HSP74_YEAST - dbPTM
HSP74_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSP74_YEAST
UniProt AC P22202
Protein Name Heat shock protein SSA4
Gene Name SSA4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 642
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MSKAVGIDLGTTYSCVAHFANDRVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQAAMNPHNTVFDAKRLIGRKFDDPEVTNDAKHYPFKVIDKGGKPVVQVEYKGETKTFTPEEISSMILTKMKETAENFLGTEVKDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKSQKEHNVLIFDLGGGTFDVSLLSIDEGVFEVKATAGDTHLGGEDFDSRLVNFLAEEFKRKNKKDLTTNQRSLRRLRTAAERAKRTLSSSAQTSIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLADSKLDKSQIDEIVLVGGSTRIPKVQKLVSDFFNGKEPNRSINPDEAVAYGAAVQAAILTGDQSSTTQDLLLLDVAPLSLGIETAGGIMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERTRTKDNNLLGKFELSGIPPAPRGVPQIEVTFDIDANGILNVSAVEKGTGKSNKITITNDKGRLSKEDIDKMVAEAEKFKAEDEQEAQRVQAKNQLESYAFTLKNSVSENNFKEKVGEEDARKLEAAAQDAINWLDASQAASTEEYKERQKELEGVANPIMSKFYGAAGGAPGAGPVPGAGAGPTGAPDNGPTVEEVD
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
12PhosphorylationVGIDLGTTYSCVAHF
CCCCCCCHHHHHHHH		16.1917287358
14PhosphorylationIDLGTTYSCVAHFAN
CCCCCHHHHHHHHCC		10.4628889911
54UbiquitinationRLIGDAAKNQAAMNP
HHHHHHHHCCHHCCC		51.8422817900
54AcetylationRLIGDAAKNQAAMNP
HHHHHHHHCCHHCCC		51.84-
86AcetylationPEVTNDAKHYPFKVI
CCCCCCCCCCCEEEE		46.6824489116
91AcetylationDAKHYPFKVIDKGGK
CCCCCCEEEECCCCC		33.5024489116
111PhosphorylationEYKGETKTFTPEEIS
EEECCCEEECHHHHH		39.9128889911
151PhosphorylationVPAYFNDSQRQATKD
EEECCCHHHCCHHCC		28.5028889911
157UbiquitinationDSQRQATKDAGTIAG
HHHCCHHCCCCCCCC		48.9023749301
161PhosphorylationQATKDAGTIAGLNVL
CHHCCCCCCCCCHHH		14.9030377154
175PhosphorylationLRIINEPTAAAIAYG
HHHCCCHHHHHHHHC		23.8121440633
185UbiquitinationAIAYGLDKKSQKEHN
HHHHCCCCCCCCCCC		60.4117644757
185AcetylationAIAYGLDKKSQKEHN
HHHHCCCCCCCCCCC		60.4125381059
186UbiquitinationIAYGLDKKSQKEHNV
HHHCCCCCCCCCCCE		58.7617644757
220PhosphorylationGVFEVKATAGDTHLG
CEEEEEECCCCCCCC		26.0027017623
224PhosphorylationVKATAGDTHLGGEDF
EEECCCCCCCCCCCH		20.3419779198
233PhosphorylationLGGEDFDSRLVNFLA
CCCCCHHHHHHHHHH		27.7527017623
244AcetylationNFLAEEFKRKNKKDL
HHHHHHHHHHCCCCC		66.7824489116
244UbiquitinationNFLAEEFKRKNKKDL
HHHHHHHHHHCCCCC		66.7817644757
246UbiquitinationLAEEFKRKNKKDLTT
HHHHHHHHCCCCCCH		73.9517644757
317AcetylationSTLEPVEKVLADSKL
HCCHHHHHHHCCCCC		42.6624489116
323AcetylationEKVLADSKLDKSQID
HHHHCCCCCCHHHCC		62.3425381059
338PhosphorylationEIVLVGGSTRIPKVQ
EEEEECCCCCCHHHH		14.4828889911
339PhosphorylationIVLVGGSTRIPKVQK
EEEECCCCCCHHHHH		35.5728889911
343UbiquitinationGGSTRIPKVQKLVSD
CCCCCCHHHHHHHHH		55.7322817900
346UbiquitinationTRIPKVQKLVSDFFN
CCCHHHHHHHHHHHC		54.5722817900
416PhosphorylationTKLIPRNSTIPTKKS
HHCCCCCCCCCCCHH		29.0622369663
417PhosphorylationKLIPRNSTIPTKKSE
HCCCCCCCCCCCHHH		34.2322369663
420PhosphorylationPRNSTIPTKKSEVFS
CCCCCCCCCHHHHHE		47.4521440633
421UbiquitinationRNSTIPTKKSEVFST
CCCCCCCCHHHHHEE		49.2823749301
422UbiquitinationNSTIPTKKSEVFSTY
CCCCCCCHHHHHEEE		55.0923749301
423PhosphorylationSTIPTKKSEVFSTYA
CCCCCCHHHHHEEEC		40.3222369663
427PhosphorylationTKKSEVFSTYADNQP
CCHHHHHEEECCCCC		26.1922369663
428PhosphorylationKKSEVFSTYADNQPG
CHHHHHEEECCCCCC		15.9722369663
429PhosphorylationKSEVFSTYADNQPGV
HHHHHEEECCCCCCE		15.6822369663
449UbiquitinationEGERTRTKDNNLLGK
ECCCCCCCCCCEEEE		55.9923749301
456UbiquitinationKDNNLLGKFELSGIP
CCCCEEEEEEECCCC		35.3223749301
460PhosphorylationLLGKFELSGIPPAPR
EEEEEEECCCCCCCC		27.7222369663
491UbiquitinationLNVSAVEKGTGKSNK
EEEEEEECCCCCCCC		55.9917644757
493PhosphorylationVSAVEKGTGKSNKIT
EEEEECCCCCCCCEE		53.1322369663
495UbiquitinationAVEKGTGKSNKITIT
EEECCCCCCCCEEEE		51.1722817900
496PhosphorylationVEKGTGKSNKITITN
EECCCCCCCCEEEEC		44.7122369663
498UbiquitinationKGTGKSNKITITNDK
CCCCCCCCEEEECCC		48.6023749301
500PhosphorylationTGKSNKITITNDKGR
CCCCCCEEEECCCCC		24.2922369663
502PhosphorylationKSNKITITNDKGRLS
CCCCEEEECCCCCCC		28.8122369663
505UbiquitinationKITITNDKGRLSKED
CEEEECCCCCCCHHH		48.2623749301
509PhosphorylationTNDKGRLSKEDIDKM
ECCCCCCCHHHHHHH		32.4129136822
510UbiquitinationNDKGRLSKEDIDKMV
CCCCCCCHHHHHHHH		65.0922817900
515AcetylationLSKEDIDKMVAEAEK
CCHHHHHHHHHHHHH		35.2922865919
522AcetylationKMVAEAEKFKAEDEQ
HHHHHHHHHCCCCHH		60.2524489116
522UbiquitinationKMVAEAEKFKAEDEQ
HHHHHHHHHCCCCHH		60.2523749301
524AcetylationVAEAEKFKAEDEQEA
HHHHHHHCCCCHHHH		63.0324489116
537UbiquitinationEAQRVQAKNQLESYA
HHHHHHHHHHHHHHH		28.3024961812
550PhosphorylationYAFTLKNSVSENNFK
HHHHHCCCCCCCCHH		25.9821126336
552PhosphorylationFTLKNSVSENNFKEK
HHHCCCCCCCCHHHH		34.1322369663
595AcetylationEEYKERQKELEGVAN
HHHHHHHHHHHHHHH		71.1824489116
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 HSP74_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSP74_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 HSP74_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP73_YEASTSSA3genetic
3302682
IMB4_YEASTKAP123physical
16429126
CLH_YEASTCHC1physical
16429126
MSN5_YEASTMSN5physical
17020589
NUP82_YEASTNUP82physical
17020589
GSP1_YEASTGSP1physical
17020589
UTP8_YEASTUTP8physical
19536198
G3P3_YEASTTDH3physical
19536198
ISW2_YEASTISW2physical
19536198
HSP71_YEASTSSA1physical
19536198
HSP72_YEASTSSA2physical
19536198
HSP73_YEASTSSA3physical
19536198
SSB1_YEASTSSB1physical
19536198
HSP7F_YEASTSSE1physical
19536198
CG13_YEASTCLN3physical
23217712
COX5A_YEASTCOX5Agenetic
27708008
CDC48_YEASTCDC48genetic
27708008
LCB2_YEASTLCB2genetic
27708008
SDA1_YEASTSDA1genetic
27708008
CH10_YEASTHSP10genetic
27708008
APC5_YEASTAPC5genetic
27708008
BCS1_YEASTBCS1genetic
27708008
VPS24_YEASTVPS24genetic
27708008
MDM35_YEASTMDM35genetic
27708008
ERG3_YEASTERG3genetic
27708008
COQ11_YEASTYLR290Cgenetic
27708008
SWS2_YEASTSWS2genetic
27708008
NOP12_YEASTNOP12genetic
27708008
CY1_YEASTCYT1genetic
27708008
COX10_YEASTCOX10genetic
27708008
QCR2_YEASTQCR2genetic
27708008
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSP74_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-423; THR-493 ANDSER-552, AND MASS SPECTROMETRY.

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