Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Importin subunit alpha-3  

UniProtKB / Swiss-Prot ID :  IMA3_HUMAN

Gene Name (Synonyms) : 
KPNA3, QIP2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm (By similarity). Nucleus (By similarity). 

Protein Function :  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. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non- classical NLS. Recognizes NLSs of influenza A virus nucleoprotein probably through ARM repeats 7-9. 

Protein Sequence MAENPSLENHRIKSFKNKGRDVETMRRHRNEVTVELRKNKRDEHLLKKRNVPQEESLEDSDVDADFKAQN...
Predicted Secondary Structure CCCCCCCHHHHHHHHHHCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCHHHCCCCCHHHHHHHHH...
Protein Variant
LocationDescription
291P -> S (in dbSNP:rs1043015). VAR_014454
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAENPS
---CCCCCC
25.85UniProtKB
Link-
6PhosphoserineAENPSLENH
CCCCCCHHH
60.95Phosphositeplus
Link-
24PhosphothreonineRDVETMRRH
CCHHHHHHH
18.80HPRD
Link-
24PhosphothreonineRDVETMRRH
CCHHHHHHH
18.80SysPTM
Link-
56PhosphoserinePQEESLEDS
CCHHHCCCC
35.98HPRD
Link-
56PhosphoserinePQEESLEDS
CCHHHCCCC
35.98PhosphoELM
Link-
56PhosphoserinePQEESLEDS
CCHHHCCCC
35.98Phosphositeplus
Link-
56PhosphoserinePQEESLEDS
CCHHHCCCC
35.98SysPTM
Link-
56Phosphoserine.PQEESLEDS
CCHHHCCCC
35.98UniProtKB
Link-
60PhosphoserineSLEDSDVDA
HCCCCCHHH
30.11HPRD
Link-
60PhosphoserineSLEDSDVDA
HCCCCCHHH
30.11PhosphoELM
Link-
60PhosphoserineSLEDSDVDA
HCCCCCHHH
30.11Phosphositeplus
Link-
60PhosphoserineSLEDSDVDA
HCCCCCHHH
30.11SysPTM
Link-
60Phosphoserine.SLEDSDVDA
HCCCCCHHH
30.11UniProtKB
Link-
425PhosphoserineSVKDSQVVQ
CCCCHHHHH
21.11Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
MDM4_HUMANphysical interactionMINT-1958692MINT16511560
NFKB1_HUMANphysical interactionMINT-48648MINT14743216
NFKB1_HUMANphysical interactionDIP:44838EDIP14743216
TGM2_HUMANin vivo
yeast 2-hybrid
HPRD:03536HPRD10100610
FA50B_HUMANyeast 2-hybridHPRD:03536HPRD16189514
RCC1_HUMANin vitroHPRD:03536HPRD10744690
P80C_HUMANyeast 2-hybridHPRD:03536HPRD16713569
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-56 AND SER-60, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-60, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-56 AND SER-60, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-60, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures