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Importin subunit alpha-7 (Karyopherin subunit alpha-6)

 IMA7_HUMAN              Reviewed;         536 AA.
O60684; B2RDC7; D3DPP5; Q5VVU3;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
02-JUN-2021, entry version 185.
RecName: Full=Importin subunit alpha-7;
AltName: Full=Karyopherin subunit alpha-6;
Name=KPNA6; Synonyms=IPOA7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH KPNB1, AND TISSUE
SPECIFICITY.
PubMed=10523667; DOI=10.1128/mcb.19.11.7782;
Koehler M., Speck C., Christiansen M., Bischoff F.R., Prehn S., Haller H.,
Goerlich D., Hartmann E.;
"Evidence for distinct substrate specificities of importin alpha family
members in nuclear protein import.";
Mol. Cell. Biol. 19:7782-7791(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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].
TISSUE=Uterus;
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 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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND 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).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
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).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-113, 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).
[14]
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).
-!- 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. {ECO:0000269|PubMed:10523667}.
-!- SUBUNIT: Interacts with ZIC3 (By similarity). Forms a complex with
importin subunit beta-1. {ECO:0000250, ECO:0000269|PubMed:10523667}.
-!- SUBUNIT: (Microbial infection) Interacts with ebolavirus protein VP24.
{ECO:0000269|PubMed:17928350}.
-!- INTERACTION:
O60684; X5D778: ANKRD11; NbExp=5; IntAct=EBI-359923, EBI-17183751;
O60684; Q92688: ANP32B; NbExp=3; IntAct=EBI-359923, EBI-762428;
O60684; Q96C86: DCPS; NbExp=5; IntAct=EBI-359923, EBI-3917181;
O60684; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-359923, EBI-6658203;
O60684; O14893: GEMIN2; NbExp=5; IntAct=EBI-359923, EBI-443648;
O60684; P01583: IL1A; NbExp=3; IntAct=EBI-359923, EBI-1749782;
O60684; O75564-2: JRK; NbExp=3; IntAct=EBI-359923, EBI-17181882;
O60684; Q92993: KAT5; NbExp=3; IntAct=EBI-359923, EBI-399080;
O60684; Q14974: KPNB1; NbExp=2; IntAct=EBI-359923, EBI-286758;
O60684; P20700: LMNB1; NbExp=3; IntAct=EBI-359923, EBI-968218;
O60684; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-359923, EBI-716006;
O60684; Q9HAN9: NMNAT1; NbExp=3; IntAct=EBI-359923, EBI-3917542;
O60684; P46087: NOP2; NbExp=3; IntAct=EBI-359923, EBI-356811;
O60684; Q9UKX7: NUP50; NbExp=6; IntAct=EBI-359923, EBI-2371082;
O60684; Q9BUI4: POLR3C; NbExp=5; IntAct=EBI-359923, EBI-5452779;
O60684; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-359923, EBI-11956563;
O60684; P78424: POU6F2; NbExp=3; IntAct=EBI-359923, EBI-12029004;
O60684; O43148: RNMT; NbExp=3; IntAct=EBI-359923, EBI-877832;
O60684; Q15637: SF1; NbExp=4; IntAct=EBI-359923, EBI-744603;
O60684; Q16594: TAF9; NbExp=4; IntAct=EBI-359923, EBI-712521;
O60684; P03466: NP; Xeno; NbExp=5; IntAct=EBI-359923, EBI-2547640;
O60684; P31345: PB2; Xeno; NbExp=3; IntAct=EBI-359923, EBI-6051231;
O60684; Q05322: VP24; Xeno; NbExp=7; IntAct=EBI-359923, EBI-6153153;
-!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10523667}.
-!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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EMBL; AF060543; AAC15233.1; -; mRNA.
EMBL; AK315490; BAG37874.1; -; mRNA.
EMBL; BT009843; AAP88845.1; -; mRNA.
EMBL; AL445248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL049795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX07567.1; -; Genomic_DNA.
EMBL; CH471059; EAX07568.1; -; Genomic_DNA.
EMBL; BC020520; AAH20520.1; -; mRNA.
CCDS; CCDS352.1; -.
RefSeq; NP_036448.1; NM_012316.4.
PDB; 4UAD; X-ray; 2.42 A; A=59-536.
PDBsum; 4UAD; -.
SMR; O60684; -.
BioGRID; 117163; 126.
ComplexPortal; CPX-1064; Importin complex, KPNA6 variant.
DIP; DIP-27609N; -.
ELM; O60684; -.
IntAct; O60684; 80.
MINT; O60684; -.
STRING; 9606.ENSP00000362728; -.
TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
iPTMnet; O60684; -.
MetOSite; O60684; -.
PhosphoSitePlus; O60684; -.
SwissPalm; O60684; -.
BioMuta; KPNA6; -.
EPD; O60684; -.
jPOST; O60684; -.
MassIVE; O60684; -.
MaxQB; O60684; -.
PaxDb; O60684; -.
PeptideAtlas; O60684; -.
PRIDE; O60684; -.
ProteomicsDB; 49527; -.
Antibodypedia; 16877; 177 antibodies.
DNASU; 23633; -.
Ensembl; ENST00000373625; ENSP00000362728; ENSG00000025800.
GeneID; 23633; -.
KEGG; hsa:23633; -.
UCSC; uc001bug.4; human.
CTD; 23633; -.
DisGeNET; 23633; -.
GeneCards; KPNA6; -.
HGNC; HGNC:6399; KPNA6.
HPA; ENSG00000025800; Low tissue specificity.
MIM; 610563; gene.
neXtProt; NX_O60684; -.
OpenTargets; ENSG00000025800; -.
PharmGKB; PA30190; -.
VEuPathDB; HostDB:ENSG00000025800.13; -.
eggNOG; KOG0166; Eukaryota.
GeneTree; ENSGT01030000234650; -.
HOGENOM; CLU_018084_6_0_1; -.
InParanoid; O60684; -.
OMA; GEQEANQ; -.
OrthoDB; 1111872at2759; -.
PhylomeDB; O60684; -.
TreeFam; TF354205; -.
PathwayCommons; O60684; -.
SignaLink; O60684; -.
SIGNOR; O60684; -.
BioGRID-ORCS; 23633; 100 hits in 1008 CRISPR screens.
ChiTaRS; KPNA6; human.
GeneWiki; KPNA6; -.
GenomeRNAi; 23633; -.
Pharos; O60684; Tbio.
PRO; PR:O60684; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; O60684; protein.
Bgee; ENSG00000025800; Expressed in buccal mucosa cell and 255 other tissues.
ExpressionAtlas; O60684; baseline and differential.
Genevisible; O60684; HS.
GO; GO:0005737; C:cytoplasm; IEA:InterPro.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0075506; P:entry of viral genome into host nucleus through nuclear pore complex via importin; IMP:MGI.
GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
GO; GO:0030682; P:mitigation of host defenses by symbiont; IEA:Ensembl.
GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:1903902; P:positive regulation of viral life cycle; IMP:MGI.
GO; GO:0019079; P:viral genome replication; 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; 3.
PROSITE; PS51214; IBB; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Host-virus interaction; Phosphoprotein;
Protein transport; Reference proteome; Repeat; Transport.
CHAIN 1..536
/note="Importin subunit alpha-7"
/id="PRO_0000120729"
DOMAIN 1..60
/note="IBB"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
REPEAT 76..115
/note="ARM 1; truncated"
REPEAT 116..159
/note="ARM 2"
REPEAT 160..204
/note="ARM 3"
REPEAT 205..243
/note="ARM 4"
REPEAT 244..288
/note="ARM 5"
REPEAT 289..328
/note="ARM 6"
REPEAT 329..370
/note="ARM 7"
REPEAT 371..410
/note="ARM 8"
REPEAT 411..453
/note="ARM 9"
REPEAT 457..502
/note="ARM 10; atypical"
REGION 1..29
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 147..239
/note="NLS binding site (major)"
/evidence="ECO:0000250"
REGION 316..404
/note="NLS binding site (minor)"
/evidence="ECO:0000250"
MOTIF 45..54
/note="Nuclear localization signal"
/evidence="ECO:0000250"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0007744|PubMed:19413330,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378"
MOD_RES 6
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18691976,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
MOD_RES 113
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
HELIX 83..89
/evidence="ECO:0007829|PDB:4UAD"
HELIX 94..108
/evidence="ECO:0007829|PDB:4UAD"
STRAND 111..113
/evidence="ECO:0007829|PDB:4UAD"
HELIX 116..121
/evidence="ECO:0007829|PDB:4UAD"
HELIX 125..132
/evidence="ECO:0007829|PDB:4UAD"
HELIX 139..152
/evidence="ECO:0007829|PDB:4UAD"
HELIX 157..165
/evidence="ECO:0007829|PDB:4UAD"
HELIX 168..174
/evidence="ECO:0007829|PDB:4UAD"
HELIX 175..177
/evidence="ECO:0007829|PDB:4UAD"
HELIX 181..195
/evidence="ECO:0007829|PDB:4UAD"
HELIX 199..207
/evidence="ECO:0007829|PDB:4UAD"
HELIX 211..220
/evidence="ECO:0007829|PDB:4UAD"
HELIX 224..238
/evidence="ECO:0007829|PDB:4UAD"
HELIX 247..249
/evidence="ECO:0007829|PDB:4UAD"
HELIX 251..253
/evidence="ECO:0007829|PDB:4UAD"
HELIX 254..260
/evidence="ECO:0007829|PDB:4UAD"
HELIX 266..279
/evidence="ECO:0007829|PDB:4UAD"
STRAND 281..283
/evidence="ECO:0007829|PDB:4UAD"
HELIX 284..292
/evidence="ECO:0007829|PDB:4UAD"
HELIX 296..301
/evidence="ECO:0007829|PDB:4UAD"
HELIX 302..304
/evidence="ECO:0007829|PDB:4UAD"
HELIX 308..321
/evidence="ECO:0007829|PDB:4UAD"
HELIX 326..333
/evidence="ECO:0007829|PDB:4UAD"
TURN 334..336
/evidence="ECO:0007829|PDB:4UAD"
HELIX 338..344
/evidence="ECO:0007829|PDB:4UAD"
HELIX 350..363
/evidence="ECO:0007829|PDB:4UAD"
HELIX 368..376
/evidence="ECO:0007829|PDB:4UAD"
HELIX 380..389
/evidence="ECO:0007829|PDB:4UAD"
HELIX 392..408
/evidence="ECO:0007829|PDB:4UAD"
HELIX 411..419
/evidence="ECO:0007829|PDB:4UAD"
HELIX 423..427
/evidence="ECO:0007829|PDB:4UAD"
HELIX 428..431
/evidence="ECO:0007829|PDB:4UAD"
HELIX 435..455
/evidence="ECO:0007829|PDB:4UAD"
TURN 456..459
/evidence="ECO:0007829|PDB:4UAD"
HELIX 467..472
/evidence="ECO:0007829|PDB:4UAD"
HELIX 475..481
/evidence="ECO:0007829|PDB:4UAD"
HELIX 482..484
/evidence="ECO:0007829|PDB:4UAD"
HELIX 488..501
/evidence="ECO:0007829|PDB:4UAD"
SEQUENCE 536 AA; 60030 MW; 9D0E27482B9BDED3 CRC64;
METMASPGKD NYRMKSYKNN ALNPEEMRRR REEEGIQLRK QKREQQLFKR RNVELINEEA
AMFDSLLMDS YVSSTTGESV ITREMVEMLF SDDSDLQLAT TQKFRKLLSK EPSPPIDEVI
NTPRVVDRFV EFLKRNENCT LQFEAAWALT NIASGTSQQT KIVIEAGAVP IFIELLNSDF
EDVQEQAVWA LGNIAGDSSV CRDYVLNCSI LNPLLTLLTK STRLTMTRNA VWALSNLCRG
KNPPPEFAKV SPCLPVLSRL LFSSDSDLLA DACWALSYLS DGPNEKIQAV IDSGVCRRLV
ELLMHNDYKV ASPALRAVGN IVTGDDIQTQ VILNCSALPC LLHLLSSPKE SIRKEACWTI
SNITAGNRAQ IQAVIDANIF PVLIEILQKA EFRTRKEAAW AITNATSGGT PEQIRYLVSL
GCIKPLCDLL TVMDSKIVQV ALNGLENILR LGEQEGKRSG SGVNPYCGLI EEAYGLDKIE
FLQSHENQEI YQKAFDLIEH YFGVEDDDSS LAPQVDETQQ QFIFQQPEAP MEGFQL


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Pathways :
WP1566: Citrate cycle (TCA cycle)
WP1614: 1- and 2-Methylnaphthalene degradation
WP1655: Geraniol degradation
WP2199: Seed Development
WP1003: Ovarian Infertility Genes
WP1963: The effect of Glucocorticoids on target gene expression
WP1618: alpha-Linolenic acid metabolism
WP296: TCA Cycle - biocyc
WP1644: DNA replication
WP402: ERK1 - ERK2 MAPK cascade
WP1163: TNF-alpha NF-kB Signaling Pathway
WP2100: AhR pathway
WP1225: estrogen signalling
WP1671: Methane metabolism
WP537: Translation Factors
WP1693: Purine metabolism
WP773: Ovarian Infertility Genes
WP1434: Osteopontin Signaling
WP231: TNF alpha Signaling Pathway
WP246: TNF-alpha NF-kB Signaling Pathway
WP1718: Vitamin B6 metabolism
WP929: TNF-alpha NF-kB Signaling Pathway
WP1904: RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways
WP273: Ovarian Infertility Genes
WP1634: Butanoate metabolism

Related Genes :
[Kpna6 Kpna5] Importin subunit alpha-7 (Importin alpha-S2) (Karyopherin subunit alpha-6)
[KPNA6 IPOA7] Importin subunit alpha-7 (Karyopherin subunit alpha-6)
[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]
[SRP1 KAP60 YNL189W N1606] Importin subunit alpha (Karyopherin subunit alpha) (Karyopherin-60) (Serine-rich RNA polymerase I suppressor protein)
[KPNA5] Importin subunit alpha-6 (Karyopherin subunit alpha-5)
[KPNA3 QIP2] Importin subunit alpha-4 (Importin alpha Q2) (Qip2) (Karyopherin subunit alpha-3) (SRP1-gamma)
[KPNA2 RCH1 SRP1] Importin subunit alpha-1 (Karyopherin subunit alpha-2) (RAG cohort protein 1) (SRP1-alpha)
[Kpna1] Importin subunit alpha-5 (Importin alpha-5) (Karyopherin subunit alpha-1)
[Kpna1 Rch2] Importin subunit alpha-5 (Importin alpha-S1) (Karyopherin subunit alpha-1) (Nucleoprotein interactor 1) (NPI-1) (RAG cohort protein 2) (SRP1-beta)
[Kpna7] Importin subunit alpha-8 (Karyopherin subunit alpha-7)
[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)
[KPNA4 QIP1] Importin subunit alpha-3 (Importin alpha Q1) (Qip1) (Karyopherin subunit alpha-4)
[imp1 SPBC1604.08c] Importin subunit alpha-2 (Importin-1) (Karyopherin subunit alpha-2)
[ima-3 F32E10.4] Importin subunit alpha-3 (Karyopherin subunit alpha-3)
[Pen CG4799] Importin subunit alpha (Karyopherin subunit alpha) (Pendulin)
[KPNB1 NTF97] Importin subunit beta-1 (Importin-90) (Karyopherin subunit beta-1) (Nuclear factor p97) (Pore targeting complex 97 kDa subunit) (PTAC97)
[ima-2 F26B1.3] Importin subunit alpha-2 (Karyopherin subunit alpha-2)
[cut15 SPCC962.03c] Importin subunit alpha-1 (Cell untimely torn protein 15) (Karyopherin subunit alpha-1) (Serine-rich RNA polymerase I suppressor protein)
[Kpna4 Qip1] Importin subunit alpha-3 (Importin alpha Q1) (Qip1) (Karyopherin subunit alpha-4)
[Kpnb1] Importin subunit beta-1 (Karyopherin subunit beta-1) (Nuclear factor p97) (Pore targeting complex 97 kDa subunit) (PTAC97)
[Kpnb1 Impnb] Importin subunit beta-1 (Karyopherin subunit beta-1) (Nuclear factor p97) (Pore targeting complex 97 kDa subunit) (PTAC97) (SCG)
[KPNA1] Importin subunit alpha-5 (Karyopherin subunit alpha-1) [Cleaved into: Importin subunit alpha-5, 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]
[KPNA1] Importin subunit alpha-5 (Karyopherin subunit alpha-1) [Cleaved into: Importin subunit alpha-5, N-terminally processed]
[kapA srp1 AN2142] Importin subunit alpha (Karyopherin alpha)
[Kpna3 Qip2] Importin subunit alpha-4 (Importin alpha Q2) (Qip2) (Karyopherin subunit alpha-3)
[ima-1 T19B10.7] Importin subunit alpha-1 (Karyopherin subunit alpha-1)
[KPNB1 At5g53480 MNC6.1] Importin subunit beta-1 (Karyopherin subunit beta-1) (ATKPNB1)
[Lama3] Laminin subunit alpha-3 (Epiligrin subunit alpha) (Kalinin subunit alpha) (Laminin-5 subunit alpha) (Laminin-6 subunit alpha) (Laminin-7 subunit alpha) (Nicein subunit alpha)
[Atp6v1a Atp6a1 Atp6a2 Atp6v1a1] V-type proton ATPase catalytic subunit A (V-ATPase subunit A) (EC 7.1.2.2) (V-ATPase 69 kDa subunit) (Vacuolar proton pump subunit alpha)

Bibliography :