RTC1_YEAST - dbPTM
RTC1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RTC1_YEAST
UniProt AC Q08281
Protein Name Restriction of telomere capping protein 1
Gene Name RTC1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1341
Subcellular Localization Vacuole membrane
Peripheral membrane protein .
Protein Description Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis. May be involved in a process influencing telomere capping..
Protein Sequence MSLSPHVENASIPKGSTPIPKNRNVSSIGKGEFLGSSSSNNSSFRMNHYSNSGQPSVLDSIRRPNLTPTFSYSNGVYMPESHRTSSFNDSYLPYDKNPYAKTTGSMSNKSNMKIKTKKNAINTNTRKSSGLIYTTKVDKELSSIDKVNDPNINGLVCAGKTHLGLYKFSPSDRSIKCVHDFITPNSNTSTRGTTSLLPKLSKRTRQNKFSTIADVKTGFNNYKNCIAVCNNSTAISIYDLNKSSSIDNPLITSLCEHTRSINSFDFNMVESNLIISGGQDSCVKIWDLRSNKSKSSNRSDISINTASDSIRDVKWMPGYNFASKNDQGSSTYGNLKSGYKFASIHDSGYLLKFDLRQPAQYEKKLNAHTGPGLCLNWHPNQEYIATGGRDGKCCLWFVGDNANAAENTVLNYGNSPSLHAPNTSLNNSGSLAFPKLTINTGYPVTKLKFKPAYSSNIYNSLLGISSMGDEAEVRIYSLARKYIPKHVLLSETPSLGLVWWDENLIFNIDKGTRINGWDINKEPTVLENLSKNTTTWRDLDGNGLLSVDQEIGSYEVVEPELQPTSSTTCKKHPGTIKNPKNGNPENQGIIGGIKKGFSHTGLTSFTPERPPTLKAGPTFSTKSLTLASGASSFNSSSASLTSLTPQTENREEIAIEPPCIITLDIPQIFNNIRLTKIAHSRKKNVISESSSMKNSPVEKFKYLARQLKFSYIREHNVSDSADTAYKNDIENIDVVKNATETHGDNTTTTNNNDDGDDDDDDDDDDKIIESHLLKKYNFPENNTWATLMNEKVNNKKSKRNSSSSREFDEKDVRSSISSISASRQSHDRARKIDKNVEAELQEKIQTLVDLISIATHNASVYLSIDDLTNFKIWILIRDSLLWDLKWMTSSQISSDNASNMDANESSDFEAGENLKTGKEFPEEDGAGTSGAESLVEERPQAFRANSDEPSDAEKKPVSKLKEQLKNTEIIPYAQPNEDSDEVLTKLKELQNQRLESRTKMGETVSDDVIIEEDEHEHQEEEQPHDSPTKSAQFHASPIAKSIPILQKREHRKSFIDTFMLHSPNGYNGDTDIGNEDDNISPRFTYNSVSPRSKVSSLQSYATTTSQLETFKKLSSHTAPIIGSPRHAPSRPDSIGREQLSSSLTKKLAKCKKIIADPPWDTKKLIKQLYNQATETGNVVLTVNILFLFQTIYQITEIDIAKDAIAHFLLLLHRYELFGIAADVLKYCPFEDIMGSEGDQSSIRLFCERCGELITNESSKEKLRAEAQQTGNKKIMDKFGYWYCDSCKKKNTSCVLCERPLKKLTMVILPCGHEGHFQCIQEWFLDENEQECPGGCPGVAFI
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
2Phosphorylation------MSLSPHVEN
------CCCCCCCCC
49.1922369663
4Phosphorylation----MSLSPHVENAS
----CCCCCCCCCCC
23.4222369663
11PhosphorylationSPHVENASIPKGSTP
CCCCCCCCCCCCCCC
51.5122369663
17PhosphorylationASIPKGSTPIPKNRN
CCCCCCCCCCCCCCC
33.6328889911
26PhosphorylationIPKNRNVSSIGKGEF
CCCCCCCCCCCCCCC
21.5619823750
27PhosphorylationPKNRNVSSIGKGEFL
CCCCCCCCCCCCCCC
30.9519823750
36PhosphorylationGKGEFLGSSSSNNSS
CCCCCCCCCCCCCCC
29.2422369663
37PhosphorylationKGEFLGSSSSNNSSF
CCCCCCCCCCCCCCE
35.6722369663
38PhosphorylationGEFLGSSSSNNSSFR
CCCCCCCCCCCCCEE
38.4922369663
39PhosphorylationEFLGSSSSNNSSFRM
CCCCCCCCCCCCEEE
41.8122369663
42PhosphorylationGSSSSNNSSFRMNHY
CCCCCCCCCEEEECC
34.7922369663
43PhosphorylationSSSSNNSSFRMNHYS
CCCCCCCCEEEECCC
20.9922369663
60PhosphorylationGQPSVLDSIRRPNLT
CCCCHHHHCCCCCCC
17.5219779198
67PhosphorylationSIRRPNLTPTFSYSN
HCCCCCCCCEEEECC
27.2419779198
69PhosphorylationRRPNLTPTFSYSNGV
CCCCCCCEEEECCCE
21.7019779198
72PhosphorylationNLTPTFSYSNGVYMP
CCCCEEEECCCEECC
11.2828132839
73PhosphorylationLTPTFSYSNGVYMPE
CCCEEEECCCEECCC
26.3828889911
77PhosphorylationFSYSNGVYMPESHRT
EEECCCEECCCCCCC
14.3528132839
84PhosphorylationYMPESHRTSSFNDSY
ECCCCCCCCCCCCCC
24.2522369663
85PhosphorylationMPESHRTSSFNDSYL
CCCCCCCCCCCCCCC
32.6522369663
86PhosphorylationPESHRTSSFNDSYLP
CCCCCCCCCCCCCCC
27.7022369663
90PhosphorylationRTSSFNDSYLPYDKN
CCCCCCCCCCCCCCC
29.6729136822
91PhosphorylationTSSFNDSYLPYDKNP
CCCCCCCCCCCCCCC
17.9829136822
94PhosphorylationFNDSYLPYDKNPYAK
CCCCCCCCCCCCCCC
36.6329136822
102PhosphorylationDKNPYAKTTGSMSNK
CCCCCCCCCCCCCCC
28.3728889911
103PhosphorylationKNPYAKTTGSMSNKS
CCCCCCCCCCCCCCC
26.9328889911
105PhosphorylationPYAKTTGSMSNKSNM
CCCCCCCCCCCCCCC
19.5628889911
107PhosphorylationAKTTGSMSNKSNMKI
CCCCCCCCCCCCCCE
42.6828889911
293PhosphorylationWDLRSNKSKSSNRSD
EECCCCCCCCCCCCC
41.8626447709
295PhosphorylationLRSNKSKSSNRSDIS
CCCCCCCCCCCCCCE
39.6826447709
296PhosphorylationRSNKSKSSNRSDISI
CCCCCCCCCCCCCEE
39.7426447709
299PhosphorylationKSKSSNRSDISINTA
CCCCCCCCCCEEEHH
43.4726447709
598PhosphorylationGGIKKGFSHTGLTSF
CCCCCCCCCCCCCCC
28.8921440633
600PhosphorylationIKKGFSHTGLTSFTP
CCCCCCCCCCCCCCC
32.4629688323
603PhosphorylationGFSHTGLTSFTPERP
CCCCCCCCCCCCCCC
24.1229688323
604PhosphorylationFSHTGLTSFTPERPP
CCCCCCCCCCCCCCC
31.9721440633
606PhosphorylationHTGLTSFTPERPPTL
CCCCCCCCCCCCCCC
24.8129688323
612PhosphorylationFTPERPPTLKAGPTF
CCCCCCCCCCCCCCC
43.5029688323
618PhosphorylationPTLKAGPTFSTKSLT
CCCCCCCCCCCCEEE
29.3322369663
620PhosphorylationLKAGPTFSTKSLTLA
CCCCCCCCCCEEEEC
37.0922369663
621PhosphorylationKAGPTFSTKSLTLAS
CCCCCCCCCEEEECC
22.0622369663
632PhosphorylationTLASGASSFNSSSAS
EECCCCCCCCCCCCC
28.1022890988
637PhosphorylationASSFNSSSASLTSLT
CCCCCCCCCCCCCCC
23.0022890988
642PhosphorylationSSSASLTSLTPQTEN
CCCCCCCCCCCCCCC
35.2222890988
687PhosphorylationSRKKNVISESSSMKN
HCCCCCCCCCHHCCC
27.4327017623
691PhosphorylationNVISESSSMKNSPVE
CCCCCCHHCCCCHHH
42.9527017623
695PhosphorylationESSSMKNSPVEKFKY
CCHHCCCCHHHHHHH
25.4621440633
747PhosphorylationETHGDNTTTTNNNDD
EECCCCCCCCCCCCC
37.5721551504
801PhosphorylationNKKSKRNSSSSREFD
CCCCCCCCCCCCCCC
35.3117287358
802PhosphorylationKKSKRNSSSSREFDE
CCCCCCCCCCCCCCH
35.5619823750
803PhosphorylationKSKRNSSSSREFDEK
CCCCCCCCCCCCCHH
32.9821551504
804PhosphorylationSKRNSSSSREFDEKD
CCCCCCCCCCCCHHH
37.4617287358
814PhosphorylationFDEKDVRSSISSISA
CCHHHHHHHHHHHHH
31.6919795423
815PhosphorylationDEKDVRSSISSISAS
CHHHHHHHHHHHHHH
18.8723749301
817PhosphorylationKDVRSSISSISASRQ
HHHHHHHHHHHHHHH
24.4619795423
818PhosphorylationDVRSSISSISASRQS
HHHHHHHHHHHHHHH
20.9222369663
820PhosphorylationRSSISSISASRQSHD
HHHHHHHHHHHHHHH
23.3422369663
822PhosphorylationSISSISASRQSHDRA
HHHHHHHHHHHHHHH
24.8622369663
928PhosphorylationPEEDGAGTSGAESLV
CCCCCCCCCCHHHHH
24.3721440633
929PhosphorylationEEDGAGTSGAESLVE
CCCCCCCCCHHHHHH
34.7821440633
933PhosphorylationAGTSGAESLVEERPQ
CCCCCHHHHHHHCCH
36.8621440633
946PhosphorylationPQAFRANSDEPSDAE
CHHHHCCCCCCCHHH
42.2224930733
950PhosphorylationRANSDEPSDAEKKPV
HCCCCCCCHHHCCCH
47.6117563356
958PhosphorylationDAEKKPVSKLKEQLK
HHHCCCHHHHHHHHH
40.5828889911
979PhosphorylationYAQPNEDSDEVLTKL
CCCCCCCHHHHHHHH
29.5027214570
1026PhosphorylationEEEQPHDSPTKSAQF
CCCCCCCCCCHHHEE
31.2821440633
1028PhosphorylationEQPHDSPTKSAQFHA
CCCCCCCCHHHEEEC
41.4024961812
1030PhosphorylationPHDSPTKSAQFHASP
CCCCCCHHHEEECCH
29.7629136822
1036PhosphorylationKSAQFHASPIAKSIP
HHHEEECCHHHHHCC
14.3117330950
1053PhosphorylationQKREHRKSFIDTFML
CCHHHHHHCCCEEEC
27.6521440633
1062PhosphorylationIDTFMLHSPNGYNGD
CCEEECCCCCCCCCC
18.9921440633
1066PhosphorylationMLHSPNGYNGDTDIG
ECCCCCCCCCCCCCC
23.7019779198
1080PhosphorylationGNEDDNISPRFTYNS
CCCCCCCCCCCCCCC
19.1021440633
1084PhosphorylationDNISPRFTYNSVSPR
CCCCCCCCCCCCCCC
24.0727017623
1085PhosphorylationNISPRFTYNSVSPRS
CCCCCCCCCCCCCCH
11.6128889911
1087PhosphorylationSPRFTYNSVSPRSKV
CCCCCCCCCCCCHHH
17.3522369663
1089PhosphorylationRFTYNSVSPRSKVSS
CCCCCCCCCCHHHHH
17.8922369663
1095PhosphorylationVSPRSKVSSLQSYAT
CCCCHHHHHHHHHCC
29.1220377248
1096PhosphorylationSPRSKVSSLQSYATT
CCCHHHHHHHHHCCC
33.1523749301
1099PhosphorylationSKVSSLQSYATTTSQ
HHHHHHHHHCCCHHH
23.2521551504
1102PhosphorylationSSLQSYATTTSQLET
HHHHHHCCCHHHHHH
23.5219779198
1104PhosphorylationLQSYATTTSQLETFK
HHHHCCCHHHHHHHH
15.3221551504
1105PhosphorylationQSYATTTSQLETFKK
HHHCCCHHHHHHHHH
30.5820377248
1109PhosphorylationTTTSQLETFKKLSSH
CCHHHHHHHHHHHCC
49.7123749301
1114PhosphorylationLETFKKLSSHTAPII
HHHHHHHHCCCCCCC
29.0219823750
1115PhosphorylationETFKKLSSHTAPIIG
HHHHHHHCCCCCCCC
34.9823749301
1117PhosphorylationFKKLSSHTAPIIGSP
HHHHHCCCCCCCCCC
35.7619779198
1123PhosphorylationHTAPIIGSPRHAPSR
CCCCCCCCCCCCCCC
14.3517330950
1129PhosphorylationGSPRHAPSRPDSIGR
CCCCCCCCCCCCCCH
58.1719823750
1133PhosphorylationHAPSRPDSIGREQLS
CCCCCCCCCCHHHHC
29.6219823750
1140PhosphorylationSIGREQLSSSLTKKL
CCCHHHHCHHHHHHH
19.9919823750
1141PhosphorylationIGREQLSSSLTKKLA
CCHHHHCHHHHHHHH
37.6519823750
1142PhosphorylationGREQLSSSLTKKLAK
CHHHHCHHHHHHHHH
36.3623749301
1144PhosphorylationEQLSSSLTKKLAKCK
HHHCHHHHHHHHHCC
28.2524961812

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 RTC1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RTC1_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 RTC1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IML1_YEASTIML1physical
21454883
NPR3_YEASTNPR3physical
21454883
WDR59_YEASTMTC5physical
21454883
SEA4_YEASTSEA4physical
21454883
NPR2_YEASTNPR2physical
21454883
SEH1_YEASTSEH1physical
21454883
SEC13_YEASTSEC13physical
21454883
WDR59_YEASTMTC5genetic
21454883
SEA4_YEASTSEA4genetic
21454883
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
ECM8_YEASTECM8genetic
27708008
CCZ1_YEASTCCZ1genetic
27708008
VAM6_YEASTVAM6genetic
27708008
WDR59_YEASTMTC5genetic
27708008
NPR3_YEASTNPR3genetic
27708008
SEF1_YEASTSEF1genetic
27708008
GID7_YEASTGID7genetic
27708008
RV161_YEASTRVS161genetic
27708008
DHAS_YEASTHOM2genetic
27708008
ACL4_YEASTYDR161Wgenetic
27708008
UME6_YEASTUME6genetic
27708008
SUM1_YEASTSUM1genetic
27708008
RV167_YEASTRVS167genetic
27708008
SNX41_YEASTSNX41genetic
27708008
CEM1_YEASTCEM1genetic
27708008
BMH1_YEASTBMH1genetic
27708008
PIB2_YEASTPIB2genetic
27708008
YG21_YEASTYGR053Cgenetic
27708008
DBF2_YEASTDBF2genetic
27708008
VMA21_YEASTVMA21genetic
27708008
PSA3_YEASTPRE9genetic
27708008
ERV29_YEASTERV29genetic
27708008
SSBP1_YEASTSBP1genetic
27708008
GRE3_YEASTGRE3genetic
27708008
TOR1_YEASTTOR1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
DGR2_YEASTDGR2genetic
27708008
DBP7_YEASTDBP7genetic
27708008
OAF3_YEASTOAF3genetic
27708008
MLP1_YEASTMLP1genetic
27708008
COA4_YEASTCOA4genetic
27708008
YL415_YEASTYLR415Cgenetic
27708008
FKBP4_YEASTFPR4genetic
27708008
RGM1_YEASTRGM1genetic
27708008
MLF3_YEASTMLF3genetic
27708008
VTC3_YEASTVTC3genetic
27708008
LGE1_YEASTLGE1genetic
27708008
POC4_YEASTPOC4genetic
27708008
VPS4_YEASTVPS4genetic
27708008
KOG1_YEASTKOG1genetic
27811238
IML1_YEASTIML1physical
25073740
WDR59_YEASTMTC5physical
25073740
NPR3_YEASTNPR3physical
25073740
SEA4_YEASTSEA4physical
25073740
SEH1_YEASTSEH1physical
25073740
SEC13_YEASTSEC13physical
25073740
TOR1_YEASTTOR1physical
25073740
KOG1_YEASTKOG1physical
25073740
NPR2_YEASTNPR2physical
25073740
LST8_YEASTLST8physical
25073740
PMA1_YEASTPMA1physical
25073740
VPS1_YEASTVPS1physical
25073740
MS116_YEASTMSS116physical
25073740
RFA1_YEASTRFA1physical
25073740
RAD52_YEASTRAD52physical
25073740
HRR25_YEASTHRR25physical
25073740
IMDH3_YEASTIMD3physical
25073740
RUVB1_YEASTRVB1physical
25073740
RUVB2_YEASTRVB2physical
25073740
FKBP4_YEASTFPR4physical
25073740
ALF_YEASTFBA1physical
25073740
ACT_YEASTACT1physical
25073740
MG101_YEASTMGM101physical
25073740
YRA1_YEASTYRA1physical
25073740
PMG1_YEASTGPM1physical
25073740
RIM1_YEASTRIM1physical
25073740
RRP5_YEASTRRP5physical
25073740
PRP43_YEASTPRP43physical
25073740
DED1_YEASTDED1physical
25073740
NOP58_YEASTNOP58physical
25073740
NSR1_YEASTNSR1physical
25073740
NOP56_YEASTNOP56physical
25073740
FBRL_YEASTNOP1physical
25073740
IML1_YEASTIML1genetic
23716719
NPR2_YEASTNPR2genetic
23716719
NPR3_YEASTNPR3genetic
23716719

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RTC1_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-86; SER-620; SER-946;SER-1036; SER-1080; SER-1087; SER-1089; SER-1123; SER-1129 ANDSER-1133, 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-946 AND SER-950, 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-801 AND SER-804, ANDMASS SPECTROMETRY.
"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-1036 AND SER-1123, ANDMASS SPECTROMETRY.
"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-1089 AND SER-1123, ANDMASS SPECTROMETRY.

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