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P52292 (IMA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Importin subunit alpha-1
Alternative name(s):
Karyopherin subunit alpha-2
RAG cohort protein 1
SRP1-alpha
Gene names
Name:KPNA2
Synonyms:RCH1, SRP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length529 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

Heterodimer; with KPNB1. Interacts with ANP32E By similarity. Component of a complex containing CSE1L, RAN and KPNA2. Interacts directly with CSE1L. Interacts with HIV-1 Vpr and PLAG1. Interacts with APEX1 (via N-terminus). Interacts with ARL4A, CTNNBL1 and NBN. Interacts with SNAI1 (via zinc fingers) and SNAI2 (via zinc fingers). Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.24 Ref.28 Ref.29

Subcellular location

Cytoplasm. Nucleus Ref.8.

Tissue specificity

Expressed ubiquitously.

Domain

Consists of an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import. Ref.9

The IBB domain is thought to act as an intrasteric autoregulatory sequence by interacting with the internal autoinhibitory NLS. Binding of KPNB1 probably overlaps the internal NLS and contributes to a high affinity for cytoplasmic NLS-containing cargo substrates. After dissociation of the importin/substrate complex in the nucleus the internal autohibitory NLS contributes to a low affinity for nuclear NLS-containing proteins By similarity. Ref.9

The major and minor NLS binding sites are mainly involved in recognition of simple or bipartite NLS motifs. Structurally located within in a helical surface groove they contain several conserved Trp and Asn residues of the corresponding third helices (H3) of ARM repeats which mainly contribute to binding By similarity. Ref.9

Sequence similarities

Belongs to the importin alpha family.

Contains 10 ARM repeats.

Contains 1 IBB domain.

Mass spectrometry

Molecular mass is 57861.92 Da from positions 1 - 529. Determined by MALDI. Ref.15

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 529528Importin subunit alpha-1
PRO_0000120722

Regions

Domain2 – 6059IBB
Repeat71 – 11141ARM 1; truncated
Repeat112 – 15140ARM 2
Repeat152 – 19342ARM 3
Repeat200 – 24445ARM 4
Repeat246 – 28237ARM 5
Repeat283 – 32240ARM 6
Repeat325 – 36440ARM 7
Repeat367 – 40943ARM 8
Repeat410 – 45647ARM 9
Repeat457 – 49640ARM 10; atypical
Region142 – 23897NLS binding site (major) By similarity
Region315 – 40389NLS binding site (minor) By similarity
Motif45 – 5410Nuclear localization signal By similarity
Compositional bias28 – 314Poly-Arg
Compositional bias499 – 5024Poly-Glu

Amino acid modifications

Modified residue21N-acetylserine Ref.6 Ref.23 Ref.30 Ref.31
Modified residue621Phosphoserine Ref.19 Ref.22 Ref.25 Ref.26 Ref.30
Modified residue4901Phosphoserine Ref.22 Ref.26

Natural variations

Natural variant1571A → V. Ref.3 Ref.5
Corresponds to variant rs17850032 [ dbSNP | Ensembl ].
VAR_067625
Natural variant1651P → R. Ref.2
Corresponds to variant rs11545989 [ dbSNP | Ensembl ].
VAR_013137
Natural variant3651G → S.
Corresponds to variant rs1059558 [ dbSNP | Ensembl ].
VAR_067626
Natural variant4301T → P.
Corresponds to variant rs1059538 [ dbSNP | Ensembl ].
VAR_014453
Natural variant4531K → N. Ref.3 Ref.5
Corresponds to variant rs17850031 [ dbSNP | Ensembl ].
VAR_067627

Secondary structure

..................................................................... 529
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52292 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: B0F94A0475B80EED

FASTA52957,862
        10         20         30         40         50         60 
MSTNENANTP AARLHRFKNK GKDSTEMRRR RIEVNVELRK AKKDDQMLKR RNVSSFPDDA 

        70         80         90        100        110        120 
TSPLQENRNN QGTVNWSVDD IVKGINSSNV ENQLQATQAA RKLLSREKQP PIDNIIRAGL 

       130        140        150        160        170        180 
IPKFVSFLGR TDCSPIQFES AWALTNIASG TSEQTKAVVD GGAIPAFISL LASPHAHISE 

       190        200        210        220        230        240 
QAVWALGNIA GDGSVFRDLV IKYGAVDPLL ALLAVPDMSS LACGYLRNLT WTLSNLCRNK 

       250        260        270        280        290        300 
NPAPPIDAVE QILPTLVRLL HHDDPEVLAD TCWAISYLTD GPNERIGMVV KTGVVPQLVK 

       310        320        330        340        350        360 
LLGASELPIV TPALRAIGNI VTGTDEQTQV VIDAGALAVF PSLLTNPKTN IQKEATWTMS 

       370        380        390        400        410        420 
NITAGRQDQI QQVVNHGLVP FLVSVLSKAD FKTQKEAVWA VTNYTSGGTV EQIVYLVHCG 

       430        440        450        460        470        480 
IIEPLMNLLT AKDTKIILVI LDAISNIFQA AEKLGETEKL SIMIEECGGL DKIEALQNHE 

       490        500        510        520 
NESVYKASLS LIEKYFSVEE EEDQNVVPET TSEGYTFQVQ DGAPGTFNF 

« Hide

References

« Hide 'large scale' references
[1]"Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences."
Weis K., Mattaj I.W., Lamond A.I.
Science 268:1049-1053(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Genomic structure of karyopherin alpha2 (KPNA2) within a low-copy repeat on chromosome 17q23-q24 and mutation analysis in patients with Russell-Silver syndrome."
Doerr S., Schlicker M., Hansmann I.
Hum. Genet. 109:479-486(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-165.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-157 AND ASN-453.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-157 AND ASN-453.
Tissue: Bone marrow and Testis.
[6]Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13; 69-101; 107-117; 239-258; 292-315; 354-388 AND 487-494, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hepatoma.
[7]"Rch1, a protein that specifically interacts with the RAG-1 recombination-activating protein."
Cuomo C.A., Kirch S.A., Gyuris J., Brent R., Oettinger M.A.
Proc. Natl. Acad. Sci. U.S.A. 91:6156-6160(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-529.
Tissue: Cervix carcinoma.
[8]"Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal and beta subunit interacts with peptide repeat-containing nucleoporins."
Moroianu J., Hijikata M., Blobel G., Radu A.
Proc. Natl. Acad. Sci. U.S.A. 92:6532-6536(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[9]"The conserved amino-terminal domain of hSRP1 alpha is essential for nuclear protein import."
Weis K., Ryder U., Lamond A.I.
EMBO J. 15:1818-1825(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN IBB.
[10]"Export of importin-alpha from the nucleus is mediated by a specific nuclear transport factor."
Kutay U., Bischoff F.R., Kostka S., Kraft R., Goerlich D.
Cell 90:1061-1071(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH RAN AND CSE1L.
[11]"Viral protein R regulates nuclear import of the HIV-1 pre-integration complex."
Popov S., Rexach M., Zybarth G., Reiling N., Lee M.A., Ratner L., Lane C.M., Moore M.S., Blobel G., Bukrinsky M.
EMBO J. 17:909-917(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 VPR.
[12]"Determination of the functional domain organization of the importin alpha nuclear import factor."
Herold A., Truant R., Wiegand H., Cullen B.R.
J. Cell Biol. 143:309-318(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH XPO2/CSE1L.
[13]"ARL4, an ARF-like protein that is developmentally regulated and localized to nuclei and nucleoli."
Lin C.Y., Huang P.H., Liao W.L., Cheng H.J., Huang C.F., Kuo J.C., Patton W.A., Massenburg D., Moss J., Lee F.J.
J. Biol. Chem. 275:37815-37823(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARL4A.
[14]"Identification of a karyopherin alpha 2 recognition site in PLAG1, which functions as a nuclear localization signal."
Braem C.V., Kas K., Meyen E., Debiec-Rychter M., Van De Ven W.J.M., Voz M.L.
J. Biol. Chem. 277:19673-19678(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLAG1.
[15]"Cluster analysis of an extensive human breast cancer cell line protein expression map database."
Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
Tissue: Mammary cancer.
[16]"Importin KPNA2 is required for proper nuclear localization and multiple functions of NBS1."
Tseng S.-F., Chang C.-Y., Wu K.-J., Teng S.-C.
J. Biol. Chem. 280:39594-39600(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NBN.
[17]"Analysis of nuclear transport signals in the human apurinic/apyrimidinic endonuclease (APE1/Ref1)."
Jackson E.B., Theriot C.A., Chattopadhyay R., Mitra S., Izumi T.
Nucleic Acids Res. 33:3303-3312(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APEX1.
[18]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Characterization of Snail nuclear import pathways as representatives of C2H2 zinc finger transcription factors."
Mingot J.M., Vega S., Maestro B., Sanz J.M., Nieto M.A.
J. Cell Sci. 122:1452-1460(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNAI1 AND SNAI2.
[25]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[26]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Importin alpha protein acts as a negative regulator for Snail protein nuclear import."
Sekimoto T., Miyamoto Y., Arai S., Yoneda Y.
J. Biol. Chem. 286:15126-15131(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNAI1.
[29]"CTNNBL1 is a novel nuclear localization sequence-binding protein that recognizes RNA-splicing factors CDC5L and Prp31."
Ganesh K., Adam S., Taylor B., Simpson P., Rada C., Neuberger M.
J. Biol. Chem. 286:17091-17102(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTNNBL1.
[30]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"Structure of importin-beta bound to the IBB domain of importin-alpha."
Cingolani G., Petosa C., Weis K., Muller C.W.
Nature 399:221-229(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 11-54.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28386 mRNA. Translation: AAA69957.1.
AJ303086 Genomic DNA. Translation: CAC83080.1.
BT006665 mRNA. Translation: AAP35311.1.
CH471099 Genomic DNA. Translation: EAW89041.1.
BC005978 mRNA. Translation: AAH05978.1.
BC146905 mRNA. Translation: AAI46906.1.
U09559 mRNA. Translation: AAA65700.1.
PIRA56516.
RefSeqNP_002257.1. NM_002266.2.
UniGeneHs.594238.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EFXX-ray3.00C204-212[»]
1QGKX-ray2.50B11-54[»]
1QGRX-ray2.30B28-54[»]
3FEXX-ray3.55C70-529[»]
3FEYX-ray2.20C70-529[»]
4E4VX-ray2.53A/B70-529[»]
ProteinModelPortalP52292.
SMRP52292. Positions 11-499.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110036. 130 interactions.
DIPDIP-6205N.
IntActP52292. 73 interactions.
MINTMINT-94121.
STRING9606.ENSP00000332455.

Chemistry

BindingDBP52292.
ChEMBLCHEMBL1741187.

PTM databases

PhosphoSiteP52292.

Polymorphism databases

DMDM1708480.

2D gel databases

SWISS-2DPAGEP52292.

Proteomic databases

PaxDbP52292.
PeptideAtlasP52292.
PRIDEP52292.

Protocols and materials databases

DNASU3838.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330459; ENSP00000332455; ENSG00000182481.
ENST00000537025; ENSP00000438483; ENSG00000182481.
ENST00000571293; ENSP00000460119; ENSG00000262472.
ENST00000574083; ENSP00000460025; ENSG00000262472.
GeneID3838.
KEGGhsa:3838.
UCSCuc002jgk.3. human.

Organism-specific databases

CTD3838.
GeneCardsGC17P066031.
HGNCHGNC:6395. KPNA2.
HPACAB015460.
HPA041270.
MIM600685. gene.
neXtProtNX_P52292.
PharmGKBPA30186.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5064.
HOGENOMHOG000167616.
HOVERGENHBG001846.
InParanoidP52292.
KOK15043.
OMANETEKLC.
PhylomeDBP52292.
TreeFamTF101178.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP52292.

Gene expression databases

ArrayExpressP52292.
BgeeP52292.
CleanExHS_KPNA2.
GenevestigatorP52292.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR002652. Importin-a_IBB.
IPR024931. Importing_su_alpha.
[Graphical view]
PfamPF00514. Arm. 8 hits.
PF01749. IBB. 1 hit.
[Graphical view]
PIRSFPIRSF005673. Importin_alpha. 1 hit.
SMARTSM00185. ARM. 8 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50176. ARM_REPEAT. 5 hits.
PS51214. IBB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKPNA2. human.
EvolutionaryTraceP52292.
GeneWikiKaryopherin_alpha_2.
GenomeRNAi3838.
NextBio15087.
PROP52292.
SOURCESearch...

Entry information

Entry nameIMA1_HUMAN
AccessionPrimary (citable) accession number: P52292
Secondary accession number(s): B9EJD6, Q53YE3, Q9BRU5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM