APE2_YEAST - dbPTM
APE2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APE2_YEAST
UniProt AC P32454
Protein Name Aminopeptidase 2, mitochondrial
Gene Name APE2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 952
Subcellular Localization Periplasm. Cytoplasm. Mitochondrion.
Protein Description Involved in the cellular supply of leucine from externally offered leucine-containing dipeptide substrates..
Protein Sequence MPIVRWLLLKSAVRGSSLIGKAHPCLRSIAAHPRYLSNVYSPPAGVSRSLRINVMWKQSKLTPPRFVKIMNRRPLFTETSHACAKCQKTSQLLNKTPNREILPDNVVPLHYDLTVEPDFKTFKFEGSVKIELKINNPAIDTVTLNTVDTDIHSAKIGDVTSSEIISEEEQQVTTFAFPKGTMSSFKGNAFLDIKFTGILNDNMAGFYRAKYEDKLTGETKYMATTQMEPTDARRAFPCFDEPNLKASFAITLVSDPSLTHLSNMDVKNEYVKDGKKVTLFNTTPKMSTYLVAFIVAELKYVESKNFRIPVRVYATPGNEKHGQFAADLTAKTLAFFEKTFGIQYPLPKMDNVAVHEFSAGAMENWGLVTYRVVDLLLDKDNSTLDRIQRVAEVVQHELAHQWFGNLVTMDWWEGLWLNEGFATWMSWYSCNEFQPEWKVWEQYVTDTLQHALSLDSLRSSHPIEVPVKKADEINQIFDAISYSKGASLLRMISKWLGEETFIKGVSQYLNKFKYGNAKTEDLWDALADASGKDVRSVMNIWTKKVGFPVISVSEDGNGKITFRQNRYLSTADVKPDEDKTIYPVFLALKTKNGVDSSVVLSERSKTIELEDPTFFKVNSEQSGIYITSYTDERWAKLGQQADLLSVEDRVGLVADVKTLSASGYTSTTNFLNLVSKWNNEKSFVVWDQIINSISSMKSTWLFEPKETQDALDNFTKQLISGMTHHLGWEFKSSDSFSTQRLKVTMFGAACAARDADVEKAALKMFTDYCSGNKEAIPALIKPIVFNTVARVGGAENYEKVYKIYLDPISNDEKLAALRSLGRFKEPKLLERTLGYLFDGTVLNQDIYIPMQGMRAHQEGVEALWNWVKKNWDELVKRLPPGLSMLGSVVTLGTSGFTSMQKIDEIKKFFATKSTKGFDQSLAQSLDTITSKAQWVNRDRDVVNKYLKENGYY
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
133UbiquitinationGSVKIELKINNPAID
EEEEEEEEECCCCCE
30.5117644757
141PhosphorylationINNPAIDTVTLNTVD
ECCCCCEEEEEEECC
14.8522369663
143PhosphorylationNPAIDTVTLNTVDTD
CCCCEEEEEEECCCC
19.1822369663
146PhosphorylationIDTVTLNTVDTDIHS
CEEEEEEECCCCCHH
23.9122369663
149PhosphorylationVTLNTVDTDIHSAKI
EEEEECCCCCHHCCC
32.3022369663
153PhosphorylationTVDTDIHSAKIGDVT
ECCCCCHHCCCCCCC
31.4322369663
155UbiquitinationDTDIHSAKIGDVTSS
CCCCHHCCCCCCCHH
50.6817644757
245UbiquitinationCFDEPNLKASFAITL
CCCCCCCEEEEEEEE
48.9317644757
247PhosphorylationDEPNLKASFAITLVS
CCCCCEEEEEEEEEC
17.3922369663
251PhosphorylationLKASFAITLVSDPSL
CEEEEEEEEECCCCC
20.0622369663
254PhosphorylationSFAITLVSDPSLTHL
EEEEEEECCCCCCCC
47.0922369663
257PhosphorylationITLVSDPSLTHLSNM
EEEECCCCCCCCCCC
51.3922369663
259PhosphorylationLVSDPSLTHLSNMDV
EECCCCCCCCCCCCC
25.7122369663
262PhosphorylationDPSLTHLSNMDVKNE
CCCCCCCCCCCCCCC
23.6222369663
320AcetylationYATPGNEKHGQFAAD
EECCCCCCCCCHHHH
57.9724489116
338UbiquitinationKTLAFFEKTFGIQYP
HHHHHHHHHHCCCCC
43.9523749301
348UbiquitinationGIQYPLPKMDNVAVH
CCCCCCCCCCCEEEE
67.5717644757
379AcetylationVVDLLLDKDNSTLDR
HHHHHHCCCCCHHHH
59.8024489116
381N-linked_GlycosylationDLLLDKDNSTLDRIQ
HHHHCCCCCHHHHHH
42.51-
494UbiquitinationSLLRMISKWLGEETF
HHHHHHHHHHCCCHH
35.2023749301
494AcetylationSLLRMISKWLGEETF
HHHHHHHHHHCCCHH
35.2024489116
511AcetylationGVSQYLNKFKYGNAK
HHHHHHHHCCCCCCC
40.4124489116
518AcetylationKFKYGNAKTEDLWDA
HCCCCCCCCHHHHHH
57.3524489116
532AcetylationALADASGKDVRSVMN
HHHHCCCCCHHHHHH
51.0224489116
553PhosphorylationGFPVISVSEDGNGKI
CCEEEEEECCCCCEE
24.1527017623
567PhosphorylationITFRQNRYLSTADVK
EEEECCCEECCCCCC
16.7422369663
569PhosphorylationFRQNRYLSTADVKPD
EECCCEECCCCCCCC
16.7721440633
570PhosphorylationRQNRYLSTADVKPDE
ECCCEECCCCCCCCC
25.0422369663
574AcetylationYLSTADVKPDEDKTI
EECCCCCCCCCCCCC
47.5024489116
579AcetylationDVKPDEDKTIYPVFL
CCCCCCCCCCCEEEE
34.4724489116
596PhosphorylationKTKNGVDSSVVLSER
EECCCCCCEEEEECC
23.7222369663
597PhosphorylationTKNGVDSSVVLSERS
ECCCCCCEEEEECCC
16.2822369663
604PhosphorylationSVVLSERSKTIELED
EEEEECCCCEEEECC
30.0522369663
605AcetylationVVLSERSKTIELEDP
EEEECCCCEEEECCC
60.8024489116
605UbiquitinationVVLSERSKTIELEDP
EEEECCCCEEEECCC
60.8023749301
606PhosphorylationVLSERSKTIELEDPT
EEECCCCEEEECCCC
22.4122369663
619PhosphorylationPTFFKVNSEQSGIYI
CCEEEECCCCCCEEE
39.7528889911
625PhosphorylationNSEQSGIYITSYTDE
CCCCCCEEEEEECHH
11.1528889911
627PhosphorylationEQSGIYITSYTDERW
CCCCEEEEEECHHHH
9.9428889911
628PhosphorylationQSGIYITSYTDERWA
CCCEEEEEECHHHHH
19.2428889911
629PhosphorylationSGIYITSYTDERWAK
CCEEEEEECHHHHHH
15.0128889911
630PhosphorylationGIYITSYTDERWAKL
CEEEEEECHHHHHHH
31.0228889911
705UbiquitinationSTWLFEPKETQDALD
CCCCCCCCHHHHHHH
67.2217644757
705AcetylationSTWLFEPKETQDALD
CCCCCCCCHHHHHHH
67.2224489116
713N-linked_GlycosylationETQDALDNFTKQLIS
HHHHHHHHHHHHHHH
47.54-
716UbiquitinationDALDNFTKQLISGMT
HHHHHHHHHHHHHCH
38.6817644757
720PhosphorylationNFTKQLISGMTHHLG
HHHHHHHHHCHHHCC
30.9819823750
723PhosphorylationKQLISGMTHHLGWEF
HHHHHHCHHHCCCEE
15.0719823750
766PhosphorylationKAALKMFTDYCSGNK
HHHHHHHHHHHCCCH
23.6628889911
799AcetylationGGAENYEKVYKIYLD
CCCCCHHHEEEEEEC
40.2724489116
799SuccinylationGGAENYEKVYKIYLD
CCCCCHHHEEEEEEC
40.2723954790
802AcetylationENYEKVYKIYLDPIS
CCHHHEEEEEECCCC
28.0624489116
813AcetylationDPISNDEKLAALRSL
CCCCCHHHHHHHHHC
46.4124489116
813UbiquitinationDPISNDEKLAALRSL
CCCCCHHHHHHHHHC
46.4124961812
827AcetylationLGRFKEPKLLERTLG
CCCCCCHHHHHHHHH
67.7924489116
868UbiquitinationEALWNWVKKNWDELV
HHHHHHHHHCHHHHH
31.8117644757
869AcetylationALWNWVKKNWDELVK
HHHHHHHHCHHHHHH
54.3624489116
869UbiquitinationALWNWVKKNWDELVK
HHHHHHHHCHHHHHH
54.3617644757
876AcetylationKNWDELVKRLPPGLS
HCHHHHHHHCCCCHH
61.9224489116
893PhosphorylationGSVVTLGTSGFTSMQ
CEEEEECCCCCCCHH
28.8719779198
898PhosphorylationLGTSGFTSMQKIDEI
ECCCCCCCHHHHHHH
19.5619779198

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 APE2_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of APE2_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 APE2_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VHR2_YEASTVHR2physical
16554755
ACON_YEASTACO1physical
16429126
MKT1_YEASTMKT1physical
16429126
FHP_YEASTYHB1physical
16429126
BUD4_YEASTBUD4physical
16429126
MDHM_YEASTMDH1physical
16429126
HSP60_YEASTHSP60physical
16429126
MRP8_YEASTMRP8physical
18719252
SSB1_YEASTSSB1physical
19536198
MFG1_YEASTMFG1genetic
20093466
UFD2_YEASTUFD2genetic
20093466
CRD1_YEASTCRD1genetic
20093466
HNT2_YEASTHNT2genetic
20093466
BCS1_YEASTBCS1genetic
20093466
SDC1_YEASTSDC1genetic
20093466
RAD51_YEASTRAD51genetic
20093466
RIM15_YEASTRIM15genetic
20093466
ADH4_YEASTADH4genetic
20093466
YGY5_YEASTYGL235Wgenetic
20093466
PUS2_YEASTPUS2genetic
20093466
QCR9_YEASTQCR9genetic
20093466
PHB2_YEASTPHB2genetic
20093466
TNA1_YEASTTNA1genetic
20093466
RRM3_YEASTRRM3genetic
20093466
GIC1_YEASTGIC1genetic
20093466
FMC1_YEASTFMC1genetic
20093466
YPS6_YEASTYPS6genetic
20093466
PEX2_YEASTPEX2genetic
20093466
F26_YEASTFBP26genetic
20093466
LPLA_YEASTAIM22genetic
20093466
MOG1_YEASTMOG1genetic
20093466
FPS1_YEASTFPS1genetic
20093466
PER33_YEASTPER33genetic
20093466
PEX13_YEASTPEX13genetic
20093466
UPS1_YEASTUPS1genetic
20093466
STP3_YEASTSTP3genetic
20093466
YL413_YEASTINA1genetic
20093466
OST6_YEASTOST6genetic
20093466
SSO2_YEASTSSO2genetic
20093466
INP1_YEASTINP1genetic
20093466
YN8H_YEASTYNR029Cgenetic
20093466
GAS4_YEASTGAS4genetic
20093466
CSN10_YEASTRRI2genetic
20093466
ADH1_YEASTADH1genetic
20093466
HPH1_YEASTFRT1genetic
20093466
HAP5_YEASTHAP5genetic
20093466
WDR6_YEASTRTT10genetic
20093466
ISU1_YEASTISU1genetic
20093466
RIM15_YEASTRIM15genetic
22282571
AMN1_YEASTAMN1genetic
27708008
AFR1_YEASTAFR1genetic
27708008
MRM2_YEASTMRM2genetic
27708008
LSB6_YEASTLSB6genetic
27708008
REE1_YEASTREE1genetic
27708008
PUN1_YEASTPUN1genetic
27708008
VPS27_YEASTVPS27genetic
27708008
VPH1_YEASTVPH1genetic
27708008
ECM15_YEASTECM15genetic
27708008
MBA1_YEASTMBA1genetic
27708008
CRD1_YEASTCRD1genetic
27708008
UFD2_YEASTUFD2genetic
27708008
PEX5_YEASTPEX5genetic
27708008
HNT2_YEASTHNT2genetic
27708008
BCS1_YEASTBCS1genetic
27708008
STP1_YEASTSTP1genetic
27708008
SDC1_YEASTSDC1genetic
27708008
RAD51_YEASTRAD51genetic
27708008
ODPA_YEASTPDA1genetic
27708008
AROC_YEASTARO2genetic
27708008
MED5_YEASTNUT1genetic
27708008
PSA3_YEASTPRE9genetic
27708008
QCR9_YEASTQCR9genetic
27708008
TNA1_YEASTTNA1genetic
27708008
DUR3_YEASTDUR3genetic
27708008
NPR3_YEASTNPR3genetic
27708008
RRM3_YEASTRRM3genetic
27708008
YPS6_YEASTYPS6genetic
27708008
LPLA_YEASTAIM22genetic
27708008
LSM1_YEASTLSM1genetic
27708008
YJU6_YEASTYJL206Cgenetic
27708008
PEX2_YEASTPEX2genetic
27708008
MOG1_YEASTMOG1genetic
27708008
FPS1_YEASTFPS1genetic
27708008
PEX13_YEASTPEX13genetic
27708008
UPS1_YEASTUPS1genetic
27708008
STP3_YEASTSTP3genetic
27708008
MAC1_YEASTMAC1genetic
27708008
PEX12_YEASTPEX12genetic
27708008
SSO2_YEASTSSO2genetic
27708008
INP1_YEASTINP1genetic
27708008
SCS7_YEASTSCS7genetic
27708008
NGL2_YEASTNGL2genetic
27708008
ELP6_YEASTELP6genetic
27708008
CTU2_YEASTNCS2genetic
27708008
NDJ1_YEASTNDJ1genetic
27708008
CSN10_YEASTRRI2genetic
27708008
VPS17_YEASTVPS17genetic
27708008
SUCA_YEASTLSC1genetic
27708008
SNC2_YEASTSNC2genetic
27708008
TRM44_YEASTTRM44genetic
27708008
PMA2_YEASTPMA2genetic
27708008
MGR2_YEASTMGR2genetic
27708008
ISU1_YEASTISU1genetic
27708008
FRK1_YEASTFRK1genetic
27708008
WDR6_YEASTRTT10genetic
27708008
EAF3_YEASTEAF3genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of APE2_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 THR-606, AND MASSSPECTROMETRY.

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