O00410 (IPO5_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 129.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Importin-5 Short name=Imp5 Alternative name(s): Importin subunit beta-3 Karyopherin beta-3 Ran-binding protein 5 Short name=RanBP5 | ||||
| Gene names |
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| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 1097 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the 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 By similarity. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Ref.8 |
| Subunit structure | Binds RPL23A, RPS7 and RPL5. Interacts with H2A, H2B, H3 and H4 histones By similarity. Binds to HIV-1 Rev. Ref.8 Ref.10 |
| Subcellular location | Cytoplasm. Nucleus. Nucleus › nucleolus. Note: Nucleus; nuclear rim. Found particularly in the nuclear rim and nucleolus. |
| Sequence similarities | Belongs to the importin beta family. Contains 6 HEAT repeats. Contains 1 importin N-terminal domain. |
| Sequence caution | The sequence CAA70103.1 differs from that shown. Reason: Frameshift at position 18. Isoform 3: The sequence CAA70103.1 differs from that shown. Reason: Frameshift at position 18. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| GABARAP | O95166 | 6 | EBI-356424,EBI-712001 | |
| GABARAPL1 | Q9H0R8 | 4 | EBI-356424,EBI-746969 | |
| GABARAPL2 | P60520 | 5 | EBI-356424,EBI-720116 | |
| MAP1LC3B | Q9GZQ8 | 2 | EBI-356424,EBI-373144 | |
| MAP1LC3C | Q9BXW4 | 2 | EBI-356424,EBI-2603996 |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: O00410-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: O00410-2) The sequence of this isoform differs from the canonical sequence as follows: 1-60: Missing. | ||||||
| Isoform 3 (identifier: O00410-3) The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → MPEDQVGKLEATENTISAM |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.7 | ||||||
| Chain | 2 – 1097 | 1096 | Importin-5 | PRO_0000120771 | |||||
Regions | |||||||||
| Domain | 28 – 99 | 72 | Importin N-terminal | ||||||
| Repeat | 212 – 249 | 38 | HEAT 1 | ||||||
| Repeat | 395 – 432 | 38 | HEAT 2 | ||||||
| Repeat | 437 – 475 | 39 | HEAT 3 | ||||||
| Repeat | 859 – 897 | 39 | HEAT 4 | ||||||
| Repeat | 901 – 938 | 38 | HEAT 5 | ||||||
| Repeat | 942 – 979 | 38 | HEAT 6 | ||||||
| Region | 325 – 375 | 51 | Ran-GTP binding By similarity | ||||||
| Compositional bias | 2 – 6 | 5 | Poly-Ala | ||||||
| Compositional bias | 460 – 465 | 6 | Poly-Ala | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.7 | ||||||
| Modified residue | 827 | 1 | Phosphoserine Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 60 | 60 | Missing in isoform 2. | VSP_037587 | |||||
| Alternative sequence | 1 | 1 | M → MPEDQVGKLEATENTISAM in isoform 3. | VSP_037774 | |||||
| Natural variant | 286 | 1 | L → I. Corresponds to variant rs1053814 [ dbSNP | Ensembl ]. | VAR_012029 | |||||
| Natural variant | 525 | 1 | E → K. Corresponds to variant rs632729 [ dbSNP | Ensembl ]. | VAR_012030 | |||||
| Natural variant | 549 | 1 | E → K. Corresponds to variant rs484770 [ dbSNP | Ensembl ]. | VAR_012031 | |||||
| Natural variant | 905 | 1 | Y → C. Corresponds to variant rs1804740 [ dbSNP | Ensembl ]. | VAR_012032 | |||||
| Natural variant | 969 | 1 | T → I. Corresponds to variant rs1804741 [ dbSNP | Ensembl ]. | VAR_012033 | |||||
Experimental info | |||||||||
| Sequence conflict | 538 | 1 | L → R in AAH45640. Ref.6 | ||||||
| Sequence conflict | 826 – 827 | 2 | ES → GT in AAC51317. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and characterization of human karyopherin beta3." Yaseen N.R., Blobel G. Proc. Natl. Acad. Sci. U.S.A. 94:4451-4456(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION. Tissue: Bone marrow. |
| [2] | "Ran-binding protein 5 (RanBP5) is related to the nuclear transport factor importin-beta but interacts differently with RanBP1." Deane R., Schaeffer W., Zimmermann H.-P., Mueller L., Goerlich D., Prehn S., Ponstingl H., Bischoff F.R. Mol. Cell. Biol. 17:5087-5096(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). |
| [3] | "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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Testis. |
| [4] | "The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. Ross M.T.Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | 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. Venter J.C.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [6] | "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] (ISOFORMS 1 AND 3). Tissue: Lung and Testis. |
| [7] | Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M. Submitted (MAY-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: T-cell. |
| [8] | "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: FUNCTION, NUCLEAR LOCALIZATION SIGNAL RECOGNITION, INTERACTION WITH RPL23A; RPS7 AND RPL5. |
| [9] | "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [10] | "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. |
| [11] | "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [12] | "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-827, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [13] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [14] | "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [15] | "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 | U72761 mRNA. Translation: AAC51317.1. Y08890 mRNA. Translation: CAA70103.1. Frameshift. AK302812 mRNA. Translation: BAG64012.1. AL356580, AL137120 Genomic DNA. Translation: CAI13757.1. AL137120, AL356580 Genomic DNA. Translation: CAI16520.1. CH471085 Genomic DNA. Translation: EAX08980.1. BC001497 mRNA. Translation: AAH01497.1. BC019309 mRNA. Translation: AAH19309.1. BC045640 mRNA. Translation: AAH45640.1. |
| IPI | IPI00793443. IPI00937471. IPI00939304. |
| RefSeq | NP_002262.3. NM_002271.4. |
| UniGene | Hs.712598. |
3D structure databases | |
| ProteinModelPortal | O00410. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-41042N. |
| IntAct | O00410. 16 interactions. |
| MINT | MINT-132356. |
| STRING | 9606.ENSP00000261574. |
PTM databases | |
| PhosphoSite | O00410. |
Proteomic databases | |
| PaxDb | O00410. |
| PRIDE | O00410. |
Protocols and materials databases | |
| DNASU | 3843. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000261574; ENSP00000261574; ENSG00000065150. ENST00000357602; ENSP00000350219; ENSG00000065150. ENST00000490680; ENSP00000418393; ENSG00000065150. |
| GeneID | 3843. |
| KEGG | hsa:3843. |
| UCSC | uc001vne.3. human. uc001vnf.1. human. |
Organism-specific databases | |
| CTD | 3843. |
| GeneCards | GC13P098605. |
| H-InvDB | HIX0174410. |
| HGNC | HGNC:6402. IPO5. |
| HPA | CAB009110. |
| MIM | 602008. gene. |
| neXtProt | NX_O00410. |
| PharmGKB | PA30193. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | COG5215. |
| HOGENOM | HOG000209725. |
| HOVERGEN | HBG006156. |
| InParanoid | O00410. |
| OMA | FHDGVRV. |
| OrthoDB | EOG4XGZZ8. |
Gene expression databases | |
| ArrayExpress | O00410. |
| Bgee | O00410. |
| CleanEx | HS_IPO5. |
| Genevestigator | O00410. |
| GermOnline | ENSG00000065150. Homo sapiens. |
Family and domain databases | |
| Gene3D | 1.25.10.10. 3 hits. |
| InterPro | IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR000357. HEAT. IPR001494. Importin-beta_N. [Graphical view] |
| Pfam | PF02985. HEAT. 2 hits. [Graphical view] |
| SUPFAM | SSF48371. ARM-type_fold. 2 hits. |
| PROSITE | PS50077. HEAT_REPEAT. False negative. PS50166. IMPORTIN_B_NT. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | IPO5. human. |
| GenomeRNAi | 3843. |
| NextBio | 15125. |
| SOURCE | Search... |
Entry information
| Entry name | IPO5_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O00410 Secondary accession number(s): B4DZA0 Q86XC7 | ||||||||
| Entry history |
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| 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. | ||||||||
Relevant documents
| Human chromosome 13 Human chromosome 13: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
