dbPTM

AP3B2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AP3B2_MOUSE
UniProt AC	Q9JME5
Protein Name	AP-3 complex subunit beta-2
Gene Name	Ap3b2
Organism	Mus musculus (Mouse).
Sequence Length	1082
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 non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals..
Protein Sequence	MSAAPAYSEDKGGSAGPGEPEYGHDPASGGIFSSDYKRHDDLKEMLDTNKDSLKLEAMKRIVAMIARGKNASDLFPAVVKNVACKNIEVKKLVYVYLVRYAEEQQDLALLSISTFQRGLKDPNQLIRASALRVLSSIRVPIIVPIMMLAIKEAASDMSPYVRKTAAHAIPKLYSLDSDQKDQLIEVIEKLLADKTTLVAGSVVMAFEEVCPERIDLIHKNYRKLCNLLIDVEEWGQVVIISMLTRYARTQFLSPTQNESLLEENPEKAFYGSEEDEAKGPGSEEAATAALPARKPYVMDPDHRLLLRNTKPLLQSRSAAVVMAVAQLYFHLAPKAEVGVIAKALVRLLRSHSEVQYVVLQNVATMSIKRRGMFEPYLKSFYIRSTDPTQIKILKLEVLTNLANETNIPTVLREFQTYIRSMDKDFVAATIQAIGRCATNIGRVRDTCLNGLVQLLSNRDELVVAESVVVIKKLLQMQPAQHGEIIKHLAKLTDNIQVPMARASILWLIGEYCEHVPKIAPDVLRKMAKSFTAEEDIVKLQVINLAAKLYLTNSKQTKLLTQYVLSLAKYDQNYDIRDRARFTRQLIVPSEQGGALSRHAKKLFLAPKPAPILESSFKDRDHFQLGSLSHLLNAKATGYQELPDWPEEAPDPSVRNVEVPEWTKCSNREKRKEKEKPFYSDSEGESGPTESADSEPESESESESKSSSGSGSGESSSESDNEEEDEEKGGGSESEQSEEEDEKKKKTKKKKASEGHREGSSSEEGSDSSSSSESEVTSESEEEQVEPASWRKKTPPGSKSAPVAKEISLLDLEDFTPPSVQPVSPPMVVSTSLAADLEGLTLTDSSLVPSLLSPVSSIGRQELLHRVAGEGLSVDYAFSRQPFSGDPHMVSLHIYFSNNSETPIKGLHVGTPKLPAGISIQEFPEIESLAPGESTTTVMGINFCDSTQAANFQLCTQTRQFYVSIQPPVGELMAPVFMSENEFKKEQGKLTGMNEITEKLTLPDTCRSDHMVVQKVTATANLGRVPCGTSDEYRFAGRTLTSGSLVLLTLDARAAGAAQLTVNSEKMVIGTMLVKDVIQALTQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
37	Ubiquitination	GIFSSDYKRHDDLKE CCCCCCCCCCHHHHH	48.52	22790023
135	Phosphorylation	ASALRVLSSIRVPII HHHHHHHHCCCCCCH	22.36	25159016
136	Phosphorylation	SALRVLSSIRVPIIV HHHHHHHCCCCCCHH	15.39	25159016
189	Ubiquitination	QLIEVIEKLLADKTT HHHHHHHHHHCCCCC	37.36	22790023
253	Phosphorylation	YARTQFLSPTQNESL HHHHHCCCCCCCHHH	27.47	29899451
259	Phosphorylation	LSPTQNESLLEENPE CCCCCCHHHHHHCHH	45.89	25521595
270	Phosphorylation	ENPEKAFYGSEEDEA HCHHHHCCCCHHCCC	25.30	25521595
272	Phosphorylation	PEKAFYGSEEDEAKG HHHHCCCCHHCCCCC	26.83	25521595
282	Phosphorylation	DEAKGPGSEEAATAA CCCCCCCCHHHHHHC	35.08	25521595
287	Phosphorylation	PGSEEAATAALPARK CCCHHHHHHCCCCCC	21.36	25619855
296	Phosphorylation	ALPARKPYVMDPDHR CCCCCCCCCCCCCHH	16.08	29899451
517	Ubiquitination	EYCEHVPKIAPDVLR HHHHCCCHHCHHHHH	50.87	-
554	Ubiquitination	KLYLTNSKQTKLLTQ HHHCCCCHHHHHHHH	65.15	-
601	Ubiquitination	ALSRHAKKLFLAPKP CCHHHHHHHHCCCCC	45.30	22790023
731	Phosphorylation	DEEKGGGSESEQSEE HHHCCCCCHHHHCHH	41.02	25521595
733	Phosphorylation	EKGGGSESEQSEEED HCCCCCHHHHCHHHH	42.50	25521595
736	Phosphorylation	GGSESEQSEEEDEKK CCCHHHHCHHHHHHH	42.81	25521595
760	Phosphorylation	EGHREGSSSEEGSDS HCCCCCCCCCCCCCC	53.26	28494245
761	Phosphorylation	GHREGSSSEEGSDSS CCCCCCCCCCCCCCC	41.17	28494245
793	Phosphorylation	PASWRKKTPPGSKSA CCCCCCCCCCCCCCC	37.44	22817900
910	Phosphorylation	IKGLHVGTPKLPAGI CCEEECCCCCCCCCC	19.03	25521595
1016	Phosphorylation	HMVVQKVTATANLGR CEEEEEEEEECCCCC	25.90	22871156

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 AP3B2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AP3B2_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 AP3B2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of AP3B2_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of AP3B2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272 AND SER-282, ANDMASS SPECTROMETRY.	17114649 [Abstract]