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O95373 (IPO7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Importin-7

Short name=Imp7
Alternative name(s):
Ran-binding protein 7
Short name=RanBP7
Gene names
Name:IPO7
Synonyms:RANBP7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1038 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with the importin-beta subunit KPNB1. Acting autonomously, is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. 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. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with KPNB1 mediates the nuclear import of H1 histone and the Ran-binding site of IPO7 is not required but synergizes with that of KPNB1 in importin/substrate complex dissociation. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In vitro, mediates the nuclear import of HIV-1 reverse transcription complex (RTC) integrase. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Ref.1 Ref.10 Ref.12

Subunit structure

Interacts with H2A, H2B, H3 and H4 histones By similarity. Forms a heterodimer with KPNB1. Interacts with KPNB1, SNUPN, XPO1, RPL23A, RPS7, RPL5 and HIV-1 reverse transcription complex integrase. Binds directly to nuclear pore complexes By similarity. Interacts with H2A, H2B, H3 and H4 histones. Binds to HIV-1 Rev. Ref.1 Ref.10 Ref.11 Ref.12 Ref.14

Subcellular location

Cytoplasm. Nucleus.

Sequence similarities

Belongs to the importin beta family.

Contains 1 importin N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10381038Importin-7
PRO_0000120750

Regions

Domain22 – 10180Importin N-terminal
Compositional bias885 – 95773Asp-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.6 Ref.16 Ref.18 Ref.19
Modified residue8861Phosphoserine Ref.15
Modified residue8981Phosphothreonine Ref.15
Modified residue9031Phosphoserine Ref.15

Natural variations

Natural variant1111T → N.
Corresponds to variant rs11042340 [ dbSNP | Ensembl ].
VAR_050003

Experimental info

Mutagenesis611K → A or D: Lowered affinity for RanGTP-binding. Ref.10

Sequences

Sequence LengthMass (Da)Tools
O95373 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 355237CA1DA2D313

FASTA1,038119,517
        10         20         30         40         50         60 
MDPNTIIEAL RGTMDPALRE AAERQLNEAH KSLNFVSTLL QITMSEQLDL PVRQAGVIYL 

        70         80         90        100        110        120 
KNMITQYWPD RETAPGDISP YTIPEEDRHC IRENIVEAII HSPELIRVQL TTCIHHIIKH 

       130        140        150        160        170        180 
DYPSRWTAIV DKIGFYLQSD NSACWLGILL CLYQLVKNYE YKKPEERSPL VAAMQHFLPV 

       190        200        210        220        230        240 
LKDRFIQLLS DQSDQSVLIQ KQIFKIFYAL VQYTLPLELI NQQNLTEWIE ILKTVVNRDV 

       250        260        270        280        290        300 
PNETLQVEED DRPELPWWKC KKWALHILAR LFERYGSPGN VSKEYNEFAE VFLKAFAVGV 

       310        320        330        340        350        360 
QQVLLKVLYQ YKEKQYMAPR VLQQTLNYIN QGVSHALTWK NLKPHIQGII QDVIFPLMCY 

       370        380        390        400        410        420 
TDADEELWQE DPYEYIRMKF DVFEDFISPT TAAQTLLFTA CSKRKEVLQK TMGFCYQILT 

       430        440        450        460        470        480 
EPNADPRKKD GALHMIGSLA EILLKKKIYK DQMEYMLQNH VFPLFSSELG YMRARACWVL 

       490        500        510        520        530        540 
HYFCEVKFKS DQNLQTALEL TRRCLIDDRE MPVKVEAAIA LQVLISNQEK AKEYITPFIR 

       550        560        570        580        590        600 
PVMQALLHII RETENDDLTN VIQKMICEYS EEVTPIAVEM TQHLAMTFNQ VIQTGPDEEG 

       610        620        630        640        650        660 
SDDKAVTAMG ILNTIDTLLS VVEDHKEITQ QLEGICLQVI GTVLQQHVLE FYEEIFSLAH 

       670        680        690        700        710        720 
SLTCQQVSPQ MWQLLPLVFE VFQQDGFDYF TDMMPLLHNY VTVDTDTLLS DTKYLEMIYS 

       730        740        750        760        770        780 
MCKKVLTGVA GEDAECHAAK LLEVIILQCK GRGIDQCIPL FVEAALERLT REVKTSELRT 

       790        800        810        820        830        840 
MCLQVAIAAL YYNPHLLLNT LENLRFPNNV EPVTNHFITQ WLNDVDCFLG LHDRKMCVLG 

       850        860        870        880        890        900 
LCALIDMEQI PQVLNQVSGQ ILPAFILLFN GLKRAYACHA EHENDSDDDD EAEDDDETEE 

       910        920        930        940        950        960 
LGSDEDDIDE DGQEYLEILA KQAGEDGDDE DWEEDDAEET ALEGYSTIID DEDNPVDEYQ 

       970        980        990       1000       1010       1020 
IFKAIFQTIQ NRNPVWYQAL THGLNEEQRK QLQDIATLAD QRRAAHESKM IEKHGGYKFS 

      1030 
APVVPSSFNF GGPAPGMN 

« Hide

References

« Hide 'large scale' references
[1]"Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells."
Jaekel S., Goerlich D.
EMBO J. 17:4491-4502(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RPL23A; RPS7; RPL5 AND KPNB1.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Uterus.
[3]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-11, ACETYLATION AT MET-1.
Tissue: Platelet.
[7]"Comparative sequencing of a 1 Mb region in man (chromosome 11p15) and mouse (chromosome 7)."
Cichutek A., Winterpacht A., Hankeln T., Schmidt E.R., Zabel B.U.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-1038.
Tissue: Blood.
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 831-1038.
Tissue: Testis.
[9]"A novel class of RanGTP binding proteins."
Goerlich D., Dabrowski M., Bischoff F.R., Kutay U., Bork P., Hartmann E., Prehn S., Izaurralde E.
J. Cell Biol. 138:65-80(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[10]"The importin beta/importin 7 heterodimer is a functional nuclear import receptor for histone H1."
Jaekel S., Albig W., Kutay U., Bischoff F.R., Schwamborn K., Doenecke D., Goerlich D.
EMBO J. 18:2411-2423(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH H1 HISTONE AND KPNB1, MUTAGENESIS OF LYS-61.
[11]"CRM1-mediated recycling of snurportin 1 to the cytoplasm."
Paraskeva E., Izaurralde E., Bischoff F.R., Huber J., Kutay U., Hartmann E., Luehrmann R., Goerlich D.
J. Cell Biol. 145:255-264(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN EXPORT RECEPTOR COMPLEX, INTERACTION WITH KPNB1; SNUPN AND XPO1.
[12]"Nuclear import of HIV-1 intracellular reverse transcription complexes is mediated by importin 7."
Fassati A., Goerlich D., Harrison I., Zaytseva L., Mingot J.-M.
EMBO J. 22:3675-3685(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH INTEGRASE OF HIV-1 REVERSE TRANSCRIPTION COMPLEX.
[13]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Multiple importins function as nuclear transport receptors for the Rev protein of human immunodeficiency virus type 1."
Arnold M., Nath A., Hauber J., Kehlenbach R.H.
J. Biol. Chem. 281:20883-20890(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 REV.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886; THR-898 AND SER-903, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF098799 mRNA. Translation: AAC68903.1.
AK312885 mRNA. Translation: BAG35733.1.
AC055845 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68593.1.
BC114929 mRNA. Translation: AAI14930.1.
AJ295844 Genomic DNA. Translation: CAC17609.1.
AL137335 mRNA. Translation: CAB70698.1.
PIRT46501.
RefSeqNP_006382.1. NM_006391.2.
UniGeneHs.744911.

3D structure databases

ProteinModelPortalO95373.
SMRO95373. Positions 2-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115782. 33 interactions.
DIPDIP-32574N.
IntActO95373. 14 interactions.
MINTMINT-5003960.
STRING9606.ENSP00000369042.

PTM databases

PhosphoSiteO95373.

Proteomic databases

PaxDbO95373.
PRIDEO95373.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379719; ENSP00000369042; ENSG00000205339.
GeneID10527.
KEGGhsa:10527.
UCSCuc001mho.3. human.

Organism-specific databases

CTD10527.
GeneCardsGC11P009362.
HGNCHGNC:9852. IPO7.
HPAHPA019002.
MIM605586. gene.
neXtProtNX_O95373.
PharmGKBPA34213.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5656.
HOGENOMHOG000006586.
HOVERGENHBG006824.
InParanoidO95373.
OMAHAVTWKN.
OrthoDBEOG7TF787.
PhylomeDBO95373.
TreeFamTF300634.

Gene expression databases

ArrayExpressO95373.
BgeeO95373.
CleanExHS_IPO7.
GenevestigatorO95373.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013713. Cse1.
IPR001494. Importin-beta_N.
[Graphical view]
PfamPF08506. Cse1. 1 hit.
PF03810. IBN_N. 1 hit.
[Graphical view]
SMARTSM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 2 hits.
PROSITEPS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIPO7. human.
GeneWikiIPO7.
GenomeRNAi10527.
NextBio39938.
PROO95373.
SOURCESearch...

Entry information

Entry nameIPO7_HUMAN
AccessionPrimary (citable) accession number: O95373
Secondary accession number(s): A6NNM5 expand/collapse secondary AC list , B2R786, Q1RMF7, Q9H177, Q9NTE3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM