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Importin subunit alpha-5 (Karyopherin subunit alpha-1) (Nucleoprotein interactor 1) (NPI-1) (RAG cohort protein 2) (SRP1-beta) [Cleaved into: Importin subunit alpha-5, N-terminally processed]

 IMA5_HUMAN              Reviewed;         538 AA.
P52294; D3DN93; Q6IBQ9; Q9BQ56;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
02-JUN-2021, entry version 220.
RecName: Full=Importin subunit alpha-5;
AltName: Full=Karyopherin subunit alpha-1;
AltName: Full=Nucleoprotein interactor 1;
Short=NPI-1;
AltName: Full=RAG cohort protein 2;
AltName: Full=SRP1-beta;
Contains:
RecName: Full=Importin subunit alpha-5, N-terminally processed;
Name=KPNA1; Synonyms=RCH2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7831767; DOI=10.1016/s0042-6822(95)80026-3;
O'Neill R.E., Palese P.;
"NPI-1, the human homolog of SRP-1, interacts with influenza virus
nucleoprotein.";
Virology 206:116-125(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-73.
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-73.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-73.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-73.
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH RAG1.
PubMed=8052633; DOI=10.1073/pnas.91.16.7633;
Cortes P., Ye Z.-S., Baltimore D.;
"RAG-1 interacts with the repeated amino acid motif of the human homologue
of the yeast protein SRP1.";
Proc. Natl. Acad. Sci. U.S.A. 91:7633-7637(1994).
[8]
CHARACTERIZATION.
PubMed=7892216; DOI=10.1073/pnas.92.6.2008;
Moroianu J., Blobel G., Radu A.;
"Previously identified protein of uncertain function is karyopherin alpha
and together with karyopherin beta docks import substrate at nuclear pore
complexes.";
Proc. Natl. Acad. Sci. U.S.A. 92:2008-2011(1995).
[9]
PROTEIN SEQUENCE OF 481-495, AND DOMAINS IBB.
PubMed=8692858; DOI=10.1073/pnas.93.13.6572;
Moroianu J., Blobel G., Radu A.;
"The binding site of karyopherin alpha for karyopherin beta overlaps with a
nuclear localization sequence.";
Proc. Natl. Acad. Sci. U.S.A. 93:6572-6576(1996).
[10]
SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=7604027; DOI=10.1073/pnas.92.14.6532;
Moroianu J., Hijikata M., Blobel G., Radu A.;
"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.";
Proc. Natl. Acad. Sci. U.S.A. 92:6532-6536(1995).
[11]
INTERACTION WITH HIV-1 VPR (MICROBIAL INFECTION).
PubMed=9463369; DOI=10.1093/emboj/17.4.909;
Popov S., Rexach M., Zybarth G., Reiling N., Lee M.A., Ratner L.,
Lane C.M., Moore M.S., Blobel G., Bukrinsky M.;
"Viral protein R regulates nuclear import of the HIV-1 pre-integration
complex.";
EMBO J. 17:909-917(1998).
[12]
INTERACTION WITH HCMV UL84 (MICROBIAL INFECTION).
PubMed=12610148; DOI=10.1128/jvi.77.6.3734-3748.2003;
Lischka P., Sorg G., Kann M., Winkler M., Stamminger T.;
"A nonconventional nuclear localization signal within the UL84 protein of
human cytomegalovirus mediates nuclear import via the importin alpha/beta
pathway.";
J. Virol. 77:3734-3748(2003).
[13]
INTERACTION WITH APEX1.
PubMed=15942031; DOI=10.1093/nar/gki641;
Jackson E.B., Theriot C.A., Chattopadhyay R., Mitra S., Izumi T.;
"Analysis of nuclear transport signals in the human apurinic/apyrimidinic
endonuclease (APE1/Ref1).";
Nucleic Acids Res. 33:3303-3312(2005).
[14]
INTERACTION WITH EBOLAVIRUS VP24 (MICROBIAL INFECTION).
PubMed=16698996; DOI=10.1128/jvi.02349-05;
Reid S.P., Leung L.W., Hartman A.L., Martinez O., Shaw M.L.,
Carbonnelle C., Volchkov V.E., Nichol S.T., Basler C.F.;
"Ebola virus VP24 binds karyopherin alpha-1 and blocks STAT1 nuclear
accumulation.";
J. Virol. 80:5156-5167(2006).
[15]
INTERACTION WITH VENEZUELAN EQUINE ENCEPHALITIS VIRUS PROTEASE NSP2
(MICROBIAL INFECTION).
PubMed=17652399; DOI=10.1128/jvi.00371-07;
Montgomery S.A., Johnston R.E.;
"Nuclear import and export of Venezuelan equine encephalitis virus
nonstructural protein 2.";
J. Virol. 81:10268-10279(2007).
[16]
INTERACTION WITH EBOLAVIRUS VP24 (MICROBIAL INFECTION).
PubMed=17928350; DOI=10.1128/jvi.01097-07;
Reid S.P., Valmas C., Martinez O., Sanchez F.M., Basler C.F.;
"Ebola virus VP24 proteins inhibit the interaction of NPI-1 subfamily
karyopherin alpha proteins with activated STAT1.";
J. Virol. 81:13469-13477(2007).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[18]
UBIQUITINATION.
PubMed=19118899; DOI=10.1016/j.molimm.2008.11.009;
Simkus C., Makiya M., Jones J.M.;
"Karyopherin alpha 1 is a putative substrate of the RAG1 ubiquitin
ligase.";
Mol. Immunol. 46:1319-1325(2009).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
INTERACTION WITH SNAI1.
PubMed=21454664; DOI=10.1074/jbc.m110.213579;
Sekimoto T., Miyamoto Y., Arai S., Yoneda Y.;
"Importin alpha protein acts as a negative regulator for Snail protein
nuclear import.";
J. Biol. Chem. 286:15126-15131(2011).
[21]
INTERACTION WITH CTNNBL1 AND AICDA.
PubMed=21385873; DOI=10.1074/jbc.m110.208769;
Ganesh K., Adam S., Taylor B., Simpson P., Rada C., Neuberger M.;
"CTNNBL1 is a novel nuclear localization sequence-binding protein that
recognizes RNA-splicing factors CDC5L and Prp31.";
J. Biol. Chem. 286:17091-17102(2011).
[22]
INTERACTION WITH DCAF8.
PubMed=22500989; DOI=10.1016/j.febslet.2012.02.053;
Wu F., Wang S., Xing J., Li M., Zheng C.;
"Characterization of nuclear import and export signals determining the
subcellular localization of WD repeat-containing protein 42A (WDR42A).";
FEBS Lett. 586:1079-1085(2012).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
INTERACTION WITH ITSN1 ISOFORM 2.
PubMed=29599122; DOI=10.1042/bcj20170897;
Alvisi G., Paolini L., Contarini A., Zambarda C., Di Antonio V.,
Colosini A., Mercandelli N., Timmoneri M., Palu G., Caimi L., Ricotta D.,
Radeghieri A.;
"Intersectin goes nuclear: secret life of an endocytic protein.";
Biochem. J. 475:1455-1472(2018).
-!- 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.
-!- SUBUNIT: Heterodimer; with KPNB1 (PubMed:7604027). Interacts with
ANP32E (By similarity). Interacts with ZIC3 (By similarity). Interacts
with NSMF; the interaction occurs in a calcium-independent manner after
synaptic NMDA receptor stimulation and is required for nuclear import
of NSMF but is competed by CABP1 (By similarity). Interacts with APEX1
(PubMed:15942031). Interacts with RAG1 (PubMed:8052633). Interacts with
CTNNBL1 (via its N-terminal) (PubMed:21385873). Interacts with AICDA
(via its NLS) (PubMed:21385873). Interacts with SNAI1 (via zinc
fingers) (PubMed:21454664). Interacts with DCAF8 (PubMed:22500989).
Interacts with ITSN1 isoform 2 (PubMed:29599122).
{ECO:0000250|UniProtKB:P83953, ECO:0000250|UniProtKB:Q60960,
ECO:0000269|PubMed:15942031, ECO:0000269|PubMed:21385873,
ECO:0000269|PubMed:21454664, ECO:0000269|PubMed:22500989,
ECO:0000269|PubMed:29599122, ECO:0000269|PubMed:7604027,
ECO:0000269|PubMed:8052633}.
-!- SUBUNIT: (Microbial infection) Interacts with human
cytomegalovirus/HCMV UL84. {ECO:0000269|PubMed:12610148}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Vpr.
{ECO:0000269|PubMed:9463369}.
-!- SUBUNIT: (Microbial infection) Interacts with ebolavirus protein VP24.
{ECO:0000269|PubMed:16698996, ECO:0000269|PubMed:17928350}.
-!- SUBUNIT: (Microbial infection) Interacts with the venezuelan equine
encephalitis virus protease nsP2; this interaction probably allows the
active transport of protease nsP2 into the host nucleus.
{ECO:0000269|PubMed:17652399}.
-!- INTERACTION:
P52294; Q9GZX7: AICDA; NbExp=2; IntAct=EBI-358383, EBI-3834328;
P52294; Q92688: ANP32B; NbExp=8; IntAct=EBI-358383, EBI-762428;
P52294; Q9HAZ1: CLK4; NbExp=3; IntAct=EBI-358383, EBI-633400;
P52294; Q5TAQ9: DCAF8; NbExp=2; IntAct=EBI-358383, EBI-740686;
P52294; Q13255: GRM1; NbExp=2; IntAct=EBI-358383, EBI-8527352;
P52294; Q14974: KPNB1; NbExp=3; IntAct=EBI-358383, EBI-286758;
P52294; P20700: LMNB1; NbExp=4; IntAct=EBI-358383, EBI-968218;
P52294; Q9BQ69: MACROD1; NbExp=3; IntAct=EBI-358383, EBI-5324932;
P52294; Q9HAN9: NMNAT1; NbExp=3; IntAct=EBI-358383, EBI-3917542;
P52294; Q9UKX7: NUP50; NbExp=8; IntAct=EBI-358383, EBI-2371082;
P52294; Q9BUI4: POLR3C; NbExp=3; IntAct=EBI-358383, EBI-5452779;
P52294; Q15637: SF1; NbExp=3; IntAct=EBI-358383, EBI-744603;
P52294; P42224: STAT1; NbExp=4; IntAct=EBI-358383, EBI-1057697;
P52294; Q16594: TAF9; NbExp=4; IntAct=EBI-358383, EBI-712521;
P52294; K9N643: ORF4b; Xeno; NbExp=3; IntAct=EBI-358383, EBI-25641007;
P52294; B4URF7: PB2; Xeno; NbExp=2; IntAct=EBI-358383, EBI-6050648;
P52294; P31345: PB2; Xeno; NbExp=3; IntAct=EBI-358383, EBI-6051231;
P52294; PRO_0000037548 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-358383, EBI-6863741;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7604027}. Nucleus
{ECO:0000269|PubMed:7604027}.
-!- 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.
{ECO:0000269|PubMed:8692858}.
-!- DOMAIN: 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). {ECO:0000250}.
-!- DOMAIN: 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). {ECO:0000250}.
-!- PTM: Polyubiquitinated in the presence of RAG1 (in vitro).
{ECO:0000269|PubMed:19118899}.
-!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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EMBL; S75295; AAC60648.1; -; mRNA.
EMBL; BT006959; AAP35605.1; -; mRNA.
EMBL; CR456743; CAG33024.1; -; mRNA.
EMBL; AC083798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC096861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW79482.1; -; Genomic_DNA.
EMBL; CH471052; EAW79483.1; -; Genomic_DNA.
EMBL; BC002374; AAH02374.1; -; mRNA.
EMBL; BC003009; AAH03009.1; -; mRNA.
CCDS; CCDS3013.1; -.
PIR; I59931; I59931.
RefSeq; NP_002255.3; NM_002264.3.
RefSeq; XP_005247494.1; XM_005247437.3.
PDB; 2JDQ; X-ray; 2.20 A; A/B=66-512.
PDB; 3TJ3; X-ray; 2.70 A; A/B=66-512.
PDB; 4B18; X-ray; 2.52 A; A=66-512.
PDB; 6WX9; X-ray; 2.80 A; A=73-538.
PDBsum; 2JDQ; -.
PDBsum; 3TJ3; -.
PDBsum; 4B18; -.
PDBsum; 6WX9; -.
SMR; P52294; -.
BioGRID; 110034; 170.
ComplexPortal; CPX-1055; Importin complex, KPNA1 variant.
CORUM; P52294; -.
DIP; DIP-29296N; -.
ELM; P52294; -.
IntAct; P52294; 113.
MINT; P52294; -.
STRING; 9606.ENSP00000343701; -.
TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
iPTMnet; P52294; -.
PhosphoSitePlus; P52294; -.
BioMuta; KPNA1; -.
DMDM; 296439328; -.
EPD; P52294; -.
jPOST; P52294; -.
MassIVE; P52294; -.
MaxQB; P52294; -.
PaxDb; P52294; -.
PeptideAtlas; P52294; -.
PRIDE; P52294; -.
ProteomicsDB; 56476; -.
Antibodypedia; 32899; 382 antibodies.
DNASU; 3836; -.
Ensembl; ENST00000344337; ENSP00000343701; ENSG00000114030.
GeneID; 3836; -.
KEGG; hsa:3836; -.
UCSC; uc003efe.3; human.
CTD; 3836; -.
DisGeNET; 3836; -.
GeneCards; KPNA1; -.
HGNC; HGNC:6394; KPNA1.
HPA; ENSG00000114030; Tissue enhanced (skeletal).
MIM; 600686; gene.
neXtProt; NX_P52294; -.
OpenTargets; ENSG00000114030; -.
PharmGKB; PA30185; -.
VEuPathDB; HostDB:ENSG00000114030.12; -.
eggNOG; KOG0166; Eukaryota.
GeneTree; ENSGT01030000234650; -.
HOGENOM; CLU_018084_6_0_1; -.
InParanoid; P52294; -.
OMA; NAYAQMI; -.
OrthoDB; 1111872at2759; -.
PhylomeDB; P52294; -.
TreeFam; TF354205; -.
PathwayCommons; P52294; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-140342; Apoptosis induced DNA fragmentation.
Reactome; R-HSA-162592; Integration of provirus.
Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
Reactome; R-HSA-9636249; Inhibition of nitric oxide production.
SignaLink; P52294; -.
SIGNOR; P52294; -.
BioGRID-ORCS; 3836; 7 hits in 1001 CRISPR screens.
ChiTaRS; KPNA1; human.
EvolutionaryTrace; P52294; -.
GeneWiki; Karyopherin_alpha_1; -.
GenomeRNAi; 3836; -.
Pharos; P52294; Tbio.
PRO; PR:P52294; -.
Proteomes; UP000005640; Chromosome 3.
RNAct; P52294; protein.
Bgee; ENSG00000114030; Expressed in biceps brachii and 235 other tissues.
ExpressionAtlas; P52294; baseline and differential.
Genevisible; P52294; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0061608; F:nuclear import signal receptor activity; IBA:GO_Central.
GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
GO; GO:0006309; P:apoptotic DNA fragmentation; TAS:Reactome.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0019054; P:modulation by virus of host cellular process; TAS:Reactome.
GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IBA:GO_Central.
GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0000018; P:regulation of DNA recombination; TAS:ProtInc.
GO; GO:0014901; P:satellite cell activation involved in skeletal muscle regeneration; IEA:Ensembl.
GO; GO:0014841; P:skeletal muscle satellite cell proliferation; IEA:Ensembl.
Gene3D; 1.20.5.690; -; 1.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR032413; Arm_3.
InterPro; IPR000225; Armadillo.
InterPro; IPR002652; Importin-a_IBB.
InterPro; IPR036975; Importin-a_IBB_sf.
InterPro; IPR024931; Importin_alpha.
Pfam; PF00514; Arm; 8.
Pfam; PF16186; Arm_3; 1.
Pfam; PF01749; IBB; 1.
PIRSF; PIRSF005673; Importin_alpha; 1.
SMART; SM00185; ARM; 8.
SUPFAM; SSF48371; SSF48371; 1.
PROSITE; PS50176; ARM_REPEAT; 4.
PROSITE; PS51214; IBB; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
Host-virus interaction; Nucleus; Phosphoprotein; Protein transport;
Reference proteome; Repeat; Transport; Ubl conjugation.
CHAIN 1..538
/note="Importin subunit alpha-5"
/id="PRO_0000120719"
INIT_MET 1
/note="Removed; alternate"
/evidence="ECO:0007744|PubMed:22814378"
CHAIN 2..538
/note="Importin subunit alpha-5, N-terminally processed"
/id="PRO_0000424491"
DOMAIN 1..57
/note="IBB"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
REPEAT 77..117
/note="ARM 1; truncated"
REPEAT 118..161
/note="ARM 2"
REPEAT 162..206
/note="ARM 3"
REPEAT 207..245
/note="ARM 4"
REPEAT 246..290
/note="ARM 5"
REPEAT 291..330
/note="ARM 6"
REPEAT 331..372
/note="ARM 7"
REPEAT 373..412
/note="ARM 8"
REPEAT 413..457
/note="ARM 9"
REPEAT 460..504
/note="ARM 10; atypical"
REGION 1..36
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 149..241
/note="NLS binding site (major)"
/evidence="ECO:0000250"
REGION 245..437
/note="Binding to RAG1"
REGION 318..406
/note="NLS binding site (minor)"
/evidence="ECO:0000250"
MOTIF 42..51
/note="Nuclear localization signal"
/evidence="ECO:0000250"
COMPBIAS 10..36
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0007744|PubMed:22814378"
MOD_RES 2
/note="N-acetylthreonine; in Importin subunit alpha-5, N-
terminally processed"
/evidence="ECO:0007744|PubMed:22814378"
MOD_RES 3
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 63
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:24275569"
VARIANT 73
/note="S -> N (in dbSNP:rs4678193)"
/evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
ECO:0000269|Ref.3, ECO:0000269|Ref.5"
/id="VAR_050002"
CONFLICT 142
/note="T -> S (in Ref. 1; AAC60648)"
/evidence="ECO:0000305"
CONFLICT 169
/note="G -> R (in Ref. 1; AAC60648)"
/evidence="ECO:0000305"
HELIX 85..92
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 96..111
/evidence="ECO:0007829|PDB:2JDQ"
STRAND 112..115
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 118..122
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 127..135
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 141..155
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 159..167
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 170..177
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 183..197
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 201..209
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 213..219
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 226..240
/evidence="ECO:0007829|PDB:2JDQ"
STRAND 243..245
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 249..251
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 253..255
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 256..262
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 268..281
/evidence="ECO:0007829|PDB:2JDQ"
STRAND 283..285
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 286..294
/evidence="ECO:0007829|PDB:2JDQ"
TURN 295..297
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 298..304
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 310..323
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 328..335
/evidence="ECO:0007829|PDB:2JDQ"
TURN 336..338
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 339..346
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 352..365
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 370..378
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 381..391
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 394..410
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 413..422
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 425..430
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 431..433
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 437..460
/evidence="ECO:0007829|PDB:2JDQ"
STRAND 461..463
/evidence="ECO:0007829|PDB:3TJ3"
HELIX 468..476
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 478..485
/evidence="ECO:0007829|PDB:2JDQ"
HELIX 487..504
/evidence="ECO:0007829|PDB:2JDQ"
SEQUENCE 538 AA; 60222 MW; E8407A3352D6051C CRC64;
MTTPGKENFR LKSYKNKSLN PDEMRRRREE EGLQLRKQKR EEQLFKRRNV ATAEEETEEE
VMSDGGFHEA QISNMEMAPG GVITSDMIEM IFSKSPEQQL SATQKFRKLL SKEPNPPIDE
VISTPGVVAR FVEFLKRKEN CTLQFESAWV LTNIASGNSL QTRIVIQAGA VPIFIELLSS
EFEDVQEQAV WALGNIAGDS TMCRDYVLDC NILPPLLQLF SKQNRLTMTR NAVWALSNLC
RGKSPPPEFA KVSPCLNVLS WLLFVSDTDV LADACWALSY LSDGPNDKIQ AVIDAGVCRR
LVELLMHNDY KVVSPALRAV GNIVTGDDIQ TQVILNCSAL QSLLHLLSSP KESIKKEACW
TISNITAGNR AQIQTVIDAN IFPALISILQ TAEFRTRKEA AWAITNATSG GSAEQIKYLV
ELGCIKPLCD LLTVMDSKIV QVALNGLENI LRLGEQEAKR NGTGINPYCA LIEEAYGLDK
IEFLQSHENQ EIYQKAFDLI EHYFGTEDED SSIAPQVDLN QQQYIFQQCE APMEGFQL


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Related Genes :
[KPNA1 RCH2] Importin subunit alpha-5 (Karyopherin subunit alpha-1) (Nucleoprotein interactor 1) (NPI-1) (RAG cohort protein 2) (SRP1-beta) [Cleaved into: Importin subunit alpha-5, N-terminally processed]
[Kpna1 Rch2] Importin subunit alpha-5 (Importin alpha-S1) (Karyopherin subunit alpha-1) (Nucleoprotein interactor 1) (NPI-1) (RAG cohort protein 2) (SRP1-beta)
[KPNA2 RCH1 SRP1] Importin subunit alpha-1 (Karyopherin subunit alpha-2) (RAG cohort protein 1) (SRP1-alpha)
[Kpna2 Rch1] Importin subunit alpha-1 (Importin alpha P1) (Karyopherin subunit alpha-2) (Pendulin) (Pore targeting complex 58 kDa subunit) (PTAC58) (RAG cohort protein 1) (SRP1-alpha)
[SRP1 KAP60 YNL189W N1606] Importin subunit alpha (Karyopherin subunit alpha) (Karyopherin-60) (Serine-rich RNA polymerase I suppressor protein)
[KPNA3 QIP2] Importin subunit alpha-4 (Importin alpha Q2) (Qip2) (Karyopherin subunit alpha-3) (SRP1-gamma)
[KPNA1] Importin subunit alpha-5 (Karyopherin subunit alpha-1) [Cleaved into: Importin subunit alpha-5, N-terminally processed]
[KPNA1] Importin subunit alpha-5 (Karyopherin subunit alpha-1) [Cleaved into: Importin subunit alpha-5, N-terminally processed]
[Kpna1] Importin subunit alpha-5 (Importin alpha-5) (Karyopherin subunit alpha-1)
[KPNA5] Importin subunit alpha-6 (Karyopherin subunit alpha-5)
[Ywhab] 14-3-3 protein beta/alpha (Protein kinase C inhibitor protein 1) (KCIP-1) [Cleaved into: 14-3-3 protein beta/alpha, N-terminally processed]
[iaaA spt ybiK b0828 JW0812] Isoaspartyl peptidase (EC 3.4.19.5) (Beta-aspartyl-peptidase) (EcAIII) (Isoaspartyl dipeptidase) [Cleaved into: Isoaspartyl peptidase subunit alpha; Isoaspartyl peptidase subunit beta]
[GSTA1] Glutathione S-transferase A1 (EC 2.5.1.18) (13-hydroperoxyoctadecadienoate peroxidase) (EC 1.11.1.-) (Androst-5-ene-3,17-dione isomerase) (EC 5.3.3.-) (GST HA subunit 1) (GST class-alpha member 1) (GST-epsilon) (GSTA1-1) (GTH1) [Cleaved into: Glutathione S-transferase A1, N-terminally processed]
[KPNA6 IPOA7] Importin subunit alpha-7 (Karyopherin subunit alpha-6)
[psmA1 psmA HVO_1091] Proteasome subunit alpha 1 (20S proteasome alpha subunit 1) (Proteasome core protein PsmA 1) [Cleaved into: Proteasome subunit alpha 1, N-terminally processed]
[ima-2 F26B1.3] Importin subunit alpha-2 (Karyopherin subunit alpha-2)
[Kpna6 Kpna5] Importin subunit alpha-7 (Importin alpha-S2) (Karyopherin subunit alpha-6)
[kapA srp1 AN2142] Importin subunit alpha (Karyopherin alpha)
[KPNA4 QIP1] Importin subunit alpha-3 (Importin alpha Q1) (Qip1) (Karyopherin subunit alpha-4)
[Prkar1a] cAMP-dependent protein kinase type I-alpha regulatory subunit [Cleaved into: cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed]
[Rack1 Gnb2-rs1 Gnb2l1] Receptor of activated protein C kinase 1 (12-3) (Guanine nucleotide-binding protein subunit beta-2-like 1) (Receptor for activated C kinase) (Receptor of activated protein kinase C 1) (p205) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed (Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed)]
[imp1 SPBC1604.08c] Importin subunit alpha-2 (Importin-1) (Karyopherin subunit alpha-2)
[RACK1 GNB2L1 HLC7 PIG21] Receptor of activated protein C kinase 1 (Cell proliferation-inducing gene 21 protein) (Guanine nucleotide-binding protein subunit beta-2-like 1) (Guanine nucleotide-binding protein subunit beta-like protein 12.3) (Human lung cancer oncogene 7 protein) (HLC-7) (Receptor for activated C kinase) (Small ribosomal subunit protein RACK1) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed (Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed)]
[PRKAR1A] cAMP-dependent protein kinase type I-alpha regulatory subunit [Cleaved into: cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed]
[ima-3 F32E10.4] Importin subunit alpha-3 (Karyopherin subunit alpha-3)
[KPNB1 NTF97] Importin subunit beta-1 (Importin-90) (Karyopherin subunit beta-1) (Nuclear factor p97) (Pore targeting complex 97 kDa subunit) (PTAC97)
[Prkar1a] cAMP-dependent protein kinase type I-alpha regulatory subunit [Cleaved into: cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed]
[Kpna4 Qip1] Importin subunit alpha-3 (Importin alpha Q1) (Qip1) (Karyopherin subunit alpha-4)
[gag-pol] Gag-Pol polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; Spacer peptide (SP) (p3); Nucleocapsid protein p12; Protease p15 (EC 3.4.23.-); Reverse transcriptase beta-subunit (RT-beta); Reverse transcriptase alpha-subunit (RT-alpha) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-) (pp32); p4]
[YWHAB] 14-3-3 protein beta/alpha (Protein 1054) (Protein kinase C inhibitor protein 1) (KCIP-1) [Cleaved into: 14-3-3 protein beta/alpha, N-terminally processed]

Bibliography :