SPC97_YEAST - dbPTM
SPC97_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPC97_YEAST
UniProt AC P38863
Protein Name Spindle pole body component SPC97
Gene Name SPC97
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 823
Subcellular Localization Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.
Protein Description Involved in microtubule organization by the microtubule organizing center, the spindle pole body (SPB). Probably part of the microtubule attachment site at the SPB..
Protein Sequence MEIKEVDDRAELLRYTNNIPLLGKLVNHQPLWSTNPKLKSFSLEKISAPDQRRVQEALVVKDLLNVLIGLEGTYIRYFNDYEPSDPETPIEFKIAKKMDPSFKTFSRRIVRYGKQYMILTRAYEKWSDTSFGMVLQRFAYEIRRFLEDVYLKTLVERLERDFNKVPNFSIRELEQIINETEVNKQMELLYNIYEEIFREIEERRTNQSSQEDFNNFMDSMKNESSLHLRLMVAFDTTVYPVPKGGAILKIFQQKILENLGDRSSVMFLKKLLNNISQDYCTMLYEWLTQGILNDPYQEFMTYDDLEGKTDNIFDTRDRAWDTQYFIRKDVLLRDCDSEEDKNLLFKMLRTGILLKVVRASLQIPTIPSNSSDITIQEINDFADLMEGSNLELYVDKCYSRANEIFLKLFFQGYDLINVLKHLQQIFLGYQSGHNVLKFLTKNMGELTKHYRNDNNANYDKLLQNFELERQSENPNNLMRQLLMIQFDTETLPQVLSHYLQIYPEVPENNSANDDSDPLMHANNFKNMNAILFDELSKERTGAYHGSNLELYTPKSAIYHLKFDINIPYPLNIIISRTCMIKYQIILRYQLVLQYHSRLLDETWMDLNKTPSWKYRGYSHTVKRRIVRATRVLHAKMNHFIKTIMEYFNQNVIDKEVYSLEKCYRNPTLAVAIQNELEGGLTNIMTNRCLSDLIPLQLQIFDIVYKFCKFIKSMRAKLCQLDPVLYEKHKSGMMKTLNEGYRTNNGGQEDVGYQEDAALELIQKLIEYISNASSIFRKCLINFTQELSTEKFDFYDSSSVDAAGIERVLYSIVPPRSASASSQR
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
47PhosphorylationSFSLEKISAPDQRRV
CCCCCCCCCCCHHHH		44.8328889911
205PhosphorylationREIEERRTNQSSQED
HHHHHHHCCCCCHHH		43.7830377154
208PhosphorylationEERRTNQSSQEDFNN
HHHHCCCCCHHHHHH		35.7428889911
209PhosphorylationERRTNQSSQEDFNNF
HHHCCCCCHHHHHHH		28.0225752575
219PhosphorylationDFNNFMDSMKNESSL
HHHHHHHHHCCCCCH		21.6223749301
224PhosphorylationMDSMKNESSLHLRLM
HHHHCCCCCHHHHEE		47.8230377154
236PhosphorylationRLMVAFDTTVYPVPK
HEEEEECCEEEECCC		16.2328889911
237PhosphorylationLMVAFDTTVYPVPKG
EEEEECCEEEECCCC		21.6428889911
239PhosphorylationVAFDTTVYPVPKGGA
EEECCEEEECCCCCH		9.0925315811
429PhosphorylationLQQIFLGYQSGHNVL
HHHHHHHCCCHHHHH		11.1421700874
510PhosphorylationPEVPENNSANDDSDP
CCCCCCCCCCCCCCC		39.7821700874
540PhosphorylationDELSKERTGAYHGSN
HHHCCCCCCCCCCCC		27.5321700874
546PhosphorylationRTGAYHGSNLELYTP
CCCCCCCCCEEEECC		25.5730377154
552PhosphorylationGSNLELYTPKSAIYH
CCCEEEECCCCHHEE		36.5421700874
554AcetylationNLELYTPKSAIYHLK
CEEEECCCCHHEEEE		44.7324489116
602PhosphorylationHSRLLDETWMDLNKT
HHHHHHCCCCCCCCC		26.2524930733
740PhosphorylationMKTLNEGYRTNNGGQ
CCCCCCCCCCCCCCC		14.2128889911
818PhosphorylationIVPPRSASASSQR--
ECCCCCCCCCCCC--		29.9027214570
821PhosphorylationPRSASASSQR-----
CCCCCCCCCC-----		29.6827214570
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 SPC97_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPC97_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 SPC97_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPC72_YEASTSPC72physical
12970190
SPC98_YEASTSPC98physical
12970190
STU2_YEASTSTU2physical
12970190
TBG_YEASTTUB4physical
12970190
SPC98_YEASTSPC98physical
9130700
SPC98_YEASTSPC98physical
9670012
SPC98_YEASTSPC98physical
9384578
TBG_YEASTTUB4physical
9130700
TBG_YEASTTUB4physical
9670012
TBG_YEASTTUB4physical
9384578
SPC98_YEASTSPC98physical
11950928
TBG_YEASTTUB4physical
11950928
SPC98_YEASTSPC98physical
9693376
TBG_YEASTTUB4physical
9693376
TBG_YEASTTUB4physical
10428957
TBG_YEASTTUB4physical
9529377
SPC72_YEASTSPC72physical
10428957
SPC98_YEASTSPC98physical
10428957
SPC98_YEASTSPC98physical
9529377
SPC98_YEASTSPC98genetic
9130700
TBG_YEASTTUB4genetic
9130700
SP110_YEASTSPC110genetic
11278681
SPC72_YEASTSPC72physical
16554755
TBG_YEASTTUB4physical
16554755
SPC98_YEASTSPC98physical
16554755
SPC72_YEASTSPC72physical
16429126
SPC98_YEASTSPC98physical
16429126
TBG_YEASTTUB4physical
16429126
DAL80_YEASTDAL80physical
17634282
TBG_YEASTTUB4physical
17634282
SPC98_YEASTSPC98physical
17634282
TBG_YEASTTUB4physical
17978090
SPC98_YEASTSPC98physical
17978090
SP110_YEASTSPC110physical
17978090
SP110_YEASTSPC110genetic
9693376
SPC98_YEASTSPC98physical
19723581
TBG_YEASTTUB4physical
21573187
SPC98_YEASTSPC98physical
21573187
SPC72_YEASTSPC72physical
21573187
SP110_YEASTSPC110physical
21573187
SPC98_YEASTSPC98physical
24161932
TBG_YEASTTUB4physical
24161932
TBG_YEASTTUB4physical
25897084
SPC98_YEASTSPC98physical
25897084
SP110_YEASTSPC110physical
25897084
SPC72_YEASTSPC72physical
25897084
CALM_YEASTCMD1physical
25897084
NUD1_YEASTNUD1physical
25897084
SPC42_YEASTSPC42physical
25897084
SPC29_YEASTSPC29physical
25897084
CNM67_YEASTCNM67physical
25897084
KAR1_YEASTKAR1physical
25897084
SFI1_YEASTSFI1physical
25897084
CDC31_YEASTCDC31physical
25897084
MPS3_YEASTMPS3physical
25897084
NBP1_YEASTNBP1physical
25897084
BBP1_YEASTBBP1physical
25897084
MPS2_YEASTMPS2physical
25897084
NDC1_YEASTNDC1physical
25897084
NDJ1_YEASTNDJ1physical
25897084
DYHC_YEASTDYN1genetic
25971801
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPC97_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-208 AND SER-209, ANDMASS SPECTROMETRY.

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