HSP42_YEAST - dbPTM
HSP42_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSP42_YEAST
UniProt AC Q12329
Protein Name Heat shock protein 42
Gene Name HSP42
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 375
Subcellular Localization
Protein Description
Protein Sequence MSFYQPSLSLYDVLNALSNQTGQRGQQGYPRQPQRPQRYHPHYGQVHVGGHHPRHHPLYSRYNGVPNTYYYQFPGQAYYYSPEYGYDDEDGEEEDQDEDMVGDSGTTRQEDGGEDSNSRRYPSYYHCNTARNNRTNQQANSLNDLLTALIGVPPYEGTEPEIEANTEQEGEKGEEKDKKDKSEAPKEEAGETNKEKPLNQLEESSRPPLAKKSSSFAHLQAPSPIPDPLQVSKPETRMDLPFSPEVNVYDTEDTYVVVLALPGANSRAFHIDYHPSSHEMLIKGKIEDRVGIDEKFLKITELKYGAFERTVKFPVLPRIKDEEIKATYNNGLLQIKVPKIVNDTEKPKPKKRIAIEEIPDEELEFEENPNPTVEN
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
9PhosphorylationSFYQPSLSLYDVLNA
CCCCCCCHHHHHHHH		29.2630377154
11PhosphorylationYQPSLSLYDVLNALS
CCCCCHHHHHHHHHH		10.7130377154
18PhosphorylationYDVLNALSNQTGQRG
HHHHHHHHCCCCCCC		25.2030377154
21PhosphorylationLNALSNQTGQRGQQG
HHHHHCCCCCCCCCC		39.2630377154
123PhosphorylationSNSRRYPSYYHCNTA
CCCCCCCCCCCCCHH		29.4130377154
129PhosphorylationPSYYHCNTARNNRTN
CCCCCCCHHCCCCCH		32.1830377154
141PhosphorylationRTNQQANSLNDLLTA
CCHHHHHHHHHHHHH		31.4030377154
179UbiquitinationKGEEKDKKDKSEAPK
CCCCCCCCCCCCCCH		79.2217644757
181UbiquitinationEEKDKKDKSEAPKEE
CCCCCCCCCCCCHHH		60.1017644757
182PhosphorylationEKDKKDKSEAPKEEA
CCCCCCCCCCCHHHH		49.4721082442
186UbiquitinationKDKSEAPKEEAGETN
CCCCCCCHHHHCCCC		75.2017644757
192PhosphorylationPKEEAGETNKEKPLN
CHHHHCCCCCCCHHH		51.1529136822
194UbiquitinationEEAGETNKEKPLNQL
HHHCCCCCCCHHHHH		74.6317644757
196UbiquitinationAGETNKEKPLNQLEE
HCCCCCCCHHHHHHH		57.3123749301
211UbiquitinationSSRPPLAKKSSSFAH
HCCCCCCCCCCCCCC		61.9517644757
212UbiquitinationSRPPLAKKSSSFAHL
CCCCCCCCCCCCCCC		50.3823749301
213PhosphorylationRPPLAKKSSSFAHLQ
CCCCCCCCCCCCCCC		30.4322369663
214PhosphorylationPPLAKKSSSFAHLQA
CCCCCCCCCCCCCCC		38.0522369663
215PhosphorylationPLAKKSSSFAHLQAP
CCCCCCCCCCCCCCC		33.2822369663
223PhosphorylationFAHLQAPSPIPDPLQ
CCCCCCCCCCCCCCC		38.1822369663
232PhosphorylationIPDPLQVSKPETRMD
CCCCCCCCCCCCCCC		29.5422890988
233AcetylationPDPLQVSKPETRMDL
CCCCCCCCCCCCCCC		48.2824489116
233UbiquitinationPDPLQVSKPETRMDL
CCCCCCCCCCCCCCC		48.2817644757
236PhosphorylationLQVSKPETRMDLPFS
CCCCCCCCCCCCCCC		39.5622890988
283UbiquitinationSSHEMLIKGKIEDRV
CHHHHEEECCHHHCC		50.6317644757
295AcetylationDRVGIDEKFLKITEL
HCCCCCHHHHHHHEE		52.8524489116
303UbiquitinationFLKITELKYGAFERT
HHHHHEECCCCCCCE		35.0924961812
312AcetylationGAFERTVKFPVLPRI
CCCCCEECCCCCCCC		43.2524489116
312UbiquitinationGAFERTVKFPVLPRI
CCCCCEECCCCCCCC		43.2517644757
325UbiquitinationRIKDEEIKATYNNGL
CCCCHHHHEEEECCE		37.6517644757
336UbiquitinationNNGLLQIKVPKIVND
ECCEEEEECCCCCCC		39.2517644757
339UbiquitinationLLQIKVPKIVNDTEK
EEEEECCCCCCCCCC		63.3717644757
344PhosphorylationVPKIVNDTEKPKPKK
CCCCCCCCCCCCCCC		40.4823749301
346UbiquitinationKIVNDTEKPKPKKRI
CCCCCCCCCCCCCEE		61.5117644757
348UbiquitinationVNDTEKPKPKKRIAI
CCCCCCCCCCCEEEE		79.2317644757
350UbiquitinationDTEKPKPKKRIAIEE
CCCCCCCCCEEEEEE		61.8917644757
351UbiquitinationTEKPKPKKRIAIEEI
CCCCCCCCEEEEEEC		58.5317644757
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 HSP42_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSP42_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 HSP42_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP42_YEASTHSP42physical
8576246
HSP42_YEASTHSP42physical
11967834
BCA2_YEASTBAT2physical
16554755
GLNA_YEASTGLN1physical
16554755
GLNA_YEASTGLN1physical
16429126
TBB_YEASTTUB2physical
16429126
MDN1_YEASTMDN1physical
16429126
RPB2_YEASTRPB2physical
16429126
PYR1_YEASTURA2physical
16429126
RPA2_YEASTRPA135physical
16429126
PEX11_YEASTPEX11physical
18467557
PEX14_YEASTPEX14physical
18467557
HSP42_YEASTHSP42physical
18719252
ATG34_YEASTATG34physical
18719252
ADA2_YEASTADA2physical
18719252
SMT3_YEASTSMT3physical
18719252
PRP43_YEASTPRP43physical
19536198
STH1_YEASTSTH1physical
19536198
UBP15_YEASTUBP15physical
19536198
HSP72_YEASTSSA2physical
19536198
HSP7F_YEASTSSE1physical
19536198
HSP79_YEASTSSE2physical
19536198
SIS1_YEASTSIS1genetic
22723742
MAS5_YEASTYDJ1genetic
22723742
TSL1_YEASTTSL1physical
24412193
CUR1_YEASTCUR1genetic
24938787
RPN8_YEASTRPN8physical
25919710
IHO1_HUMANCCDC36physical
27107014
TAD2A_HUMANTADA2Aphysical
27107014
MDFI_HUMANMDFIphysical
27107014
BANP_HUMANBANPphysical
27107014
PLS1_HUMANPLSCR1physical
27107014
UBX11_HUMANUBXN11physical
27107014
GASP2_HUMANGPRASP2physical
27107014
DMRTB_HUMANDMRTB1physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSP42_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-182; SER-213; SER-214;SER-215 AND SER-223, 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; SER-214 ANDSER-215, AND MASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND MASSSPECTROMETRY.

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