P52292 (IMA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Importin subunit alpha-2

Alternative name(s):
Karyopherin subunit alpha-2
RAG cohort protein 1
SRP1-alpha

Gene names

Name:	KPNA2
Synonyms:	RCH1, SRP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.23 Ref.27 Ref.28
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

Ontologies

Keywords
Biological process	Host-virus interaction Protein transport Transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA metabolic process Traceable author statement PubMed 9168958. Source: ProtInc G2 phase of mitotic cell cycle Traceable author statement PubMed 7565597. Source: ProtInc M phase specific microtubule process Traceable author statement PubMed 7565597. Source: ProtInc NLS-bearing substrate import into nucleus Inferred from direct assay PubMed 17324944. Source: UniProtKB cytokine-mediated signaling pathway Traceable author statement. Source: Reactome regulation of DNA recombination Traceable author statement Ref.7. Source: ProtInc virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	nuclear localization sequence binding Inferred from direct assay PubMed 17324944. Source: UniProtKB protein transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRCA1	P38398	3	EBI-349938,EBI-349905
JUN	P05412	2	EBI-349938,EBI-852823

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 529

528

Importin subunit alpha-2

PRO_0000120722

Regions

Domain

2 – 60

59

IBB

Repeat

71 – 111

41

ARM 1; truncated

Repeat

112 – 151

40

ARM 2

Repeat

152 – 193

42

ARM 3

Repeat

200 – 244

45

ARM 4

Repeat

246 – 282

37

ARM 5

Repeat

283 – 322

40

ARM 6

Repeat

325 – 364

40

ARM 7

Repeat

367 – 409

43

ARM 8

Repeat

410 – 456

47

ARM 9

Repeat

457 – 496

40

ARM 10; atypical

Region

142 – 238

97

NLS binding site (major) By similarity

Region

315 – 403

89

NLS binding site (minor) By similarity

Motif

45 – 54

10

Nuclear localization signal By similarity

Compositional bias

28 – 31

4

Poly-Arg

Compositional bias

499 – 502

4

Poly-Glu

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.6 Ref.29

Modified residue

62

1

Phosphoserine Ref.19 Ref.22 Ref.24 Ref.25 Ref.29

Modified residue

490

1

Phosphoserine Ref.22 Ref.25

Natural variations

Natural variant

157

1

A → V. Ref.3 Ref.5
Corresponds to variant rs17850032 [ dbSNP | Ensembl ].

VAR_067625

Natural variant

165

1

P → R. Ref.2
Corresponds to variant rs11545989 [ dbSNP | Ensembl ].

VAR_013137

Natural variant

365

1

G → S.
Corresponds to variant rs1059558 [ dbSNP | Ensembl ].

VAR_067626

Natural variant

430

1

T → P.
Corresponds to variant rs1059538 [ dbSNP | Ensembl ].

VAR_014453

Natural variant

453

1

K → N. Ref.3 Ref.5
Corresponds to variant rs17850031 [ dbSNP | Ensembl ].

VAR_067627

Secondary structure

1

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529

Helix Strand Turn

Details...

Helix

14 – 16

3

Turn

18 – 21

4

Helix

30 – 48

19

Helix

78 – 85

8

Helix

90 – 104

15

Beta strand

106 – 108

3

Helix

112 – 117

6

Helix

120 – 129

10

Helix

134 – 147

14

Helix

152 – 160

9

Helix

163 – 170

8

Helix

176 – 190

15

Helix

194 – 202

9

Helix

206 – 211

6

Helix

223 – 236

14

Helix

246 – 259

14

Helix

265 – 279

15

Helix

283 – 291

9

Helix

295 – 301

7

Helix

307 – 320

14

Helix

325 – 333

9

Helix

336 – 344

9

Helix

349 – 362

14

Helix

367 – 375

9

Helix

379 – 388

10

Helix

391 – 407

17

Helix

410 – 418

9

Helix

422 – 427

6

Helix

428 – 430

3

Helix

434 – 453

20

Helix

457 – 466

10

Helix

469 – 475

7

Helix

476 – 478

3

Helix

482 – 495

14

Sequences

	Sequence		Length	Mass (Da)
	P52292 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: B0F94A0475B80EED	FASTA	529	57,862
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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: IDENTIFICATION OF IBB DOMAIN.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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.
[24]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[25]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"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].
[27]	"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.
[28]	"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.
[29]	"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, MASS SPECTROMETRY.
[30]	"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.

IPI

IPI00002214.

PIR

A56516.

RefSeq

NP_002257.1. NM_002266.2.

UniGene

Hs.594238.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EFX	X-ray	3.00	C	204-212	[»]
1QGK	X-ray	2.50	B	11-54	[»]
1QGR	X-ray	2.30	B	28-54	[»]
3FEX	X-ray	3.55	C	70-529	[»]
3FEY	X-ray	2.20	C	70-529	[»]

ProteinModelPortal

P52292.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6205N.

IntAct

P52292. 56 interactions.

MINT

MINT-94121.

STRING

9606.ENSP00000332455.

PTM databases

PhosphoSite

P52292.

Polymorphism databases

DMDM

1708480.

2D gel databases

SWISS-2DPAGE

P52292.

Proteomic databases

PaxDb

P52292.

PeptideAtlas

P52292.

PRIDE

P52292.

Protocols and materials databases

DNASU

3838.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000330459; ENSP00000332455; ENSG00000182481.
ENST00000537025; ENSP00000438483; ENSG00000182481.
ENST00000571293; ENSP00000460119; ENSG00000262472.
ENST00000574083; ENSP00000460025; ENSG00000262472.

GeneID

3838.

KEGG

hsa:3838.

UCSC

uc002jgk.3. human.

Organism-specific databases

CTD

3838.

GeneCards

GC17P066031.

HGNC

HGNC:6395. KPNA2.

HPA

CAB015460.

MIM

600685. gene.

neXtProt

NX_P52292.

PharmGKB

PA30186.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5064.

HOGENOM

HOG000167616.

HOVERGEN

HBG001846.

InParanoid

P52292.

KO

K15043.

OMA

HEEARIR.

OrthoDB

EOG4JWVDH.

PhylomeDB

P52292.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3pathway. Regulation of cytoplasmic and nuclear SMAD2/3 signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.

Reactome

REACT_6900. Immune System.

Gene expression databases

Bgee

P52292.

CleanEx

HS_KPNA2.

Genevestigator

P52292.

GermOnline

ENSG00000182481. Homo sapiens.

Family and domain databases

Gene3D

1.25.10.10. 1 hit.

InterPro

IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR002652. Importin-a_IBB.
IPR024931. Importing_su_alpha.
[Graphical view]

Pfam

PF00514. Arm. 8 hits.
PF01749. IBB. 1 hit.
[Graphical view]

PIRSF

PIRSF005673. Importin_alpha. 1 hit.

SMART

SM00185. ARM. 8 hits.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.

PROSITE

PS50176. ARM_REPEAT. 5 hits.
PS51214. IBB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P52292.

ChEMBL

CHEMBL1741187.

ChiTaRS

KPNA2. human.

EvolutionaryTrace

P52292.

GenomeRNAi

3838.

NextBio

15087.

SOURCE

Search...

Entry information

Entry name

IMA2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 157 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.