYHSPWSKVARRLLWKFKIVRLLVFYVTGLDLGGINKDQGIFATVQKQVKKLASTENSNGVLSDSKPIRFTYVLYENQRRWLGIGWKPSMLSYERTPWTDEFLNEAPSPENFHLPEETNTMVWRWVDKTWRLDMTNDGAIQVPNSKARTSADPSPDEGFIYYDNTWKKPSKEDSFSKYTRRRRWVRTAELVKTSDFDESVINSNRNSAIEQKVEENSTNGLTAEQELGSNKQEKDNAKKVGEPTTEETKEFAEASNINEGEFERISSTDEEVLKSRARDRLAKVLDDTEEKEQSNPTIGRDSKKAV
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------MSGNTTNVH
------CCCCCCCHH		40.5330377154
2Acetylation------MSGNTTNVH
------CCCCCCCHH		40.5322814378
5Phosphorylation---MSGNTTNVHETR
---CCCCCCCHHHHH		24.2330377154
11PhosphorylationNTTNVHETRAKFAET
CCCCHHHHHHHHHHH		22.5030377154
37UbiquitinationVIRAALEKNEAESGV
HHHHHHHHCCHHCCC		62.0223749301
37AcetylationVIRAALEKNEAESGV
HHHHHHHHCCHHCCC		62.0224489116
42PhosphorylationLEKNEAESGVSEDND
HHHCCHHCCCCCCCC		52.0929136822
45PhosphorylationNEAESGVSEDNDNGS
CCHHCCCCCCCCCCC		42.6421551504
52PhosphorylationSEDNDNGSLEKVNVA
CCCCCCCCEEEEEEE		39.3422369663
60PhosphorylationLEKVNVATSPLLTST
EEEEEEECCCCCCCC		26.9624961812
61PhosphorylationEKVNVATSPLLTSTP
EEEEEECCCCCCCCC		12.1028889911
218PhosphorylationMVGMFLLTYHSPWSK
HHHHHHHHHCCHHHH		22.7228889911
219PhosphorylationVGMFLLTYHSPWSKV
HHHHHHHHCCHHHHH		10.5628889911
221PhosphorylationMFLLTYHSPWSKVAR
HHHHHHCCHHHHHHH		20.0428889911
283AcetylationNGVLSDSKPIRFTYV
CCCCCCCCCEEEEEE		49.8324489116
288PhosphorylationDSKPIRFTYVLYENQ
CCCCEEEEEEEECCC		11.6728889911
289PhosphorylationSKPIRFTYVLYENQR
CCCEEEEEEEECCCC		5.9228889911
410PhosphorylationRTAELVKTSDFDESV
HHHHHHHCCCCCHHH		26.5022890988
411PhosphorylationTAELVKTSDFDESVI
HHHHHHCCCCCHHHH		30.4822890988
416PhosphorylationKTSDFDESVINSNRN
HCCCCCHHHHCCCCC		30.0922890988
420PhosphorylationFDESVINSNRNSAIE
CCHHHHCCCCCHHHH		26.4922369663
424PhosphorylationVINSNRNSAIEQKVE
HHCCCCCHHHHHHHH		27.6422369663
434PhosphorylationEQKVEENSTNGLTAE
HHHHHHCCCCCCCHH		26.9124909858
435PhosphorylationQKVEENSTNGLTAEQ
HHHHHCCCCCCCHHH		44.9128889911
439PhosphorylationENSTNGLTAEQELGS
HCCCCCCCHHHHHCC		29.5530377154
446PhosphorylationTAEQELGSNKQEKDN
CHHHHHCCCHHHHHH		54.1824961812
461PhosphorylationAKKVGEPTTEETKEF
HHCCCCCCCHHHHHH		42.4028889911
484PhosphorylationGEFERISSTDEEVLK
CCCEECCCCCHHHHH		37.1927214570
485PhosphorylationEFERISSTDEEVLKS
CCEECCCCCHHHHHH		40.4125752575
500AcetylationRARDRLAKVLDDTEE
HHHHHHHHHHCCHHH		48.1725381059
508UbiquitinationVLDDTEEKEQSNPTI
HHCCHHHHHHHCCCC		55.6223749301
508AcetylationVLDDTEEKEQSNPTI
HHCCHHHHHHHCCCC		55.6224489116
514PhosphorylationEKEQSNPTIGRDSKK
HHHHHCCCCCCCCCC		40.0728889911
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 PEX30_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PEX30_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 PEX30_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PEX29_YEASTPEX29physical
11283351
PEX29_YEASTPEX29physical
14617799
PEX32_YEASTPEX32physical
14617799
PEX31_YEASTPEX31physical
14617799
PEX19_YEASTPEX19physical
16551610
PEX30_YEASTPEX30physical
11283351
PEX30_YEASTPEX30physical
18467557
PEX30_YEASTPEX30physical
22940862
KPC1_YEASTPKC1genetic
27708008
CDC1_YEASTCDC1genetic
27708008
PAN1_YEASTPAN1genetic
27708008
SRP54_YEASTSRP54genetic
27708008
PEX29_YEASTPEX29physical
27129769
RTN1_YEASTRTN1physical
27129769
YOP1_YEASTYOP1physical
27129769
SCS2_YEASTSCS2physical
27129769
DPM1_YEASTDPM1physical
27129769
YET3_YEASTYET3physical
27129769
POM33_YEASTPOM33physical
27129769
PEX32_YEASTPEX32physical
27129769
TCB3_YEASTTCB3physical
27129769
ACS1_YEASTACS1physical
27129769
BFR1_YEASTBFR1physical
27129769
HRP1_YEASTHRP1physical
27129769
SNU13_YEASTSNU13physical
27129769
PEX28_YEASTPEX28physical
27129769
NOP58_YEASTNOP58physical
27129769
EF1A_YEASTTEF2physical
27129769
PBP4_YEASTPBP4physical
27129769
IF2P_YEASTFUN12physical
27129769
KPYK1_YEASTCDC19physical
27129769
ODP2_YEASTLAT1physical
27129769
NOP56_YEASTNOP56physical
27129769
RLA0_YEASTRPP0physical
27129769
STM1_YEASTSTM1physical
27129769
SRP54_YEASTSRP54physical
27129769
NHP2_YEASTNHP2physical
27129769
ALF_YEASTFBA1physical
27129769
ADH2_YEASTADH2physical
27129769
PMG1_YEASTGPM1physical
27129769
DEF1_YEASTDEF1physical
27129769
CARP_YEASTPEP4physical
27129769
FBRL_YEASTNOP1physical
27129769
SEY1_YEASTSEY1physical
27129769
PUF4_YEASTPUF4physical
27129769
SCS22_YEASTSCS22physical
27129769
SC61A_YEASTSEC61physical
27129769
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PEX30_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-52; SER-61; SER-420;SER-424; SER-484 AND THR-485, AND MASS SPECTROMETRY.

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