IMA5_HUMAN
ID IMA5_HUMAN Reviewed; 538 AA.
AC P52294; D3DN93; Q6IBQ9; Q9BQ56;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Importin subunit alpha-5;
DE AltName: Full=Karyopherin subunit alpha-1;
DE AltName: Full=Nucleoprotein interactor 1;
DE Short=NPI-1;
DE AltName: Full=RAG cohort protein 2;
DE AltName: Full=SRP1-beta;
DE Contains:
DE RecName: Full=Importin subunit alpha-5, N-terminally processed;
GN Name=KPNA1; Synonyms=RCH2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7831767; DOI=10.1016/s0042-6822(95)80026-3;
RA O'Neill R.E., Palese P.;
RT "NPI-1, the human homolog of SRP-1, interacts with influenza virus
RT nucleoprotein.";
RL Virology 206:116-125(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-73.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-73.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-73.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-73.
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH RAG1.
RX PubMed=8052633; DOI=10.1073/pnas.91.16.7633;
RA Cortes P., Ye Z.-S., Baltimore D.;
RT "RAG-1 interacts with the repeated amino acid motif of the human homologue
RT of the yeast protein SRP1.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7633-7637(1994).
RN [8]
RP CHARACTERIZATION.
RX PubMed=7892216; DOI=10.1073/pnas.92.6.2008;
RA Moroianu J., Blobel G., Radu A.;
RT "Previously identified protein of uncertain function is karyopherin alpha
RT and together with karyopherin beta docks import substrate at nuclear pore
RT complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:2008-2011(1995).
RN [9]
RP PROTEIN SEQUENCE OF 481-495, AND DOMAINS IBB.
RX PubMed=8692858; DOI=10.1073/pnas.93.13.6572;
RA Moroianu J., Blobel G., Radu A.;
RT "The binding site of karyopherin alpha for karyopherin beta overlaps with a
RT nuclear localization sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:6572-6576(1996).
RN [10]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=7604027; DOI=10.1073/pnas.92.14.6532;
RA Moroianu J., Hijikata M., Blobel G., Radu A.;
RT "Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1
RT or alpha 2 subunit binds nuclear localization signal and beta subunit
RT interacts with peptide repeat-containing nucleoporins.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:6532-6536(1995).
RN [11]
RP INTERACTION WITH HIV-1 VPR (MICROBIAL INFECTION).
RX PubMed=9463369; DOI=10.1093/emboj/17.4.909;
RA Popov S., Rexach M., Zybarth G., Reiling N., Lee M.A., Ratner L.,
RA Lane C.M., Moore M.S., Blobel G., Bukrinsky M.;
RT "Viral protein R regulates nuclear import of the HIV-1 pre-integration
RT complex.";
RL EMBO J. 17:909-917(1998).
RN [12]
RP INTERACTION WITH HCMV UL84 (MICROBIAL INFECTION).
RX PubMed=12610148; DOI=10.1128/jvi.77.6.3734-3748.2003;
RA Lischka P., Sorg G., Kann M., Winkler M., Stamminger T.;
RT "A nonconventional nuclear localization signal within the UL84 protein of
RT human cytomegalovirus mediates nuclear import via the importin alpha/beta
RT pathway.";
RL J. Virol. 77:3734-3748(2003).
RN [13]
RP INTERACTION WITH APEX1.
RX PubMed=15942031; DOI=10.1093/nar/gki641;
RA Jackson E.B., Theriot C.A., Chattopadhyay R., Mitra S., Izumi T.;
RT "Analysis of nuclear transport signals in the human apurinic/apyrimidinic
RT endonuclease (APE1/Ref1).";
RL Nucleic Acids Res. 33:3303-3312(2005).
RN [14]
RP INTERACTION WITH EBOLAVIRUS VP24 (MICROBIAL INFECTION).
RX PubMed=16698996; DOI=10.1128/jvi.02349-05;
RA Reid S.P., Leung L.W., Hartman A.L., Martinez O., Shaw M.L.,
RA Carbonnelle C., Volchkov V.E., Nichol S.T., Basler C.F.;
RT "Ebola virus VP24 binds karyopherin alpha-1 and blocks STAT1 nuclear
RT accumulation.";
RL J. Virol. 80:5156-5167(2006).
RN [15]
RP INTERACTION WITH VENEZUELAN EQUINE ENCEPHALITIS VIRUS PROTEASE NSP2
RP (MICROBIAL INFECTION).
RX PubMed=17652399; DOI=10.1128/jvi.00371-07;
RA Montgomery S.A., Johnston R.E.;
RT "Nuclear import and export of Venezuelan equine encephalitis virus
RT nonstructural protein 2.";
RL J. Virol. 81:10268-10279(2007).
RN [16]
RP INTERACTION WITH EBOLAVIRUS VP24 (MICROBIAL INFECTION).
RX PubMed=17928350; DOI=10.1128/jvi.01097-07;
RA Reid S.P., Valmas C., Martinez O., Sanchez F.M., Basler C.F.;
RT "Ebola virus VP24 proteins inhibit the interaction of NPI-1 subfamily
RT karyopherin alpha proteins with activated STAT1.";
RL J. Virol. 81:13469-13477(2007).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [18]
RP UBIQUITINATION.
RX PubMed=19118899; DOI=10.1016/j.molimm.2008.11.009;
RA Simkus C., Makiya M., Jones J.M.;
RT "Karyopherin alpha 1 is a putative substrate of the RAG1 ubiquitin
RT ligase.";
RL Mol. Immunol. 46:1319-1325(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP INTERACTION WITH SNAI1.
RX PubMed=21454664; DOI=10.1074/jbc.m110.213579;
RA Sekimoto T., Miyamoto Y., Arai S., Yoneda Y.;
RT "Importin alpha protein acts as a negative regulator for Snail protein
RT nuclear import.";
RL J. Biol. Chem. 286:15126-15131(2011).
RN [21]
RP INTERACTION WITH CTNNBL1 AND AICDA.
RX PubMed=21385873; DOI=10.1074/jbc.m110.208769;
RA Ganesh K., Adam S., Taylor B., Simpson P., Rada C., Neuberger M.;
RT "CTNNBL1 is a novel nuclear localization sequence-binding protein that
RT recognizes RNA-splicing factors CDC5L and Prp31.";
RL J. Biol. Chem. 286:17091-17102(2011).
RN [22]
RP INTERACTION WITH DCAF8.
RX PubMed=22500989; DOI=10.1016/j.febslet.2012.02.053;
RA Wu F., Wang S., Xing J., Li M., Zheng C.;
RT "Characterization of nuclear import and export signals determining the
RT subcellular localization of WD repeat-containing protein 42A (WDR42A).";
RL FEBS Lett. 586:1079-1085(2012).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [26]
RP INTERACTION WITH ITSN1 ISOFORM 2.
RX PubMed=29599122; DOI=10.1042/bcj20170897;
RA Alvisi G., Paolini L., Contarini A., Zambarda C., Di Antonio V.,
RA Colosini A., Mercandelli N., Timmoneri M., Palu G., Caimi L., Ricotta D.,
RA Radeghieri A.;
RT "Intersectin goes nuclear: secret life of an endocytic protein.";
RL Biochem. J. 475:1455-1472(2018).
CC -!- FUNCTION: Functions in nuclear protein import as an adapter protein for
CC nuclear receptor KPNB1. Binds specifically and directly to substrates
CC containing either a simple or bipartite NLS motif. Docking of the
CC importin/substrate complex to the nuclear pore complex (NPC) is
CC mediated by KPNB1 through binding to nucleoporin FxFG repeats and the
CC complex is subsequently translocated through the pore by an energy
CC requiring, Ran-dependent mechanism. At the nucleoplasmic side of the
CC NPC, Ran binds to importin-beta and the three components separate and
CC importin-alpha and -beta are re-exported from the nucleus to the
CC cytoplasm where GTP hydrolysis releases Ran from importin. The
CC directionality of nuclear import is thought to be conferred by an
CC asymmetric distribution of the GTP- and GDP-bound forms of Ran between
CC the cytoplasm and nucleus. In vitro, mediates the nuclear import of
CC human cytomegalovirus UL84 by recognizing a non-classical NLS.
CC -!- SUBUNIT: Heterodimer; with KPNB1 (PubMed:7604027). Interacts with
CC ANP32E (By similarity). Interacts with ZIC3 (By similarity). Interacts
CC with NSMF; the interaction occurs in a calcium-independent manner after
CC synaptic NMDA receptor stimulation and is required for nuclear import
CC of NSMF but is competed by CABP1 (By similarity). Interacts with APEX1
CC (PubMed:15942031). Interacts with RAG1 (PubMed:8052633). Interacts with
CC CTNNBL1 (via its N-terminal) (PubMed:21385873). Interacts with AICDA
CC (via its NLS) (PubMed:21385873). Interacts with SNAI1 (via zinc
CC fingers) (PubMed:21454664). Interacts with DCAF8 (PubMed:22500989).
CC Interacts with ITSN1 isoform 2 (PubMed:29599122). Interacts with TALDO1
CC isoform 1 (By similarity). {ECO:0000250|UniProtKB:P83953,
CC ECO:0000250|UniProtKB:Q60960, ECO:0000269|PubMed:15942031,
CC ECO:0000269|PubMed:21385873, ECO:0000269|PubMed:21454664,
CC ECO:0000269|PubMed:22500989, ECO:0000269|PubMed:29599122,
CC ECO:0000269|PubMed:7604027, ECO:0000269|PubMed:8052633}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human
CC cytomegalovirus/HCMV UL84. {ECO:0000269|PubMed:12610148}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Vpr.
CC {ECO:0000269|PubMed:9463369}.
CC -!- SUBUNIT: (Microbial infection) Interacts with ebolavirus protein VP24.
CC {ECO:0000269|PubMed:16698996, ECO:0000269|PubMed:17928350}.
CC -!- SUBUNIT: (Microbial infection) Interacts with the venezuelan equine
CC encephalitis virus protease nsP2; this interaction probably allows the
CC active transport of protease nsP2 into the host nucleus.
CC {ECO:0000269|PubMed:17652399}.
CC -!- INTERACTION:
CC P52294; Q9GZX7: AICDA; NbExp=2; IntAct=EBI-358383, EBI-3834328;
CC P52294; Q92688: ANP32B; NbExp=8; IntAct=EBI-358383, EBI-762428;
CC P52294; Q9HAZ1: CLK4; NbExp=3; IntAct=EBI-358383, EBI-633400;
CC P52294; Q5TAQ9: DCAF8; NbExp=2; IntAct=EBI-358383, EBI-740686;
CC P52294; Q13255: GRM1; NbExp=2; IntAct=EBI-358383, EBI-8527352;
CC P52294; Q14974: KPNB1; NbExp=3; IntAct=EBI-358383, EBI-286758;
CC P52294; P20700: LMNB1; NbExp=4; IntAct=EBI-358383, EBI-968218;
CC P52294; Q9BQ69: MACROD1; NbExp=3; IntAct=EBI-358383, EBI-5324932;
CC P52294; Q9HAN9: NMNAT1; NbExp=3; IntAct=EBI-358383, EBI-3917542;
CC P52294; Q9UKX7: NUP50; NbExp=8; IntAct=EBI-358383, EBI-2371082;
CC P52294; Q9BUI4: POLR3C; NbExp=3; IntAct=EBI-358383, EBI-5452779;
CC P52294; Q15637: SF1; NbExp=3; IntAct=EBI-358383, EBI-744603;
CC P52294; P42224: STAT1; NbExp=4; IntAct=EBI-358383, EBI-1057697;
CC P52294; Q16594: TAF9; NbExp=4; IntAct=EBI-358383, EBI-712521;
CC P52294; K9N643: ORF4b; Xeno; NbExp=3; IntAct=EBI-358383, EBI-25641007;
CC P52294; B4URF7: PB2; Xeno; NbExp=2; IntAct=EBI-358383, EBI-6050648;
CC P52294; P31345: PB2; Xeno; NbExp=3; IntAct=EBI-358383, EBI-6051231;
CC P52294; PRO_0000037548 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-358383, EBI-6863741;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7604027}. Nucleus
CC {ECO:0000269|PubMed:7604027}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC -!- DOMAIN: Consists of an N-terminal hydrophilic region, a hydrophobic
CC central region composed of 10 repeats, and a short hydrophilic C-
CC terminus. The N-terminal hydrophilic region contains the importin beta
CC binding domain (IBB domain), which is sufficient for binding importin
CC beta and essential for nuclear protein import.
CC {ECO:0000269|PubMed:8692858}.
CC -!- DOMAIN: The IBB domain is thought to act as an intrasteric
CC autoregulatory sequence by interacting with the internal autoinhibitory
CC NLS. Binding of KPNB1 probably overlaps the internal NLS and
CC contributes to a high affinity for cytoplasmic NLS-containing cargo
CC substrates. After dissociation of the importin/substrate complex in the
CC nucleus the internal autohibitory NLS contributes to a low affinity for
CC nuclear NLS-containing proteins (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The major and minor NLS binding sites are mainly involved in
CC recognition of simple or bipartite NLS motifs. Structurally located
CC within in a helical surface groove they contain several conserved Trp
CC and Asn residues of the corresponding third helices (H3) of ARM repeats
CC which mainly contribute to binding (By similarity). {ECO:0000250}.
CC -!- PTM: Polyubiquitinated in the presence of RAG1 (in vitro).
CC {ECO:0000269|PubMed:19118899}.
CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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DR EMBL; S75295; AAC60648.1; -; mRNA.
DR EMBL; BT006959; AAP35605.1; -; mRNA.
DR EMBL; CR456743; CAG33024.1; -; mRNA.
DR EMBL; AC083798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79482.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79483.1; -; Genomic_DNA.
DR EMBL; BC002374; AAH02374.1; -; mRNA.
DR EMBL; BC003009; AAH03009.1; -; mRNA.
DR CCDS; CCDS3013.1; -.
DR PIR; I59931; I59931.
DR RefSeq; NP_002255.3; NM_002264.3.
DR RefSeq; XP_005247494.1; XM_005247437.3.
DR PDB; 2JDQ; X-ray; 2.20 A; A/B=66-512.
DR PDB; 3TJ3; X-ray; 2.70 A; A/B=66-512.
DR PDB; 4B18; X-ray; 2.52 A; A=66-512.
DR PDB; 6WX9; X-ray; 2.80 A; A=73-538.
DR PDBsum; 2JDQ; -.
DR PDBsum; 3TJ3; -.
DR PDBsum; 4B18; -.
DR PDBsum; 6WX9; -.
DR AlphaFoldDB; P52294; -.
DR SMR; P52294; -.
DR BioGRID; 110034; 301.
DR ComplexPortal; CPX-1055; Importin complex, KPNA1 variant.
DR CORUM; P52294; -.
DR DIP; DIP-29296N; -.
DR ELM; P52294; -.
DR IntAct; P52294; 116.
DR MINT; P52294; -.
DR STRING; 9606.ENSP00000343701; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR iPTMnet; P52294; -.
DR PhosphoSitePlus; P52294; -.
DR BioMuta; KPNA1; -.
DR DMDM; 296439328; -.
DR EPD; P52294; -.
DR jPOST; P52294; -.
DR MassIVE; P52294; -.
DR MaxQB; P52294; -.
DR PaxDb; P52294; -.
DR PeptideAtlas; P52294; -.
DR PRIDE; P52294; -.
DR ProteomicsDB; 56476; -.
DR Antibodypedia; 32899; 394 antibodies from 39 providers.
DR DNASU; 3836; -.
DR Ensembl; ENST00000344337.11; ENSP00000343701.6; ENSG00000114030.13.
DR GeneID; 3836; -.
DR KEGG; hsa:3836; -.
DR MANE-Select; ENST00000344337.11; ENSP00000343701.6; NM_002264.4; NP_002255.3.
DR UCSC; uc003efe.3; human.
DR CTD; 3836; -.
DR DisGeNET; 3836; -.
DR GeneCards; KPNA1; -.
DR HGNC; HGNC:6394; KPNA1.
DR HPA; ENSG00000114030; Low tissue specificity.
DR MIM; 600686; gene.
DR neXtProt; NX_P52294; -.
DR OpenTargets; ENSG00000114030; -.
DR PharmGKB; PA30185; -.
DR VEuPathDB; HostDB:ENSG00000114030; -.
DR eggNOG; KOG0166; Eukaryota.
DR GeneTree; ENSGT01050000244950; -.
DR HOGENOM; CLU_018084_6_0_1; -.
DR InParanoid; P52294; -.
DR OMA; MTEMIFS; -.
DR OrthoDB; 1111872at2759; -.
DR PhylomeDB; P52294; -.
DR TreeFam; TF354205; -.
DR PathwayCommons; P52294; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-140342; Apoptosis induced DNA fragmentation.
DR Reactome; R-HSA-162592; Integration of provirus.
DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR Reactome; R-HSA-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR Reactome; R-HSA-9636249; Inhibition of nitric oxide production.
DR SignaLink; P52294; -.
DR SIGNOR; P52294; -.
DR BioGRID-ORCS; 3836; 12 hits in 1087 CRISPR screens.
DR ChiTaRS; KPNA1; human.
DR EvolutionaryTrace; P52294; -.
DR GeneWiki; Karyopherin_alpha_1; -.
DR GenomeRNAi; 3836; -.
DR Pharos; P52294; Tbio.
DR PRO; PR:P52294; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P52294; protein.
DR Bgee; ENSG00000114030; Expressed in gluteal muscle and 202 other tissues.
DR ExpressionAtlas; P52294; baseline and differential.
DR Genevisible; P52294; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IPI:ComplexPortal.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IBA:GO_Central.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0000018; P:regulation of DNA recombination; TAS:ProtInc.
DR GO; GO:0014901; P:satellite cell activation involved in skeletal muscle regeneration; IEA:Ensembl.
DR GO; GO:0014841; P:skeletal muscle satellite cell proliferation; IEA:Ensembl.
DR Gene3D; 1.20.5.690; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032413; Arm_3.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR002652; Importin-a_IBB.
DR InterPro; IPR036975; Importin-a_IBB_sf.
DR InterPro; IPR024931; Importin_alpha.
DR Pfam; PF00514; Arm; 8.
DR Pfam; PF16186; Arm_3; 1.
DR Pfam; PF01749; IBB; 1.
DR PIRSF; PIRSF005673; Importin_alpha; 1.
DR SMART; SM00185; ARM; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 4.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport; Ubl conjugation.
FT CHAIN 1..538
FT /note="Importin subunit alpha-5"
FT /id="PRO_0000120719"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..538
FT /note="Importin subunit alpha-5, N-terminally processed"
FT /id="PRO_0000424491"
FT DOMAIN 1..57
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REPEAT 77..117
FT /note="ARM 1; truncated"
FT REPEAT 118..161
FT /note="ARM 2"
FT REPEAT 162..206
FT /note="ARM 3"
FT REPEAT 207..245
FT /note="ARM 4"
FT REPEAT 246..290
FT /note="ARM 5"
FT REPEAT 291..330
FT /note="ARM 6"
FT REPEAT 331..372
FT /note="ARM 7"
FT REPEAT 373..412
FT /note="ARM 8"
FT REPEAT 413..457
FT /note="ARM 9"
FT REPEAT 460..504
FT /note="ARM 10; atypical"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..241
FT /note="NLS binding site (major)"
FT /evidence="ECO:0000250"
FT REGION 245..437
FT /note="Binding to RAG1"
FT REGION 318..406
FT /note="NLS binding site (minor)"
FT /evidence="ECO:0000250"
FT MOTIF 42..51
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 10..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Importin subunit alpha-5, N-
FT terminally processed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 73
FT /note="S -> N (in dbSNP:rs4678193)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.5"
FT /id="VAR_050002"
FT CONFLICT 142
FT /note="T -> S (in Ref. 1; AAC60648)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="G -> R (in Ref. 1; AAC60648)"
FT /evidence="ECO:0000305"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 96..111
FT /evidence="ECO:0007829|PDB:2JDQ"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 183..197
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 226..240
FT /evidence="ECO:0007829|PDB:2JDQ"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 256..262
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:2JDQ"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 286..294
FT /evidence="ECO:0007829|PDB:2JDQ"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 310..323
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 328..335
FT /evidence="ECO:0007829|PDB:2JDQ"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 339..346
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 352..365
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 370..378
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 381..391
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 394..410
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 413..422
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 425..430
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 437..460
FT /evidence="ECO:0007829|PDB:2JDQ"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:3TJ3"
FT HELIX 468..476
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 478..485
FT /evidence="ECO:0007829|PDB:2JDQ"
FT HELIX 487..504
FT /evidence="ECO:0007829|PDB:2JDQ"
SQ 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
