UBXN6_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UBXN6_MOUSE
• UniProt AC: Q99PL6
• Protein Name: UBX domain-containing protein 6 {ECO:0000305}
• Gene Name: Ubxn6 {ECO:0000312|MGI:MGI:1913780}
• Organism: Mus musculus (Mouse).
• Sequence Length: 442
• Subcellular Localization: Cytoplasm . Cytoplasm, cytosol . Membrane ; Peripheral membrane protein . Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Early endosome membrane ; Peripheral membrane protein . Late endosome membrane ; Peripheral membrane p
• Protein Description: May negatively regulate the ATPase activity of VCP, an ATP-driven segregase that associates with different cofactors to control a wide variety of cellular processes. As a cofactor of VCP, it may play a role in the transport of CAV1 to lysosomes for degradation. It may also play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Together with VCP and other cofactors, it may play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes..
• Protein Sequence: MKKFFQEIKADIKFKSAGPGQKLTDSAGEKTTKGKSPQLALRQPRQGPTDEAQMAAAAALARLEQKQPRARGPTSQDSIRNQVRKELQAEATSSNNPGAPGTNSVPEPKEEISPHLAVPGVFFICPLTGVTLRRDQRDAHIKQAILSHFSTDPVAASIMKIHTFNRDRDRVKLGVDTIAKYLDNIHLHPEEEKYQKIKLQNKVFQERINCLEGSHEFFEAIGFKKVTLPVPDQEGQEEFYVLGEDARAQPQNLARHKQQLLDAEPVRATLDRQLRVFRPSALASHFELPSDFFSLTAEEVKREQRLRTEAVERLSSLRTKAMREKEEQRELRKYTYALVRVRLPDGCLLQGTFYAREKLSALFRFVREALQNDWLPFELRASGGQKLEENEALALNECGLVPSALLTFSWDASVLEDIRAAGAEPAKSVLRPELLAAIEQLS

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
36	Phosphorylation	EKTTKGKSPQLALRQ CCCCCCCCHHHHHCC	26.92	26824392
74	Phosphorylation	QPRARGPTSQDSIRN CHHHCCCCCHHHHHH	41.67	30635358
75	Phosphorylation	PRARGPTSQDSIRNQ HHHCCCCCHHHHHHH	34.81	29899451
78	Phosphorylation	RGPTSQDSIRNQVRK CCCCCHHHHHHHHHH	18.79	22324799
92	Phosphorylation	KELQAEATSSNNPGA HHHHHHHHCCCCCCC	24.96	23567750
94	Phosphorylation	LQAEATSSNNPGAPG HHHHHHCCCCCCCCC	35.95	23567750
102	Phosphorylation	NNPGAPGTNSVPEPK CCCCCCCCCCCCCCH	24.22	23567750
113	Phosphorylation	PEPKEEISPHLAVPG CCCHHHCCCCCCCCE	15.00	22817900
160	Ubiquitination	PVAASIMKIHTFNRD HHHHHHHHHEECCCC	29.66	22790023
194	Phosphorylation	LHPEEEKYQKIKLQN CCCCHHHHHHHHHHH	20.51	-
315	Phosphorylation	TEAVERLSSLRTKAM HHHHHHHHHHHHHHH	33.28	28725479
316	Phosphorylation	EAVERLSSLRTKAMR HHHHHHHHHHHHHHH	26.85	28725479
319	Phosphorylation	ERLSSLRTKAMREKE HHHHHHHHHHHHHHH	28.57	-
333	Malonylation	EEQRELRKYTYALVR HHHHHHHHHCEEEEE	55.35	26320211
442	Phosphorylation	LAAIEQLS------- HHHHHHHC-------	37.56	22324799

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

Oops, there are no upstream regulatory protein records of UBXN6_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UBXN6_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 UBXN6_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of UBXN6_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASSSPECTROMETRY.
PubMed: 19367708