O95373 (IPO7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Importin-7
Short name=Imp7

Alternative name(s):
Ran-binding protein 7
Short name=RanBP7

Gene names

Name:	IPO7
Synonyms:	RANBP7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1038 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Host-virus interaction Protein transport Transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein import into nucleus Inferred from electronic annotation. Source: Compara signal transduction Traceable author statement Ref.9. Source: ProtInc virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA nuclear pore Traceable author statement Ref.9. Source: ProtInc
Molecular_function	Ran GTPase binding Traceable author statement Ref.9. Source: ProtInc protein transporter activity Inferred from electronic annotation. Source: InterPro small GTPase regulator activity Traceable author statement Ref.9. Source: ProtInc transporter activity Traceable author statement Ref.9. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1038	1038	Importin-7		PRO_0000120750
Regions
	Domain	22 – 101	80	Importin N-terminal
	Compositional bias	885 – 957	73	Asp-rich
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.6
	Modified residue	886	1	Phosphoserine Ref.15
	Modified residue	898	1	Phosphothreonine Ref.15
	Modified residue	903	1	Phosphoserine Ref.15
Natural variations
	Natural variant	111	1	T → N. Corresponds to variant rs11042340 [ dbSNP | Ensembl ].		VAR_050003
Experimental info
	Mutagenesis	61	1	K → A or D: Lowered affinity for RanGTP-binding. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	O95373 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 355237CA1DA2D313	FASTA	1,038	119,517
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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].
+	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.
IPI	IPI00007402.
PIR	T46501.
RefSeq	NP_006382.1. NM_006391.2.
UniGene	Hs.740445.
3D structure databases
ProteinModelPortal	O95373.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-32574N.
IntAct	O95373. 11 interactions.
MINT	MINT-5003960.
STRING	9606.ENSP00000369042.
PTM databases
PhosphoSite	O95373.
Proteomic databases
PaxDb	O95373.
PRIDE	O95373.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000379719; ENSP00000369042; ENSG00000205339.
GeneID	10527.
KEGG	hsa:10527.
UCSC	uc001mho.3. human.
Organism-specific databases
CTD	10527.
GeneCards	GC11P009362.
HGNC	HGNC:9852. IPO7.
HPA	HPA019002.
MIM	605586. gene.
neXtProt	NX_O95373.
PharmGKB	PA34213.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5656.
HOGENOM	HOG000006586.
HOVERGEN	HBG006824.
InParanoid	O95373.
OMA	HAVTWKN.
OrthoDB	EOG4N30N5.
Gene expression databases
ArrayExpress	O95373.
Bgee	O95373.
CleanEx	HS_IPO7.
Genevestigator	O95373.
Family and domain databases
Gene3D	1.25.10.10. 2 hits.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR013713. Exportin/Importin_Cse1-like. IPR001494. Importin-beta_N. [Graphical view]
Pfam	PF08506. Cse1. 1 hit. PF03810. IBN_N. 1 hit. [Graphical view]
SMART	SM00913. IBN_N. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS50166. IMPORTIN_B_NT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	IPO7. human.
GenomeRNAi	10527.
NextBio	39938.
SOURCE	Search...

Entry information

Entry name

IPO7_HUMAN

Accession

Primary (citable) accession number: O95373
Secondary accession number(s): A6NNM5 , B2R786, Q1RMF7, Q9H177, Q9NTE3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.