VPS39_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: VPS39_HUMAN
• UniProt AC: Q96JC1
• Protein Name: Vam6/Vps39-like protein
• Gene Name: VPS39
• Organism: Homo sapiens (Human).
• 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 ves
• Protein Description: 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. Does not affect TGF-beta-induced SMAD2 or SMAD3 phosphorylation, nor SMAD2/SMAD4 complex formation.; 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. [PubMed: 23351085 Involved in homotypic vesicle fusions between late endosomes and in heterotypic fusions between late endosomes and lysosomes]
• Protein Sequence: MHDAFEPVPILEKLPLQIDCLAAWEEWLLVGTKQGHLLLYRIRKDVVPADVASPESGSCNRFEVTLEKSNKNFSKKIQQIHVVSQFKILVSLLENNIYVHDLLTFQQITTVSKAKGASLFTCDLQHTETGEEVLRMCVAVKKKLQLYFWKDREFHELQGDFSVPDVPKSMAWCENSICVGFKRDYYLIRVDGKGSIKELFPTGKQLEPLVAPLADGKVAVGQDDLTVVLNEEGICTQKCALNWTDIPVAMEHQPPYIIAVLPRYVEIRTFEPRLLVQSIELQRPRFITSGGSNIIYVASNHFVWRLIPVPMATQIQQLLQDKQFELALQLAEMKDDSDSEKQQQIHHIKNLYAFNLFCQKRFDESMQVFAKLGTDPTHVMGLYPDLLPTDYRKQLQYPNPLPVLSGAELEKAHLALIDYLTQKRSQLVKKLNDSDHQSSTSPLMEGTPTIKSKKKLLQIIDTTLLKCYLHTNVALVAPLLRLENNHCHIEESEHVLKKAHKYSELIILYEKKGLHEKALQVLVDQSKKANSPLKGHERTVQYLQHLGTENLHLIFSYSVWVLRDFPEDGLKIFTEDLPEVESLPRDRVLGFLIENFKGLAIPYLEHIIHVWEETGSRFHNCLIQLYCEKVQGLMKEYLLSFPAGKTPVPAGEEEGELGEYRQKLLMFLEISSYYDPGRLICDFPFDGLLEERALLLGRMGKHEQALFIYVHILKDTRMAEEYCHKHYDRNKDGNKDVYLSLLRMYLSPPSIHCLGPIKLELLEPKANLQAALQVLELHHSKLDTTKALNLLPANTQINDIRIFLEKVLEENAQKKRFNQVLKNLLHAEFLRVQEERILHQQVKCIITEEKVCMVCKKKIGNSAFARYPNGVVVHYFCSKEVNPADT

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
141	Acetylation	LRMCVAVKKKLQLYF HHHHHHHHHHEEEEE	34.16	27452117
193 (in isoform 2)	Ubiquitination	-	45.05	21906983
202	Phosphorylation	SIKELFPTGKQLEPL CHHHCCCCCCCCCCE	50.07	-
204	Ubiquitination	KELFPTGKQLEPLVA HHCCCCCCCCCCEEE	54.94	2190698
204 (in isoform 1)	Ubiquitination	-	54.94	21906983
269	Phosphorylation	PRYVEIRTFEPRLLV CCEEEEEEECCEEEE	37.70	30622161
278	Phosphorylation	EPRLLVQSIELQRPR CCEEEEEEEEECCCE	15.56	30622161
339	Phosphorylation	EMKDDSDSEKQQQIH HCCCCCCCHHHHHHH	51.12	20873877
393	Ubiquitination	LLPTDYRKQLQYPNP CCCCCHHHHCCCCCC	49.48	-
411	Ubiquitination	LSGAELEKAHLALID CCCHHHHHHHHHHHH	54.45	-
434	Phosphorylation	LVKKLNDSDHQSSTS HHHHHCCCCCCCCCC	35.60	27732954
438	Phosphorylation	LNDSDHQSSTSPLME HCCCCCCCCCCCCCC	31.96	27732954
439	Phosphorylation	NDSDHQSSTSPLMEG CCCCCCCCCCCCCCC	26.74	25850435
440	Phosphorylation	DSDHQSSTSPLMEGT CCCCCCCCCCCCCCC	39.34	25850435
441	Phosphorylation	SDHQSSTSPLMEGTP CCCCCCCCCCCCCCC	20.27	25850435
447	Phosphorylation	TSPLMEGTPTIKSKK CCCCCCCCCCHHCHH	12.17	23312004
449	Phosphorylation	PLMEGTPTIKSKKKL CCCCCCCCHHCHHHH	40.66	17929957
452	Phosphorylation	EGTPTIKSKKKLLQI CCCCCHHCHHHHHHH	45.95	17929957
528	Ubiquitination	VLVDQSKKANSPLKG HHHHCHHHCCCCCCC	59.03	-
645	Ubiquitination	LLSFPAGKTPVPAGE HHHCCCCCCCCCCCC	52.33	-
646	Phosphorylation	LSFPAGKTPVPAGEE HHCCCCCCCCCCCCC	28.71	25159151
725	Ubiquitination	MAEEYCHKHYDRNKD HHHHHHHHHCCCCCC	40.06	-
781	Ubiquitination	VLELHHSKLDTTKAL HHHHCHHCCCHHHHH	46.13	-
786	Ubiquitination	HSKLDTTKALNLLPA HHCCCHHHHHHCCCC	53.63	-
806	Ubiquitination	DIRIFLEKVLEENAQ HHHHHHHHHHHHHHH	55.02	-
822	Ubiquitination	KRFNQVLKNLLHAEF HHHHHHHHHHHHHHH	46.85	-
843	Ubiquitination	RILHQQVKCIITEEK HHHHHHEEEEECCCC	18.51	-
879	Ubiquitination	VVHYFCSKEVNPADT EEEEEECCCCCCCCC	67.85	-

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

Oops, there are no upstream regulatory protein records of VPS39_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of VPS39_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VPS39_HUMAN	VPS39	physical	11448994
UVRAG_HUMAN	UVRAG	physical	18552835
XPO6_HUMAN	XPO6	physical	22939629
VPS11_HUMAN	VPS11	physical	28514442
KS6C1_HUMAN	RPS6KC1	physical	28514442
UBP54_HUMAN	USP54	physical	28514442
NPAT_HUMAN	NPAT	physical	28514442

Drug and Disease Associations

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