Full text data of IPO5
IPO5
(KPNB3, RANBP5)
[Confidence: high (present in two of the MS resources)]
Importin-5; Imp5 (Importin subunit beta-3; Karyopherin beta-3; Ran-binding protein 5; RanBP5)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Importin-5; Imp5 (Importin subunit beta-3; Karyopherin beta-3; Ran-binding protein 5; RanBP5)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00329200
IPI00329200 Importin beta-3 Functions in nuclear protein import as nuclear transport receptor: mediates nuclear import of H2A, H2B, H3 and H4 histones, interacts with H2A, H2B, H3 and H4 histones soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic and nuclear n/a expected molecular weight found in band found in band > 188 kDa
IPI00329200 Importin beta-3 Functions in nuclear protein import as nuclear transport receptor: mediates nuclear import of H2A, H2B, H3 and H4 histones, interacts with H2A, H2B, H3 and H4 histones soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic and nuclear n/a expected molecular weight found in band found in band > 188 kDa
UniProt
O00410
ID IPO5_HUMAN Reviewed; 1097 AA.
AC O00410; B4DZA0; O15257; Q5T578; Q86XC7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=Importin-5;
DE Short=Imp5;
DE AltName: Full=Importin subunit beta-3;
DE AltName: Full=Karyopherin beta-3;
DE AltName: Full=Ran-binding protein 5;
DE Short=RanBP5;
GN Name=IPO5; Synonyms=KPNB3, RANBP5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Bone marrow;
RX PubMed=9114010; DOI=10.1073/pnas.94.9.4451;
RA Yaseen N.R., Blobel G.;
RT "Cloning and characterization of human karyopherin beta3.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4451-4456(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=9271386;
RA Deane R., Schaeffer W., Zimmermann H.-P., Mueller L., Goerlich D.,
RA Prehn S., Ponstingl H., Bischoff F.R.;
RT "Ran-binding protein 5 (RanBP5) is related to the nuclear transport
RT factor importin-beta but interacts differently with RanBP1.";
RL Mol. Cell. Biol. 17:5087-5096(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Lung, and Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [8]
RP FUNCTION, NUCLEAR LOCALIZATION SIGNAL RECOGNITION, AND INTERACTION
RP WITH RPL23A; RPS7 AND RPL5.
RX PubMed=9687515; DOI=10.1093/emboj/17.15.4491;
RA Jaekel S., Goerlich D.;
RT "Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import
RT of ribosomal proteins in mammalian cells.";
RL EMBO J. 17:4491-4502(1998).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP INTERACTION WITH HIV-1 REV.
RX PubMed=16704975; DOI=10.1074/jbc.M602189200;
RA Arnold M., Nath A., Hauber J., Kehlenbach R.H.;
RT "Multiple importins function as nuclear transport receptors for the
RT Rev protein of human immunodeficiency virus type 1.";
RL J. Biol. Chem. 281:20883-20890(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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.,
RA Buerckstuemmer T., 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Functions in nuclear protein import as nuclear transport
CC receptor. Serves as receptor for nuclear localization signals
CC (NLS) in cargo substrates. Is thought to mediate docking of the
CC importin/substrate complex to the nuclear pore complex (NPC)
CC through binding to nucleoporin and the complex is subsequently
CC translocated through the pore by an energy requiring, Ran-
CC dependent mechanism. At the nucleoplasmic side of the NPC, Ran
CC binds to the importin, the importin/substrate complex dissociates
CC and importin is re-exported from the nucleus to the cytoplasm
CC where GTP hydrolysis releases Ran. The directionality of nuclear
CC import is thought to be conferred by an asymmetric distribution of
CC the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC nucleus (By similarity). Mediates the nuclear import of ribosomal
CC proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import
CC receptor binding (BIB) domain of RPL23A. In vitro, mediates
CC nuclear import of H2A, H2B, H3 and H4 histones. In case of HIV-1
CC infection, binds and mediates the nuclear import of HIV-1 Rev.
CC -!- SUBUNIT: Binds RPL23A, RPS7 and RPL5. Interacts with H2A, H2B, H3
CC and H4 histones (By similarity). Binds to HIV-1 Rev.
CC -!- INTERACTION:
CC O95166:GABARAP; NbExp=6; IntAct=EBI-356424, EBI-712001;
CC Q9H0R8:GABARAPL1; NbExp=4; IntAct=EBI-356424, EBI-746969;
CC P60520:GABARAPL2; NbExp=5; IntAct=EBI-356424, EBI-720116;
CC Q9GZQ8:MAP1LC3B; NbExp=2; IntAct=EBI-356424, EBI-373144;
CC Q9BXW4:MAP1LC3C; NbExp=2; IntAct=EBI-356424, EBI-2603996;
CC P18124:RPL7; NbExp=4; IntAct=EBI-356424, EBI-350806;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus.
CC Note=Nucleus; nuclear rim. Found particularly in the nuclear rim
CC and nucleolus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O00410-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00410-2; Sequence=VSP_037587;
CC Name=3;
CC IsoId=O00410-3; Sequence=VSP_037774;
CC Note=Ref.2 (CAA70103) sequence differs from that shown due to a
CC frameshift in position 18;
CC -!- SIMILARITY: Belongs to the importin beta family.
CC -!- SIMILARITY: Contains 6 HEAT repeats.
CC -!- SIMILARITY: Contains 1 importin N-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA70103.1; Type=Frameshift; Positions=18;
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DR EMBL; U72761; AAC51317.1; -; mRNA.
DR EMBL; Y08890; CAA70103.1; ALT_FRAME; mRNA.
DR EMBL; AK302812; BAG64012.1; -; mRNA.
DR EMBL; AL356580; CAI13757.1; -; Genomic_DNA.
DR EMBL; AL137120; CAI13757.1; JOINED; Genomic_DNA.
DR EMBL; AL137120; CAI16520.1; -; Genomic_DNA.
DR EMBL; AL356580; CAI16520.1; JOINED; Genomic_DNA.
DR EMBL; CH471085; EAX08980.1; -; Genomic_DNA.
DR EMBL; BC001497; AAH01497.1; -; mRNA.
DR EMBL; BC019309; AAH19309.1; -; mRNA.
DR EMBL; BC045640; AAH45640.1; -; mRNA.
DR RefSeq; NP_002262.3; NM_002271.4.
DR RefSeq; XP_005254105.1; XM_005254048.1.
DR RefSeq; XP_005254106.1; XM_005254049.1.
DR RefSeq; XP_005254107.1; XM_005254050.1.
DR RefSeq; XP_005254108.1; XM_005254051.1.
DR RefSeq; XP_005254109.1; XM_005254052.1.
DR RefSeq; XP_005254110.1; XM_005254053.1.
DR UniGene; Hs.712598; -.
DR ProteinModelPortal; O00410; -.
DR SMR; O00410; 14-607.
DR DIP; DIP-41042N; -.
DR IntAct; O00410; 23.
DR MINT; MINT-132356; -.
DR STRING; 9606.ENSP00000261574; -.
DR PhosphoSite; O00410; -.
DR PaxDb; O00410; -.
DR PRIDE; O00410; -.
DR DNASU; 3843; -.
DR Ensembl; ENST00000261574; ENSP00000261574; ENSG00000065150.
DR Ensembl; ENST00000357602; ENSP00000350219; ENSG00000065150.
DR Ensembl; ENST00000490680; ENSP00000418393; ENSG00000065150.
DR GeneID; 3843; -.
DR KEGG; hsa:3843; -.
DR UCSC; uc001vnf.1; human.
DR CTD; 3843; -.
DR GeneCards; GC13P098605; -.
DR H-InvDB; HIX0174410; -.
DR HGNC; HGNC:6402; IPO5.
DR HPA; CAB009110; -.
DR MIM; 602008; gene.
DR neXtProt; NX_O00410; -.
DR PharmGKB; PA30193; -.
DR eggNOG; COG5215; -.
DR HOGENOM; HOG000209725; -.
DR HOVERGEN; HBG006156; -.
DR InParanoid; O00410; -.
DR OMA; IEHCSPS; -.
DR OrthoDB; EOG7Q5HCD; -.
DR ChiTaRS; IPO5; human.
DR GeneWiki; RANBP5; -.
DR GenomeRNAi; 3843; -.
DR NextBio; 15125; -.
DR PRO; PR:O00410; -.
DR ArrayExpress; O00410; -.
DR Bgee; O00410; -.
DR CleanEx; HS_IPO5; -.
DR Genevestigator; O00410; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005095; F:GTPase inhibitor activity; TAS:ProtInc.
DR GO; GO:0008565; F:protein transporter activity; ISS:UniProtKB.
DR GO; GO:0008536; F:Ran GTPase binding; TAS:ProtInc.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0006610; P:ribosomal protein import into nucleus; IDA:UniProtKB.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF02985; HEAT; 2.
DR SUPFAM; SSF48371; SSF48371; 3.
DR PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Host-virus interaction; Nucleus;
KW Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
KW Repeat; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1097 Importin-5.
FT /FTId=PRO_0000120771.
FT DOMAIN 28 99 Importin N-terminal.
FT REPEAT 212 249 HEAT 1.
FT REPEAT 395 432 HEAT 2.
FT REPEAT 437 475 HEAT 3.
FT REPEAT 859 897 HEAT 4.
FT REPEAT 901 938 HEAT 5.
FT REPEAT 942 979 HEAT 6.
FT REGION 325 375 Ran-GTP binding (By similarity).
FT COMPBIAS 2 6 Poly-Ala.
FT COMPBIAS 460 465 Poly-Ala.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 827 827 Phosphoserine.
FT VAR_SEQ 1 60 Missing (in isoform 2).
FT /FTId=VSP_037587.
FT VAR_SEQ 1 1 M -> MPEDQVGKLEATENTISAM (in isoform 3).
FT /FTId=VSP_037774.
FT VARIANT 286 286 L -> I (in dbSNP:rs1053814).
FT /FTId=VAR_012029.
FT VARIANT 525 525 E -> K (in dbSNP:rs632729).
FT /FTId=VAR_012030.
FT VARIANT 549 549 E -> K (in dbSNP:rs484770).
FT /FTId=VAR_012031.
FT VARIANT 905 905 Y -> C (in dbSNP:rs1804740).
FT /FTId=VAR_012032.
FT VARIANT 969 969 T -> I (in dbSNP:rs1804741).
FT /FTId=VAR_012033.
FT CONFLICT 538 538 L -> R (in Ref. 6; AAH45640).
FT CONFLICT 826 827 ES -> GT (in Ref. 1; AAC51317).
SQ SEQUENCE 1097 AA; 123630 MW; 1864AD23513F2DE1 CRC64;
MAAAAAEQQQ FYLLLGNLLS PDNVVRKQAE ETYENIPGQS KITFLLQAIR NTTAAEEARQ
MAAVLLRRLL SSAFDEVYPA LPSDVQTAIK SELLMIIQME TQSSMRKKVC DIAAELARNL
IDEDGNNQWP EGLKFLFDSV SSQNVGLREA ALHIFWNFPG IFGNQQQHYL DVIKRMLVQC
MQDQEHPSIR TLSARATAAF ILANEHNVAL FKHFADLLPG FLQAVNDSCY QNDDSVLKSL
VEIADTVPKY LRPHLEATLQ LSLKLCGDTS LNNMQRQLAL EVIVTLSETA AAMLRKHTNI
VAQTIPQMLA MMVDLEEDED WANADELEDD DFDSNAVAGE SALDRMACGL GGKLVLPMIK
EHIMQMLQNP DWKYRHAGLM ALSAIGEGCH QQMEGILNEI VNFVLLFLQD PHPRVRYAAC
NAVGQMATDF APGFQKKFHE KVIAALLQTM EDQGNQRVQA HAAAALINFT EDCPKSLLIP
YLDNLVKHLH SIMVLKLQEL IQKGTKLVLE QVVTSIASVA DTAEEKFVPY YDLFMPSLKH
IVENAVQKEL RLLRGKTIEC ISLIGLAVGK EKFMQDASDV MQLLLKTQTD FNDMEDDDPQ
ISYMISAWAR MCKILGKEFQ QYLPVVMGPL MKTASIKPEV ALLDTQDMEN MSDDDGWEFV
NLGDQQSFGI KTAGLEEKST ACQMLVCYAK ELKEGFVEYT EQVVKLMVPL LKFYFHDGVR
VAAAESMPLL LECARVRGPE YLTQMWHFMC DALIKAIGTE PDSDVLSEIM HSFAKCIEVM
GDGCLNNEHF EELGGILKAK LEEHFKNQEL RQVKRQDEDY DEQVEESLQD EDDNDVYILT
KVSDILHSIF SSYKEKVLPW FEQLLPLIVN LICPHRPWPD RQWGLCIFDD VIEHCSPASF
KYAEYFLRPM LQYVCDNSPE VRQAAAYGLG VMAQYGGDNY RPFCTEALPL LVRVIQSADS
KTKENVNATE NCISAVGKIM KFKPDCVNVE EVLPHWLSWL PLHEDKEEAV QTFNYLCDLI
ESNHPIVLGP NNTNLPKIFS IIAEGEMHEA IKHEDPCAKR LANVVRQVQT SGGLWTECIA
QLSPEQQAAI QELLNSA
//
ID IPO5_HUMAN Reviewed; 1097 AA.
AC O00410; B4DZA0; O15257; Q5T578; Q86XC7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 135.
DE RecName: Full=Importin-5;
DE Short=Imp5;
DE AltName: Full=Importin subunit beta-3;
DE AltName: Full=Karyopherin beta-3;
DE AltName: Full=Ran-binding protein 5;
DE Short=RanBP5;
GN Name=IPO5; Synonyms=KPNB3, RANBP5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Bone marrow;
RX PubMed=9114010; DOI=10.1073/pnas.94.9.4451;
RA Yaseen N.R., Blobel G.;
RT "Cloning and characterization of human karyopherin beta3.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4451-4456(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=9271386;
RA Deane R., Schaeffer W., Zimmermann H.-P., Mueller L., Goerlich D.,
RA Prehn S., Ponstingl H., Bischoff F.R.;
RT "Ran-binding protein 5 (RanBP5) is related to the nuclear transport
RT factor importin-beta but interacts differently with RanBP1.";
RL Mol. Cell. Biol. 17:5087-5096(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Lung, and Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [8]
RP FUNCTION, NUCLEAR LOCALIZATION SIGNAL RECOGNITION, AND INTERACTION
RP WITH RPL23A; RPS7 AND RPL5.
RX PubMed=9687515; DOI=10.1093/emboj/17.15.4491;
RA Jaekel S., Goerlich D.;
RT "Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import
RT of ribosomal proteins in mammalian cells.";
RL EMBO J. 17:4491-4502(1998).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP INTERACTION WITH HIV-1 REV.
RX PubMed=16704975; DOI=10.1074/jbc.M602189200;
RA Arnold M., Nath A., Hauber J., Kehlenbach R.H.;
RT "Multiple importins function as nuclear transport receptors for the
RT Rev protein of human immunodeficiency virus type 1.";
RL J. Biol. Chem. 281:20883-20890(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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.,
RA Buerckstuemmer T., 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Functions in nuclear protein import as nuclear transport
CC receptor. Serves as receptor for nuclear localization signals
CC (NLS) in cargo substrates. Is thought to mediate docking of the
CC importin/substrate complex to the nuclear pore complex (NPC)
CC through binding to nucleoporin and the complex is subsequently
CC translocated through the pore by an energy requiring, Ran-
CC dependent mechanism. At the nucleoplasmic side of the NPC, Ran
CC binds to the importin, the importin/substrate complex dissociates
CC and importin is re-exported from the nucleus to the cytoplasm
CC where GTP hydrolysis releases Ran. The directionality of nuclear
CC import is thought to be conferred by an asymmetric distribution of
CC the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC nucleus (By similarity). Mediates the nuclear import of ribosomal
CC proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import
CC receptor binding (BIB) domain of RPL23A. In vitro, mediates
CC nuclear import of H2A, H2B, H3 and H4 histones. In case of HIV-1
CC infection, binds and mediates the nuclear import of HIV-1 Rev.
CC -!- SUBUNIT: Binds RPL23A, RPS7 and RPL5. Interacts with H2A, H2B, H3
CC and H4 histones (By similarity). Binds to HIV-1 Rev.
CC -!- INTERACTION:
CC O95166:GABARAP; NbExp=6; IntAct=EBI-356424, EBI-712001;
CC Q9H0R8:GABARAPL1; NbExp=4; IntAct=EBI-356424, EBI-746969;
CC P60520:GABARAPL2; NbExp=5; IntAct=EBI-356424, EBI-720116;
CC Q9GZQ8:MAP1LC3B; NbExp=2; IntAct=EBI-356424, EBI-373144;
CC Q9BXW4:MAP1LC3C; NbExp=2; IntAct=EBI-356424, EBI-2603996;
CC P18124:RPL7; NbExp=4; IntAct=EBI-356424, EBI-350806;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus.
CC Note=Nucleus; nuclear rim. Found particularly in the nuclear rim
CC and nucleolus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O00410-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00410-2; Sequence=VSP_037587;
CC Name=3;
CC IsoId=O00410-3; Sequence=VSP_037774;
CC Note=Ref.2 (CAA70103) sequence differs from that shown due to a
CC frameshift in position 18;
CC -!- SIMILARITY: Belongs to the importin beta family.
CC -!- SIMILARITY: Contains 6 HEAT repeats.
CC -!- SIMILARITY: Contains 1 importin N-terminal domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA70103.1; Type=Frameshift; Positions=18;
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DR EMBL; U72761; AAC51317.1; -; mRNA.
DR EMBL; Y08890; CAA70103.1; ALT_FRAME; mRNA.
DR EMBL; AK302812; BAG64012.1; -; mRNA.
DR EMBL; AL356580; CAI13757.1; -; Genomic_DNA.
DR EMBL; AL137120; CAI13757.1; JOINED; Genomic_DNA.
DR EMBL; AL137120; CAI16520.1; -; Genomic_DNA.
DR EMBL; AL356580; CAI16520.1; JOINED; Genomic_DNA.
DR EMBL; CH471085; EAX08980.1; -; Genomic_DNA.
DR EMBL; BC001497; AAH01497.1; -; mRNA.
DR EMBL; BC019309; AAH19309.1; -; mRNA.
DR EMBL; BC045640; AAH45640.1; -; mRNA.
DR RefSeq; NP_002262.3; NM_002271.4.
DR RefSeq; XP_005254105.1; XM_005254048.1.
DR RefSeq; XP_005254106.1; XM_005254049.1.
DR RefSeq; XP_005254107.1; XM_005254050.1.
DR RefSeq; XP_005254108.1; XM_005254051.1.
DR RefSeq; XP_005254109.1; XM_005254052.1.
DR RefSeq; XP_005254110.1; XM_005254053.1.
DR UniGene; Hs.712598; -.
DR ProteinModelPortal; O00410; -.
DR SMR; O00410; 14-607.
DR DIP; DIP-41042N; -.
DR IntAct; O00410; 23.
DR MINT; MINT-132356; -.
DR STRING; 9606.ENSP00000261574; -.
DR PhosphoSite; O00410; -.
DR PaxDb; O00410; -.
DR PRIDE; O00410; -.
DR DNASU; 3843; -.
DR Ensembl; ENST00000261574; ENSP00000261574; ENSG00000065150.
DR Ensembl; ENST00000357602; ENSP00000350219; ENSG00000065150.
DR Ensembl; ENST00000490680; ENSP00000418393; ENSG00000065150.
DR GeneID; 3843; -.
DR KEGG; hsa:3843; -.
DR UCSC; uc001vnf.1; human.
DR CTD; 3843; -.
DR GeneCards; GC13P098605; -.
DR H-InvDB; HIX0174410; -.
DR HGNC; HGNC:6402; IPO5.
DR HPA; CAB009110; -.
DR MIM; 602008; gene.
DR neXtProt; NX_O00410; -.
DR PharmGKB; PA30193; -.
DR eggNOG; COG5215; -.
DR HOGENOM; HOG000209725; -.
DR HOVERGEN; HBG006156; -.
DR InParanoid; O00410; -.
DR OMA; IEHCSPS; -.
DR OrthoDB; EOG7Q5HCD; -.
DR ChiTaRS; IPO5; human.
DR GeneWiki; RANBP5; -.
DR GenomeRNAi; 3843; -.
DR NextBio; 15125; -.
DR PRO; PR:O00410; -.
DR ArrayExpress; O00410; -.
DR Bgee; O00410; -.
DR CleanEx; HS_IPO5; -.
DR Genevestigator; O00410; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005095; F:GTPase inhibitor activity; TAS:ProtInc.
DR GO; GO:0008565; F:protein transporter activity; ISS:UniProtKB.
DR GO; GO:0008536; F:Ran GTPase binding; TAS:ProtInc.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0006610; P:ribosomal protein import into nucleus; IDA:UniProtKB.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF02985; HEAT; 2.
DR SUPFAM; SSF48371; SSF48371; 3.
DR PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Host-virus interaction; Nucleus;
KW Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
KW Repeat; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1097 Importin-5.
FT /FTId=PRO_0000120771.
FT DOMAIN 28 99 Importin N-terminal.
FT REPEAT 212 249 HEAT 1.
FT REPEAT 395 432 HEAT 2.
FT REPEAT 437 475 HEAT 3.
FT REPEAT 859 897 HEAT 4.
FT REPEAT 901 938 HEAT 5.
FT REPEAT 942 979 HEAT 6.
FT REGION 325 375 Ran-GTP binding (By similarity).
FT COMPBIAS 2 6 Poly-Ala.
FT COMPBIAS 460 465 Poly-Ala.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 827 827 Phosphoserine.
FT VAR_SEQ 1 60 Missing (in isoform 2).
FT /FTId=VSP_037587.
FT VAR_SEQ 1 1 M -> MPEDQVGKLEATENTISAM (in isoform 3).
FT /FTId=VSP_037774.
FT VARIANT 286 286 L -> I (in dbSNP:rs1053814).
FT /FTId=VAR_012029.
FT VARIANT 525 525 E -> K (in dbSNP:rs632729).
FT /FTId=VAR_012030.
FT VARIANT 549 549 E -> K (in dbSNP:rs484770).
FT /FTId=VAR_012031.
FT VARIANT 905 905 Y -> C (in dbSNP:rs1804740).
FT /FTId=VAR_012032.
FT VARIANT 969 969 T -> I (in dbSNP:rs1804741).
FT /FTId=VAR_012033.
FT CONFLICT 538 538 L -> R (in Ref. 6; AAH45640).
FT CONFLICT 826 827 ES -> GT (in Ref. 1; AAC51317).
SQ SEQUENCE 1097 AA; 123630 MW; 1864AD23513F2DE1 CRC64;
MAAAAAEQQQ FYLLLGNLLS PDNVVRKQAE ETYENIPGQS KITFLLQAIR NTTAAEEARQ
MAAVLLRRLL SSAFDEVYPA LPSDVQTAIK SELLMIIQME TQSSMRKKVC DIAAELARNL
IDEDGNNQWP EGLKFLFDSV SSQNVGLREA ALHIFWNFPG IFGNQQQHYL DVIKRMLVQC
MQDQEHPSIR TLSARATAAF ILANEHNVAL FKHFADLLPG FLQAVNDSCY QNDDSVLKSL
VEIADTVPKY LRPHLEATLQ LSLKLCGDTS LNNMQRQLAL EVIVTLSETA AAMLRKHTNI
VAQTIPQMLA MMVDLEEDED WANADELEDD DFDSNAVAGE SALDRMACGL GGKLVLPMIK
EHIMQMLQNP DWKYRHAGLM ALSAIGEGCH QQMEGILNEI VNFVLLFLQD PHPRVRYAAC
NAVGQMATDF APGFQKKFHE KVIAALLQTM EDQGNQRVQA HAAAALINFT EDCPKSLLIP
YLDNLVKHLH SIMVLKLQEL IQKGTKLVLE QVVTSIASVA DTAEEKFVPY YDLFMPSLKH
IVENAVQKEL RLLRGKTIEC ISLIGLAVGK EKFMQDASDV MQLLLKTQTD FNDMEDDDPQ
ISYMISAWAR MCKILGKEFQ QYLPVVMGPL MKTASIKPEV ALLDTQDMEN MSDDDGWEFV
NLGDQQSFGI KTAGLEEKST ACQMLVCYAK ELKEGFVEYT EQVVKLMVPL LKFYFHDGVR
VAAAESMPLL LECARVRGPE YLTQMWHFMC DALIKAIGTE PDSDVLSEIM HSFAKCIEVM
GDGCLNNEHF EELGGILKAK LEEHFKNQEL RQVKRQDEDY DEQVEESLQD EDDNDVYILT
KVSDILHSIF SSYKEKVLPW FEQLLPLIVN LICPHRPWPD RQWGLCIFDD VIEHCSPASF
KYAEYFLRPM LQYVCDNSPE VRQAAAYGLG VMAQYGGDNY RPFCTEALPL LVRVIQSADS
KTKENVNATE NCISAVGKIM KFKPDCVNVE EVLPHWLSWL PLHEDKEEAV QTFNYLCDLI
ESNHPIVLGP NNTNLPKIFS IIAEGEMHEA IKHEDPCAKR LANVVRQVQT SGGLWTECIA
QLSPEQQAAI QELLNSA
//
MIM
602008
*RECORD*
*FIELD* NO
602008
*FIELD* TI
*602008 RAN-BINDING PROTEIN 5; RANBP5
;;KARYOPHERIN BETA-3; KPNB3;;
IMPORTIN BETA-3;;
read moreIMPORTIN 5; IPO5
*FIELD* TX
DESCRIPTION
Nuclear import of proteins is mediated by the karyopherins (see 600685)
and other proteins. Karyopherin beta-3 is believed to be a nuclear
transport factor involved in the import of ribosomal proteins (Yaseen
and Blobel, 1997).
CLONING
Yaseen and Blobel (1997) found a sequence in the EST database with
significant homology to yeast Kap121p/Pse1p, which is involved in
protein secretion and the nuclear import of ribosomal and other
proteins. They cloned the human homolog from a bone marrow cDNA library.
The human gene encodes a 1,097-amino acid polypeptide with a predicted
mass of 123 kD, in agreement with the observed size of native
karyopherin beta-3. The protein sequence shows 28% identity to yeast
Kap121p/Pse1p and 17% identity to human karyopherin beta-1. Yaseen and
Blobel (1997) reported that the sequence contains 2 putative binding
sites for Ras-related nuclear protein (601179). Using
immunofluorescence, Yaseen and Blobel (1997) demonstrated that
karyopherin beta-3 is localized mainly to the cytosol and the nucleus,
particularly the nuclear rim, in HeLa cells. They showed that
karyopherin beta-3 binds to repeat-containing nucleoporins, Ran-GDP,
Ran-GTP, and 2 ribosomal proteins.
*FIELD* RF
1. Yaseen, N. R.; Blobel, G.: Cloning and characterization of human
karyopherin beta 3. Proc. Nat. Acad. Sci. 94: 4451-4456, 1997.
*FIELD* CD
Jennifer P. Macke: 9/19/1997
*FIELD* ED
alopez: 03/15/2010
wwang: 3/26/2007
alopez: 10/3/1997
alopez: 9/23/1997
*RECORD*
*FIELD* NO
602008
*FIELD* TI
*602008 RAN-BINDING PROTEIN 5; RANBP5
;;KARYOPHERIN BETA-3; KPNB3;;
IMPORTIN BETA-3;;
read moreIMPORTIN 5; IPO5
*FIELD* TX
DESCRIPTION
Nuclear import of proteins is mediated by the karyopherins (see 600685)
and other proteins. Karyopherin beta-3 is believed to be a nuclear
transport factor involved in the import of ribosomal proteins (Yaseen
and Blobel, 1997).
CLONING
Yaseen and Blobel (1997) found a sequence in the EST database with
significant homology to yeast Kap121p/Pse1p, which is involved in
protein secretion and the nuclear import of ribosomal and other
proteins. They cloned the human homolog from a bone marrow cDNA library.
The human gene encodes a 1,097-amino acid polypeptide with a predicted
mass of 123 kD, in agreement with the observed size of native
karyopherin beta-3. The protein sequence shows 28% identity to yeast
Kap121p/Pse1p and 17% identity to human karyopherin beta-1. Yaseen and
Blobel (1997) reported that the sequence contains 2 putative binding
sites for Ras-related nuclear protein (601179). Using
immunofluorescence, Yaseen and Blobel (1997) demonstrated that
karyopherin beta-3 is localized mainly to the cytosol and the nucleus,
particularly the nuclear rim, in HeLa cells. They showed that
karyopherin beta-3 binds to repeat-containing nucleoporins, Ran-GDP,
Ran-GTP, and 2 ribosomal proteins.
*FIELD* RF
1. Yaseen, N. R.; Blobel, G.: Cloning and characterization of human
karyopherin beta 3. Proc. Nat. Acad. Sci. 94: 4451-4456, 1997.
*FIELD* CD
Jennifer P. Macke: 9/19/1997
*FIELD* ED
alopez: 03/15/2010
wwang: 3/26/2007
alopez: 10/3/1997
alopez: 9/23/1997