dbPTM

AP1M1_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AP1M1_RAT
UniProt AC	Q32Q06
Protein Name	AP-1 complex subunit mu-1
Gene Name	Ap1m1 {ECO:0000312\|RGD:1307653}
Organism	Rattus norvegicus (Rat).
Sequence Length	423
Subcellular Localization	Cytoplasmic vesicle, clathrin-coated vesicle membrane Peripheral membrane protein Cytoplasmic side. Golgi apparatus. 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 (By similarity)..
Protein Sequence	MSASAVYVLDLKGKVLICRNYRGDVDMSEVEHFMPILMEKEEEGMLSPILAHGGVRFMWIKHNNLYLVATSKKNACVSLVFSFLYKVVQVFSEYFKELEEESIRDNFVIIYELLDELMDFGYPQTTDSKILQEYITQEGHKLETGAPRPPATVTNAVSWRSEGIKYRKNEVFLDVIEAVNLLVSANGNVLRSEIVGSIKMRVFLSGMPELRLGLNDKVLFDNTGRGKSKSVELEDVKFHQCVRLSRFENDRTISFIPPDGEFELMSYRLNTHVKPLIWIESVIEKHSHSRIEYMVKAKSQFKRRSTANNVEIHIPVPNDADSPKFKTTVGSVKWVPENSEIVWSIKSFPGGKEYLMRAHFGLPSVEAEDKEGKPPISVKFEIPYFTTSGIQVRYLKIIEKSGYQALPWVRYITQNGDYQLRTQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSASAVYVL ------CCCCEEEEE	30.82	-
4	Phosphorylation	----MSASAVYVLDL ----CCCCEEEEEEC	15.80	26022182
7	Phosphorylation	-MSASAVYVLDLKGK -CCCCEEEEEECCCC	8.60	26022182
144	Phosphorylation	QEGHKLETGAPRPPA HCCCCCCCCCCCCCC	49.43	28432305
152	Phosphorylation	GAPRPPATVTNAVSW CCCCCCCEEEHHCCC	33.37	29779826
154	Phosphorylation	PRPPATVTNAVSWRS CCCCCEEEHHCCCCC	17.07	29779826
158	Phosphorylation	ATVTNAVSWRSEGIK CEEEHHCCCCCCCCC	17.86	28432305
223	Phosphorylation	DKVLFDNTGRGKSKS CEEEECCCCCCCCCC	30.05	25403869
274	Acetylation	YRLNTHVKPLIWIES EECCCCCCCEEEEEH	26.88	22902405
324	Acetylation	PNDADSPKFKTTVGS CCCCCCCCCCCEECE	64.54	22902405
396	Acetylation	GIQVRYLKIIEKSGY CCEEEEEEEHHHHCC	32.48	22902405

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_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AP1M1_RAT !!

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
MARHB_RAT	March11	physical	17604280

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of AP1M1_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites."; Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-152 AND THR-154, ANDMASS SPECTROMETRY.	16641100 [Abstract]