HSP7F_YEAST - dbPTM
HSP7F_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSP7F_YEAST
UniProt AC P32589
Protein Name Heat shock protein homolog SSE1
Gene Name SSE1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 693
Subcellular Localization Cytoplasm .
Protein Description Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures..
Protein Sequence MSTPFGLDLGNNNSVLAVARNRGIDIVVNEVSNRSTPSVVGFGPKNRYLGETGKNKQTSNIKNTVANLKRIIGLDYHHPDFEQESKHFTSKLVELDDKKTGAEVRFAGEKHVFSATQLAAMFIDKVKDTVKQDTKANITDVCIAVPPWYTEEQRYNIADAARIAGLNPVRIVNDVTAAGVSYGIFKTDLPEGEEKPRIVAFVDIGHSSYTCSIMAFKKGQLKVLGTACDKHFGGRDFDLAITEHFADEFKTKYKIDIRENPKAYNRILTAAEKLKKVLSANTNAPFSVESVMNDVDVSSQLSREELEELVKPLLERVTEPVTKALAQAKLSAEEVDFVEIIGGTTRIPTLKQSISEAFGKPLSTTLNQDEAIAKGAAFICAIHSPTLRVRPFKFEDIHPYSVSYSWDKQVEDEDHMEVFPAGSSFPSTKLITLNRTGDFSMAASYTDITQLPPNTPEQIANWEITGVQLPEGQDSVPVKLKLRCDPSGLHTIEEAYTIEDIEVEEPIPLPEDAPEDAEQEFKKVTKTVKKDDLTIVAHTFGLDAKKLNELIEKENEMLAQDKLVAETEDRKNTLEEYIYTLRGKLEEEYAPFASDAEKTKLQGMLNKAEEWLYDEGFDSIKAKYIAKYEELASLGNIIRGRYLAKEEEKKQAIRSKQEASQMAAMAEKLAAQRKAEAEKKEEKKDTEGDVDMD
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------MSTPFGLDL
------CCCCCCEEC
44.809298649
2Phosphorylation------MSTPFGLDL
------CCCCCCEEC
44.8028152593
3Phosphorylation-----MSTPFGLDLG
-----CCCCCCEECC
22.7228152593
32PhosphorylationDIVVNEVSNRSTPSV
CEEEEECCCCCCCCC
21.9828889911
35PhosphorylationVNEVSNRSTPSVVGF
EEECCCCCCCCCCEE
49.2528889911
36PhosphorylationNEVSNRSTPSVVGFG
EECCCCCCCCCCEEC
19.1521440633
38PhosphorylationVSNRSTPSVVGFGPK
CCCCCCCCCCEECCC
29.5328152593
452-HydroxyisobutyrylationSVVGFGPKNRYLGET
CCCEECCCCCCCCCC
55.20-
45AcetylationSVVGFGPKNRYLGET
CCCEECCCCCCCCCC
55.2024489116
45SuccinylationSVVGFGPKNRYLGET
CCCEECCCCCCCCCC
55.2023954790
48PhosphorylationGFGPKNRYLGETGKN
EECCCCCCCCCCCCC
28.5828889911
62SuccinylationNKQTSNIKNTVANLK
CCCCCCHHHHHHHHH
51.3023954790
64PhosphorylationQTSNIKNTVANLKRI
CCCCHHHHHHHHHHH
18.9228889911
692-HydroxyisobutyrylationKNTVANLKRIIGLDY
HHHHHHHHHHHCCCC
41.16-
69SuccinylationKNTVANLKRIIGLDY
HHHHHHHHHHHCCCC
41.1623954790
85PhosphorylationHPDFEQESKHFTSKL
CCCHHHHHHHHHHCE
30.9924961812
86AcetylationPDFEQESKHFTSKLV
CCHHHHHHHHHHCEE
41.8224489116
86UbiquitinationPDFEQESKHFTSKLV
CCHHHHHHHHHHCEE
41.8223749301
89PhosphorylationEQESKHFTSKLVELD
HHHHHHHHHCEEECC
25.3528889911
90PhosphorylationQESKHFTSKLVELDD
HHHHHHHHCEEECCC
24.0528889911
91AcetylationESKHFTSKLVELDDK
HHHHHHHCEEECCCC
54.1924489116
91UbiquitinationESKHFTSKLVELDDK
HHHHHHHCEEECCCC
54.1922817900
98AcetylationKLVELDDKKTGAEVR
CEEECCCCCCCCEEE
52.4824489116
992-HydroxyisobutyrylationLVELDDKKTGAEVRF
EEECCCCCCCCEEEE
60.22-
99AcetylationLVELDDKKTGAEVRF
EEECCCCCCCCEEEE
60.2224489116
99SuccinylationLVELDDKKTGAEVRF
EEECCCCCCCCEEEE
60.2223954790
114PhosphorylationAGEKHVFSATQLAAM
CCCCCEEEHHHHHHH
29.3521440633
1252-HydroxyisobutyrylationLAAMFIDKVKDTVKQ
HHHHHHHHHHHHHHH
46.50-
125UbiquitinationLAAMFIDKVKDTVKQ
HHHHHHHHHHHHHHH
46.5022106047
1272-HydroxyisobutyrylationAMFIDKVKDTVKQDT
HHHHHHHHHHHHHCC
54.12-
1312-HydroxyisobutyrylationDKVKDTVKQDTKANI
HHHHHHHHHCCCCCC
44.54-
131SuccinylationDKVKDTVKQDTKANI
HHHHHHHHHCCCCCC
44.5423954790
186AcetylationGVSYGIFKTDLPEGE
CCCCEEEECCCCCCC
38.9324489116
1952-HydroxyisobutyrylationDLPEGEEKPRIVAFV
CCCCCCCCCEEEEEE
34.98-
195AcetylationDLPEGEEKPRIVAFV
CCCCCCCCCEEEEEE
34.9824489116
195UbiquitinationDLPEGEEKPRIVAFV
CCCCCCCCCEEEEEE
34.9823749301
222AcetylationAFKKGQLKVLGTACD
EEECCCEEEEEEECC
27.7622865919
226PhosphorylationGQLKVLGTACDKHFG
CCEEEEEEECCHHCC
21.6828152593
230AcetylationVLGTACDKHFGGRDF
EEEEECCHHCCCCCC
40.4924489116
230UbiquitinationVLGTACDKHFGGRDF
EEEEECCHHCCCCCC
40.4923749301
242PhosphorylationRDFDLAITEHFADEF
CCCEEEEHHHHHHHH
20.1417287358
262AcetylationIDIRENPKAYNRILT
CCCCCCHHHHHHHHH
75.0824489116
262SuccinylationIDIRENPKAYNRILT
CCCCCCHHHHHHHHH
75.0823954790
273AcetylationRILTAAEKLKKVLSA
HHHHHHHHHHHHHCC
61.9624489116
273UbiquitinationRILTAAEKLKKVLSA
HHHHHHHHHHHHHCC
61.9623749301
275AcetylationLTAAEKLKKVLSANT
HHHHHHHHHHHCCCC
52.4824489116
311AcetylationEELEELVKPLLERVT
HHHHHHHHHHHHHCC
42.4424489116
3232-HydroxyisobutyrylationRVTEPVTKALAQAKL
HCCHHHHHHHHHHCC
41.45-
323AcetylationRVTEPVTKALAQAKL
HCCHHHHHHHHHHCC
41.4522865919
323UbiquitinationRVTEPVTKALAQAKL
HCCHHHHHHHHHHCC
41.4523749301
351UbiquitinationTTRIPTLKQSISEAF
CCCCCHHHHHHHHHH
44.4724961812
353PhosphorylationRIPTLKQSISEAFGK
CCCHHHHHHHHHHCC
26.8819823750
355PhosphorylationPTLKQSISEAFGKPL
CHHHHHHHHHHCCCC
28.2829136822
360AcetylationSISEAFGKPLSTTLN
HHHHHHCCCCCCCCC
36.0124489116
363PhosphorylationEAFGKPLSTTLNQDE
HHHCCCCCCCCCHHH
28.0721440633
365PhosphorylationFGKPLSTTLNQDEAI
HCCCCCCCCCHHHHH
21.9729136822
384PhosphorylationAFICAIHSPTLRVRP
CEEEECCCCCEEECC
17.2922369663
386PhosphorylationICAIHSPTLRVRPFK
EEECCCCCEEECCCC
30.1522369663
393AcetylationTLRVRPFKFEDIHPY
CEEECCCCCCCCCCC
50.9924489116
393UbiquitinationTLRVRPFKFEDIHPY
CEEECCCCCCCCCCC
50.9924961812
400PhosphorylationKFEDIHPYSVSYSWD
CCCCCCCCEEEEECC
13.9324961812
401PhosphorylationFEDIHPYSVSYSWDK
CCCCCCCEEEEECCC
14.7224961812
403PhosphorylationDIHPYSVSYSWDKQV
CCCCCEEEEECCCCC
13.9124961812
404PhosphorylationIHPYSVSYSWDKQVE
CCCCEEEEECCCCCC
16.1824961812
405PhosphorylationHPYSVSYSWDKQVED
CCCEEEEECCCCCCC
22.6924961812
423PhosphorylationMEVFPAGSSFPSTKL
EEEECCCCCCCCCEE
30.8022369663
424PhosphorylationEVFPAGSSFPSTKLI
EEECCCCCCCCCEEE
40.0123749301
427PhosphorylationPAGSSFPSTKLITLN
CCCCCCCCCEEEEEC
35.8422369663
428PhosphorylationAGSSFPSTKLITLNR
CCCCCCCCEEEEECC
30.0621440633
429AcetylationGSSFPSTKLITLNRT
CCCCCCCEEEEECCC
42.0824489116
429UbiquitinationGSSFPSTKLITLNRT
CCCCCCCEEEEECCC
42.0823749301
529AcetylationKKVTKTVKKDDLTIV
HHHHHCCCHHCEEEE
56.5724489116
529SuccinylationKKVTKTVKKDDLTIV
HHHHHCCCHHCEEEE
56.5723954790
530AcetylationKVTKTVKKDDLTIVA
HHHHCCCHHCEEEEE
52.7324489116
545AcetylationHTFGLDAKKLNELIE
EECCCCHHHHHHHHH
58.4224489116
545SuccinylationHTFGLDAKKLNELIE
EECCCCHHHHHHHHH
58.4223954790
553AcetylationKLNELIEKENEMLAQ
HHHHHHHHHHHHHHH
59.8724489116
562AcetylationNEMLAQDKLVAETED
HHHHHHCHHHHCCCH
32.5524489116
571AcetylationVAETEDRKNTLEEYI
HHCCCHHHHHHHHHH
67.6124489116
571UbiquitinationVAETEDRKNTLEEYI
HHCCCHHHHHHHHHH
67.6124961812
5842-HydroxyisobutyrylationYIYTLRGKLEEEYAP
HHHHHHHHHHHHHCC
46.41-
584AcetylationYIYTLRGKLEEEYAP
HHHHHHHHHHHHHCC
46.4124489116
584UbiquitinationYIYTLRGKLEEEYAP
HHHHHHHHHHHHHCC
46.4123749301
594PhosphorylationEEYAPFASDAEKTKL
HHHCCCCCHHHHHHH
37.4228889911
598AcetylationPFASDAEKTKLQGML
CCCCHHHHHHHHHHH
53.3224489116
599PhosphorylationFASDAEKTKLQGMLN
CCCHHHHHHHHHHHH
28.6122369663
6002-HydroxyisobutyrylationASDAEKTKLQGMLNK
CCHHHHHHHHHHHHH
50.29-
607UbiquitinationKLQGMLNKAEEWLYD
HHHHHHHHHHHHHHH
53.8923749301
6212-HydroxyisobutyrylationDEGFDSIKAKYIAKY
HCCCHHHHHHHHHHH
42.66-
621AcetylationDEGFDSIKAKYIAKY
HCCCHHHHHHHHHHH
42.6624489116
621SuccinylationDEGFDSIKAKYIAKY
HCCCHHHHHHHHHHH
42.6623954790
6232-HydroxyisobutyrylationGFDSIKAKYIAKYEE
CCHHHHHHHHHHHHH
31.99-
623UbiquitinationGFDSIKAKYIAKYEE
CCHHHHHHHHHHHHH
31.9922817900
627AcetylationIKAKYIAKYEELASL
HHHHHHHHHHHHHHC
43.5724489116
627SuccinylationIKAKYIAKYEELASL
HHHHHHHHHHHHHHC
43.5723954790
627UbiquitinationIKAKYIAKYEELASL
HHHHHHHHHHHHHHC
43.5724961812
633PhosphorylationAKYEELASLGNIIRG
HHHHHHHHCHHHHHH
49.8130377154
642PhosphorylationGNIIRGRYLAKEEEK
HHHHHHHHHCCHHHH
17.5222369663
645AcetylationIRGRYLAKEEEKKQA
HHHHHHCCHHHHHHH
64.1624489116
645SuccinylationIRGRYLAKEEEKKQA
HHHHHHCCHHHHHHH
64.1623954790
649AcetylationYLAKEEEKKQAIRSK
HHCCHHHHHHHHHHH
54.1624489116
655PhosphorylationEKKQAIRSKQEASQM
HHHHHHHHHHHHHHH
32.3623749301
656AcetylationKKQAIRSKQEASQMA
HHHHHHHHHHHHHHH
42.1625381059
656UbiquitinationKKQAIRSKQEASQMA
HHHHHHHHHHHHHHH
42.1623749301
660PhosphorylationIRSKQEASQMAAMAE
HHHHHHHHHHHHHHH
21.5325752575
668AcetylationQMAAMAEKLAAQRKA
HHHHHHHHHHHHHHH
33.6124489116
668UbiquitinationQMAAMAEKLAAQRKA
HHHHHHHHHHHHHHH
33.6123749301
683UbiquitinationEAEKKEEKKDTEGDV
HHHHHHHHCCCCCCC
57.9723749301
684UbiquitinationAEKKEEKKDTEGDVD
HHHHHHHCCCCCCCC
73.4923749301
686PhosphorylationKKEEKKDTEGDVDMD
HHHHHCCCCCCCCCC
51.2325521595

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 HSP7F_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSP7F_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 HSP7F_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GBLP_YEASTASC1physical
11805826
CLH_YEASTCHC1physical
11805826
TSA1_YEASTTSA1physical
11805826
FHP_YEASTYHB1physical
11805826
HSP71_YEASTSSA1physical
16221677
HSP72_YEASTSSA2physical
16221677
SSB2_YEASTSSB2physical
16221677
SSB1_YEASTSSB1physical
16221677
SSB2_YEASTSSB2physical
16219770
HSP71_YEASTSSA1physical
16219770
HSP72_YEASTSSA2physical
16219770
SSB1_YEASTSSB1physical
16219770
HSF_YEASTHSF1genetic
10480867
STI1_YEASTSTI1genetic
10480867
HSP79_YEASTSSE2genetic
15879503
IRA1_YEASTIRA1genetic
15879503
IRA2_YEASTIRA2genetic
15879503
KAPR_YEASTBCY1genetic
15879503
PDE2_YEASTPDE2genetic
15879503
MPG1_YEASTPSA1physical
16429126
TSA1_YEASTTSA1physical
16429126
RSSA2_YEASTRPS0Bphysical
16429126
CLH_YEASTCHC1physical
16429126
FHP_YEASTYHB1physical
16429126
HSP71_YEASTSSA1physical
16688211
SSB1_YEASTSSB1physical
16688211
HSP79_YEASTSSE2genetic
16688211
HSP74_HUMANHSPA4physical
17154545
HSP7F_YEASTSSE1physical
17923091
HSP79_YEASTSSE2genetic
17947402
FES1_YEASTFES1genetic
17947402
APOB_HUMANAPOBphysical
17823116
HSP71_YEASTSSA1physical
18218635
HSP79_YEASTSSE2genetic
18478233
FES1_YEASTFES1genetic
18478233
MBP1_YEASTMBP1genetic
18478233
HSP71_YEASTSSA1physical
18555782
HSP7C_BOVINHSPA8physical
18550409
CDC27_YEASTCDC27physical
19536198
REB1_YEASTREB1physical
19536198
BUD3_YEASTBUD3physical
19536198
HCM1_YEASTHCM1physical
19536198
DBP10_YEASTDBP10physical
19536198
USO1_YEASTUSO1physical
19536198
UAP1_YEASTQRI1physical
19536198
PST2_YEASTPST2physical
19536198
RSC3_YEASTRSC3physical
19536198
TFC6_YEASTTFC6physical
19536198
UBA2_YEASTUBA2physical
19536198
NOP3_YEASTNPL3physical
19536198
RPN3_YEASTRPN3physical
19536198
CDC20_YEASTCDC20physical
19536198
ARO8_YEASTARO8physical
19536198
MTG2_YEASTMTG2physical
19536198
GPP1_YEASTGPP1physical
19536198
AYR1_YEASTAYR1physical
19536198
EAF6_YEASTEAF6physical
19536198
MET5_YEASTMET5physical
19536198
DEF1_YEASTDEF1physical
19536198
T2EB_YEASTTFA2physical
19536198
ACS2_YEASTACS2physical
19536198
IMB1_YEASTKAP95physical
19536198
SOV1_YEASTSOV1physical
19536198
NAM7_YEASTNAM7physical
19536198
AIP1_YEASTAIP1physical
19536198
PO152_YEASTPOM152physical
19536198
SYKM_YEASTMSK1physical
19536198
DPOA_YEASTPOL1physical
19536198
RAP1_YEASTRAP1physical
19536198
EMW1_YEASTEMW1physical
19536198
BUD17_YEASTBUD17physical
19536198
GLRX5_YEASTGRX5physical
19536198
GIP3_YEASTGIP3physical
19536198
WDR6_YEASTRTT10physical
19536198
FAS2_YEASTFAS2physical
19536198
THP3_YEASTTHP3physical
19536198
ASR1_YEASTASR1physical
19536198
RPN7_YEASTRPN7physical
19536198
TAZ1_YEASTTAZ1physical
19536198
NOC4_YEASTNOC4physical
19536198
ORC4_YEASTORC4physical
19536198
BSP1_YEASTBSP1physical
19536198
SKI3_YEASTSKI3physical
19536198
HSP82_YEASTHSP82physical
19536198
HSP71_YEASTSSA1physical
19536198
HSP72_YEASTSSA2physical
19536198
HSP74_YEASTSSA4physical
19536198
SSB1_YEASTSSB1physical
19536198
SSB2_YEASTSSB2physical
19536198
HSP42_YEASTHSP42physical
19536198
MAS5_YEASTYDJ1physical
19536198
HSP79_YEASTSSE2physical
19536198
SIS1_YEASTSIS1physical
19536198
HSP71_YEASTSSA1physical
18948593
FES1_YEASTFES1genetic
18335038
SNL1_YEASTSNL1genetic
18335038
SWI4_YEASTSWI4genetic
18478233
SWI6_YEASTSWI6genetic
18478233
CDC37_YEASTCDC37genetic
14742721
SCH9_YEASTSCH9genetic
15879503
YPK9_YEASTYPK9genetic
22457822
SSB1_YEASTSSB1physical
22635919
HSP71_YEASTSSA1physical
22635919
HSP72_YEASTSSA2physical
22635919
IVY1_YEASTIVY1physical
22875988
FES1_YEASTFES1genetic
23797105
HSP79_YEASTSSE2genetic
23797105
FES1_YEASTFES1genetic
24671421
HSP71_YEASTSSA1physical
24671421
HSP72_YEASTSSA2physical
24671421
SSB1_YEASTSSB1physical
24671421
SSB2_YEASTSSB2physical
24671421
SNF5_YEASTSNF5genetic
27708008
MDM10_YEASTMDM10genetic
27708008
LTE1_YEASTLTE1genetic
27708008
HSP79_YEASTSSE2genetic
27708008
NDH2_YEASTNDE2genetic
27708008
BLM10_YEASTBLM10genetic
27708008
ATG1_YEASTATG1genetic
27708008
PFD3_YEASTPAC10genetic
27708008
MAD2_YEASTMAD2genetic
27708008
ENV10_YEASTENV10genetic
27708008
PFD6_YEASTYKE2genetic
27708008
SAM37_YEASTSAM37genetic
27708008
PFD4_YEASTGIM3genetic
27708008
PMP1_YEASTPMP1physical
26404137
HSP71_YEASTSSA1physical
28539411
SSB1_YEASTSSB1physical
28539411
UTP21_YEASTUTP21genetic
24647762
MDFI_HUMANMDFIphysical
27107014
FES1_YEASTFES1genetic
29507114

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSP7F_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins.";
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.;
Electrophoresis 18:1347-1360(1997).
Cited for: ACETYLATION AT SER-2.
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-36 AND SER-660, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND MASSSPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, AND MASSSPECTROMETRY.

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