SDS23_YEAST - dbPTM
SDS23_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SDS23_YEAST
UniProt AC P53172
Protein Name Protein SDS23
Gene Name SDS23
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 527
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Involved in DNA replication and cell separation during budding..
Protein Sequence MPQNTRHTSIVEMLSTPPQLPNSTDLNSLSEQTDKNTEANKSDTESLHKSISKSSSSSSLSTLDNTEYSNNNGNSLSTLNSQNLLSVHRQEWQHTPLSNLVEQNKLIFIRGSISVEEAFNTLVKHQLTSLPVENFPGDMNCLTFDYNDLNAYLLLVLNRIKVSNDKITSDCQNGKSVPVGEIVKLTPKNPFYKLPETENLSTVIGILGSGVHRVAITNVEMTQIKGILSQRRLIKYLWENARSFPNLKPLLDSSLEELNIGVLNAARDKPTFKQSRVISIQGDEHLIMALHKMYVERISSIAVVDPQGNLIGNISVTDVKHVTRTSQYPLLHNTCRHFVSVILNLRGLETGKDSFPIFHVYPTSSLARTFAKLVATKSHRLWIVQPNDNQPTASSEKSSSPSPSTPPVTTLPSLASSYHSNTQSSRMANSPVLKSSDTSNNKINVNINLSGPSPSQPQSPSATMPPPQSPSNCPASPTPAHFEKEYRTGKLIGVVSLTDILSVLARKQTHHKEIDPQMARKQRGHIG
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
5Phosphorylation---MPQNTRHTSIVE
---CCCCCCCCCHHH
20.6924961812
8PhosphorylationMPQNTRHTSIVEMLS
CCCCCCCCCHHHHHC
19.5022369663
9PhosphorylationPQNTRHTSIVEMLST
CCCCCCCCHHHHHCC
20.6422369663
15PhosphorylationTSIVEMLSTPPQLPN
CCHHHHHCCCCCCCC
37.2422369663
16PhosphorylationSIVEMLSTPPQLPNS
CHHHHHCCCCCCCCC
34.7222369663
23PhosphorylationTPPQLPNSTDLNSLS
CCCCCCCCCCHHHHC
22.7419779198
24PhosphorylationPPQLPNSTDLNSLSE
CCCCCCCCCHHHHCH
51.6619779198
28PhosphorylationPNSTDLNSLSEQTDK
CCCCCHHHHCHHCCC
40.3422369663
30PhosphorylationSTDLNSLSEQTDKNT
CCCHHHHCHHCCCCC
27.7222369663
33PhosphorylationLNSLSEQTDKNTEAN
HHHHCHHCCCCCCCC
44.9122369663
37PhosphorylationSEQTDKNTEANKSDT
CHHCCCCCCCCHHHH
42.0622890988
42PhosphorylationKNTEANKSDTESLHK
CCCCCCHHHHHHHHH
49.9622369663
44PhosphorylationTEANKSDTESLHKSI
CCCCHHHHHHHHHHH
34.2722890988
46PhosphorylationANKSDTESLHKSISK
CCHHHHHHHHHHHHC
37.5522369663
54PhosphorylationLHKSISKSSSSSSLS
HHHHHHCCCCCCCCC
28.7623749301
55PhosphorylationHKSISKSSSSSSLST
HHHHHCCCCCCCCCC
37.6719779198
56PhosphorylationKSISKSSSSSSLSTL
HHHHCCCCCCCCCCC
41.1328889911
57PhosphorylationSISKSSSSSSLSTLD
HHHCCCCCCCCCCCC
26.3723749301
58PhosphorylationISKSSSSSSLSTLDN
HHCCCCCCCCCCCCC
36.9319779198
59PhosphorylationSKSSSSSSLSTLDNT
HCCCCCCCCCCCCCC
28.4319779198
61PhosphorylationSSSSSSLSTLDNTEY
CCCCCCCCCCCCCCC
28.9519779198
62PhosphorylationSSSSSLSTLDNTEYS
CCCCCCCCCCCCCCC
43.3419779198
66PhosphorylationSLSTLDNTEYSNNNG
CCCCCCCCCCCCCCC
35.6523749301
68PhosphorylationSTLDNTEYSNNNGNS
CCCCCCCCCCCCCCC
18.0523749301
166UbiquitinationRIKVSNDKITSDCQN
CCEECCCCCCCCCCC
52.7323749301
176PhosphorylationSDCQNGKSVPVGEIV
CCCCCCCCCCCHHEE
32.8121126336
235AcetylationLSQRRLIKYLWENAR
HHHHHHHHHHHHHHH
38.5924489116
352AcetylationLRGLETGKDSFPIFH
HCCCCCCCCCCCEEE
58.5824489116
372UbiquitinationSLARTFAKLVATKSH
HHHHHHHHHHHCCCC
39.0223749301
372AcetylationSLARTFAKLVATKSH
HHHHHHHHHHHCCCC
39.0224489116
392PhosphorylationQPNDNQPTASSEKSS
CCCCCCCCCCCCCCC
29.4323749301
398PhosphorylationPTASSEKSSSPSPST
CCCCCCCCCCCCCCC
31.8122369663
399PhosphorylationTASSEKSSSPSPSTP
CCCCCCCCCCCCCCC
58.2920377248
400PhosphorylationASSEKSSSPSPSTPP
CCCCCCCCCCCCCCC
36.1722369663
402PhosphorylationSEKSSSPSPSTPPVT
CCCCCCCCCCCCCCC
33.1720377248
404PhosphorylationKSSSPSPSTPPVTTL
CCCCCCCCCCCCCCC
58.8620377248
405PhosphorylationSSSPSPSTPPVTTLP
CCCCCCCCCCCCCCH
34.6922369663
409PhosphorylationSPSTPPVTTLPSLAS
CCCCCCCCCCHHHHH
28.5222369663
410PhosphorylationPSTPPVTTLPSLASS
CCCCCCCCCHHHHHH
36.5822369663
413PhosphorylationPPVTTLPSLASSYHS
CCCCCCHHHHHHHCC
39.4122369663
416PhosphorylationTTLPSLASSYHSNTQ
CCCHHHHHHHCCCCC
36.4022369663
417PhosphorylationTLPSLASSYHSNTQS
CCHHHHHHHCCCCCC
22.6620377248
418PhosphorylationLPSLASSYHSNTQSS
CHHHHHHHCCCCCCC
13.5320377248
420PhosphorylationSLASSYHSNTQSSRM
HHHHHHCCCCCCCCC
33.0822369663
422PhosphorylationASSYHSNTQSSRMAN
HHHHCCCCCCCCCCC
32.6120377248
424PhosphorylationSYHSNTQSSRMANSP
HHCCCCCCCCCCCCC
20.2020377248
425PhosphorylationYHSNTQSSRMANSPV
HCCCCCCCCCCCCCC
19.0920377248
430PhosphorylationQSSRMANSPVLKSSD
CCCCCCCCCCCCCCC
13.5722369663
434AcetylationMANSPVLKSSDTSNN
CCCCCCCCCCCCCCC
48.4225381059
438PhosphorylationPVLKSSDTSNNKINV
CCCCCCCCCCCEEEE
34.9919779198
439PhosphorylationVLKSSDTSNNKINVN
CCCCCCCCCCEEEEE
43.3119779198
450PhosphorylationINVNINLSGPSPSQP
EEEEEECCCCCCCCC
44.1420377248
453PhosphorylationNINLSGPSPSQPQSP
EEECCCCCCCCCCCC
40.4821440633
455PhosphorylationNLSGPSPSQPQSPSA
ECCCCCCCCCCCCCC
59.8521551504
459PhosphorylationPSPSQPQSPSATMPP
CCCCCCCCCCCCCCC
27.7520377248
461PhosphorylationPSQPQSPSATMPPPQ
CCCCCCCCCCCCCCC
41.4320377248
463PhosphorylationQPQSPSATMPPPQSP
CCCCCCCCCCCCCCC
34.2521440633
469PhosphorylationATMPPPQSPSNCPAS
CCCCCCCCCCCCCCC
35.7520377248
471PhosphorylationMPPPQSPSNCPASPT
CCCCCCCCCCCCCCC
57.2019779198
476PhosphorylationSPSNCPASPTPAHFE
CCCCCCCCCCCCCHH
17.9120377248
478PhosphorylationSNCPASPTPAHFEKE
CCCCCCCCCCCHHHH
30.5220377248

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 SDS23_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SDS23_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 SDS23_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SDS24_YEASTSDS24genetic
16041152
QDR2_YEASTQDR2physical
18467557
HXT1_YEASTHXT1physical
18467557
PDR12_YEASTPDR12physical
18467557
TCB3_YEASTTCB3physical
18467557
TPO3_YEASTTPO3physical
18467557
DIP5_YEASTDIP5physical
18467557
DUR3_YEASTDUR3physical
18467557
SFK1_YEASTSFK1physical
18467557
MID2_YEASTMID2physical
18467557
GCN1_YEASTGCN1physical
18467557
PDR5_YEASTPDR5physical
18467557
HNM1_YEASTHNM1physical
18467557
YL413_YEASTINA1physical
18467557
MUP1_YEASTMUP1physical
18467557
SDS24_YEASTSDS24genetic
21360731
PP11_YEASTSIT4genetic
21360731
GPI16_YEASTGPI16genetic
27708008
LPP1_YEASTLPP1genetic
27708008
TBP7_YEASTYTA7genetic
27708008
INM1_YEASTINM1genetic
27708008
RL6B_YEASTRPL6Bgenetic
27708008
RL9B_YEASTRPL9Bgenetic
27708008
NOP12_YEASTNOP12genetic
27708008
MED8_YEASTMED8genetic
27708008
DPOD_YEASTPOL3genetic
27708008
TIM22_YEASTTIM22genetic
27708008
TAF12_YEASTTAF12genetic
27708008
CDC37_YEASTCDC37genetic
27708008
PCF11_YEASTPCF11genetic
27708008
SEC20_YEASTSEC20genetic
27708008
CDC4_YEASTCDC4genetic
27708008
YPT1_YEASTYPT1genetic
27708008
KTHY_YEASTCDC8genetic
27708008
RSC4_YEASTRSC4genetic
27708008
PRP24_YEASTPRP24genetic
27708008
LST8_YEASTLST8genetic
27708008
SEC12_YEASTSEC12genetic
27708008
NAB3_YEASTNAB3genetic
27708008
HPH2_YEASTFRT2genetic
27708008
AIM4_YEASTAIM4genetic
27708008
INO2_YEASTINO2genetic
27708008
WDR59_YEASTMTC5genetic
27708008
LSM6_YEASTLSM6genetic
27708008
RV167_YEASTRVS167genetic
27708008
URC2_YEASTURC2genetic
27708008
RGI1_YEASTRGI1genetic
27708008
GYP8_YEASTGYP8genetic
27708008
HXKA_YEASTHXK1genetic
27708008
GOSR1_YEASTGOS1genetic
27708008
RL8A_YEASTRPL8Agenetic
27708008
FLX1_YEASTFLX1genetic
27708008
VPS53_YEASTVPS53genetic
27708008
NCA3_YEASTNCA3genetic
27708008
NCE1_YEASTNCE101genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
YKH7_YEASTYKL077Wgenetic
27708008
CWP2_YEASTCWP2genetic
27708008
CTK1_YEASTCTK1genetic
27708008
PRY2_YEASTPRY2genetic
27708008
DAL80_YEASTDAL80genetic
27708008
UBP11_YEASTUBP11genetic
27708008
RM39_YEASTMRPL39genetic
27708008
PFKA2_YEASTPFK2genetic
27708008
MKS1_YEASTMKS1genetic
27708008
HMI1_YEASTHMI1genetic
27708008
HPF1_YEASTHPF1genetic
27708008
FYV12_YEASTFYV12genetic
27708008
LGE1_YEASTLGE1genetic
27708008
QCR2_YEASTQCR2genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SDS23_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-42; SER-400 AND SER-430,AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399 AND SER-400, ANDMASS SPECTROMETRY.
"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 SER-42 AND SER-46, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430, 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-430, AND MASSSPECTROMETRY.

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