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-4  

UniProtKB / Swiss-Prot ID :  IMA4_HUMAN

Gene Name (Synonyms) : 
KPNA4, QIP1  

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. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a nonclassical NLS. 

Protein Sequence MADNEKLDNQRLKNFKNKGRDLETMRRQRNEVVVELRKNKRDEHLLKRRNVPHEDICEDSDIDGDYRVQN...
Predicted Secondary Structure CCCCCCCCHHHHHHHHCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCHHHHHHHHHHC...
Protein Variant -
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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
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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.---MADNEK
---CCCCCC
28.47UniProtKB
Link-
60PhosphoserineICEDSDIDG
CCCCHHHHH
17.74HPRD
Link-
60PhosphoserineICEDSDIDG
CCCCHHHHH
17.74PhosphoELM
Link-
60PhosphoserineICEDSDIDG
CCCCHHHHH
17.74Phosphositeplus
Link-
60PhosphoserineICEDSDIDG
CCCCHHHHH
17.74SysPTM
Link-
60Phosphoserine.ICEDSDIDG
CCCCHHHHH
17.74UniProtKB
Link-
66PhosphotyrosineIDGDYRVQN
HHHHHHHHC
20.43HPRD
Link-
66PhosphotyrosineIDGDYRVQN
HHHHHHHHC
20.43PhosphoELM
Link-
66PhosphotyrosineIDGDYRVQN
HHHHHHHHC
20.43Phosphositeplus
Link-
71PhosphothreonineRVQNTSLEA
HHHCCHHHH
20.00HPRD
Link-
221PhosphothreonineLRNVTWVMV
HHHHHHHHH
18.85Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
NFKB1_HUMANphysical interactionMINT-48538MINT14743216
NFKB1_HUMANphysical interactionMINT-48651MINT14743216
TGM2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:04275HPRD10100610
RECQ1_HUMANin vitro
yeast 2-hybrid
HPRD:04275HPRD9168958
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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, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-60, AND MASSSPECTROMETRY.
"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-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