AP2M_YEAST - dbPTM
AP2M_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP2M_YEAST
UniProt AC Q99186
Protein Name AP-2 complex subunit mu
Gene Name APM4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 491
Subcellular Localization Membrane, clathrin-coated pit. Cytoplasmic vesicle, clathrin-coated vesicle membrane.
Protein Description Component 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..
Protein Sequence MISGVLVYSSRGELVLNKFFKNSLKRSISDIFRVQVINNLDVRSPVLTLGSTTFHHIRSRHGDNLWLVTITRSNANSAAIWEFLYKLDAVMNAYRLDREEALKEEFMIVHEMLDIMLGGNGIPIDTELNSVIAQMSVKPVRNMGGLLDSPDGNDVLSSSSSPTSSAGELHFPKFLTKRSSSFLGQGDSTSDFYDNNKITWRPKGIIHKKDEVFLYVNERINILVSRDGSILKSYVDGTIDITTHLSGTPICRFGLNDSLGMQSEDEKKWLAQQQRHSGSDFGNKNFIPKAAAGSVLLEDCKFHECVSLDKFNRNHIIEFVPPDGSMELMKYHVRDNINLPFKVTPIVTHSTRDNEIDYRITLKSLFPGKLSAKDVVLHIPVPPSTVDCKISVSNGHCKFVPEENAMIWRFNKYNGLTENTLSAVTVSTSDTTQLNLQQWTRPPISLEFEVMMFSNSGLVVRYFTISGKDSKHRAVKWIKYISKAGSYEVRY
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
27PhosphorylationFKNSLKRSISDIFRV
HHHHHHHCHHHHHEE		25.5128889911
29PhosphorylationNSLKRSISDIFRVQV
HHHHHCHHHHHEEEE		26.3727214570
149PhosphorylationNMGGLLDSPDGNDVL
CCCCCCCCCCCCCCC		25.5125752575
157PhosphorylationPDGNDVLSSSSSPTS
CCCCCCCCCCCCCCC		28.2021440633
158PhosphorylationDGNDVLSSSSSPTSS
CCCCCCCCCCCCCCC		30.0321440633
159PhosphorylationGNDVLSSSSSPTSSA
CCCCCCCCCCCCCCC		31.3128889911
160PhosphorylationNDVLSSSSSPTSSAG
CCCCCCCCCCCCCCC		42.1428152593
161PhosphorylationDVLSSSSSPTSSAGE
CCCCCCCCCCCCCCC		33.8625752575
163PhosphorylationLSSSSSPTSSAGELH
CCCCCCCCCCCCCCC		36.9419779198
164PhosphorylationSSSSSPTSSAGELHF
CCCCCCCCCCCCCCC		22.9028889911
165PhosphorylationSSSSPTSSAGELHFP
CCCCCCCCCCCCCCC		42.6519779198
176PhosphorylationLHFPKFLTKRSSSFL
CCCCHHHCCCCCCCC		27.7820377248
179PhosphorylationPKFLTKRSSSFLGQG
CHHHCCCCCCCCCCC		31.7122369663
180PhosphorylationKFLTKRSSSFLGQGD
HHHCCCCCCCCCCCC		29.1925521595
181PhosphorylationFLTKRSSSFLGQGDS
HHCCCCCCCCCCCCC		26.2425521595
188PhosphorylationSFLGQGDSTSDFYDN
CCCCCCCCCHHCCCC		36.3122369663
189PhosphorylationFLGQGDSTSDFYDNN
CCCCCCCCHHCCCCC		36.7420377248
190PhosphorylationLGQGDSTSDFYDNNK
CCCCCCCHHCCCCCE		29.6720377248
193PhosphorylationGDSTSDFYDNNKITW
CCCCHHCCCCCEEEE		23.8119779198
277PhosphorylationLAQQQRHSGSDFGNK
HHHHHHHCCCCCCCC		42.0319823750
279PhosphorylationQQQRHSGSDFGNKNF
HHHHHCCCCCCCCCC		32.5521440633
466PhosphorylationVVRYFTISGKDSKHR
EEEEEEEECCCCHHH		36.4128889911
470PhosphorylationFTISGKDSKHRAVKW
EEEECCCCHHHHHHH		33.5728889911
480PhosphorylationRAVKWIKYISKAGSY
HHHHHHHHHHHCCCC		10.9926447709
482PhosphorylationVKWIKYISKAGSYEV
HHHHHHHHHCCCCCC		17.2326447709
486PhosphorylationKYISKAGSYEVRY--
HHHHHCCCCCCCC--		23.9926447709
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 AP2M_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP2M_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 AP2M_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PMM_YEASTSEC53physical
11805837
AP2B_YEASTAPL1physical
10564262
AP1M1_YEASTAPM1physical
10564262
AP2S_YEASTAPS2physical
10564262
AP2B_YEASTAPL1physical
16429126
REI1_YEASTREI1genetic
20093466
ATU1_YEASTPCA1genetic
20093466
RV161_YEASTRVS161genetic
20093466
PP2C1_YEASTPTC1genetic
20093466
RV167_YEASTRVS167genetic
20093466
SWI6_YEASTSWI6genetic
20093466
PHO23_YEASTPHO23genetic
20093466
EOS1_YEASTEOS1genetic
20093466
SWR1_YEASTSWR1genetic
21987634
VAC8_YEASTVAC8genetic
21987634
TDA5_YEASTTDA5genetic
21987634
MID2_YEASTMID2physical
24460703
KPC1_YEASTPKC1physical
25346786
AP2B_YEASTAPL1physical
25346786
CAN_YEASTNCE103physical
25346786
RAD18_YEASTRAD18physical
25346786
GEA1_YEASTGEA1physical
25346786
IF2P_YEASTFUN12physical
25346786
AK_YEASTHOM3physical
25346786
DMA1_YEASTDMA1physical
25346786
ATG11_YEASTATG11physical
25346786
SWI6_YEASTSWI6genetic
27708008
REI1_YEASTREI1genetic
27708008
RV161_YEASTRVS161genetic
27708008
RV167_YEASTRVS167genetic
27708008
UBP3_YEASTUBP3genetic
27708008
MRM2_YEASTMRM2genetic
27708008
YJ24_YEASTKCH1genetic
27708008
PFKA2_YEASTPFK2genetic
27708008
SUR1_YEASTSUR1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AP2M_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-179; SER-180 ANDSER-181, 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-277, 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-277, AND MASSSPECTROMETRY.

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