AP1M1_MOUSE - dbPTM
AP1M1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP1M1_MOUSE
UniProt AC P35585
Protein Name AP-1 complex subunit mu-1
Gene Name Ap1m1
Organism Mus musculus (Mouse).
Sequence Length 423
Subcellular Localization Golgi apparatus. Cytoplasmic vesicle, clathrin-coated vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.
Protein Description Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules..
Protein Sequence MSASAVYVLDLKGKVLICRNYRGDVDMSEVEHFMPILMEKEEEGMLSPILAHGGVRFMWIKHNNLYLVATSKKNACVSLVFSFLYKVVQVFSEYFKELEEESIRDNFVIIYELLDELMDFGYPQTTDSKILQEYITQEGHKLETGAPRPPATVTNAVSWRSEGIKYRKNEVFLDVIEAVNLLVSANGNVLRSEIVGSIKMRVFLSGMPELRLGLNDKVLFDNTGRGKSKSVELEDVKFHQCVRLSRFENDRTISFIPPDGEFELMSYRLNTHVKPLIWIESVIEKHSHSRIEYMVKAKSQFKRRSTANNVEIHIPVPNDADSPKFKTTVGSVKWVPENSEIVWSVKSFPGGKEYLMRAHFGLPSVEAEDKEGKPPISVKFEIPYFTTSGIQVRYLKIIEKSGYQALPWVRYITQNGDYQLRTQ
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
2Acetylation------MSASAVYVL
------CCCCEEEEE
30.82-
12AcetylationAVYVLDLKGKVLICR
EEEEEECCCCEEEEC
57.2523954790
12SuccinylationAVYVLDLKGKVLICR
EEEEEECCCCEEEEC
57.2523954790
144PhosphorylationQEGHKLETGAPRPPA
HCCCCCCCCCCCCCC
49.4325619855
152PhosphorylationGAPRPPATVTNAVSW
CCCCCCCEEEHHCCC
33.3725521595
154PhosphorylationPRPPATVTNAVSWRS
CCCCCEEEHHCCCCC
17.0725521595
158PhosphorylationATVTNAVSWRSEGIK
CEEEHHCCCCCCCCC
17.8625619855
165MalonylationSWRSEGIKYRKNEVF
CCCCCCCCCCCCCCH
50.2726320211
165AcetylationSWRSEGIKYRKNEVF
CCCCCCCCCCCCCCH
50.2715618271
223PhosphorylationDKVLFDNTGRGKSKS
CEEEECCCCCCCCCC
30.0525521595
229MalonylationNTGRGKSKSVELEDV
CCCCCCCCCEEHHHC
63.1026320211
245PhosphorylationFHQCVRLSRFENDRT
EEEEEEHHHCCCCCE
25.1023140645
296PhosphoglycerylationSRIEYMVKAKSQFKR
CCHHHHHHCHHHHCC
33.30-
322PhosphorylationPVPNDADSPKFKTTV
CCCCCCCCCCCCCEE
31.5430635358
324AcetylationPNDADSPKFKTTVGS
CCCCCCCCCCCEECE
64.5423954790
326UbiquitinationDADSPKFKTTVGSVK
CCCCCCCCCEECEEE
49.79-
326MalonylationDADSPKFKTTVGSVK
CCCCCCCCCEECEEE
49.7926320211
384PhosphorylationSVKFEIPYFTTSGIQ
EEEEEECEEECCCCE
21.1520531401
386PhosphorylationKFEIPYFTTSGIQVR
EEEECEEECCCCEEE
17.7620531401
388PhosphorylationEIPYFTTSGIQVRYL
EECEEECCCCEEEEE
30.7325367039
396MalonylationGIQVRYLKIIEKSGY
CCEEEEEEEHHHHCC
32.4826320211
400UbiquitinationRYLKIIEKSGYQALP
EEEEEHHHHCCCCCC
38.4822790023

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 AP1M1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP1M1_MOUSE !!

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 AP1M1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AP1M1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AP1M1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-152 AND THR-154, ANDMASS SPECTROMETRY.

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