IMA1_MOUSE - dbPTM
IMA1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IMA1_MOUSE
UniProt AC P52293
Protein Name Importin subunit alpha-1 {ECO:0000305}
Gene Name Kpna2 {ECO:0000312|MGI:MGI:103561}
Organism Mus musculus (Mouse).
Sequence Length 529
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 MSTNENANLPAARLNRFKNKGKDSTEMRRRRIEVNVELRKAKKDEQMLKRRNVSSFPDDATSPLQENRNNQGTVNWSVEDIVKGINSNNLESQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGKTDCSPIQFESAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNIAGDGSAFRDLVIKHGAIDPLLALLAVPDLSTLACGYLRNLTWTLSNLCRNKNPAPPLDAVEQILPTLVRLLHHNDPEVLADSCWAISYLTDGPNERIEMVVKKGVVPQLVKLLGATELPIVTPALRAIGNIVTGTDEQTQKVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQIQQVVNHGLVPFLVGVLSKADFKTQKEAAWAITNYTSGGTVEQIVYLVHCGIIEPLMNLLSAKDTKIIQVILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQRHENESVYKASLNLIEKYFSVEEEEDQNVVPETTSEGFAFQVQDGAPGTFNF
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 Orthologous
Protein Cluster
2Acetylation------MSTNENANL
------CCCCCCCCC
43.22-
2Phosphorylation------MSTNENANL
------CCCCCCCCC
43.2222006019
3Phosphorylation-----MSTNENANLP
-----CCCCCCCCCC
34.4617242355
24PhosphorylationFKNKGKDSTEMRRRR
HHHCCCCCHHHHHHH
5.4227149854
25PhosphorylationKNKGKDSTEMRRRRI
HHCCCCCHHHHHHHH
27.2325266776
54PhosphorylationMLKRRNVSSFPDDAT
HHHHCCCCCCCCCCC
52.6027149854
55PhosphorylationLKRRNVSSFPDDATS
HHHCCCCCCCCCCCC
68.6926824392
61PhosphorylationSSFPDDATSPLQENR
CCCCCCCCCCCHHHC
5.1427087446
62PhosphorylationSFPDDATSPLQENRN
CCCCCCCCCCHHHCC
3.2325521595
73PhosphorylationENRNNQGTVNWSVED
HHCCCCCCCCCCHHH
29.7023984901
77PhosphorylationNQGTVNWSVEDIVKG
CCCCCCCCHHHHHHC
3.6723984901
108UbiquitinationRKLLSREKQPPIDNI
HHHHHCCCCCCCHHH
57.8422790023
108AcetylationRKLLSREKQPPIDNI
HHHHHCCCCCCCHHH
57.8423806337
126PhosphorylationGLIPKFVSFLGKTDC
CCHHHHHHHHCCCCC
25.2122006019
202UbiquitinationAFRDLVIKHGAIDPL
HHHHHHHHCCCCHHH
1.72-
240UbiquitinationLSNLCRNKNPAPPLD
HHHHHCCCCCCCCHH
6.7022790023
300UbiquitinationGVVPQLVKLLGATEL
CHHHHHHHHHCCCCC
37.65-
348UbiquitinationPSLLTNPKTNIQKEA
HHHHCCCCCCHHHHH
51.4522790023
459UbiquitinationEKLGETEKLSIMIEE
HHHCCCHHHHHHHHH
45.72-
483PhosphorylationLQRHENESVYKASLN
HHHCCCHHHHHHHHH
9.5427841257
486UbiquitinationHENESVYKASLNLIE
CCCHHHHHHHHHHHH
34.6122790023

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

Oops, there are no upstream regulatory protein records of IMA1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IMA1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of IMA1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LEF1_HUMANLEF1physical
8631802
PCY1A_MOUSEPcyt1aphysical
19332566
PLCB1_RATPlcb1physical
23665500
IMA1_MOUSEKpna2physical
23665500
IMB1_MOUSEKpnb1physical
23665500
TIF1B_HUMANTRIM28physical
25960296
CBX1_HUMANCBX1physical
25960296
SART3_HUMANSART3physical
27060135

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IMA1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND MASSSPECTROMETRY.

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