IMA5_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IMA5_MOUSE
• UniProt AC: Q60960
• Protein Name: Importin subunit alpha-5
• Gene Name: Kpna1
• Organism: Mus musculus (Mouse).
• Sequence Length: 538
• Subcellular Localization: Cytoplasm. Nucleus.
• Protein Description: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus..
• Protein Sequence: MSTPGKENFRLKSYKNKSLNPDEMRRRREEEGLQLRKQKREEQLFKRRNVATAEEETEEEVMSDGGFHEAQINNMEMAPGGVITSDMTDMIFSNSPEQQLSATQKFRKLLSKEPNPPIDEVINTPGVVARFVEFLKRKENCTLQFESAWVLTNIASGNSLQTRNVIQAGAVPIFIELLSSEFEDVQEQAVWALGNIAGDSTMCRDYVLNCNILPPLLQLFSKQNRLTMTRNAVWALSNLCRGKSPPPEFAKVSPCLNVLSWLLFVSDTDVLADACWALSYLSDGPNDKIQAVIDAGVCRRLVELLMHNDYKVVSPALRAVGNIVTGDDIQTQVILNCSALQSLLHLLSSPKESIKKEACWTISNITAGNRAQIQTVIDANMFPALISILQTAEFRTRKEAAWAITNATSGGSAEQIKYLVELGCIKPLCDLLTVMDAKIVQVALNGLENILRLGEQEAKRNGSGINPYCALIEEAYGLDKIEFLQSHENQEIYQKAFDLIEHYFGTEDEDSSIAPQVDLSQQQYIFQQCEAPMEGFQL

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
1	Acetylation	-------MSTPGKEN -------CCCCCCCC		-
2	Phosphorylation	------MSTPGKENF ------CCCCCCCCC		22006019
3	Phosphorylation	-----MSTPGKENFR -----CCCCCCCCCC		17242355
18	Phosphorylation	LKSYKNKSLNPDEMR CCCCCCCCCCHHHHH		29899451
42	Ubiquitination	LRKQKREEQLFKRRN HHHHHHHHHHHHHHC		27667366
63	Phosphorylation	ETEEEVMSDGGFHEA HCHHHHHHCCCCCHH		-
136	Ubiquitination	ARFVEFLKRKENCTL HHHHHHHHHHCCCEE		22790023
136	Acetylation	ARFVEFLKRKENCTL HHHHHHHHHHCCCEE		22826441
243	Ubiquitination	LSNLCRGKSPPPEFA HHHHHCCCCCCHHHH		27667366
244	Phosphorylation	SNLCRGKSPPPEFAK HHHHCCCCCCHHHHC		24899341
361	Phosphorylation	IKKEACWTISNITAG HHHHHCEEECCCCCC		25159016
363	Phosphorylation	KEACWTISNITAGNR HHHCEEECCCCCCCH		25159016
366	Phosphorylation	CWTISNITAGNRAQI CEEECCCCCCCHHHH		25159016
398	Ubiquitination	TAEFRTRKEAAWAIT HHHHHCHHHHHHHHH		22790023

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
-	K	Ubiquitination	E3 ubiquitin ligase	Rag1	P15919	PMID:22199232

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IMA5_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 IMA5_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LEF1_HUMAN	LEF1	physical	8631802
TIF1B_HUMAN	TRIM28	physical	25960296
CBX1_HUMAN	CBX1	physical	25960296

Drug and Disease Associations

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