SPC72_YEAST - dbPTM
SPC72_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPC72_YEAST
UniProt AC P39723
Protein Name Spindle pole component SPC72
Gene Name SPC72
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 622
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body . localised at the outer plaque and the bridge of the spindle pole body.
Protein Description Spindle pole body component that acts as the gamma-tubulin complex-binding protein of the SPB outer plaque. Anchors cytoplasmic microtubules at the at the half bridge of the spindle pole body (SPB) and accordingly functions in nuclear position and spindle orientation, including anaphase spindle migration into the bud. Recruits KIN4 kinase to both SPBs when cytoplasmic microtubules are defective. Links cytoplasmic microtubules with spindle orientation checkpoint (SPOC) components and, therefore, could function as part of the sensors of spindle orientation defects. Is strictly required for mating and karyogamy..
Protein Sequence MVRRWIPSGRHLRNNDNTGDDDDSEFTNSMDSGMSIPSLRDSMTTRSSHNDPIKPALMNDSNKVKNLEKELTNAKIKIQVLYEYIRRIPNKDGNAPSLGNDTDFRNSIIEGLNLEINKLKQDLKAKEVEYQDTLQFVQENLENSESIVNTINHLLSFILTHFNEQDENAHLLDKEERETLEETLELSSDYVLEKMDTLSKFIIQFLQDFLHSKSRAESKQDKEEFLSLAQSSPAGSQLESRDSPSSKEENTDGGYQNDEIHDSNNHIDTENVMANSTSLPISAVESRFEKTLDTQLEIVIENLHKEYDQFINSIRLKFEKSQKLEKIIASKLNEQSHLLDSLELEENSSSVIEKQDHLISQLKEKIESQSVLINNLEKLKEDIIKMKQNEKVLTKELETQTKINKLKENNWDSYINDLEKQINDLQIDKSEEFHVIQNQLDKLDLENYQLKNQLNTLDNQKLILSQYESNFIKFNQNLLLHLDSIFNILQKILQESSIAQFDRKMKSIKSVPNALKNLNLIQPKLESLYTFIETALESIINSYISSLISMETPEQPHQQGNELTATPNKELTLRIEELQRRWISERERRKLDANASEARIKALEQENESLRSKLFNLSINNP
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
18PhosphorylationHLRNNDNTGDDDDSE
CCCCCCCCCCCCCCH		44.8727017623
27PhosphorylationDDDDSEFTNSMDSGM
CCCCCHHHHHHCCCC		23.4921700874
29PhosphorylationDDSEFTNSMDSGMSI
CCCHHHHHHCCCCCC		22.4021700874
35PhosphorylationNSMDSGMSIPSLRDS
HHHCCCCCCCHHHHH		34.5727017623
47PhosphorylationRDSMTTRSSHNDPIK
HHHCCCCCCCCCCCC		33.5819779198
48PhosphorylationDSMTTRSSHNDPIKP
HHCCCCCCCCCCCCH		24.0228889911
97PhosphorylationNKDGNAPSLGNDTDF
CCCCCCCCCCCCHHH		46.6421700874
107PhosphorylationNDTDFRNSIIEGLNL
CCHHHHHHHHHHHHH		22.2321700874
227PhosphorylationQDKEEFLSLAQSSPA
CCHHHHHHHHHCCCC		27.2921700874
231PhosphorylationEFLSLAQSSPAGSQL
HHHHHHHCCCCCCCC		32.4521700874
232PhosphorylationFLSLAQSSPAGSQLE
HHHHHHCCCCCCCCC		13.4923749301
236PhosphorylationAQSSPAGSQLESRDS
HHCCCCCCCCCCCCC		33.4328132839
240PhosphorylationPAGSQLESRDSPSSK
CCCCCCCCCCCCCCC		50.4027017623
245PhosphorylationLESRDSPSSKEENTD
CCCCCCCCCCCCCCC		58.9827017623
255PhosphorylationEENTDGGYQNDEIHD
CCCCCCCCCCCCCCC		15.0719779198
263PhosphorylationQNDEIHDSNNHIDTE
CCCCCCCCCCCCCHH		25.9321700874
269PhosphorylationDSNNHIDTENVMANS
CCCCCCCHHHCCCCC		28.9319779198
291PhosphorylationVESRFEKTLDTQLEI
HHHHHHHHHHHHHHH		23.7521551504
294PhosphorylationRFEKTLDTQLEIVIE
HHHHHHHHHHHHHHH		37.8621551504
348PhosphorylationSLELEENSSSVIEKQ
HHCCCCCCCHHHHHH		27.5421700874
349PhosphorylationLELEENSSSVIEKQD
HCCCCCCCHHHHHHH		39.9621700874
350PhosphorylationELEENSSSVIEKQDH
CCCCCCCHHHHHHHH		27.2521700874
401PhosphorylationTKELETQTKINKLKE
HHHHHHHHHHHHHHH		41.1121700874
413PhosphorylationLKENNWDSYINDLEK
HHHCCHHHHHHHHHH		21.3721700874
430PhosphorylationNDLQIDKSEEFHVIQ
CCCCCCCHHHHHHHH		38.3121440633
510PhosphorylationRKMKSIKSVPNALKN
HHHHHCCCHHHHHHC		40.9321700874
552PhosphorylationSSLISMETPEQPHQQ
HHHHCCCCCCCCCCC		24.3921700874
564PhosphorylationHQQGNELTATPNKEL
CCCCCCCCCCCCCCH		23.4721700874
566PhosphorylationQGNELTATPNKELTL
CCCCCCCCCCCCHHH		23.3521700874
572PhosphorylationATPNKELTLRIEELQ
CCCCCCHHHHHHHHH		18.3221700874
590AcetylationISERERRKLDANASE
HCHHHHHHHCCCHHH		57.8723572591
618PhosphorylationRSKLFNLSINNP---
HHHHHHCCCCCC---		25.1128152593
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 SPC72_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPC72_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 SPC72_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPC97_YEASTSPC97physical
12970190
SPC98_YEASTSPC98physical
12970190
STU2_YEASTSTU2physical
12970190
TBG_YEASTTUB4physical
12970190
SPC97_YEASTSPC97physical
9670012
SPC98_YEASTSPC98physical
9670012
SPC72_YEASTSPC72physical
9606209
SPC97_YEASTSPC97genetic
9670012
SPC98_YEASTSPC98genetic
9670012
TBG_YEASTTUB4genetic
9670012
CNM67_YEASTCNM67genetic
11950945
DYHC_YEASTDYN1genetic
11950945
KAR3_YEASTKAR3genetic
11950945
KAR9_YEASTKAR9genetic
11950945
KIP2_YEASTKIP2genetic
11950945
KIP3_YEASTKIP3genetic
11950945
NUM1_YEASTNUM1genetic
11950945
TBG_YEASTTUB4genetic
12970190
BFA1_YEASTBFA1genetic
10949022
BUB2_YEASTBUB2genetic
10949022
KIN4_YEASTKIN4physical
17967947
SPC97_YEASTSPC97physical
18850724
SPC72_YEASTSPC72physical
18850724
XPO1_YEASTCRM1physical
18573877
CDC5_YEASTCDC5physical
15509790
SPC72_YEASTSPC72physical
22875988
SGM1_YEASTSGM1physical
22875988
END3_YEASTEND3physical
22875988
VPS20_YEASTVPS20physical
22875988
IMH1_YEASTIMH1physical
22875988
CASP_YEASTCOY1physical
22875988
HPH2_YEASTFRT2physical
22875988
RTG3_YEASTRTG3physical
22875988
KPC1_YEASTPKC1physical
22875988
ATG14_YEASTATG14physical
22875988
ARE1_YEASTARE1physical
22875988
TUP1_YEASTTUP1physical
22875988
IVY1_YEASTIVY1physical
22875988
YAP6_YEASTYAP6physical
22875988
HDA2_YEASTHDA2physical
22875988
SHE9_YEASTSHE9physical
22875988
SPC25_YEASTSPC25physical
22875988
TSC11_YEASTTSC11physical
22875988
MED3_YEASTPGD1physical
22875988
ATG1_YEASTATG1physical
22875988
SEC9_YEASTSEC9physical
22875988
KEL2_YEASTKEL2physical
22875988
AP18B_YEASTYAP1802physical
22875988
ETP1_YEASTETP1physical
22875988
LAM4_YEASTYHR080Cphysical
22875988
LNP_YEASTLNP1physical
22875988
SKN7_YEASTSKN7physical
22875988
NOT3_YEASTNOT3physical
22875988
SNX4_YEASTSNX4physical
22875988
YJE9_YEASTYJL049Wphysical
22875988
SET2_YEASTSET2physical
22875988
SWE1_YEASTSWE1physical
22875988
RE107_YEASTREC107physical
22875988
LHS1_YEASTLHS1physical
22875988
SMY1_YEASTSMY1physical
22875988
DID2_YEASTDID2physical
22875988
SNF7_YEASTSNF7physical
22875988
YL031_YEASTYLR031Wphysical
22875988
CDC3_YEASTCDC3physical
22875988
AP1_YEASTYAP1physical
22875988
RNA1_YEASTRNA1physical
22875988
NUF2_YEASTNUF2physical
22875988
VPS5_YEASTVPS5physical
22875988
NIP80_YEASTNIP100physical
22875988
SSO1_YEASTSSO1physical
22875988
NCA2_YEASTNCA2physical
22875988
YAP8_YEASTARR1physical
22875988
SPR3_YEASTSPR3physical
22875988
NTR2_YEASTNTR2physical
22875988
RRP17_YEASTRRP17physical
22875988
HSP74_YEASTSSA4physical
22875988
CCM1_YEASTCCM1physical
22875988
KEL1_YEASTKEL1physical
22875988
OM45_YEASTOM45physical
22875988
MPS3_YEASTMPS3physical
22875988
VPS53_YEASTVPS53physical
22875988
YJ41B_YEASTYJL113Wphysical
22875988
ENT2_YEASTENT2physical
22875988
RCF1_YEASTRCF1physical
22875988
NDH1_YEASTNDE1physical
22875988
SGO1_YEASTSGO1physical
22875988
RGA1_YEASTRGA1physical
22875988
SCD5_YEASTSCD5physical
22875988
SKS1_YEASTSKS1physical
22875988
LGE1_YEASTLGE1physical
22875988
ATG11_YEASTATG11physical
22875988
EAF7_YEASTEAF7physical
23572591
TBG_YEASTTUB4physical
23810537
KAR9_YEASTKAR9physical
23810537
BFA1_YEASTBFA1physical
23810537
BUB2_YEASTBUB2genetic
23810537
BFA1_YEASTBFA1physical
27159239
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPC72_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-232, AND MASSSPECTROMETRY.

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