CTR1_YEAST - dbPTM
CTR1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTR1_YEAST
UniProt AC P49573
Protein Name Copper transport protein CTR1
Gene Name CTR1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 406
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Required for high affinity copper (probably reduced Cu I) transport into the cell..
Protein Sequence MEGMNMGSSMNMDAMSSASKTVASSMASMSMDAMSSASKTILSSMSSMSMEAMSSASKTLASTMSSMASMSMGSSSMSGMSMSMSSTPTSSASAQTTSDSSMSGMSGMSSSDNSSSSGMDMDMSMGMNYYLTPTYKNYPVLFHHLHANNSGKAFGIFLLFVVAAFVYKLLLFVSWCLEVHWFKKWDKQNKYSTLPSANSKDEGKHYDTENNFEIQGLPKLPNLLSDIFVPSLMDLFHDIIRAFLVFTSTMIIYMLMLATMSFVLTYVFAVITGLALSEVFFNRCKIAMLKRWDIQREIQKAKSCPGFGNCQCGRHPEPSPDPIAVADTTSGSDQSTRLEKNNESKVAISENNQKKTPTQEEGCNCATDSGKNQANIERDILENSKLQEQSGNMDQNLLPAEKFTHN
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
8PhosphorylationMEGMNMGSSMNMDAM
CCCCCCCCCCCHHHH		18.6930377154
9PhosphorylationEGMNMGSSMNMDAMS
CCCCCCCCCCHHHHH		14.4028132839
16PhosphorylationSMNMDAMSSASKTVA
CCCHHHHHHHHHHHH		25.1928132839
19PhosphorylationMDAMSSASKTVASSM
HHHHHHHHHHHHHHH		30.7028132839
24PhosphorylationSASKTVASSMASMSM
HHHHHHHHHHHHHCH		19.1330377154
28PhosphorylationTVASSMASMSMDAMS
HHHHHHHHHCHHHHH		11.6230377154
35PhosphorylationSMSMDAMSSASKTIL
HHCHHHHHHHHHHHH		25.1930377154
40PhosphorylationAMSSASKTILSSMSS
HHHHHHHHHHHHHHH		25.3427017623
49PhosphorylationLSSMSSMSMEAMSSA
HHHHHHHCHHHHHHH		18.5427017623
54PhosphorylationSMSMEAMSSASKTLA
HHCHHHHHHHHHHHH		29.7827017623
55PhosphorylationMSMEAMSSASKTLAS
HCHHHHHHHHHHHHH		24.3927017623
113N-linked_GlycosylationSGMSSSDNSSSSGMD
CCCCCCCCCCCCCCC		45.82-
148N-linked_GlycosylationLFHHLHANNSGKAFG
EEEEEECCCCCHHHH		32.24-
193PhosphorylationDKQNKYSTLPSANSK
CCCCCCCCCCCCCCC		39.3320377248
196PhosphorylationNKYSTLPSANSKDEG
CCCCCCCCCCCCCCC		43.1022369663
199PhosphorylationSTLPSANSKDEGKHY
CCCCCCCCCCCCCCC		41.0022369663
200UbiquitinationTLPSANSKDEGKHYD
CCCCCCCCCCCCCCC		60.6522817900
204UbiquitinationANSKDEGKHYDTENN
CCCCCCCCCCCCCCC		36.6222817900
300UbiquitinationDIQREIQKAKSCPGF
HHHHHHHHHHCCCCC		64.5422817900
302UbiquitinationQREIQKAKSCPGFGN
HHHHHHHHCCCCCCC		60.6723749301
303PhosphorylationREIQKAKSCPGFGNC
HHHHHHHCCCCCCCC		30.3323749301
319PhosphorylationCGRHPEPSPDPIAVA
CCCCCCCCCCCCEEE		40.0325005228
328PhosphorylationDPIAVADTTSGSDQS
CCCEEEECCCCCCCC		17.0820377248
329PhosphorylationPIAVADTTSGSDQST
CCEEEECCCCCCCCH		31.4720377248
330PhosphorylationIAVADTTSGSDQSTR
CEEEECCCCCCCCHH		38.0920377248
332PhosphorylationVADTTSGSDQSTRLE
EEECCCCCCCCHHHH		32.0420377248
335PhosphorylationTTSGSDQSTRLEKNN
CCCCCCCCHHHHHCC		22.0820377248
336PhosphorylationTSGSDQSTRLEKNNE
CCCCCCCHHHHHCCC		33.3720377248
340UbiquitinationDQSTRLEKNNESKVA
CCCHHHHHCCCCCEE		70.4422817900
344PhosphorylationRLEKNNESKVAISEN
HHHHCCCCCEEECCC		34.2617330950
345UbiquitinationLEKNNESKVAISENN
HHHCCCCCEEECCCC		29.5223749301
349PhosphorylationNESKVAISENNQKKT
CCCCEEECCCCCCCC		25.2422369663
354UbiquitinationAISENNQKKTPTQEE
EECCCCCCCCCCCCC		61.8223749301
355UbiquitinationISENNQKKTPTQEEG
ECCCCCCCCCCCCCC		50.3923749301
356PhosphorylationSENNQKKTPTQEEGC
CCCCCCCCCCCCCCC		38.3125521595
358PhosphorylationNNQKKTPTQEEGCNC
CCCCCCCCCCCCCCC		54.5720377248
367PhosphorylationEEGCNCATDSGKNQA
CCCCCCCCCCCCCCH		32.6625521595
369PhosphorylationGCNCATDSGKNQANI
CCCCCCCCCCCCHHH		47.5125521595
371UbiquitinationNCATDSGKNQANIER
CCCCCCCCCCHHHHH		50.2523749301
385UbiquitinationRDILENSKLQEQSGN
HHHHHHHHHHHHHCC		66.8123749301
402UbiquitinationQNLLPAEKFTHN---
CCCCCHHHCCCC---		58.6423749301
402AcetylationQNLLPAEKFTHN---
CCCCCHHHCCCC---		58.6424489116
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
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTR1_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 CTR1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTR3_YEASTCTR3genetic
11983704
CTR1_YEASTCTR1physical
17627943
CTR1_YEASTCTR1physical
18467557
FET3_YEASTFET3genetic
12954629
SCO2_YEASTSCO2genetic
20093466
EFM2_YEASTEFM2genetic
20093466
BUD31_YEASTBUD31genetic
20093466
YD183_YEASTYDL183Cgenetic
20093466
HOSC_YEASTLYS20genetic
20093466
ATIF_YEASTINH1genetic
20093466
VAM6_YEASTVAM6genetic
20093466
SCS2_YEASTSCS2genetic
20093466
SPT2_YEASTSPT2genetic
20093466
IXR1_YEASTIXR1genetic
20093466
IRC21_YEASTIRC21genetic
20093466
PFKA2_YEASTPFK2genetic
20093466
SKY1_YEASTSKY1genetic
20093466
OCA2_YEASTOCA2genetic
20093466
PHO88_YEASTPHO88physical
16093310
MKAR_YEASTIFA38physical
16093310
HSP30_YEASTHSP30physical
16093310
YET1_YEASTYET1physical
16093310
KTR5_YEASTKTR5physical
16093310
DGK1_YEASTDGK1physical
16093310
CTR4_SCHPOctr4genetic
21273250
CTR5_SCHPOctr5genetic
21273250
CTR3_YEASTCTR3genetic
21273250
CTR2_YEASTCTR2genetic
22445756
MAC1_YEASTMAC1genetic
22445756
UBC3_YEASTCDC34genetic
27708008
TBF1_YEASTTBF1genetic
27708008
SWC3_YEASTSWC3genetic
27708008
PAT1_YEASTPAT1genetic
27708008
UBX3_YEASTUBX3genetic
27708008
EXO84_YEASTEXO84genetic
27708008
CKS1_YEASTCKS1genetic
27708008
MAK5_YEASTMAK5genetic
27708008
POP7_YEASTPOP7genetic
27708008
MCM7_YEASTMCM7genetic
27708008
CDC13_YEASTCDC13genetic
27708008
CDC1_YEASTCDC1genetic
27708008
TFB1_YEASTTFB1genetic
27708008
RPB7_YEASTRPB7genetic
27708008
TSC11_YEASTTSC11genetic
27708008
COG3_YEASTCOG3genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
STT3_YEASTSTT3genetic
27708008
PRI2_YEASTPRI2genetic
27708008
SEC22_YEASTSEC22genetic
27708008
MED11_YEASTMED11genetic
27708008
PSB2_YEASTPUP1genetic
27708008
MED4_YEASTMED4genetic
27708008
MEX67_YEASTMEX67genetic
27708008
SCS22_YEASTSCS22genetic
27708008
SFT2_YEASTSFT2genetic
27708008
SCO2_YEASTSCO2genetic
27708008
OLA1_YEASTOLA1genetic
27708008
YBP1_YEASTYBP1genetic
27708008
YB92_YEASTYBR242Wgenetic
27708008
EFM2_YEASTEFM2genetic
27708008
BUD31_YEASTBUD31genetic
27708008
VAM6_YEASTVAM6genetic
27708008
GET3_YEASTGET3genetic
27708008
ATIF_YEASTINH1genetic
27708008
HOSC_YEASTLYS20genetic
27708008
YD183_YEASTYDL183Cgenetic
27708008
OST4_YEASTOST4genetic
27708008
HNT2_YEASTHNT2genetic
27708008
SDC1_YEASTSDC1genetic
27708008
SCS2_YEASTSCS2genetic
27708008
SPT2_YEASTSPT2genetic
27708008
RTF1_YEASTRTF1genetic
27708008
ACBP_YEASTACB1genetic
27708008
MVB12_YEASTMVB12genetic
27708008
RT102_YEASTRTT102genetic
27708008
MSC7_YEASTMSC7genetic
27708008
AP18A_YEASTYAP1801genetic
27708008
PDK1_YEASTPKP1genetic
27708008
THIK_YEASTPOT1genetic
27708008
YJ24_YEASTKCH1genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
IXR1_YEASTIXR1genetic
27708008
DCOR_YEASTSPE1genetic
27708008
EI2BA_YEASTGCN3genetic
27708008
YPT6_YEASTYPT6genetic
27708008
IRC21_YEASTIRC21genetic
27708008
PFKA2_YEASTPFK2genetic
27708008
SKY1_YEASTSKY1genetic
27708008
OCA2_YEASTOCA2genetic
27708008
CTR3_YEASTCTR3genetic
27811238
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CTR1_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-319; SER-344 ANDSER-349, 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-344, 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-344; THR-356 ANDSER-369, AND MASS SPECTROMETRY.

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