P52293
Gene name |
Kpna2 |
Protein name |
Importin subunit alpha-1 |
Names |
Importin alpha P1, Karyopherin subunit alpha-2, Pendulin, Pore targeting complex 58 kDa subunit, PTAC58, RAG cohort protein 1, SRP1-alpha |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:16647 |
EC number |
|
Protein Class |
IMPORTIN ALPHA (PTHR23316) |

Descriptions
Importin-α is a nuclear import receptor that facilitates the transport of proteins with nuclear localization sequences (NLSs) into the nucleus. It is autoinhibited by its N-terminal region, which occupies the NLS-binding site, preventing unnecessary binding and import activity. Importin-α is autoinhibited in the absence of importin-β and the binding of importin-β alleviates this autoinhibition, which displaces the autoinhibitory sequence.
Autoinhibitory domains (AIDs)
Target domain |
142-238 (Major NLS-binding site); 315-403 (Minor NLS-binding site) |
Relief mechanism |
Partner binding |
Assay |
Structural analysis, Split protein assay, Deletion assay, Mutagenesis experiment |
Accessory elements
No accessory elements
References
- Fontes MR et al. (2000) "Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha", Journal of molecular biology, 297, 1183-94
- Fontes MR et al. (2003) "Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha", The Journal of biological chemistry, 278, 27981-7
- Catimel B et al. (2001) "Biophysical characterization of interactions involving importin-alpha during nuclear import", The Journal of biological chemistry, 276, 34189-98
- Pumroy RA et al. (2015) "Molecular determinants for nuclear import of influenza A PB2 by importin α isoforms 3 and 7", Structure (London, England : 1993), 23, 374-84
Autoinhibited structure
Activated structure
136 structures for P52293
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
1EJL | X-ray | 280 A | I | 70-529 | PDB |
1EJY | X-ray | 290 A | I | 70-529 | PDB |
1IAL | X-ray | 250 A | A | 44-496 | PDB |
1IQ1 | X-ray | 280 A | PDB | ||
1PJM | X-ray | 250 A | B | 70-529 | PDB |
1PJN | X-ray | 250 A | B | 70-529 | PDB |
1Q1S | X-ray | 230 A | C | 70-529 | PDB |
1Q1T | X-ray | 250 A | C | 70-529 | PDB |
1Y2A | X-ray | 220 A | C | 70-497 | PDB |
2C1M | X-ray | 220 A | A | 75-498 | PDB |
2YNR | X-ray | 230 A | A | 72-496 | PDB |
3BTR | X-ray | 260 A | C | 70-496 | PDB |
3KND | X-ray | 215 A | A | 70-529 | PDB |
3L3Q | X-ray | 230 A | A | 71-497 | PDB |
3OQS | X-ray | 200 A | A | 70-529 | PDB |
3Q5U | X-ray | 250 A | A | 70-529 | PDB |
3RZ9 | X-ray | 229 A | A | 70-529 | PDB |
3RZX | X-ray | 261 A | A | 70-529 | PDB |
3TPM | X-ray | 210 A | A | 75-496 | PDB |
3TPO | X-ray | 210 A | A | 1-529 | PDB |
3UKW | X-ray | 210 A | B | 70-529 | PDB |
3UKX | X-ray | 220 A | B | 70-529 | PDB |
3UKY | X-ray | 235 A | B | 70-529 | PDB |
3UKZ | X-ray | 230 A | B | 70-529 | PDB |
3UL0 | X-ray | 200 A | B | 70-529 | PDB |
3UL1 | X-ray | 190 A | B | 70-529 | PDB |
3UVU | X-ray | 238 A | A | 70-529 | PDB |
3VE6 | X-ray | 283 A | A | 71-496 | PDB |
3ZIN | X-ray | 200 A | A | 72-496 | PDB |
3ZIO | X-ray | 210 A | A | 72-496 | PDB |
3ZIP | X-ray | 240 A | A | 72-497 | PDB |
3ZIQ | X-ray | 210 A | A | 72-497 | PDB |
3ZIR | X-ray | 230 A | A | 72-497 | PDB |
4BA3 | X-ray | 210 A | A | 70-529 | PDB |
4HTV | X-ray | 300 A | A | 70-528 | PDB |
4MZ5 | X-ray | 210 A | E | 70-528 | PDB |
4MZ6 | X-ray | 188 A | E | 70-528 | PDB |
4OIH | X-ray | 210 A | A | 70-529 | PDB |
4U54 | X-ray | 241 A | A | 74-498 | PDB |
4U58 | X-ray | 256 A | A | 72-497 | PDB |
4U5L | X-ray | 253 A | A | 72-497 | PDB |
4U5N | X-ray | 231 A | A | 72-497 | PDB |
4U5O | X-ray | 200 A | A | 72-497 | PDB |
4U5S | X-ray | 212 A | A | 72-497 | PDB |
4U5U | X-ray | 196 A | A | 72-497 | PDB |
4U5V | X-ray | 197 A | A | 72-497 | PDB |
4UAF | X-ray | 170 A | B | 69-529 | PDB |
4YI0 | X-ray | 181 A | C | 70-529 | PDB |
4ZDU | X-ray | 230 A | A | 72-498 | PDB |
5B56 | X-ray | 230 A | A/B | 70-529 | PDB |
5CTT | X-ray | 170 A | A | 72-497 | PDB |
5D5K | X-ray | 190 A | C | 70-529 | PDB |
5E6Q | X-ray | 231 A | B | 70-529 | PDB |
5EKF | X-ray | 200 A | A | 70-529 | PDB |
5EKG | X-ray | 280 A | A | 70-529 | PDB |
5FC8 | X-ray | 210 A | E | 71-529 | PDB |
5GXW | X-ray | 239 A | A | 70-497 | PDB |
5HHG | X-ray | 220 A | E | 71-497 | PDB |
5HUW | X-ray | 195 A | C | 2-529 | PDB |
5HUY | X-ray | 198 A | C | 2-529 | PDB |
5K9S | X-ray | 240 A | A | 72-529 | PDB |
5KLR | X-ray | 220 A | B | 70-529 | PDB |
5KLT | X-ray | 260 A | B | 70-529 | PDB |
5SVZ | X-ray | 200 A | A | 70-529 | PDB |
5U5P | X-ray | 217 A | A | 70-529 | PDB |
5U5R | X-ray | 210 A | A | 70-529 | PDB |
5UMZ | X-ray | 190 A | B | 70-528 | PDB |
5V5O | X-ray | 224 A | C | 2-529 | PDB |
5V5P | X-ray | 215 A | C | 2-529 | PDB |
5W41 | X-ray | 220 A | A | 70-529 | PDB |
5W4E | X-ray | 218 A | B | 37-529 | PDB |
5W4F | X-ray | 198 A | B | 70-529 | PDB |
5W4G | X-ray | 204 A | B | 70-529 | PDB |
5WUM | X-ray | 200 A | A | 70-529 | PDB |
5WUN | X-ray | 220 A | A | 70-529 | PDB |
5X8N | X-ray | 215 A | A | 70-529 | PDB |
6BVT | X-ray | 250 A | E | 70-529 | PDB |
6BW0 | X-ray | 210 A | E | 70-529 | PDB |
6BW1 | X-ray | 220 A | E | 70-529 | PDB |
6D7M | X-ray | 219 A | B | 37-529 | PDB |
6D7N | X-ray | 230 A | B | 70-529 | PDB |
6IU7 | X-ray | 190 A | A | 72-498 | PDB |
6IUA | X-ray | 170 A | A | 72-498 | PDB |
6IW8 | X-ray | 280 A | C | 70-498 | PDB |
6IWA | X-ray | 240 A | C | 70-498 | PDB |
6K06 | X-ray | 175 A | C | 70-498 | PDB |
6MJL | X-ray | 250 A | B | 72-497 | PDB |
6P6A | X-ray | 215 A | B | 70-529 | PDB |
6P6E | X-ray | 199 A | A | 70-529 | PDB |
6WBA | X-ray | 215 A | A | 70-529 | PDB |
6WBB | X-ray | 266 A | I | 70-529 | PDB |
6WBC | X-ray | 215 A | A | 70-529 | PDB |
6WX7 | X-ray | 270 A | A | 70-529 | PDB |
7JJM | X-ray | 206 A | B | 62-529 | PDB |
7JK7 | X-ray | 196 A | B | 62-529 | PDB |
7JVO | X-ray | 220 A | A | 70-529 | PDB |
7L04 | X-ray | 226 A | E | 70-529 | PDB |
7LEQ | X-ray | 224 A | E | 70-497 | PDB |
7LET | X-ray | 240 A | E | 70-497 | PDB |
7LEU | X-ray | 282 A | E | 70-497 | PDB |
7M60 | X-ray | 230 A | A | 70-529 | PDB |
7RFX | X-ray | 210 A | A | 70-529 | PDB |
7RFZ | X-ray | 195 A | A | 70-529 | PDB |
7RG0 | X-ray | 200 A | A | 70-529 | PDB |
7RG1 | X-ray | 185 A | A | 70-529 | PDB |
7RG2 | X-ray | 200 A | A | 70-529 | PDB |
7RG3 | X-ray | 200 A | A | 70-529 | PDB |
7RG4 | X-ray | 260 A | E | 70-529 | PDB |
7RG6 | X-ray | 210 A | A | 70-529 | PDB |
7TMX | X-ray | 230 A | I | 70-529 | PDB |
7TMY | X-ray | 221 A | I | 70-529 | PDB |
7UMI | X-ray | 199 A | E | 70-529 | PDB |
8ECH | X-ray | 205 A | E | 70-529 | PDB |
8F2Q | X-ray | 270 A | A | 70-529 | PDB |
8FK3 | X-ray | 260 A | A | 70-529 | PDB |
8FUA | X-ray | 190 A | A | 70-529 | PDB |
8FUC | X-ray | 210 A | B | 70-529 | PDB |
8G8Q | X-ray | 260 A | A | 70-529 | PDB |
8G8R | X-ray | 260 A | A | 70-529 | PDB |
8G8S | X-ray | 210 A | A | 70-529 | PDB |
8HE0 | X-ray | 180 A | A | 72-498 | PDB |
8HE3 | X-ray | 190 A | A | 72-498 | PDB |
8Q8K | X-ray | 270 A | A/B | 70-529 | PDB |
8QXW | X-ray | 200 A | A | 70-529 | PDB |
8QXX | X-ray | 190 A | A | 70-529 | PDB |
8SG7 | X-ray | 240 A | B | 70-529 | PDB |
8SUD | X-ray | 210 A | A | 70-529 | PDB |
8SV0 | X-ray | 220 A | B | 70-529 | PDB |
8TUQ | X-ray | 200 A | A | 70-529 | PDB |
8TUR | X-ray | 215 A | A | 70-529 | PDB |
8TUS | X-ray | 260 A | A | 70-529 | PDB |
8TUT | X-ray | 255 A | A | 70-529 | PDB |
8TUU | X-ray | 250 A | A | 70-529 | PDB |
8TUV | X-ray | 230 A | A | 70-529 | PDB |
8U36 | X-ray | 260 A | A | 70-529 | PDB |
AF-P52293-F1 | Predicted | AlphaFoldDB |
12 variants for P52293
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
rs585114248 | 25 | T>I | No | Ensembl | |
rs581801649 | 28 | R>H | No | Ensembl | |
rs579317280 | 29 | R>C | No | Ensembl | |
rs586309464 | 35 | N>S | No | Ensembl | |
rs1131966327 | 59 | D>E | No | Ensembl | |
rs1132633019 | 94 | L>H | No | Ensembl | |
rs108391886 | 94 | L>H | No | Ensembl | |
rs1132275504 | 129 | G>D | No | Ensembl | |
rs108257647 | 129 | G>D | No | Ensembl | |
rs1131892410 | 227 | R>H | No | Ensembl | |
rs108924641 | 389 | A>V | No | Ensembl | |
rs580571730 | 505 | N>S | No | Ensembl |
No associated diseases with P52293
9 regional properties for P52293
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | Protein kinase domain | 457 - 717 | IPR000719 |
domain | Serine-threonine/tyrosine-protein kinase, catalytic domain | 458 - 712 | IPR001245 |
domain | Protein kinase C-like, phorbol ester/diacylglycerol-binding domain | 234 - 280 | IPR002219 |
domain | Raf-like Ras-binding | 155 - 227 | IPR003116 |
active_site | Serine/threonine-protein kinase, active site | 572 - 584 | IPR008271 |
binding_site | Protein kinase, ATP binding site | 463 - 483 | IPR017441 |
domain | Diacylglycerol/phorbol-ester binding | 232 - 246 | IPR020454-1 |
domain | Diacylglycerol/phorbol-ester binding | 248 - 268 | IPR020454-2 |
domain | Diacylglycerol/phorbol-ester binding | 269 - 281 | IPR020454-3 |
Functions
Description | ||
---|---|---|
EC Number | ||
Subcellular Localization |
|
|
PANTHER Family | PTHR23316 | IMPORTIN ALPHA |
PANTHER Subfamily | PTHR23316:SF12 | IMPORTIN SUBUNIT ALPHA-1 |
PANTHER Protein Class | transporter | |
PANTHER Pathway Category | No pathway information available |
7 GO annotations of cellular component
Name | Definition |
---|---|
cytoplasmic stress granule | A dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. |
cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
extrinsic component of postsynaptic specialization membrane | The component of the postsynaptic specialization membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region. |
glutamatergic synapse | A synapse that uses glutamate as a neurotransmitter. |
host cell | A cell within a host organism. Includes the host plasma membrane and any external encapsulating structures such as the host cell wall and cell envelope. |
nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
4 GO annotations of molecular function
Name | Definition |
---|---|
DNA-binding transcription factor binding | Binding to a DNA-binding transcription factor, a protein that interacts with a specific DNA sequence (sometimes referred to as a motif) within the regulatory region of a gene to modulate transcription. |
histone deacetylase binding | Binding to histone deacetylase. |
nuclear import signal receptor activity | Combining with a nuclear import signal (NIS) on a cargo to be transported, to mediate transport of the cargo through the nuclear pore, from the cytoplasm to the nuclear lumen. The cargo can be either a RNA or a protein. |
nuclear localization sequence binding | Binding to a nuclear localization sequence, a specific peptide sequence that acts as a signal to localize the protein within the nucleus. |
6 GO annotations of biological process
Name | Definition |
---|---|
entry of viral genome into host nucleus through nuclear pore complex via importin | Viral penetration into the host nucleus where the viral genome passes through the nuclear pore complex (NPC) using the cellular importin transport machinery. |
NLS-bearing protein import into nucleus | The directed movement of a protein bearing a nuclear localization signal (NLS) from the cytoplasm into the nucleus, across the nuclear envelope. |
positive regulation of viral life cycle | Any process that activates or increases the frequency, rate or extent of viral life cycle. |
postsynapse to nucleus signaling pathway | The series of molecular signals that conveys information from the postsynapse to the nucleus via cytoskeletal transport of a protein from a postsynapse to the component to the nucleus where it affects biochemical processes that occur in the nucleus (e.g DNA transcription, mRNA splicing, or DNA/histone modifications). |
protein import into nucleus | The directed movement of a protein from the cytoplasm to the nucleus. |
regulation of transcription by glucose | Any process involving glucose that modulates the frequency, rate or extent or transcription. |
31 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
Q02821 | SRP1 | Importin subunit alpha | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
Q0V7M0 | KPNA6 | Importin subunit alpha-7 | Bos taurus (Bovine) | SS |
A2VE08 | KPNA1 | Importin subunit alpha-5 | Bos taurus (Bovine) | SS |
C1JZ66 | KPNA7 | Importin subunit alpha-8 | Bos taurus (Bovine) | PR |
Q5ZML1 | KPNA1 | Importin subunit alpha-5 | Gallus gallus (Chicken) | SS |
P52295 | Pen | Importin subunit alpha | Drosophila melanogaster (Fruit fly) | SS |
P52294 | KPNA1 | Importin subunit alpha-5 | Homo sapiens (Human) | SS |
O15131 | KPNA5 | Importin subunit alpha-6 | Homo sapiens (Human) | SS |
O60684 | KPNA6 | Importin subunit alpha-7 | Homo sapiens (Human) | SS |
A9QM74 | KPNA7 | Importin subunit alpha-8 | Homo sapiens (Human) | EV |
O00505 | KPNA3 | Importin subunit alpha-4 | Homo sapiens (Human) | SS |
O00629 | KPNA4 | Importin subunit alpha-3 | Homo sapiens (Human) | SS |
P52292 | KPNA2 | Importin subunit alpha-1 | Homo sapiens (Human) | EV |
C0LLJ0 | Kpna7 | Importin subunit alpha-8 | Mus musculus (Mouse) | SS |
O35343 | Kpna4 | Importin subunit alpha-3 | Mus musculus (Mouse) | SS |
O35344 | Kpna3 | Importin subunit alpha-4 | Mus musculus (Mouse) | SS |
O35345 | Kpna6 | Importin subunit alpha-7 | Mus musculus (Mouse) | PR |
P52293 | Kpna2 | Importin subunit alpha-1 | Mus musculus (Mouse) | EV |
Q60960 | Kpna1 | Importin subunit alpha-5 | Mus musculus (Mouse) | SS |
C6K7I2 | KPNA7 | Importin subunit alpha-8 | Sus scrofa (Pig) | SS |
P83953 | Kpna1 | Importin subunit alpha-5 | Rattus norvegicus (Rat) | SS |
Q56R16 | Kpna5 | Importin subunit alpha-6 | Rattus norvegicus (Rat) | SS |
Q71VM4 | Os01g0253300 | Importin subunit alpha-1a | Oryza sativa subsp. japonica (Rice) | SS |
P91276 | ima-2 | Importin subunit alpha-2 | Caenorhabditis elegans | SS |
Q19969 | ima-3 | Importin subunit alpha-3 | Caenorhabditis elegans | SS |
O04294 | IMPA3 | Importin subunit alpha-3 | Arabidopsis thaliana (Mouse-ear cress) | SS |
Q9FJ09 | IMPA5 | Importin subunit alpha-5 | Arabidopsis thaliana (Mouse-ear cress) | SS |
Q9M9X7 | IMPA7 | Importin subunit alpha-7 | Arabidopsis thaliana (Mouse-ear cress) | SS |
Q9FWY7 | IMPA6 | Importin subunit alpha-6 | Arabidopsis thaliana (Mouse-ear cress) | SS |
O22478 | Importin subunit alpha | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | SS | |
Q503E9 | kpna5 | Importin subunit alpha-6 | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
10 | 20 | 30 | 40 | 50 | 60 |
MSTNENANLP | AARLNRFKNK | GKDSTEMRRR | RIEVNVELRK | AKKDEQMLKR | RNVSSFPDDA |
70 | 80 | 90 | 100 | 110 | 120 |
TSPLQENRNN | QGTVNWSVED | IVKGINSNNL | ESQLQATQAA | RKLLSREKQP | PIDNIIRAGL |
130 | 140 | 150 | 160 | 170 | 180 |
IPKFVSFLGK | TDCSPIQFES | AWALTNIASG | TSEQTKAVVD | GGAIPAFISL | LASPHAHISE |
190 | 200 | 210 | 220 | 230 | 240 |
QAVWALGNIA | GDGSAFRDLV | IKHGAIDPLL | ALLAVPDLST | LACGYLRNLT | WTLSNLCRNK |
250 | 260 | 270 | 280 | 290 | 300 |
NPAPPLDAVE | QILPTLVRLL | HHNDPEVLAD | SCWAISYLTD | GPNERIEMVV | KKGVVPQLVK |
310 | 320 | 330 | 340 | 350 | 360 |
LLGATELPIV | TPALRAIGNI | VTGTDEQTQK | VIDAGALAVF | PSLLTNPKTN | IQKEATWTMS |
370 | 380 | 390 | 400 | 410 | 420 |
NITAGRQDQI | QQVVNHGLVP | FLVGVLSKAD | FKTQKEAAWA | ITNYTSGGTV | EQIVYLVHCG |
430 | 440 | 450 | 460 | 470 | 480 |
IIEPLMNLLS | AKDTKIIQVI | LDAISNIFQA | AEKLGETEKL | SIMIEECGGL | DKIEALQRHE |
490 | 500 | 510 | 520 | ||
NESVYKASLN | LIEKYFSVEE | EEDQNVVPET | TSEGFAFQVQ | DGAPGTFNF |