Full text data of IPO7
IPO7
(RANBP7)
[Confidence: high (present in two of the MS resources)]
Importin-7; Imp7 (Ran-binding protein 7; RanBP7)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Importin-7; Imp7 (Ran-binding protein 7; RanBP7)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00007402
IPI00007402 Importin 7 Blood, Platelet, nuclear import 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 around 188 kDa
IPI00007402 Importin 7 Blood, Platelet, nuclear import 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 around 188 kDa
UniProt
O95373
ID IPO7_HUMAN Reviewed; 1038 AA.
AC O95373; A6NNM5; B2R786; Q1RMF7; Q9H177; Q9NTE3;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Importin-7;
DE Short=Imp7;
DE AltName: Full=Ran-binding protein 7;
DE Short=RanBP7;
GN Name=IPO7; Synonyms=RANBP7;
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], FUNCTION, AND INTERACTION WITH RPL23A;
RP RPS7; RPL5 AND KPNB1.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP PROTEIN SEQUENCE OF 1-11, AND ACETYLATION AT MET-1.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-1038.
RC TISSUE=Blood;
RA Cichutek A., Winterpacht A., Hankeln T., Schmidt E.R., Zabel B.U.;
RT "Comparative sequencing of a 1 Mb region in man (chromosome 11p15) and
RT mouse (chromosome 7).";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 831-1038.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP CHARACTERIZATION.
RX PubMed=9214382; DOI=10.1083/jcb.138.1.65;
RA Goerlich D., Dabrowski M., Bischoff F.R., Kutay U., Bork P.,
RA Hartmann E., Prehn S., Izaurralde E.;
RT "A novel class of RanGTP binding proteins.";
RL J. Cell Biol. 138:65-80(1997).
RN [10]
RP FUNCTION, INTERACTION WITH H1 HISTONE AND KPNB1, AND MUTAGENESIS OF
RP LYS-61.
RX PubMed=10228156; DOI=10.1093/emboj/18.9.2411;
RA Jaekel S., Albig W., Kutay U., Bischoff F.R., Schwamborn K.,
RA Doenecke D., Goerlich D.;
RT "The importin beta/importin 7 heterodimer is a functional nuclear
RT import receptor for histone H1.";
RL EMBO J. 18:2411-2423(1999).
RN [11]
RP IDENTIFICATION IN AN EXPORT RECEPTOR COMPLEX, AND INTERACTION WITH
RP KPNB1; SNUPN AND XPO1.
RX PubMed=10209022; DOI=10.1083/jcb.145.2.255;
RA Paraskeva E., Izaurralde E., Bischoff F.R., Huber J., Kutay U.,
RA Hartmann E., Luehrmann R., Goerlich D.;
RT "CRM1-mediated recycling of snurportin 1 to the cytoplasm.";
RL J. Cell Biol. 145:255-264(1999).
RN [12]
RP FUNCTION, AND INTERACTION WITH INTEGRASE OF HIV-1 REVERSE
RP TRANSCRIPTION COMPLEX.
RX PubMed=12853482; DOI=10.1093/emboj/cdg357;
RA Fassati A., Goerlich D., Harrison I., Zaytseva L., Mingot J.-M.;
RT "Nuclear import of HIV-1 intracellular reverse transcription complexes
RT is mediated by importin 7.";
RL EMBO J. 22:3675-3685(2003).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886; THR-898 AND
RP SER-903, AND MASS 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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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 [17]
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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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, either by acting as
CC autonomous nuclear transport receptor or as an adapter-like
CC protein in association with the importin-beta subunit KPNB1.
CC Acting autonomously, is thought to serve itself as receptor for
CC nuclear localization signals (NLS) and to promote translocation of
CC import substrates through the nuclear pore complex (NPC) by an
CC energy requiring, Ran-dependent mechanism. At the nucleoplasmic
CC side of the NPC, Ran binds to importin, the importin/substrate
CC complex dissociates and importin is re-exported from the nucleus
CC to the cytoplasm where GTP hydrolysis releases Ran. 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
CC between the cytoplasm and nucleus. Mediates autonomously the
CC nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds
CC to a beta-like import receptor binding (BIB) domain of RPL23A. In
CC association with KPNB1 mediates the nuclear import of H1 histone
CC and the Ran-binding site of IPO7 is not required but synergizes
CC with that of KPNB1 in importin/substrate complex dissociation. In
CC vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In
CC vitro, mediates the nuclear import of HIV-1 reverse transcription
CC complex (RTC) integrase. In case of HIV-1 infection, binds and
CC mediates the nuclear import of HIV-1 Rev.
CC -!- SUBUNIT: Interacts with H2A, H2B, H3 and H4 histones (By
CC similarity). Forms a heterodimer with KPNB1. Interacts with KPNB1,
CC SNUPN, XPO1, RPL23A, RPS7, RPL5 and HIV-1 reverse transcription
CC complex integrase. Binds directly to nuclear pore complexes (By
CC similarity). Interacts with H2A, H2B, H3 and H4 histones. Binds to
CC HIV-1 Rev.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SIMILARITY: Belongs to the importin beta family.
CC -!- SIMILARITY: Contains 1 importin N-terminal domain.
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DR EMBL; AF098799; AAC68903.1; -; mRNA.
DR EMBL; AK312885; BAG35733.1; -; mRNA.
DR EMBL; AC055845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68593.1; -; Genomic_DNA.
DR EMBL; BC114929; AAI14930.1; -; mRNA.
DR EMBL; AJ295844; CAC17609.1; -; Genomic_DNA.
DR EMBL; AL137335; CAB70698.1; -; mRNA.
DR PIR; T46501; T46501.
DR RefSeq; NP_006382.1; NM_006391.2.
DR UniGene; Hs.744911; -.
DR ProteinModelPortal; O95373; -.
DR SMR; O95373; 2-440.
DR DIP; DIP-32574N; -.
DR IntAct; O95373; 13.
DR MINT; MINT-5003960; -.
DR STRING; 9606.ENSP00000369042; -.
DR PhosphoSite; O95373; -.
DR PaxDb; O95373; -.
DR PRIDE; O95373; -.
DR Ensembl; ENST00000379719; ENSP00000369042; ENSG00000205339.
DR GeneID; 10527; -.
DR KEGG; hsa:10527; -.
DR UCSC; uc001mho.3; human.
DR CTD; 10527; -.
DR GeneCards; GC11P009362; -.
DR HGNC; HGNC:9852; IPO7.
DR HPA; HPA019002; -.
DR MIM; 605586; gene.
DR neXtProt; NX_O95373; -.
DR PharmGKB; PA34213; -.
DR eggNOG; COG5656; -.
DR HOGENOM; HOG000006586; -.
DR HOVERGEN; HBG006824; -.
DR InParanoid; O95373; -.
DR OMA; HAVTWKN; -.
DR OrthoDB; EOG7TF787; -.
DR ChiTaRS; IPO7; human.
DR GeneWiki; IPO7; -.
DR GenomeRNAi; 10527; -.
DR NextBio; 39938; -.
DR PRO; PR:O95373; -.
DR ArrayExpress; O95373; -.
DR Bgee; O95373; -.
DR CleanEx; HS_IPO7; -.
DR Genevestigator; O95373; -.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0008536; F:Ran GTPase binding; TAS:ProtInc.
DR GO; GO:0005083; F:small GTPase regulator activity; TAS:ProtInc.
DR GO; GO:0005215; F:transporter activity; TAS:ProtInc.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013713; Cse1.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF08506; Cse1; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Nucleus; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 1038 Importin-7.
FT /FTId=PRO_0000120750.
FT DOMAIN 22 101 Importin N-terminal.
FT COMPBIAS 885 957 Asp-rich.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 886 886 Phosphoserine.
FT MOD_RES 898 898 Phosphothreonine.
FT MOD_RES 903 903 Phosphoserine.
FT VARIANT 111 111 T -> N (in dbSNP:rs11042340).
FT /FTId=VAR_050003.
FT MUTAGEN 61 61 K->A,D: Lowered affinity for RanGTP-
FT binding.
SQ SEQUENCE 1038 AA; 119517 MW; 355237CA1DA2D313 CRC64;
MDPNTIIEAL RGTMDPALRE AAERQLNEAH KSLNFVSTLL QITMSEQLDL PVRQAGVIYL
KNMITQYWPD RETAPGDISP YTIPEEDRHC IRENIVEAII HSPELIRVQL TTCIHHIIKH
DYPSRWTAIV DKIGFYLQSD NSACWLGILL CLYQLVKNYE YKKPEERSPL VAAMQHFLPV
LKDRFIQLLS DQSDQSVLIQ KQIFKIFYAL VQYTLPLELI NQQNLTEWIE ILKTVVNRDV
PNETLQVEED DRPELPWWKC KKWALHILAR LFERYGSPGN VSKEYNEFAE VFLKAFAVGV
QQVLLKVLYQ YKEKQYMAPR VLQQTLNYIN QGVSHALTWK NLKPHIQGII QDVIFPLMCY
TDADEELWQE DPYEYIRMKF DVFEDFISPT TAAQTLLFTA CSKRKEVLQK TMGFCYQILT
EPNADPRKKD GALHMIGSLA EILLKKKIYK DQMEYMLQNH VFPLFSSELG YMRARACWVL
HYFCEVKFKS DQNLQTALEL TRRCLIDDRE MPVKVEAAIA LQVLISNQEK AKEYITPFIR
PVMQALLHII RETENDDLTN VIQKMICEYS EEVTPIAVEM TQHLAMTFNQ VIQTGPDEEG
SDDKAVTAMG ILNTIDTLLS VVEDHKEITQ QLEGICLQVI GTVLQQHVLE FYEEIFSLAH
SLTCQQVSPQ MWQLLPLVFE VFQQDGFDYF TDMMPLLHNY VTVDTDTLLS DTKYLEMIYS
MCKKVLTGVA GEDAECHAAK LLEVIILQCK GRGIDQCIPL FVEAALERLT REVKTSELRT
MCLQVAIAAL YYNPHLLLNT LENLRFPNNV EPVTNHFITQ WLNDVDCFLG LHDRKMCVLG
LCALIDMEQI PQVLNQVSGQ ILPAFILLFN GLKRAYACHA EHENDSDDDD EAEDDDETEE
LGSDEDDIDE DGQEYLEILA KQAGEDGDDE DWEEDDAEET ALEGYSTIID DEDNPVDEYQ
IFKAIFQTIQ NRNPVWYQAL THGLNEEQRK QLQDIATLAD QRRAAHESKM IEKHGGYKFS
APVVPSSFNF GGPAPGMN
//
ID IPO7_HUMAN Reviewed; 1038 AA.
AC O95373; A6NNM5; B2R786; Q1RMF7; Q9H177; Q9NTE3;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Importin-7;
DE Short=Imp7;
DE AltName: Full=Ran-binding protein 7;
DE Short=RanBP7;
GN Name=IPO7; Synonyms=RANBP7;
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], FUNCTION, AND INTERACTION WITH RPL23A;
RP RPS7; RPL5 AND KPNB1.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP PROTEIN SEQUENCE OF 1-11, AND ACETYLATION AT MET-1.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-1038.
RC TISSUE=Blood;
RA Cichutek A., Winterpacht A., Hankeln T., Schmidt E.R., Zabel B.U.;
RT "Comparative sequencing of a 1 Mb region in man (chromosome 11p15) and
RT mouse (chromosome 7).";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 831-1038.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP CHARACTERIZATION.
RX PubMed=9214382; DOI=10.1083/jcb.138.1.65;
RA Goerlich D., Dabrowski M., Bischoff F.R., Kutay U., Bork P.,
RA Hartmann E., Prehn S., Izaurralde E.;
RT "A novel class of RanGTP binding proteins.";
RL J. Cell Biol. 138:65-80(1997).
RN [10]
RP FUNCTION, INTERACTION WITH H1 HISTONE AND KPNB1, AND MUTAGENESIS OF
RP LYS-61.
RX PubMed=10228156; DOI=10.1093/emboj/18.9.2411;
RA Jaekel S., Albig W., Kutay U., Bischoff F.R., Schwamborn K.,
RA Doenecke D., Goerlich D.;
RT "The importin beta/importin 7 heterodimer is a functional nuclear
RT import receptor for histone H1.";
RL EMBO J. 18:2411-2423(1999).
RN [11]
RP IDENTIFICATION IN AN EXPORT RECEPTOR COMPLEX, AND INTERACTION WITH
RP KPNB1; SNUPN AND XPO1.
RX PubMed=10209022; DOI=10.1083/jcb.145.2.255;
RA Paraskeva E., Izaurralde E., Bischoff F.R., Huber J., Kutay U.,
RA Hartmann E., Luehrmann R., Goerlich D.;
RT "CRM1-mediated recycling of snurportin 1 to the cytoplasm.";
RL J. Cell Biol. 145:255-264(1999).
RN [12]
RP FUNCTION, AND INTERACTION WITH INTEGRASE OF HIV-1 REVERSE
RP TRANSCRIPTION COMPLEX.
RX PubMed=12853482; DOI=10.1093/emboj/cdg357;
RA Fassati A., Goerlich D., Harrison I., Zaytseva L., Mingot J.-M.;
RT "Nuclear import of HIV-1 intracellular reverse transcription complexes
RT is mediated by importin 7.";
RL EMBO J. 22:3675-3685(2003).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886; THR-898 AND
RP SER-903, AND MASS 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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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 [17]
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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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, either by acting as
CC autonomous nuclear transport receptor or as an adapter-like
CC protein in association with the importin-beta subunit KPNB1.
CC Acting autonomously, is thought to serve itself as receptor for
CC nuclear localization signals (NLS) and to promote translocation of
CC import substrates through the nuclear pore complex (NPC) by an
CC energy requiring, Ran-dependent mechanism. At the nucleoplasmic
CC side of the NPC, Ran binds to importin, the importin/substrate
CC complex dissociates and importin is re-exported from the nucleus
CC to the cytoplasm where GTP hydrolysis releases Ran. 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
CC between the cytoplasm and nucleus. Mediates autonomously the
CC nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds
CC to a beta-like import receptor binding (BIB) domain of RPL23A. In
CC association with KPNB1 mediates the nuclear import of H1 histone
CC and the Ran-binding site of IPO7 is not required but synergizes
CC with that of KPNB1 in importin/substrate complex dissociation. In
CC vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In
CC vitro, mediates the nuclear import of HIV-1 reverse transcription
CC complex (RTC) integrase. In case of HIV-1 infection, binds and
CC mediates the nuclear import of HIV-1 Rev.
CC -!- SUBUNIT: Interacts with H2A, H2B, H3 and H4 histones (By
CC similarity). Forms a heterodimer with KPNB1. Interacts with KPNB1,
CC SNUPN, XPO1, RPL23A, RPS7, RPL5 and HIV-1 reverse transcription
CC complex integrase. Binds directly to nuclear pore complexes (By
CC similarity). Interacts with H2A, H2B, H3 and H4 histones. Binds to
CC HIV-1 Rev.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SIMILARITY: Belongs to the importin beta family.
CC -!- SIMILARITY: Contains 1 importin N-terminal domain.
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DR EMBL; AF098799; AAC68903.1; -; mRNA.
DR EMBL; AK312885; BAG35733.1; -; mRNA.
DR EMBL; AC055845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68593.1; -; Genomic_DNA.
DR EMBL; BC114929; AAI14930.1; -; mRNA.
DR EMBL; AJ295844; CAC17609.1; -; Genomic_DNA.
DR EMBL; AL137335; CAB70698.1; -; mRNA.
DR PIR; T46501; T46501.
DR RefSeq; NP_006382.1; NM_006391.2.
DR UniGene; Hs.744911; -.
DR ProteinModelPortal; O95373; -.
DR SMR; O95373; 2-440.
DR DIP; DIP-32574N; -.
DR IntAct; O95373; 13.
DR MINT; MINT-5003960; -.
DR STRING; 9606.ENSP00000369042; -.
DR PhosphoSite; O95373; -.
DR PaxDb; O95373; -.
DR PRIDE; O95373; -.
DR Ensembl; ENST00000379719; ENSP00000369042; ENSG00000205339.
DR GeneID; 10527; -.
DR KEGG; hsa:10527; -.
DR UCSC; uc001mho.3; human.
DR CTD; 10527; -.
DR GeneCards; GC11P009362; -.
DR HGNC; HGNC:9852; IPO7.
DR HPA; HPA019002; -.
DR MIM; 605586; gene.
DR neXtProt; NX_O95373; -.
DR PharmGKB; PA34213; -.
DR eggNOG; COG5656; -.
DR HOGENOM; HOG000006586; -.
DR HOVERGEN; HBG006824; -.
DR InParanoid; O95373; -.
DR OMA; HAVTWKN; -.
DR OrthoDB; EOG7TF787; -.
DR ChiTaRS; IPO7; human.
DR GeneWiki; IPO7; -.
DR GenomeRNAi; 10527; -.
DR NextBio; 39938; -.
DR PRO; PR:O95373; -.
DR ArrayExpress; O95373; -.
DR Bgee; O95373; -.
DR CleanEx; HS_IPO7; -.
DR Genevestigator; O95373; -.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0008536; F:Ran GTPase binding; TAS:ProtInc.
DR GO; GO:0005083; F:small GTPase regulator activity; TAS:ProtInc.
DR GO; GO:0005215; F:transporter activity; TAS:ProtInc.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013713; Cse1.
DR InterPro; IPR001494; Importin-beta_N.
DR Pfam; PF08506; Cse1; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Nucleus; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 1038 Importin-7.
FT /FTId=PRO_0000120750.
FT DOMAIN 22 101 Importin N-terminal.
FT COMPBIAS 885 957 Asp-rich.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 886 886 Phosphoserine.
FT MOD_RES 898 898 Phosphothreonine.
FT MOD_RES 903 903 Phosphoserine.
FT VARIANT 111 111 T -> N (in dbSNP:rs11042340).
FT /FTId=VAR_050003.
FT MUTAGEN 61 61 K->A,D: Lowered affinity for RanGTP-
FT binding.
SQ SEQUENCE 1038 AA; 119517 MW; 355237CA1DA2D313 CRC64;
MDPNTIIEAL RGTMDPALRE AAERQLNEAH KSLNFVSTLL QITMSEQLDL PVRQAGVIYL
KNMITQYWPD RETAPGDISP YTIPEEDRHC IRENIVEAII HSPELIRVQL TTCIHHIIKH
DYPSRWTAIV DKIGFYLQSD NSACWLGILL CLYQLVKNYE YKKPEERSPL VAAMQHFLPV
LKDRFIQLLS DQSDQSVLIQ KQIFKIFYAL VQYTLPLELI NQQNLTEWIE ILKTVVNRDV
PNETLQVEED DRPELPWWKC KKWALHILAR LFERYGSPGN VSKEYNEFAE VFLKAFAVGV
QQVLLKVLYQ YKEKQYMAPR VLQQTLNYIN QGVSHALTWK NLKPHIQGII QDVIFPLMCY
TDADEELWQE DPYEYIRMKF DVFEDFISPT TAAQTLLFTA CSKRKEVLQK TMGFCYQILT
EPNADPRKKD GALHMIGSLA EILLKKKIYK DQMEYMLQNH VFPLFSSELG YMRARACWVL
HYFCEVKFKS DQNLQTALEL TRRCLIDDRE MPVKVEAAIA LQVLISNQEK AKEYITPFIR
PVMQALLHII RETENDDLTN VIQKMICEYS EEVTPIAVEM TQHLAMTFNQ VIQTGPDEEG
SDDKAVTAMG ILNTIDTLLS VVEDHKEITQ QLEGICLQVI GTVLQQHVLE FYEEIFSLAH
SLTCQQVSPQ MWQLLPLVFE VFQQDGFDYF TDMMPLLHNY VTVDTDTLLS DTKYLEMIYS
MCKKVLTGVA GEDAECHAAK LLEVIILQCK GRGIDQCIPL FVEAALERLT REVKTSELRT
MCLQVAIAAL YYNPHLLLNT LENLRFPNNV EPVTNHFITQ WLNDVDCFLG LHDRKMCVLG
LCALIDMEQI PQVLNQVSGQ ILPAFILLFN GLKRAYACHA EHENDSDDDD EAEDDDETEE
LGSDEDDIDE DGQEYLEILA KQAGEDGDDE DWEEDDAEET ALEGYSTIID DEDNPVDEYQ
IFKAIFQTIQ NRNPVWYQAL THGLNEEQRK QLQDIATLAD QRRAAHESKM IEKHGGYKFS
APVVPSSFNF GGPAPGMN
//
MIM
605586
*RECORD*
*FIELD* NO
605586
*FIELD* TI
*605586 IMPORTIN 7; IPO7
;;RAN-BINDING PROTEIN 7; RANBP7
*FIELD* TX
CLONING
The transport of protein and large RNAs through the nuclear pore
read morecomplexes (NPC) is an energy-dependent and regulated process. The import
of proteins with a nuclear localization signal (NLS) is accomplished by
recognition of one or more clusters of basic amino acids by the
importin-alpha/beta complex; see 600685 and 602738. The small GTPase RAN
(601179) plays a key role in NLS-dependent protein import. Gorlich et
al. (1997) purified a human Ran-binding protein, which they designated
RANBP7, from HeLa cell extract using a column with an immobilized
importin-beta-binding (IBB) domain. Both Xenopus and human RANBP7 bind
to the IBB domain of importin-alpha via importin-beta. Human RANBP7 is
approximately 95% identical to the Xenopus protein RanBP7. RANBP7
belongs to a Ran-binding protein superfamily whose members share with
importin-beta an N-terminal sequence motif that appears to account for
RanGTP binding.
GENE FUNCTION
Based on oocyte injection experiments, Gorlich et al. (1997) showed that
Xenopus RanBP7 is predominantly a cytoplasmic protein that shuttles
between nucleus and cytoplasm. Fluorescence labeling experiments
indicated that RanBP7 binds to NPC at the same site as importin-beta.
Although interaction between RanBP7 and importin-beta is unrelated to
NLS-mediated protein import, RanBP7 binds to RanGTP. RanGTP/RanBP7
binding prevents formation of the RanBP7/importin-beta complex and
dissolves preformed RanBP7/importin-beta complex. The authors
demonstrated that RanBP7 can form a trimeric complex with RanGTP and
RanBP1 (601180), and that RanBP7 inhibits GAP stimulation of the Ran
GTPase. Furthermore, RanBP7 requires nuclear RanGTP for export and is
exported as a complex with RanGTP.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RANBP7
gene to chromosome 11 (TMAP WI-31060).
*FIELD* RF
1. Gorlich, D.; Dabrowski, M.; Bischoff, F. R.; Kutay, U.; Bork, P.;
Hartmann, E.; Prehn, S.; Izaurralde, E.: A novel class of RanGTP
binding proteins. J. Cell Biol. 138: 65-80, 1997.
*FIELD* CD
Yen-Pei C. Chang: 1/25/2001
*FIELD* ED
alopez: 07/17/2009
carol: 3/13/2003
carol: 12/19/2001
carol: 2/5/2001
cwells: 1/29/2001
*RECORD*
*FIELD* NO
605586
*FIELD* TI
*605586 IMPORTIN 7; IPO7
;;RAN-BINDING PROTEIN 7; RANBP7
*FIELD* TX
CLONING
The transport of protein and large RNAs through the nuclear pore
read morecomplexes (NPC) is an energy-dependent and regulated process. The import
of proteins with a nuclear localization signal (NLS) is accomplished by
recognition of one or more clusters of basic amino acids by the
importin-alpha/beta complex; see 600685 and 602738. The small GTPase RAN
(601179) plays a key role in NLS-dependent protein import. Gorlich et
al. (1997) purified a human Ran-binding protein, which they designated
RANBP7, from HeLa cell extract using a column with an immobilized
importin-beta-binding (IBB) domain. Both Xenopus and human RANBP7 bind
to the IBB domain of importin-alpha via importin-beta. Human RANBP7 is
approximately 95% identical to the Xenopus protein RanBP7. RANBP7
belongs to a Ran-binding protein superfamily whose members share with
importin-beta an N-terminal sequence motif that appears to account for
RanGTP binding.
GENE FUNCTION
Based on oocyte injection experiments, Gorlich et al. (1997) showed that
Xenopus RanBP7 is predominantly a cytoplasmic protein that shuttles
between nucleus and cytoplasm. Fluorescence labeling experiments
indicated that RanBP7 binds to NPC at the same site as importin-beta.
Although interaction between RanBP7 and importin-beta is unrelated to
NLS-mediated protein import, RanBP7 binds to RanGTP. RanGTP/RanBP7
binding prevents formation of the RanBP7/importin-beta complex and
dissolves preformed RanBP7/importin-beta complex. The authors
demonstrated that RanBP7 can form a trimeric complex with RanGTP and
RanBP1 (601180), and that RanBP7 inhibits GAP stimulation of the Ran
GTPase. Furthermore, RanBP7 requires nuclear RanGTP for export and is
exported as a complex with RanGTP.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RANBP7
gene to chromosome 11 (TMAP WI-31060).
*FIELD* RF
1. Gorlich, D.; Dabrowski, M.; Bischoff, F. R.; Kutay, U.; Bork, P.;
Hartmann, E.; Prehn, S.; Izaurralde, E.: A novel class of RanGTP
binding proteins. J. Cell Biol. 138: 65-80, 1997.
*FIELD* CD
Yen-Pei C. Chang: 1/25/2001
*FIELD* ED
alopez: 07/17/2009
carol: 3/13/2003
carol: 12/19/2001
carol: 2/5/2001
cwells: 1/29/2001