AP2A_YEAST - dbPTM
AP2A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP2A_YEAST
UniProt AC P38065
Protein Name AP-2 complex subunit alpha
Gene Name APL3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1025
Subcellular Localization Cell membrane. Membrane, coated pit
Peripheral membrane protein
Cytoplasmic side. Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane.
Protein Description Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Alpha adaptin is a subunit of the plasma membrane adaptor. Facilitates interaction between APL1 and APS2..
Protein Sequence MDRKKTLINSSVSNNNSTIKGLQLFIADLRSAQQAQEQEKRIQSEIVKIKQHFDAAKKKQGNHDRLGGYQRKKYVAKLAYIYITSNTTKLNEILFGLEQTVELLKSSIFSEKFIGYMTLELLYERSEVVAKVNDEVNYQLMKDLSSSDDNFVMLALNFVGVVGELTNRLAYNDDITTGVFKILRSPTSSIYLKKKSALSFLALLKSNHSILTEDLQRKQLWIQRILSLLDDTENYRLTLATIPLIEFIAKYIDPSYCTRLLPQLTEILYNCVVVGTSRSSDNQFPLEYTFANMPNPWLITKVVSLLSILIASPTERDSGSLLQTNNIDNELLNKLRKCVSVAIELGTRQAQDPMERIVQNTVLFSLINFASKLDPSDEAISNSVTALCSLLTSKEINIRYLTLDSLVKLCSSSGKPAIDAVRYKNLDMIFHLLNTERDSSIVRKVVDLLYTFTDVENVKIIVDGLLQYILSPKNLAEPQIKSDIAVKIAILTEKYATDINWFVIISLQLLSLTSNTTINDDEIWQRLCQIVVNNPSLHRITCERLVDYLCKKQASEAIIKAAAFLLGEYSSLITDRISSANLFTLFAEKYFSAPNVAKAMILTTMIKLYKTSPEIGSNVIKFFQLELNSLDIELQTRSFEYLNIIQLAKVNGNTDILQILFEPMPPFNSKSNPLLKRLGSLPASAGSTTLINTPSEASSSTPDLLSKRANSSRSIMVPMPPPSRRNTIDDVNSKISSSEDFSGKDSYYSRQILAPNWREGFTRMISHKQGVLFTSSLMKVFYRITTPDAQQPYVFHISLAFINLTEWEITGLSTQIIPSKTQGNPEYLIMNINTPSTATIGPHKRAEQSYEVSIRKPFDVEDSPILAIHFKCGGSTNTINLKTAIGMTTTLISSDVNPSMHLNLAQFISRWKTLSDALGKEGEYQKSGIKLNKDFRKVETISLEDGLLLLTQTVKRLGFDIVDQTSVRSTLFVSGIIHTKSEGNFGCLMKIQYQVNGTVNVTCKTTTAGPLAKYIVECIKNVLTK
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
6Phosphorylation--MDRKKTLINSSVS
--CCCCHHHCCCCCC		35.5925521595
80PhosphorylationKYVAKLAYIYITSNT
HHHHHEEEEEECCCC		12.5127017623
82PhosphorylationVAKLAYIYITSNTTK
HHHEEEEEECCCCCH		5.8627017623
84PhosphorylationKLAYIYITSNTTKLN
HEEEEEECCCCCHHH		10.0427017623
87PhosphorylationYIYITSNTTKLNEIL
EEEECCCCCHHHHHH		25.6927017623
279PhosphorylationVVVGTSRSSDNQFPL
EEECCCCCCCCCCCE		41.6423749301
280PhosphorylationVVGTSRSSDNQFPLE
EECCCCCCCCCCCEE		39.2023749301
288PhosphorylationDNQFPLEYTFANMPN
CCCCCEEEEECCCCC		18.1623749301
318PhosphorylationASPTERDSGSLLQTN
CCCCCCCCCCCCCCC		36.1830377154
320PhosphorylationPTERDSGSLLQTNNI
CCCCCCCCCCCCCCC		29.8328889911
415UbiquitinationKLCSSSGKPAIDAVR
HHHHCCCCCCCHHHH		32.9723749301
555PhosphorylationYLCKKQASEAIIKAA
HHHHHHHHHHHHHHH		25.6821126336
592PhosphorylationLFAEKYFSAPNVAKA
HHHHHHCCCCHHHHH		39.4621126336
680PhosphorylationPLLKRLGSLPASAGS
HHHHHHCCCCCCCCC		35.4522369663
684PhosphorylationRLGSLPASAGSTTLI
HHCCCCCCCCCEEEE		31.0922369663
687PhosphorylationSLPASAGSTTLINTP
CCCCCCCCEEEECCC		20.2422369663
688PhosphorylationLPASAGSTTLINTPS
CCCCCCCEEEECCCC		25.3822369663
689PhosphorylationPASAGSTTLINTPSE
CCCCCCEEEECCCCH		27.6020377248
693PhosphorylationGSTTLINTPSEASSS
CCEEEECCCCHHCCC		22.6222369663
695PhosphorylationTTLINTPSEASSSTP
EEEECCCCHHCCCCH		43.7022369663
698PhosphorylationINTPSEASSSTPDLL
ECCCCHHCCCCHHHH		22.2925521595
699PhosphorylationNTPSEASSSTPDLLS
CCCCHHCCCCHHHHH		45.3325521595
700PhosphorylationTPSEASSSTPDLLSK
CCCHHCCCCHHHHHH		41.2725521595
701PhosphorylationPSEASSSTPDLLSKR
CCHHCCCCHHHHHHH		23.8325521595
706PhosphorylationSSTPDLLSKRANSSR
CCCHHHHHHHCCCCC		27.6522369663
707UbiquitinationSTPDLLSKRANSSRS
CCHHHHHHHCCCCCC		56.3423749301
712PhosphorylationLSKRANSSRSIMVPM
HHHHCCCCCCEEECC		29.8319779198
714PhosphorylationKRANSSRSIMVPMPP
HHCCCCCCEEECCCC		19.5828889911
723PhosphorylationMVPMPPPSRRNTIDD
EECCCCCCCCCCHHH		50.0423749301
727PhosphorylationPPPSRRNTIDDVNSK
CCCCCCCCHHHHHHH		24.7922369663
733PhosphorylationNTIDDVNSKISSSED
CCHHHHHHHCCCCCC		31.0822369663
736PhosphorylationDDVNSKISSSEDFSG
HHHHHHCCCCCCCCC		31.3922369663
737PhosphorylationDVNSKISSSEDFSGK
HHHHHCCCCCCCCCC		41.0222369663
738PhosphorylationVNSKISSSEDFSGKD
HHHHCCCCCCCCCCC		34.1022369663
742PhosphorylationISSSEDFSGKDSYYS
CCCCCCCCCCCCCHH		58.2022369663
774PhosphorylationHKQGVLFTSSLMKVF
HCCCEEEEHHHHHHH		17.1619823750
775PhosphorylationKQGVLFTSSLMKVFY
CCCEEEEHHHHHHHH		17.7219795423
776PhosphorylationQGVLFTSSLMKVFYR
CCEEEEHHHHHHHHH		29.4419823750
821PhosphorylationTQIIPSKTQGNPEYL
EEECCCCCCCCCCEE		46.1527017623
827PhosphorylationKTQGNPEYLIMNINT
CCCCCCCEEEEECCC		11.6427017623
834PhosphorylationYLIMNINTPSTATIG
EEEEECCCCCCCEEC		18.1527017623
836PhosphorylationIMNINTPSTATIGPH
EEECCCCCCCEECCC		28.7427017623
839PhosphorylationINTPSTATIGPHKRA
CCCCCCCEECCCCCC		26.9327017623
912UbiquitinationAQFISRWKTLSDALG
HHHHHHHHHHHHHHC		38.1824961812
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 AP2A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP2A_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 AP2A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AP2B_YEASTAPL1physical
11805826
AP2M_YEASTAPM4physical
11805826
AP2S_YEASTAPS2physical
11805826
IST1_YEASTIST1physical
16554755
AP2M_YEASTAPM4physical
16554755
AMPL_YEASTAPE1physical
18719252
IRC6_YEASTIRC6physical
18719252
ATIF_YEASTINH1genetic
20093466
PAR32_YEASTPAR32genetic
20093466
IME1_YEASTIME1genetic
20093466
ERG2_YEASTERG2genetic
20093466
ZRC1_YEASTZRC1genetic
20093466
TPM1_YEASTTPM1genetic
20093466
TRM11_YEASTTRM11genetic
20093466
WHI5_YEASTWHI5genetic
20093466
YO214_YEASTSPR2genetic
20093466
AP2A_YEASTAPL3physical
22940862
AP2M_YEASTAPM4physical
22940862
TRM11_YEASTTRM11genetic
27708008
AIM2_YEASTAIM2genetic
27708008
GPR1_YEASTGPR1genetic
27708008
PEX19_YEASTPEX19genetic
27708008
PAR32_YEASTPAR32genetic
27708008
YEW0_YEASTCOM2genetic
27708008
MED5_YEASTNUT1genetic
27708008
PIH1_YEASTPIH1genetic
27708008
IME1_YEASTIME1genetic
27708008
SRN2_YEASTSRN2genetic
27708008
MSC1_YEASTMSC1genetic
27708008
ZRC1_YEASTZRC1genetic
27708008
PLB3_YEASTPLB3genetic
27708008
LSP1_YEASTLSP1genetic
27708008
MDL2_YEASTMDL2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AP2A_YEAST

loading...

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-320; SER-698; SER-700;THR-701; SER-723; THR-727; SER-736; SER-737 AND SER-738, AND MASSSPECTROMETRY.
"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-698; SER-700; THR-727AND SER-738, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory