VPS39_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: VPS39_MOUSE
• UniProt AC: Q8R5L3
• Protein Name: Vam6/Vps39-like protein
• Gene Name: Vps39
• Organism: Mus musculus (Mouse).
• Sequence Length: 886
• Subcellular Localization: Cytoplasm . Lysosome membrane ; Peripheral membrane protein . Late endosome membrane ; Peripheral membrane protein . Late endosome . Lysosome . Colocalizes with TGFBR1 and TGFBR2 in cytoplasmic vesicular structures and most prominently in cortical ve
• Protein Description: May play a role in clustering and fusion of late endosomes and lysosomes (By similarity). Regulator of TGF-beta/activin signaling, inhibiting SMAD3- and activating SMAD2-dependent transcription. Acts by interfering with SMAD3/SMAD4 complex formation, this would lead to inhibition of SMAD3-dependent transcription and relieve SMAD3 inhibition of SMAD2-dependent promoters, thus increasing SMAD2-dependent transcription (By similarity).; Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act in part as a component of the putative HOPS endosomal tethering complex which is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. Involved in homotypic vesicle fusions between late endosomes and in heterotypic fusions between late endosomes and lysosomes. Required for fusion of endosomes and autophagosomes with lysosomes (By similarity)..
• Protein Sequence: MHDAFEPVPILEKLPLQIDCLAAWEEWLLVGTKQGHLLLYRIRKDVVPADVASPESGSCNRFEVTLEKSNKNFSKKIQQIHVVSQFKILVSLLENNIYVHDLLTFQQITTVSKAKGASLFTCDLQHTETGEEVLRMCVAVRKKLQLYFWKDREFHELQGDFSVPDVPKSMAWCENSICVGFKRDYYLIRVDGKGSIKELFPTGKQLEPLVAPLADGKVAVGQDDLTVVLNEEGICTQKCALNWTDIPVAMEHQPPYIVAVLPRYVEIRTLEPRLLVQSIELQRPRFITSGGSNIIYVASNHFVWRLIPVPMATQIQQLLQDKQFELALQLAEMKDDSDSEKQQQIHHIKNLYAFNLFCQKRFDESMQVFAKLGTDPTHVMGLYPDLLPTDYRKQLQYPNPLPTLSGAELEKAHLALIDYLTQKRSQLVKKLNDSDHQSSTSPLMEGTPTIKSKKKLLQIIDTTLLKCYLHTNVALVAPLLRLENNHCHIEESEHVLKKAHKYSELIILYEKKGLHEKALQVLVDQSKKANSPLKGHERTVQYLQHLGTENLHLIFSYSVWVLRDFPEDGLKIFTEDLPEVESLPRDRVLNFLIENFKALAIPYLEHIIHVWEETGSQFHNCLIQLYCEKVQSLMKDYLLSLPTGKSPVPAGEEGGELGEYRQKLLMFLEISSHYDPGRLICDFPFDGLLEERALLLGRMGKHEQALFIYVHVLKDTKMAKEYCHKHYDQNKEGNKDVYLSLLRMYLSPPSIHCLGPIKLELLEPQANLQAALQVLELHYSKLDTTKAINLLPANTQINDIRIFLEKVLEENAQKKRFNQVLKNLLHAEFLRVQEERILHQQVKCIITEEKVCMVCKKKIGNSAFARYPNGVVVHYFCSKEVNSADT

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
204	Ubiquitination	KELFPTGKQLEPLVA HHCCCCCCCCCCEEE	54.94	-
434	Phosphorylation	LVKKLNDSDHQSSTS HHHHHCCCCCCCCCC	35.60	29899451
438	Phosphorylation	LNDSDHQSSTSPLME HCCCCCCCCCCCCCC	31.96	29899451
439	Phosphorylation	NDSDHQSSTSPLMEG CCCCCCCCCCCCCCC	26.74	20415495
440	Phosphorylation	DSDHQSSTSPLMEGT CCCCCCCCCCCCCCC	39.34	20415495
441	Phosphorylation	SDHQSSTSPLMEGTP CCCCCCCCCCCCCCC	20.27	22817900
447	Phosphorylation	TSPLMEGTPTIKSKK CCCCCCCCCCHHCHH	12.17	29899451
646	Phosphorylation	LSLPTGKSPVPAGEE HCCCCCCCCCCCCCC	32.26	29899451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of VPS39_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of VPS39_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of VPS39_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of VPS39_MOUSE !!

Drug and Disease Associations

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