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KPNA4 karyopherin subunit alpha 4 [ Homo sapiens (human) ]

Gene ID: 3840, updated on 8-May-2016
Official Symbol
KPNA4provided by HGNC
Official Full Name
karyopherin subunit alpha 4provided by HGNC
Primary source
See related
Ensembl:ENSG00000186432 HPRD:04275; MIM:602970; Vega:OTTHUMG00000159033
Gene type
protein coding
RefSeq status
Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
The nuclear import of karyophilic proteins is directed by short amino acid sequences termed nuclear localization signals (NLSs). Karyopherins, or importins, are cytoplasmic proteins that recognize NLSs and dock NLS-containing proteins to the nuclear pore complex. The protein encoded by this gene shares the sequence similarity with Xenopus importin-alpha and Saccharomyces cerevisiae Srp1. This protein is found to interact with the NLSs of DNA helicase Q1 and SV40 T antigen. [provided by RefSeq, Jul 2008]
Exon count:
Annotation release Status Assembly Chr Location
107 current GRCh38.p2 (GCF_000001405.28) 3 NC_000003.12 (160494995..160565588, complement)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 3 NC_000003.11 (160212783..160283376, complement)

Chromosome 3 - NC_000003.12Genomic Context describing neighboring genes Neighboring gene tripartite motif containing 59 Neighboring gene beta-1,3-glucuronyltransferase 3 pseudogene 1 Neighboring gene small Cajal body-specific RNA 7 Neighboring gene keratin 8 pseudogene 12 Neighboring gene ribosomal protein L6 pseudogene 8

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?


Genome-Wide Association Study of Primary Dentition Pit-and-Fissure and Smooth Surface Caries.

Protein interactions

Protein Gene Interaction Pubs
Rev rev HIV-1 Rev interacting protein, karyopherin alpha 4 (KPNA4), is identified by the in-vitro binding experiments involving cytosolic or nuclear extracts from HeLa cells PubMed
Vpr vpr Full-length Vpr interacts with QIP1 through its binding to the C-terminal domain (residues 392-537) of QIP1 PubMed
integrase gag-pol HIV-1 Integrase (IN) double mutant KK215/219AA and RK263/264AA severely impairs its binding to importin 3 alpha. W179A/N183A and W348A/N352A mutations in the major and the minor NLS binding grooves of Imp alpha3 significantly reduce its binding to IN PubMed
gag-pol HIV-1 IN interacts with importin alpha by the BiFC assay and amino acids 161-173 in IN are required for the interaction with importin alpha PubMed
gag-pol A region encompassing amino acids 251-270 in the C-terminal domain of HIV-1 IN is required for importin alpha3 binding and for nuclear localization PubMed
gag-pol HIV-1 Rev disrupts both IN-TNPO3 and IN-importin alpha complexes PubMed
gag-pol Some reports indicate a possible role for the interactions between karyopherin alpha and beta with HIV-1 integrase in the nuclear import of HIV-1 preintegration complexes (PIC), while other reports indicate integrase is not involved in PIC nuclear import PubMed
gag-pol Karyopherin alpha binds to a bipartite nuclear localization signal in HIV-1 integrase (amino acids 186-189 and 211-219) PubMed
gag-pol Karyopherin alpha and beta are reported to interact with HIV-1 integrase (IN) to facilitate nuclear import of IN, however a conflicting report indicates nuclear accumulation of IN does not involve karyopherin alpha, beta 1, or beta 2 mediated pathways PubMed
matrix gag Nuclear import of HIV-1 preintegration complexes by karyopherin alpha is governed by phosphorylation of HIV-1 Matrix on tyrosine and serine, however the exact role of phosphorylation of the C-terminal tyrosine of Matrix has been debated PubMed
gag HIV-1 Matrix increases intracellular ATP content, an effect hypothesized to support the ATP-dependent nuclear import of HIV-1 preintegration complexes by karyopherin alpha PubMed
gag HIV-1 Vpr increases the affinity of karyopherin alpha to the HIV-1 Matrix nuclear localization signal, thereby mediating the nuclear import of HIV-1 preintegration complexes PubMed
gag Hsp70 stimulates the binding of HIV-1 matrix to karyopherin alpha PubMed
gag The role of HIV-1 Matrix during nuclear import of the HIV-1 preintegration complex has been controversial, however recent understanding indicates HIV-1 Matrix and Vpr proteins act in concert to facilitate nuclear import by binding to karyopherin alpha PubMed
gag HIV-1 Matrix contains two nuclear localization signals (NLS) spanning amino acids 24-33 and 110-114 that are recognized by karyopherin alpha and mediate the nuclear import of HIV-1 preintegration complexes PubMed

Go to the HIV-1, Human Interaction Database

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Products Interactant Other Gene Complex Source Pubs Description



Clone Names

  • FLJ31113, MGC12217, MGC26703

Gene Ontology Provided by GOA

Function Evidence Code Pubs
nuclear localization sequence binding IBA
Inferred from Biological aspect of Ancestor
more info
protein binding IPI
Inferred from Physical Interaction
more info
protein transporter activity IBA
Inferred from Biological aspect of Ancestor
more info
Process Evidence Code Pubs
NLS-bearing protein import into nucleus TAS
Traceable Author Statement
more info
intracellular transport of virus TAS
Traceable Author Statement
more info
modulation by virus of host process TAS
Traceable Author Statement
more info
response to hydrogen peroxide IEA
Inferred from Electronic Annotation
more info
Component Evidence Code Pubs
cytosol IBA
Inferred from Biological aspect of Ancestor
more info
cytosol TAS
Traceable Author Statement
more info
extracellular exosome IDA
Inferred from Direct Assay
more info
nuclear pore IBA
Inferred from Biological aspect of Ancestor
more info
nucleoplasm IBA
Inferred from Biological aspect of Ancestor
more info
nucleoplasm TAS
Traceable Author Statement
more info
Preferred Names
importin subunit alpha-3
importin alpha Q1
importin subunit alpha-4
karyopherin alpha 4 (importin alpha 3)
karyopherin subunit alpha-4

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_002268.4NP_002259.1  importin subunit alpha-3

    See identical proteins and their annotated locations for NP_002259.1

    Status: REVIEWED

    Source sequence(s)
    AC078868, BC034493
    Consensus CDS
    ENSP00000334373, OTTHUMP00000213880, ENST00000334256, OTTHUMT00000352960
    Conserved Domains (3) summary
    IBB; Importin beta binding domain
    SRP1; Karyopherin (importin) alpha [Intracellular trafficking and secretion]
    ARM; Armadillo/beta-catenin-like repeats. An approximately 40 amino acid long tandemly repeated sequence motif first identified in the Drosophila segment polarity gene armadillo; these repeats were also found in the mammalian armadillo homolog beta-catenin, ...

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 107 details...

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p2 Primary Assembly


  1. NC_000003.12 Reference GRCh38.p2 Primary Assembly

    160494995..160565588 complement
    GenBank, FASTA, Sequence Viewer (Graphics)

Alternate CHM1_1.1


  1. NC_018914.2 Alternate CHM1_1.1

    160175691..160246276 complement
    GenBank, FASTA, Sequence Viewer (Graphics)