NUP62_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NUP62_MOUSE
• UniProt AC: Q63850
• Protein Name: Nuclear pore glycoprotein p62
• Gene Name: Nup62
• Organism: Mus musculus (Mouse).
• Sequence Length: 526
• Subcellular Localization: Nucleus, nuclear pore complex . Cytoplasm, cytoskeleton, spindle pole . Nucleus envelope . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Central region of the nuclear pore, within the transporter. During mitotic cell division,
• Protein Description: Essential component of the nuclear pore complex. The N-terminal is probably involved in nucleocytoplasmic transport. The C-terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of p62 to the pore complex. Plays a role in mitotic cell cycle progression by regulating centrosome segregation, centriole maturation and spindle orientation. It might be involved in protein recruitment to the centrosome after nuclear breakdown..
• Protein Sequence: MSGFNFGGTGAPAGGFTFGTAKTATTTPATGFSFSASGTGTGGFNFGTPSQPAATTPSTSLFSLTTQTPTTQTPGFNFGTTPASGGTGFSLGISTPKLSLSNAAATPATANTGSFGLGSSTLTNAISSGSTSNQGTAPTGFVFGSSTTSAPSTGSTGFSFTSGSASQPGASGFSLGSVGSSAQPTALSGSPFTPATLVTTTAGATQPAAAAPTAATTSAGSTLFASIAAAPASSSATGLSLPAPVTTAATPSAGTLGFSLKAPGAAPGASTTSTTTTTTTTTTTAAAAAASTTTTGFALSLKPLVSAGPSSVAATALPASSTAAGTATGPAMTYAQLESLINKWSLELEDQERHFLQQATQVNAWDRTLIENGEKITSLHREVEKVKLDQKRLDQELDFILSQQKELEDLLSPLEESVKEQSGTIYLQHADEEREKTYKLAENIDAQLKRMAQDLKDIIEHLNMAGGPADTSDPLQQICKILNAHMDSLQWVDQSSALLQRRVEEASRVCEGRRKEQERSLRIAFD

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
2	Acetylation	------MSGFNFGGT ------CCCCCCCCC	52.68	-
2	Phosphorylation	------MSGFNFGGT ------CCCCCCCCC	52.68	26643407
377	O-linked_Glycosylation	IENGEKITSLHREVE HHCCHHHHHHHHHHH	35.98	-
378	Phosphorylation	ENGEKITSLHREVEK HCCHHHHHHHHHHHH	26.17	25338131
412	Phosphorylation	KELEDLLSPLEESVK HHHHHHHHHHHHHHH	34.43	24925903
417	Phosphorylation	LLSPLEESVKEQSGT HHHHHHHHHHHHCCC	29.16	25159016
422	Phosphorylation	EESVKEQSGTIYLQH HHHHHHHCCCEEEEE	38.71	-
472	O-linked_Glycosylation	AGGPADTSDPLQQIC CCCCCCCCCHHHHHH	37.47	-
479	S-palmitoylation	SDPLQQICKILNAHM CCHHHHHHHHHHHCH	1.63	28680068

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

Oops, there are no upstream regulatory protein records of NUP62_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NUP62_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 NUP62_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NXF1_MOUSE	Nxf1	physical	11579093
NXT1_MOUSE	Nxt1	physical	11579093

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND MASSSPECTROMETRY.
PubMed: 19144319