PPID_YEAST - dbPTM
PPID_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPID_YEAST
UniProt AC P53691
Protein Name Peptidyl-prolyl cis-trans isomerase CPR6
Gene Name CPR6
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 371
Subcellular Localization Cytoplasm.
Protein Description PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides..
Protein Sequence MTRPKTFFDISIGGKPQGRIVFELYNDIVPKTAENFLKLCEGNAGMAKTKPDVPLSYKGSIFHRVIKDFMCQFGDFTNFNGTGGESIYDEKFEDENFTVKHDKPFLLSMANAGPNTNGSQAFITCVPTPHLDGKHVVFGEVIQGKRIVRLIENQQCDQENNKPLRDVKIDDCGVLPDDYQVPENAEATPTDEYGDNYEDVLKQDEKVDLKNFDTVLKAIETVKNIGTEQFKKQNYSVALEKYVKCDKFLKEYFPEDLEKEQIEKINQLKVSIPLNIAICALKLKDYKQVLVASSEVLYAEAADEKAKAKALYRRGLAYYHVNDTDMALNDLEMATTFQPNDAAILKAIHNTKLKRKQQNEKAKKSLSKMFS
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
15AcetylationFDISIGGKPQGRIVF
EEEEECCEECCEEEE
29.0224489116
25PhosphorylationGRIVFELYNDIVPKT
CEEEEEEECCCCHHH
12.0021082442
31UbiquitinationLYNDIVPKTAENFLK
EECCCCHHHHHHHHH
49.8522817900
38AcetylationKTAENFLKLCEGNAG
HHHHHHHHHHHCCCC
47.1325381059
38UbiquitinationKTAENFLKLCEGNAG
HHHHHHHHHHHCCCC
47.1322817900
58AcetylationPDVPLSYKGSIFHRV
CCCCCCCCCHHHHHH
42.6924489116
100AcetylationEDENFTVKHDKPFLL
CCCCEEEECCCCCEE
42.9224489116
162UbiquitinationQCDQENNKPLRDVKI
CCCCCCCCCCCCCEE
57.9423749301
188PhosphorylationVPENAEATPTDEYGD
CCCCCCCCCCCCCCC
20.4426447709
190PhosphorylationENAEATPTDEYGDNY
CCCCCCCCCCCCCCH
36.7926447709
193PhosphorylationEATPTDEYGDNYEDV
CCCCCCCCCCCHHHH
32.3726447709
210UbiquitinationQDEKVDLKNFDTVLK
HCCCCCCCCHHHHHH
51.6223749301
210SuccinylationQDEKVDLKNFDTVLK
HCCCCCCCCHHHHHH
51.6223954790
210AcetylationQDEKVDLKNFDTVLK
HCCCCCCCCHHHHHH
51.6224489116
217AcetylationKNFDTVLKAIETVKN
CCHHHHHHHHHHHHH
42.8724489116
223AcetylationLKAIETVKNIGTEQF
HHHHHHHHHHCCHHH
50.7124489116
2232-HydroxyisobutyrylationLKAIETVKNIGTEQF
HHHHHHHHHHCCHHH
50.71-
223UbiquitinationLKAIETVKNIGTEQF
HHHHHHHHHHCCHHH
50.7123749301
231AcetylationNIGTEQFKKQNYSVA
HHCCHHHHHCCHHHH
53.8222865919
2312-HydroxyisobutyrylationNIGTEQFKKQNYSVA
HHCCHHHHHCCHHHH
53.82-
231UbiquitinationNIGTEQFKKQNYSVA
HHCCHHHHHCCHHHH
53.8223749301
232UbiquitinationIGTEQFKKQNYSVAL
HCCHHHHHCCHHHHH
45.1023749301
241AcetylationNYSVALEKYVKCDKF
CHHHHHHHHHCCHHH
57.0822865919
250AcetylationVKCDKFLKEYFPEDL
HCCHHHHHHHCCHHH
54.2025381059
259AcetylationYFPEDLEKEQIEKIN
HCCHHHHHHHHHHHH
63.3224489116
259UbiquitinationYFPEDLEKEQIEKIN
HCCHHHHHHHHHHHH
63.3223749301
264AcetylationLEKEQIEKINQLKVS
HHHHHHHHHHHCCCC
48.8924489116
2642-HydroxyisobutyrylationLEKEQIEKINQLKVS
HHHHHHHHHHHCCCC
48.89-
282AcetylationNIAICALKLKDYKQV
HHHHHHHHCCCCHHH
34.6624489116
293PhosphorylationYKQVLVASSEVLYAE
CHHHEEECCHHHHHH
21.3927017623
294PhosphorylationKQVLVASSEVLYAEA
HHHEEECCHHHHHHH
23.2227017623
305UbiquitinationYAEAADEKAKAKALY
HHHHCCHHHHHHHHH
56.5922817900
305AcetylationYAEAADEKAKAKALY
HHHHCCHHHHHHHHH
56.5924489116
307UbiquitinationEAADEKAKAKALYRR
HHCCHHHHHHHHHHC
62.5822817900
309UbiquitinationADEKAKAKALYRRGL
CCHHHHHHHHHHCCC
37.9122817900

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 PPID_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPID_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 PPID_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CA120_YEASTCAF120physical
11805837
TRXB1_YEASTTRR1physical
11805837
NADE_YEASTQNS1physical
11805837
ADH2_YEASTADH2physical
11805837
SLP1_YEASTSLP1physical
11805837
RCN2_YEASTRCN2physical
11805837
GPX3_YEASTHYR1physical
10688190
SBA1_YEASTSBA1physical
15364569
HSP82_YEASTHSP82physical
15364569
NADE_YEASTQNS1physical
16554755
PYR1_YEASTURA2physical
16554755
HS104_YEASTHSP104physical
16554755
HSC82_YEASTHSC82physical
16554755
HSP82_YEASTHSP82physical
16554755
RPD3_YEASTRPD3physical
8873448
XRN1_YEASTXRN1genetic
17314980
PAC11_YEASTPAC11genetic
17314980
PFD1_YEASTPFD1physical
19536198
HSC82_YEASTHSC82physical
19536198
HAP3_YEASTHAP3genetic
20093466
NUM1_YEASTNUM1genetic
20093466
EAF1_YEASTEAF1genetic
20093466
PAC11_YEASTPAC11genetic
20093466
YOR1_YEASTYOR1genetic
20093466
ARP1_YEASTARP1genetic
20093466
COXM1_YEASTCMC1genetic
20093466
SBA1_YEASTSBA1genetic
20093466
DYHC_YEASTDYN1genetic
20093466
LDB18_YEASTLDB18genetic
20093466
CIK1_YEASTCIK1genetic
20093466
DYN3_YEASTDYN3genetic
20093466
PHO23_YEASTPHO23genetic
20093466
MAS5_YEASTYDJ1genetic
20093466
IRA2_YEASTIRA2genetic
20093466
LIS1_YEASTPAC1genetic
20093466
NIP80_YEASTNIP100genetic
20093466
DAP1_YEASTDAP1genetic
20093466
CTF4_YEASTCTF4genetic
20093466
KAR3_YEASTKAR3genetic
20093466
ARL1_YEASTARL1genetic
19325107
PLMT_YEASTOPI3genetic
19325107
SEC66_YEASTSEC66genetic
19325107
TLG2_YEASTTLG2genetic
19325107
VPS9_YEASTVPS9genetic
19325107
HSC82_YEASTHSC82physical
21170051
HSP82_YEASTHSP82physical
21170051
STI1_YEASTSTI1physical
21170051
AHA1_YEASTAHA1physical
21170051
HSP82_YEASTHSP82physical
22505624
CYP7_YEASTCPR7physical
22505624
HSP74_HUMANHSPA4physical
24753260
HSP82_YEASTHSP82physical
23396352
HSP82_YEASTHSP82physical
23926110
HSP71_YEASTSSA1physical
23926110
PYR1_YEASTURA2physical
23926110
HSP82_YEASTHSP82genetic
23926110
PYR1_YEASTURA2physical
25380751
HSC82_YEASTHSC82physical
25380751
SSB1_YEASTSSB1physical
25380751
ZUO1_YEASTZUO1physical
25380751
RL6A_YEASTRPL6Aphysical
25380751
RL6B_YEASTRPL6Bphysical
25380751
RL8A_YEASTRPL8Aphysical
25380751
RL8B_YEASTRPL8Bphysical
25380751
RL9A_YEASTRPL9Aphysical
25380751
RL9B_YEASTRPL9Bphysical
25380751
RL10_YEASTRPL10physical
25380751
RL11A_YEASTRPL11Aphysical
25380751
RL11B_YEASTRPL11Bphysical
25380751
RL12A_YEASTRPL12Bphysical
25380751
RL12B_YEASTRPL12Bphysical
25380751
RL17B_YEASTRPL17Bphysical
25380751
RL20A_YEASTRPL20Bphysical
25380751
RL20B_YEASTRPL20Bphysical
25380751
RL21A_YEASTRPL21Aphysical
25380751
RL21B_YEASTRPL21Bphysical
25380751
RL25_YEASTRPL25physical
25380751
RL28_YEASTRPL28physical
25380751
RLA0_YEASTRPP0physical
25380751
RSSA1_YEASTRPS0Aphysical
25380751
RSSA2_YEASTRPS0Bphysical
25380751
RS3A1_YEASTRPS1Aphysical
25380751
RS3A2_YEASTRPS1Bphysical
25380751
RS2_YEASTRPS2physical
25380751
RS3_YEASTRPS3physical
25380751
RS4A_YEASTRPS4Aphysical
25380751
RS4B_YEASTRPS4Aphysical
25380751
RS5_YEASTRPS5physical
25380751
RS7A_YEASTRPS7Aphysical
25380751
RS12_YEASTRPS12physical
25380751
RS13_YEASTRPS13physical
25380751
RS16A_YEASTRPS16Bphysical
25380751
RS16B_YEASTRPS16Bphysical
25380751
RS17A_YEASTRPS17Aphysical
25380751
RS17B_YEASTRPS17Bphysical
25380751
RS18A_YEASTRPS18Aphysical
25380751
RS18B_YEASTRPS18Aphysical
25380751
RS20_YEASTRPS20physical
25380751
GBLP_YEASTASC1physical
25380751
SNT1_YEASTSNT1genetic
27708008
MAF1_YEASTMAF1genetic
27708008
NUM1_YEASTNUM1genetic
27708008
HTD2_YEASTHTD2genetic
27708008
ARP1_YEASTARP1genetic
27708008
SBA1_YEASTSBA1genetic
27708008
COXM1_YEASTCMC1genetic
27708008
SA190_YEASTSAP190genetic
27708008
PAM17_YEASTPAM17genetic
27708008
CTF18_YEASTCTF18genetic
27708008
JNM1_YEASTJNM1genetic
27708008
DYN3_YEASTDYN3genetic
27708008
COX5A_YEASTCOX5Agenetic
27708008
MAS5_YEASTYDJ1genetic
27708008
LIS1_YEASTPAC1genetic
27708008
NIP80_YEASTNIP100genetic
27708008
CTF4_YEASTCTF4genetic
27708008
KAR3_YEASTKAR3genetic
27708008
PMP1_YEASTPMP1physical
26404137

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PPID_YEAST

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Related Literatures of Post-Translational Modification

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