HSP73_YEAST - dbPTM
HSP73_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSP73_YEAST
UniProt AC P09435
Protein Name Heat shock protein SSA3
Gene Name SSA3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 649
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MSRAVGIDLGTTYSCVAHFSNDRVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQAAINPHNTVFDAKRLIGRKFDDPEVTTDAKHFPFKVISRDGKPVVQVEYKGETKTFTPEEISSMVLSKMKETAENYLGTTVNDAVVTVPAYFNDSQRQATKDAGTIAGMNVLRIINEPTAAAIAYGLDKKGRAEHNVLIFDLGGGTFDVSLLSIDEGVFEVKATAGDTHLGGEDFDNRLVNHLATEFKRKTKKDISNNQRSLRRLRTAAERAKRALSSSSQTSIEIDSLFEGMDFYTSLTRARFEELCADLFRSTLEPVEKVLKDSKLDKSQIDEIVLVGGSTRIPKIQKLVSDFFNGKEPNRSINPDEAVAYGAAVQAAILTGDQSTKTQDLLLLDVAPLSLGIETAGGIMTKLIPRNSTIPTKKSETFSTYADNQPGVLIQVFEGERTRTKDNNLLGKFELSGIPPAPRGVPQIDVTFDIDANGILNVSALEKGTGKSNKITITNDKGRLSKDDIDRMVSEAEKYRADDEREAERVQAKNQLESYAFTLKNTINEASFKEKVGEDDAKRLETASQETIDWLDASQAASTDEYKDRQKELEGIANPIMTKFYGAGAGAGPGAGESGGFPGSMPNSGATGGGEDTGPTVEEVD
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
CCCCCCCCEEEEEEE		16.1917287358
13PhosphorylationGIDLGTTYSCVAHFS
CCCCCCCEEEEEEEC		10.4230377154
14PhosphorylationIDLGTTYSCVAHFSN
CCCCCCEEEEEEECC		10.4617287358
69AcetylationHNTVFDAKRLIGRKF
CCCHHHHHHHHCCCC		49.9722865919
69SuccinylationHNTVFDAKRLIGRKF
CCCHHHHHHHHCCCC		49.9723954790
111PhosphorylationEYKGETKTFTPEEIS
EECCEEEEECHHHHH		39.9119823750
113PhosphorylationKGETKTFTPEEISSM
CCEEEEECHHHHHHH		34.7119823750
118PhosphorylationTFTPEEISSMVLSKM
EECHHHHHHHHHHHH		18.7019823750
119PhosphorylationFTPEEISSMVLSKMK
ECHHHHHHHHHHHHH		20.6919823750
123PhosphorylationEISSMVLSKMKETAE
HHHHHHHHHHHHHHH		21.2019823750
143PhosphorylationTVNDAVVTVPAYFND
CCCCEEEEEECCCCH		17.7422369663
147PhosphorylationAVVTVPAYFNDSQRQ
EEEEEECCCCHHHCC		9.2422369663
151PhosphorylationVPAYFNDSQRQATKD
EECCCCHHHCCHHCC		28.5022369663
156PhosphorylationNDSQRQATKDAGTIA
CHHHCCHHCCCCCCC		22.5621440633
157SuccinylationDSQRQATKDAGTIAG
HHHCCHHCCCCCCCC		48.9023954790
157AcetylationDSQRQATKDAGTIAG
HHHCCHHCCCCCCCC		48.9024489116
157UbiquitinationDSQRQATKDAGTIAG
HHHCCHHCCCCCCCC		48.9022817900
185AcetylationAIAYGLDKKGRAEHN
HHHHCCCCCCCCCCE		63.2724489116
185SuccinylationAIAYGLDKKGRAEHN
HHHHCCCCCCCCCCE		63.2723954790
185UbiquitinationAIAYGLDKKGRAEHN
HHHHCCCCCCCCCCE		63.2717644757
186UbiquitinationIAYGLDKKGRAEHNV
HHHCCCCCCCCCCEE		53.9817644757
218UbiquitinationDEGVFEVKATAGDTH
CCCEEEEEECCCCCC		32.5917644757
220PhosphorylationGVFEVKATAGDTHLG
CEEEEEECCCCCCCC		26.0023749301
224PhosphorylationVKATAGDTHLGGEDF
EEECCCCCCCCCCCH		20.3425752575
274PhosphorylationRAKRALSSSSQTSIE
HHHHHHHCCCCCCEE		34.5528889911
275PhosphorylationAKRALSSSSQTSIEI
HHHHHHCCCCCCEEH		24.0828889911
276PhosphorylationKRALSSSSQTSIEID
HHHHHCCCCCCEEHH		39.1528889911
278PhosphorylationALSSSSQTSIEIDSL
HHHCCCCCCEEHHHH		33.3527017623
293PhosphorylationFEGMDFYTSLTRARF
HCCCCHHHHHHHHHH		19.7727017623
317UbiquitinationSTLEPVEKVLKDSKL
HCCHHHHHHHCCCCC		53.7717644757
317AcetylationSTLEPVEKVLKDSKL
HCCHHHHHHHCCCCC		53.7724489116
320UbiquitinationEPVEKVLKDSKLDKS
HHHHHHHCCCCCCHH		64.0417644757
416PhosphorylationTKLIPRNSTIPTKKS
HHCCCCCCCCCCCCC		29.0620377248
417PhosphorylationKLIPRNSTIPTKKSE
HCCCCCCCCCCCCCC		34.2329136822
421UbiquitinationRNSTIPTKKSETFST
CCCCCCCCCCCCCCC		49.2823749301
421SuccinylationRNSTIPTKKSETFST
CCCCCCCCCCCCCCC		49.2823954790
421AcetylationRNSTIPTKKSETFST
CCCCCCCCCCCCCCC		49.2825381059
422UbiquitinationNSTIPTKKSETFSTY
CCCCCCCCCCCCCCC		56.8717644757
449UbiquitinationEGERTRTKDNNLLGK
ECCCCCCCCCCEEEE		55.9923749301
449SuccinylationEGERTRTKDNNLLGK
ECCCCCCCCCCEEEE		55.9923954790
449AcetylationEGERTRTKDNNLLGK
ECCCCCCCCCCEEEE		55.9924489116
456SuccinylationKDNNLLGKFELSGIP
CCCCEEEEEEECCCC		35.3223954790
456UbiquitinationKDNNLLGKFELSGIP
CCCCEEEEEEECCCC		35.3223749301
456AcetylationKDNNLLGKFELSGIP
CCCCEEEEEEECCCC		35.3224489116
460PhosphorylationLLGKFELSGIPPAPR
EEEEEEECCCCCCCC		27.7222369663
493PhosphorylationVSALEKGTGKSNKIT
EEEECCCCCCCCCEE		53.1322369663
495UbiquitinationALEKGTGKSNKITIT
EECCCCCCCCCEEEE		51.1722817900
496PhosphorylationLEKGTGKSNKITITN
ECCCCCCCCCEEEEC		44.7122369663
498UbiquitinationKGTGKSNKITITNDK
CCCCCCCCEEEECCC		48.6023749301
498AcetylationKGTGKSNKITITNDK
CCCCCCCCEEEECCC		48.6024489116
498SuccinylationKGTGKSNKITITNDK
CCCCCCCCEEEECCC		48.6023954790
500PhosphorylationTGKSNKITITNDKGR
CCCCCCEEEECCCCC		24.2922369663
502PhosphorylationKSNKITITNDKGRLS
CCCCEEEECCCCCCC		28.8122369663
505SuccinylationKITITNDKGRLSKDD
CEEEECCCCCCCHHH		48.2623954790
505AcetylationKITITNDKGRLSKDD
CEEEECCCCCCCHHH		48.2624489116
505UbiquitinationKITITNDKGRLSKDD
CEEEECCCCCCCHHH		48.2623749301
509PhosphorylationTNDKGRLSKDDIDRM
ECCCCCCCHHHHHHH		32.4529136822
510UbiquitinationNDKGRLSKDDIDRMV
CCCCCCCHHHHHHHH		65.1022817900
518PhosphorylationDDIDRMVSEAEKYRA
HHHHHHHHHHHHHCC		23.0327214570
537UbiquitinationEAERVQAKNQLESYA
HHHHHHHHHHHHHHH		28.3024961812
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 HSP73_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSP73_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 HSP73_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAS5_YEASTYDJ1physical
11320326
MED17_YEASTSRB4physical
7877695
MED18_YEASTSRB5physical
7877695
SSN3_YEASTSSN3physical
7877695
SSN8_YEASTSSN8physical
7877695
IDI1_YEASTIDI1physical
18467557
SSB1_YEASTSSB1physical
19536198
HSP74_YEASTSSA4physical
19536198
SSB2_YEASTSSB2physical
19536198
ELO2_YEASTELO2genetic
20093466
NRP1_YEASTNRP1genetic
20093466
MTU1_YEASTSLM3genetic
20093466
PHM6_YEASTPHM6genetic
20093466
OMS1_YEASTOMS1genetic
20093466
SLF1_YEASTSLF1genetic
20093466
HSP12_YEASTHSP12genetic
20093466
DBF2_YEASTDBF2genetic
20093466
HSV2_YEASTHSV2genetic
20093466
IME1_YEASTIME1genetic
20093466
COXM1_YEASTCMC1genetic
20093466
FABG_YEASTOAR1genetic
20093466
MDM35_YEASTMDM35genetic
20093466
VPS24_YEASTVPS24genetic
20093466
COQ11_YEASTYLR290Cgenetic
20093466
AMPD_YEASTAMD1genetic
20093466
SWS2_YEASTSWS2genetic
20093466
COX5A_YEASTCOX5Agenetic
20093466
DSE3_YEASTDSE3genetic
20093466
PMA2_YEASTPMA2genetic
20093466
HSP74_YEASTSSA4genetic
22138184
CG13_YEASTCLN3physical
23217712
OMS1_YEASTOMS1genetic
27708008
COXM1_YEASTCMC1genetic
27708008
COX5A_YEASTCOX5Agenetic
27708008
HAP5_YEASTHAP5genetic
27708008
RIM1_YEASTRIM1genetic
27708008
ELO2_YEASTELO2genetic
27708008
MTU1_YEASTSLM3genetic
27708008
GPR1_YEASTGPR1genetic
27708008
SLF1_YEASTSLF1genetic
27708008
CEM1_YEASTCEM1genetic
27708008
BEM2_YEASTBEM2genetic
27708008
HSP12_YEASTHSP12genetic
27708008
ATG1_YEASTATG1genetic
27708008
YGY0_YEASTYGL230Cgenetic
27708008
VMA21_YEASTVMA21genetic
27708008
QCR9_YEASTQCR9genetic
27708008
HSV2_YEASTHSV2genetic
27708008
HTD2_YEASTHTD2genetic
27708008
FLX1_YEASTFLX1genetic
27708008
LPLA_YEASTAIM22genetic
27708008
VPS35_YEASTVPS35genetic
27708008
IME1_YEASTIME1genetic
27708008
DHOM_YEASTHOM6genetic
27708008
MDM35_YEASTMDM35genetic
27708008
FABG_YEASTOAR1genetic
27708008
COQ11_YEASTYLR290Cgenetic
27708008
AMPD_YEASTAMD1genetic
27708008
LSM7_YEASTLSM7genetic
27708008
ATG3_YEASTATG3genetic
27708008
MDM38_YEASTMDM38genetic
27708008
FABD_YEASTMCT1genetic
27708008
CHL1_YEASTCHL1genetic
27708008
PMA2_YEASTPMA2genetic
27708008
COX10_YEASTCOX10genetic
27708008
HPBP1_HUMANHSPBP1physical
27107014
HSP74_YEASTSSA4genetic
28826004
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSP73_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 THR-417, AND MASSSPECTROMETRY.

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