AP2B_YEAST - dbPTM
AP2B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP2B_YEAST
UniProt AC P27351
Protein Name AP-2 complex subunit beta
Gene Name APL1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 700
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. Beta adaptin is a subunit of the plasma membrane adaptor..
Protein Sequence MSDQKVFARYKANEIVTDLQHFGVKKFKSNITRRKNALRKIIANLVLGNYGEMSVLFSELLKFWQIEDDLEVKRICHEYIRVIGALKPQQAREALPFIMDDFKSRDEKLQIMALRTLVLVPVKELSDQAFDCIISLVNHKSPPEQVTRTAIYALLDLDEIDHERVLGLSSILHDIVKAQSSSPEVIVAALHTLYSIHEKNANMEPFRIPLELAFDMLELLPELNEWNKATVLEVLTTSVVPQHYLDTHEMIELALPYLQQVNTYVVLNSLKFIMYLLNYVDVIKETLAEKLSNSVIALLDKPPELQFLVLRNVILLLLSRESSLLRLDISYFFIEYNDPIYIKDTKLECLYLLANKETLPRILEELEQYATDIDIQMSRKSVRAIGNLAVKLDEDSVHDCVAVLLDLLEFGVDYVVQEIISVFRNILRKYPNNFKANVTELVKHTEVVQEPESKNAMIWIITQYSDVIPNYLELFRVFSSNMFSETLEVQFSILNSAIKFFIRSPTKETEELCMDLLKGCIDHENNPDLRDKTLMYWRLLSLTKTSRISNAITFESLKSVLDGELPLIEMNTKLDPTVLEELELNIGTIVSIYLKPVSHIFRLNKTKLLPQSPILNPNKDLLPVVGNSFPPTGANRDRQNSESQSSTKSRKTAMMDDYDKPAEKINQLKGKRKSSSNNPSKLSRKPSTLLRKLSMKRPFS
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
87UbiquitinationIRVIGALKPQQAREA
HHHHHCCCHHHHHHH		40.0023749301
319PhosphorylationNVILLLLSRESSLLR
HHHHHHHCCCCHHHH		33.6926447709
322PhosphorylationLLLLSRESSLLRLDI
HHHHCCCCHHHHHEE		25.7726447709
323PhosphorylationLLLSRESSLLRLDIS
HHHCCCCHHHHHEEE		27.0326447709
330PhosphorylationSLLRLDISYFFIEYN
HHHHHEEEEEEEECC		18.6328889911
331PhosphorylationLLRLDISYFFIEYND
HHHHEEEEEEEECCC		11.6628889911
336PhosphorylationISYFFIEYNDPIYIK
EEEEEEECCCCEEEE		21.7628889911
341PhosphorylationIEYNDPIYIKDTKLE
EECCCCEEEECCHHH		13.8026447709
536PhosphorylationLRDKTLMYWRLLSLT
HHHHHHHHHHHHHHC		7.1828889911
541PhosphorylationLMYWRLLSLTKTSRI
HHHHHHHHHCCCCCC		38.2928889911
545PhosphorylationRLLSLTKTSRISNAI
HHHHHCCCCCCCCCC		20.2927017623
549PhosphorylationLTKTSRISNAITFES
HCCCCCCCCCCCHHH		21.0630377154
612PhosphorylationKTKLLPQSPILNPNK
CCCCCCCCCCCCCCC		16.3928889911
632PhosphorylationVGNSFPPTGANRDRQ
CCCCCCCCCCCCCCC		49.5221440633
641PhosphorylationANRDRQNSESQSSTK
CCCCCCCCCCCCCHH		30.2221440633
643PhosphorylationRDRQNSESQSSTKSR
CCCCCCCCCCCHHHC		34.8721440633
645PhosphorylationRQNSESQSSTKSRKT
CCCCCCCCCHHHCHH		49.6121551504
646PhosphorylationQNSESQSSTKSRKTA
CCCCCCCCHHHCHHH		32.0221440633
647PhosphorylationNSESQSSTKSRKTAM
CCCCCCCHHHCHHHH		37.9821440633
649PhosphorylationESQSSTKSRKTAMMD
CCCCCHHHCHHHHHC		38.8117287358
652PhosphorylationSSTKSRKTAMMDDYD
CCHHHCHHHHHCCCC		20.7617287358
660UbiquitinationAMMDDYDKPAEKINQ
HHHCCCCCHHHHHHH		39.6423749301
680PhosphorylationKSSSNNPSKLSRKPS
CCCCCCHHHHCCCHH		48.6421440633
683PhosphorylationSNNPSKLSRKPSTLL
CCCHHHHCCCHHHHH		41.8317287358
687PhosphorylationSKLSRKPSTLLRKLS
HHHCCCHHHHHHHHH		34.4225533186
688PhosphorylationKLSRKPSTLLRKLSM
HHCCCHHHHHHHHHC		38.0421440633
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 AP2B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP2B_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 AP2B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AP2S_YEASTAPS2physical
10564262
FKS1_YEASTFKS1physical
19822444
EDE1_YEASTEDE1physical
19822444
AP2A_YEASTAPL3physical
19822444
PMA1_YEASTPMA1physical
19822444
AP2M_YEASTAPM4physical
19822444
BMH2_YEASTBMH2physical
19822444
AP2S_YEASTAPS2physical
19822444
PMD1_YEASTPMD1physical
19822444
MRK1_YEASTMRK1genetic
20093466
RPN4_YEASTRPN4genetic
20093466
OCA6_YEASTOCA6genetic
20093466
XRS2_YEASTXRS2genetic
20093466
RL27B_YEASTRPL27Bgenetic
20093466
RS26B_YEASTRPS26Bgenetic
20093466
RL29_YEASTRPL29genetic
20093466
OST5_YEASTOST5genetic
20093466
PALF_YEASTRIM8genetic
20093466
CGR1_YEASTCGR1genetic
20093466
PIB2_YEASTPIB2genetic
20093466
ACBP_YEASTACB1genetic
20093466
PEX8_YEASTPEX8genetic
20093466
SLX9_YEASTSLX9genetic
20093466
YG34_YEASTYGR122Wgenetic
20093466
AMA1_YEASTAMA1genetic
20093466
SPG1_YEASTSPG1genetic
20093466
OCA5_YEASTOCA5genetic
20093466
MIP6_YEASTMIP6genetic
20093466
GIC1_YEASTGIC1genetic
20093466
PTPA1_YEASTRRD1genetic
20093466
PYR1_YEASTURA2genetic
20093466
PRY3_YEASTPRY3genetic
20093466
PYRD_YEASTURA1genetic
20093466
PEX13_YEASTPEX13genetic
20093466
CHS5_YEASTCHS5genetic
20093466
PYRC_YEASTURA4genetic
20093466
PYRE_YEASTURA5genetic
20093466
EAF7_YEASTEAF7genetic
20093466
YNL5_YEASTYNL115Cgenetic
20093466
RAS2_YEASTRAS2genetic
20093466
MKT1_YEASTMKT1genetic
20093466
NIS1_YEASTNIS1genetic
20093466
SIW14_YEASTSIW14genetic
20093466
HDA1_YEASTHDA1genetic
20093466
SWM2_YEASTSWM2genetic
20093466
HMI1_YEASTHMI1genetic
20093466
COQ10_YEASTCOQ10genetic
20093466
DFG16_YEASTDFG16genetic
20093466
VPS21_YEASTVPS21genetic
20093466
IAH1_YEASTIAH1genetic
20093466
LIPA_YEASTLIP5genetic
20093466
MDL2_YEASTMDL2genetic
20093466
AIM44_YEASTAIM44genetic
20093466
MED1_YEASTMED1genetic
20093466
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AP2B_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-687, AND MASSSPECTROMETRY.
"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-649; THR-652; SER-683AND SER-687, AND MASS SPECTROMETRY.

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